{"search_session":{},"preferences":{"l":"en","queryLanguage":"en"},"patentId":"157-672-321-546-246","frontPageModel":{"patentViewModel":{"ref":{"entityRefType":"PATENT","entityRefId":"157-672-321-546-246"},"entityMetadata":{"linkedIds":{"empty":true},"tags":[],"collections":[{"id":184804,"type":"PATENT","title":"cancer metodo","description":"metodo cancer","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":50000,"tags":[],"user":{"id":371336820,"username":"brevelo","firstName":"","lastName":"","created":"2020-09-30T00:10:43.000Z","displayName":"brevelo","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2020-10-28T00:54:30Z","updated":"2020-10-28T00:56:49Z","lastEventDate":"2020-10-28T00:56:49Z"},{"id":190767,"type":"PATENT","title":"oral cancer","description":"","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":39080,"tags":[],"user":{"id":310416190,"username":"harsha_iimb","firstName":"","lastName":"","created":"2019-03-20T03:25:41.000Z","displayName":"harsha_iimb","preferences":"{\"beta\":true}","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":true,"savedQueries":[],"created":"2021-04-28T19:37:11Z","updated":"2024-03-28T02:15:55Z","lastEventDate":"2024-03-28T02:15:55Z"},{"id":191230,"type":"PATENT","title":"CellAdhesionANDSubtrateANDCancerCell","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:10:45Z","updated":"2021-05-17T14:10:50Z","lastEventDate":"2021-05-17T14:10:50Z"},{"id":191231,"type":"PATENT","title":"CellAdhesionANDsubstrateANDLeukemia","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:13:25Z","updated":"2021-05-17T14:13:28Z","lastEventDate":"2021-05-17T14:13:28Z"}],"notes":[],"inventorships":[],"privateCollections":[],"publicCollections":[{"id":184804,"type":"PATENT","title":"cancer metodo","description":"metodo cancer","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":50000,"tags":[],"user":{"id":371336820,"username":"brevelo","firstName":"","lastName":"","created":"2020-09-30T00:10:43.000Z","displayName":"brevelo","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2020-10-28T00:54:30Z","updated":"2020-10-28T00:56:49Z","lastEventDate":"2020-10-28T00:56:49Z"},{"id":190767,"type":"PATENT","title":"oral cancer","description":"","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":39080,"tags":[],"user":{"id":310416190,"username":"harsha_iimb","firstName":"","lastName":"","created":"2019-03-20T03:25:41.000Z","displayName":"harsha_iimb","preferences":"{\"beta\":true}","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":true,"savedQueries":[],"created":"2021-04-28T19:37:11Z","updated":"2024-03-28T02:15:55Z","lastEventDate":"2024-03-28T02:15:55Z"},{"id":191230,"type":"PATENT","title":"CellAdhesionANDSubtrateANDCancerCell","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:10:45Z","updated":"2021-05-17T14:10:50Z","lastEventDate":"2021-05-17T14:10:50Z"},{"id":191231,"type":"PATENT","title":"CellAdhesionANDsubstrateANDLeukemia","description":"","access":"OPEN_ACCESS","displayAvatar":false,"attested":false,"itemCount":50000,"tags":[],"user":{"id":404574126,"username":"JaimeGarcia","firstName":"","lastName":"","created":"2021-05-17T13:10:07.000Z","displayName":"JaimeGarcia","accountType":"PERSONAL","isOauthOnly":false},"notes":[],"sharedType":"PUBLISHED","hasLinkedSavedQueries":false,"savedQueries":[],"created":"2021-05-17T14:13:25Z","updated":"2021-05-17T14:13:28Z","lastEventDate":"2021-05-17T14:13:28Z"}],"privateNotes":[],"landscapeCollections":[],"landscapeNotes":[]},"document":{"record_lens_id":"157-672-321-546-246","lens_id":["157-672-321-546-246","176-252-747-585-849"],"doc_key":"US_20160101076_A1_20160414","created":"2016-04-23T00:48:37.776","docdb_id":451223651,"lens_internal":{"earliest_lens_id_created_time":"2016-04-23T00:48:37.776","last_modified":"2024-03-25T20:21:02.386","legacy_pub_key":"US_2016_0101076_A1","has_doc_lang":true,"has_biblio_lang":true,"has_all_title_lang":true,"has_all_abstract_lang":true,"has_all_claims_lang":true,"has_description_lang":true},"jurisdiction":"US","doc_number":"20160101076","kind":"A1","date_published":"2016-04-14","year_published":2016,"ids":["US_2016_0101076_A1","157-672-321-546-246","176-252-747-585-849","US_20160101076_A1_20160414","US","20160101076","A1","US20160101076A1","US20160101076","20160101076A1"],"lang":"en","publication_type":"PATENT_APPLICATION","application_reference":{"jurisdiction":"US","doc_number":"201414890897","kind":"A","date":"2014-05-15"},"priority_claim":[{"jurisdiction":"US","doc_number":"201414890897","kind":"A","date":"2014-05-15"},{"jurisdiction":"US","doc_number":"201361823770","kind":"P","date":"2013-05-15"},{"jurisdiction":"US","doc_number":"2014038193","kind":"W","date":"2014-05-15"}],"priority_claim.source":"DOCDB","earliest_priority_claim_date":"2013-05-15","title":{"en":[{"text":"Use of Sumoylation Inhibitors for Treating Cancer","lang":"en","source":"DOCDB","data_format":"DOCDBA"}]},"title_lang":["en"],"has_title":true,"applicant":[{"name":"WEIGEL RONALD J","residence":"US","sequence":1,"app_type":"applicant"}],"applicant_count":1,"has_applicant":true,"inventor":[{"name":"WEIGEL RONALD J","residence":"US","sequence":1}],"inventor_count":1,"has_inventor":true,"agent":[],"agent_count":0,"has_agent":false,"owner":[],"owner_count":0,"owner_all":[],"owner_all_count":0,"has_owner":false,"has_examiner":false,"class_ipcr":[{"symbol":"A61K31/192","version_indicator":"2006-01-01","class_symbol_position":"F","class_value":"I","action_date":"2016-04-14","class_status":"B","class_data_source":"H","generating_office":"US","sequence":1},{"symbol":"A61K45/06","version_indicator":"2006-01-01","class_symbol_position":"L","class_value":"I","action_date":"2016-04-14","class_status":"B","class_data_source":"H","generating_office":"US","sequence":2},{"symbol":"A61N5/10","version_indicator":"2006-01-01","class_symbol_position":"L","class_value":"I","action_date":"2016-04-14","class_status":"B","class_data_source":"H","generating_office":"US","sequence":3},{"symbol":"G01N33/50","version_indicator":"2006-01-01","class_symbol_position":"L","class_value":"I","action_date":"2016-04-14","class_status":"B","class_data_source":"H","generating_office":"US","sequence":4}],"class_ipcr.first_symbol":"A61K31/192","class_ipcr.later_symbol":["A61K45/06","A61N5/10","G01N33/50"],"class_ipcr.inv_symbol":["A61K31/192","A61K45/06","A61N5/10","G01N33/50"],"class_ipcr.add_symbol":[],"class_ipcr.source":"DOCDB","class_cpc":[{"symbol":"A61K45/06","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2015-02-03","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":1},{"symbol":"G01N33/5011","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2015-02-27","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":2},{"symbol":"A61K31/192","version_indicator":"2013-01-01","class_symbol_position":"F","class_value":"I","action_date":"2014-12-12","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":3},{"symbol":"A61P35/00","version_indicator":"2018-01-01","class_symbol_position":"L","class_value":"I","action_date":"2020-03-27","class_status":"B","class_data_source":"H","generating_office":"EP","sequence":4},{"symbol":"A61K45/06","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2015-02-03","class_status":"B","class_data_source":"H","generating_office":"US","sequence":6},{"symbol":"G01N33/5011","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2015-02-27","class_status":"B","class_data_source":"H","generating_office":"US","sequence":7},{"symbol":"A61K31/192","version_indicator":"2013-01-01","class_symbol_position":"F","class_value":"I","action_date":"2014-12-12","class_status":"B","class_data_source":"H","generating_office":"US","sequence":8},{"symbol":"A61N5/10","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2016-04-14","class_status":"B","class_data_source":"H","generating_office":"US","sequence":9},{"symbol":"A61N2005/1098","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"A","action_date":"2016-04-14","class_status":"B","class_data_source":"H","generating_office":"US","sequence":10}],"class_cpc_cset":[{"class":[{"symbol":"A61K31/192","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2015-08-26","class_status":"B","class_data_source":"H","generating_office":"EP"},{"symbol":"A61K2300/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2015-08-26","class_status":"B","class_data_source":"H","generating_office":"EP"}],"sequence":5},{"class":[{"symbol":"A61K31/192","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US"},{"symbol":"A61K2300/00","version_indicator":"2013-01-01","class_symbol_position":"L","class_value":"I","action_date":"2019-10-11","class_status":"B","class_data_source":"H","generating_office":"US"}],"sequence":11}],"class_cpc.first_symbol":"A61K31/192","class_cpc.later_symbol":["A61K45/06","G01N33/5011","A61P35/00","A61K45/06","G01N33/5011","A61N5/10","A61N2005/1098"],"class_cpc.inv_symbol":["A61K45/06","G01N33/5011","A61K31/192","A61P35/00","A61K45/06","G01N33/5011","A61K31/192","A61N5/10"],"class_cpc.add_symbol":["A61N2005/1098"],"class_cpc.source":"DOCDB","class_national":[],"class_national.later_symbol":[],"reference_cited":[{"patent":{"num":1,"document_id":{"jurisdiction":"US","doc_number":"6107034","kind":"A","date":"2000-08-22","name":"WIEGEL RONALD J [US]"},"lens_id":"035-561-148-699-920","srep_office":"US","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":1}},{"patent":{"num":2,"document_id":{"jurisdiction":"US","doc_number":"6605589","kind":"B1","date":"2003-08-12","name":"UCKUN FATIH M [US], et al"},"lens_id":"070-812-252-177-332","srep_office":"US","category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"sequence":2}},{"npl":{"num":1,"text":"Sun et al. \"Inhibition of Histone Acetyltransferase Activity by Anacardic Acid Sensitizes Tumor Cells to Ionizing Radiation\". FEBS Letters. 2006; 580:4353-4356.","npl_type":"a","external_id":["10.1016/j.febslet.2006.06.092","16844118"],"record_lens_id":"042-540-235-815-556","lens_id":["179-135-615-247-633","042-540-235-815-556","134-211-983-097-340"],"sequence":3,"category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"srep_office":"US"}},{"npl":{"num":2,"text":"Hsieh et al. \"Cell Proliferation Inhibitory and Apoptosis-Inducing Properties of Anacardic Acid and Lunasin in Human Breast Cancer MDA-MB-231 Cells\". Food Chemistry. 2011; 125:630-636.","npl_type":"a","external_id":["10.1016/j.foodchem.2010.09.051"],"record_lens_id":"073-417-095-145-415","lens_id":["199-288-581-699-131","073-417-095-145-415"],"sequence":4,"category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"srep_office":"US"}},{"npl":{"num":3,"text":"Chu et al. \"Expression of GATA3 in MDA-MD-231 Triple-Negative Breast Cancer Cells Induces a Growth Inhibitory Response to TGFBeta\". PLoS ONE. 2013 April; 8(4):e61125.","npl_type":"a","external_id":["23577196","10.1371/journal.pone.0061125","pmc3620110"],"record_lens_id":"055-477-721-072-543","lens_id":["186-208-073-360-76X","183-192-932-728-33X","055-477-721-072-543"],"sequence":5,"category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"srep_office":"US"}},{"npl":{"num":4,"text":"Sheridan et al. \"CD44+/CD24- Breast Cancer Cells Exhibit Enhanced Invasive Properties: An Early Step Necessary for Metastasis\". Breast Cancer Research. 2006; 8:R59.","npl_type":"a","external_id":["pmc1779499","17062128","10.1186/bcr1610"],"record_lens_id":"089-580-466-001-893","lens_id":["158-236-652-613-98X","089-580-466-001-893","102-401-443-867-224"],"sequence":6,"category":[],"us_category":[],"cited_phase":"PRS","rel_claims":[],"srep_office":"US"}}],"reference_cited.source":"DOCDB","reference_cited.patent_count":2,"cites_patent":true,"reference_cited.npl_count":4,"reference_cited.npl_resolved_count":4,"cites_npl":true,"cites_resolved_npl":true,"cited_by":{"patent_count":2,"patent":[{"lens_id":"060-839-561-861-91X","document_id":{"jurisdiction":"WO","doc_number":"2019070807","kind":"A1"}},{"lens_id":"038-625-163-608-731","document_id":{"jurisdiction":"US","doc_number":"11052089","kind":"B2"}}]},"cited_by_patent":true,"family":{"simple":{"size":3,"id":231307394,"member":[{"lens_id":"042-903-487-239-487","document_id":{"jurisdiction":"WO","doc_number":"2014186573","kind":"A3","date":"2015-01-15"}},{"lens_id":"153-181-665-746-602","document_id":{"jurisdiction":"WO","doc_number":"2014186573","kind":"A2","date":"2014-11-20"}},{"lens_id":"157-672-321-546-246","document_id":{"jurisdiction":"US","doc_number":"20160101076","kind":"A1","date":"2016-04-14"}}]},"extended":{"size":3,"id":229892244,"member":[{"lens_id":"042-903-487-239-487","document_id":{"jurisdiction":"WO","doc_number":"2014186573","kind":"A3","date":"2015-01-15"}},{"lens_id":"153-181-665-746-602","document_id":{"jurisdiction":"WO","doc_number":"2014186573","kind":"A2","date":"2014-11-20"}},{"lens_id":"157-672-321-546-246","document_id":{"jurisdiction":"US","doc_number":"20160101076","kind":"A1","date":"2016-04-14"}}]}},"has_sequence":false,"legal_status":{"ipr_type":"patent for invention","granted":false,"earliest_filing_date":"2014-05-15","application_expiry_date":"2018-08-22","has_disclaimer":false,"patent_status":"DISCONTINUED","publication_count":1,"has_spc":false,"has_grant_event":false,"has_entry_into_national_phase":false},"abstract":{"en":[{"text":"The present invention provides methods and reagents for treating cancer cells for therapeutic purposes, by contacting with a sumoylation inhibitor in a dose effective to block sumoylation of TFAP2A. In breast cancer cells the sumoylation inhibitor induces a basal to luminal shift in phenotype. Sumoylation inhibitors also reduce the number of cancer stem cells in a cancer cell population. Inhibition of sumoylation makes cancer cells more responsive to conventional chemotherapeutic therapy and radiation therapy and decreases recurrence or development of metastases.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"abstract_lang":["en"],"has_abstract":true,"claim":{"en":[{"text":"1 . A method for treatment of cancer, the method comprising: contacting a cancer cell population with a sumoylation inhibitor in a dose effective to reduce the number of cancer cells in the population.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"2 . The method of claim 1 , wherein the dose of sumoylation inhibitor is effective to reduce levels of sumo-conjugated TFAP2A.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"3 . The method of claim 2 , wherein the method reduces the number of cancer stem cells, and reduction of cancer stem cells is monitored by determining the expression of CD44+ cells in the population.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"4 . The method of claim 1 , further comprising contacting the cancer cell population with one or more chemotherapeutic agents, wherein the population of cells has increased responsiveness to chemotherapeutic agents following contacting with a sumoylation inhibitor.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"5 . The method of claim 1 , further comprising treating the cancer cell population with radiation therapy, wherein the population of cells has increased responsiveness to radiation therapy following contacting with a sumoylation inhibitor.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"6 . The method of claim 1 , wherein the cancer cell population is a human cell population.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"7 . The method of claim 6 , wherein said cancer is a solid tumor.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"8 . The method of claim 6 , wherein said tumor is a carcinoma.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"9 . The method of claim 8 , wherein said tumor is a breast carcinoma.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"10 . The method of claim 9 , wherein the cancer cell population is a basal-type breast carcinoma, and wherein following contacting with the sumoylation inhibitor the basal-type carcinoma cells are induced to a luminal-type breast carcinoma phenotype.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"11 . The method of claim 10 , further comprising the step of monitoring expression of at least one marker indicative of the breast carcinoma phenotype.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"12 . The method of any one of claims 1 - 11 , wherein the sumoylation inhibitor is anacardic acid or a derivative or analog thereof.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"13 . The method of claim 12 , wherein the sumoylation inhibitor is gingkolic acid.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"14 . A method of screening for a candidate agent that is a sumoylation inhibitor useful in treatment of cancer, the method comprising: contacting a cancer cell with the candidate agent; and determining the concentration of sumo-conjugated TFAP2A, wherein a reduction in sumo-conjugated TFAP2A is indicative that the candidate agent is useful in cancer treatment.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"15 . The method of claim 14 , further comprising: contacting a population of cancer cells with the candidate agent; and determining the concentration of cancer stem cells, wherein a reduction in the number of cancer stem cells is indicative that the candidate agent is useful in cancer treatment.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"16 . The method of claim 15 , wherein the cancer stem cells are monitored by expression of CD44.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"claim_lang":["en"],"has_claim":true,"description":{"en":{"text":"INTRODUCTION The TFAP2C protein (TFAP2-gamma) is a sequence-specific DNA-binding transcription factor involved in the activation of several genes involved in mammary development, differentiation, and oncogenesis. It can act as either a homodimer or heterodimer with other family members and is induced during retinoic acid-mediated differentiation. It plays a role in the development of the eyes, face, body wall, limbs, and neural tube. The sequence-specific DNA-binding protein interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5′-GCCNNNGGC-3′ and activate genes involved in a large spectrum of important biological functions. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. Published studies have established a role for TFAP2C in the regulation of ESR1 (ERalpha) and ERBB2 (Her2) in breast carcinomas. TFAP2C has also been identified as a potential prognostic indicator for patients with breast tumors. Sumoylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle. The process of sumoylation involves the use of endogenous Small Ubiquitin-like Modifier (or SUMO) proteins, which are covalently attached to and detached from other proteins in cells to modify the function of those targeted proteins. SUMO proteins are similar to ubiquitin, and sumoylation is directed by an enzymatic cascade analogous to that involved in ubiquitination. In contrast to ubiquitin, SUMO is not used to tag proteins for degradation. Mature SUMO is produced when the last four amino acids of the C-terminus have been cleaved off to allow formation of an isopeptide bond between the C-terminal glycine residue of SUMO and an acceptor lysine on the target protein. SUMO modification of proteins has many functions. Among the most frequent and best studied are protein stability, nuclear-cytosolic transport, and transcriptional regulation. Typically, only a small fraction of a given protein is sumoylated and this modification is rapidly reversed by the action of desumoylating enzymes. The SUMO-1 modification of RanGAP1 (the first identified SUMO substrate) leads to its trafficking from cytosol to nuclear pore complex. The SUMO modification of hNinein leads to its movement from the centrosome to the nucleus. In many cases, SUMO modification of transcriptional regulators correlates with inhibition of transcription. There are 3 confirmed SUMO isoforms in humans; SUMO-1, SUMO-2, and SUMO-3. SUMO-2/3 show a high degree of similarity to each other and are distinct from SUMO-1. SUMO-4 shows similarity to -2/3 but it is as yet unclear whether it is a pseudogene or merely restricted in its expression pattern. PUBLICATIONS Eloranta J J, Hurst H C. Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. J Biol Chem. 2002 Aug. 23; 277(34):30798-804.Orso F, Corà D, Ubezio B, Provero P, Caselle M, Taverna D. Identification of functional TFAP2A and SP1 binding sites in new TFAP2A-modulated genes. BMC Genomics. 2010 Jun. 3; 11:355.Zhou C, Li X, Du W, Feng Y, Kong X, Li Y, Xiao L, Zhang P. Antitumor effects of ginkgolic acid in human cancer cell occur via cell cycle arrest and decrease the Bcl-2/Bax ratio to induce apoptosis. Chemotherapy. 2010; 56(5):393-402.Kessler J D, Kahle K T, Sun T, Meerbrey K L, Schlabach M R, Schmitt E M, Skinner S O, Xu Q, Li M Z, Hartman Z C, Rao M, Yu P, Dominguez-Vidana R, Liang A C, Solimini N L, Bernardi R J, Yu B, Hsu T, Golding I, Luo J, Osborne C K, Creighton C J, Hilsenbeck S G, Schiff R, Shaw C A, Elledge S J, Westbrook T F. A SUMOylation-dependent transcriptional subprogram is required for Myc-driven tumorigenesis. Science. 2012 Jan. 20; 335(6066):348-53. SUMMARY OF THE INVENTION The present invention provides methods and reagents for treating cancer cells, including but not limited to carcinomas, for therapeutic purposes. In the methods of the invention, cancer cells, including without limitation cancer stem cells, are contacted with a dose of a sumoylation inhibitor effective to block sumoylation of TFAP2A. The inhibition of TFAP2A sumoylation alters the phenotype of the cancer cell, and also makes the cell more responsive to conventional cancer therapeutics. In some embodiments, methods are provided for therapy of cancer with a sumoylation inhibitor as a single agent. In other embodiments methods are provided for a combination therapy for treating cancer with a sumoylation inhibitor and a chemotherapeutic agent, or a combination of a sumoylation inhibitor with radiation therapy. In some embodiments the sumoylation inhibitor is an anacardic acid or a derivative thereof, including, for example, ginkgolic acid. In such methods, an effective dose of a sumoylation inhibitor is administered to a cancer patient, in a combination with an effective dose of a chemotherapeutic agent or radiation therapy, wherein there is a decrease in the cancer cells present in the patient, for example a decrease in the cancer stem cells population. The synergy between treatment with sumoylation inhibitors and a chemotherapeutic agent or radiation therapy provide increased killing at equivalent or lower doses, and can sensitize otherwise resistant cells. In some embodiments of the invention, breast carcinoma cells, for example a population of basal-type breast carcinoma cells, are contacted with a sumoylation inhibitor in a dose effective to induce a shift in the carcinoma phenotype from basal-type to luminal type breast carcinoma. The induced luminal-type carcinoma cells are more responsive to a chemotherapeutic agent or radiation therapy than the basal-type cells. The methods may further comprise detecting a change in the phenotype of the cancer cells following administration of the sumoylation inhibitor, e.g. in breast cancer by detecting an increased percentage of cells expressing estrogen receptor a (ERα + cells). Such methods may comprise monitoring one or more markers indicative the breast carcinoma phenotype, e.g. estrogen receptor, progesterone receptor, etc. Many carcinomas have a cancer stem cell population that are CD44 + /CD24 −/low . A decrease in CD44 expression in the treated cell population, or a decrease in the number of CD44+ cancer stem cells can also be performed, where such a decrease is indicative of effective treatment with a sumoylation inhibitor. The subject methods are used for prophylactic or therapeutic purposes. As used herein, the term “treating” is used to refer to treatment of pre-existing cancers, including those which are in apparent remission. The treatment of ongoing disease, in order to stabilize or improve the clinical symptoms of the patient, is of particular interest. The sumoylation pathway is also used in screening assays to determine agents that are suitable for use in the methods of treatment, including without limitation screening derivatives and analogs of anacardic acids. Test compounds are screened for those that have the desired properties, through inhibition of sumoylation, which can involve inhibition of any of the molecular steps in the sumoylation pathway. Compounds of interest for screening include, without limitation, combinatorial libraries of small molecules; targeted modifications of compounds; environmental compounds, which can be derived from a wide variety of sources including plants, soil, water, foods; synthetic compounds such as chlorinated organics, polycyclic aromatic hydrocarbons, herbicides; pesticides; pharmaceuticals; and the like. BRIEF DESCRIPTION OF THE DRAWINGS FIGS. 1A-1E . Functional Specificity of TFAP2C for the Luminal Cluster Genes. FIG. 1A . Primary ERα-positive breast cancer cells derived from patient samples were transduced with lentiviral vectors encoding shRNA specific for non-targeting (NT), TFAP2A (A) or TFAP2C (C). Knockdown of TFAP2A and TFAP2C was confirmed compared to NT (data for tumor 2 and 3 shown in FIG. 9A ), *p<0.05 compared to NT. FIG. 1B . ERα RNA was assessed by RT-PCR; data for all three tumor isolates demonstrates that knockdown of TFAP2C specifically repressed ERα expression, * p<0.05 compared to NT. FIG. 1C . Western blot for ERα protein confirmed that ERα protein expression was repressed by knockdown of TFAP2C only. FIG. 1 D. Functional effects on RNA expression of luminal genes, the basal genes, MMP14, CALD1 and CD44, and the TFAP2A-specific target gene CDKN1A/p21-CIP in MCF-7 cells after knockdown of either TFAP2A or TFAP2C; data demonstrates functional specificity of TFAP2C (additional luminal genes in FIG. 9B ) with statistical differences shown comparing knockdown of TFAP2A vs. TFAP2C for all genes (p<0.05) and * p<0.05 compared to NT control. FIG. 1E . Western blot confirmed functional specificity for TFAP2C in regulation of luminal and basal genes. FIGS. 2A-2F . ChIP of TFAP2A and TFAP2C with Functional Specificity of TFAP2C Mapped to Amino Terminus. FIG. 2A . ChIP-Seq demonstrates identical binding pattern comparing TFAP2A and TFAP2C to luminal target genes ESR1/ERα, FOXA1 and FREM2; red dot indicates peak analyzed in detail in part C. FIG. 2B . Western blot of MCF-7 cells transfected with empty vector (EV) or HA epitope tagged AP-2 constructs, TFAP2C (HA-C) or TFAP2A (HA-A), and probed with antibody shown. FIG. 2C . Real-time ChIP was performed with anti-HA antibody and precipitated chromatin amplified at off-target and on-target locations for ESR1/ERα, FOXA1 and FREM2 (Woodfield et al., 2010). Data confirm specific binding of TFAP2A and TFAP2C to peaks identified by ChIP-seq with minimal binding to off-peak sites. FIG. 2D . Schematic of TFAP2A (blue) and TFAP2C (yellow) showing homologous regions and chimeric AP-2 proteins generated (all chimeras generated using TFAP2C-mut, which is construct insensitive to the siRNA); AD: Activation Domain; Di: Dimerization Domain; DBD: DNA Binding Domain; assignment of functional domains described previously (Williams and Tjian, 1991a; Williams and Tjian, 1991b). FIG. 2E . Using endogenous ERα RNA expression as functional assay, MCF-7 cells were transfected with siRNA and expression vector as diagramed in D. The data show that rescue of ERα transcriptional activity maps to the amino half of the TFAP2C protein. FIG. 2F . Experiment identical to part E, except uses expression of endogenous FREM2 and maps functional effect to the first 128 amino acids of TFAP2C. *p<0.05 compared to normalized expression in untransfected control. FIGS. 3A-3B . Yeast Two-hybrid Identifies Sumoylation Pathway Regulating Activity of TFAP2A on FREM2. FIG. 3A . Yeast two-hybrid screen using TFAP2A or TFAP2C as bait identified potential AP-2 interacting factors. Proteins from named genes are shown that were uniquely pulled out using either TFAP2A (blue) or TFAP2C (yellow) or were pulled out with both factors (green) as bait. FIG. 3B . Set of 21 factors was chosen for screening by knockdown with specific siRNAs in MCF-7 cells and assaying for effects on expression of endogenous FREM2 compared to NT siRNA (normalized to 1.0), *p<0.05 compared to NT. Two proteins identified as TFAP2A-interacting factors in yeast two-hybrid screen (PIAS1 and Ubc9/UBE2I) significantly induced FREM2 expression with knockdown. FIGS. 4A-4I . Sumoylation Functionally Linked to AP-2 Activity. FIG. 4A . Ubc9 binds to TFAP2A and TFAP2C in GST pull-down. FIG. 4B . MCF-7 cells were transfected with expression vectors for Green Fluorescent Protein-AP-2 fusion proteins demonstrating nuclear expression of GFP fusion proteins with co-localization with DAPI nuclear stain. FIG. 4C . Co-IP of GFP-TFAP2A and GFP-TFAP2C confirms protein-protein interaction between Ubc9 and both AP-2 proteins. FIG. 4D . Expression of endogenous FREM2 RNA in MCF-7 cells transfected with siRNA (normalized to NT) indicated with western blots below. Data show that FREM2 expression is not responsive to TFAP2A; however, knockdown of Ubc9 induced FREM2 expression and induction is blocked with knockdown of TFAP2A showing that FREM2 expression responds to TFAP2A in absence of sumoylation pathway, p<0.05 compared to NT. FIG. 4E . Sumoylation using in vitro assay demonstrates wild type TFAP2A is sumoylated by SUMO-1, -2 or -3, whereas, TFAP2A K10R mutant has significantly reduced sumoylation. FIG. 4F . MCF-7 cells co-transfected with expression vector for TFAP2A or K10R mutant construct for SUMO-1, -2 or -3. Data show that wild-type TFAP2A is sumoylated in vivo, whereas the K10R mutant is not. FIG. 4G . Protein from MCF-7 cells was immunoprecipitated (IP) using IgG or anti-TFAP2A antibody; protein was eluted from beads (E) and prewashes (P1 and P2) were assayed; load is un-precipitated extract; western blot was probed with anti-SUMO2/3 antibody. FIG. 4H . TFAP2C was sumoylated in vitro with SUMO-1, -2 or -3; *indicates sumoylated form of TFAP2C. FIG. 4I . MCF-7 cells transfected with expression vectors for SUMO-1, -2 or -3 and western blot probed with TFAP2C shows evidence for sumoylation with SUMO-1; *indicates location of sumoylated TFAP2C. FIGS. 5A-5E . Functional Effects of TFAP2A-K10R Mutant and Sumoylation Inhibition. FIG. 5A . Expression of luminal genes in MCF-7 cells transfected with wildtype TFAP2A or K10R mutant. K10R mutant induced luminal genes but wild-type TFAP2A did not. Both wild-type and K10R mutant TFAP2A induced CDKN1A/p21. FIG. 5B . Protein expression from western blots performed in triplicate with example of western blot below showing FREM2 protein expression induced by K10R but not wild-type TFAP2A. FIG. 5C . Expression of luminal cluster genes ESR1/ERα, KRT8 and FREM2 in sKD-C cells transfected with empty vector (EV) or expression vector for TFAP2A or K10R-TFAP2A mutant, with expression normalized to EV. K10R induced expression of luminal target genes, whereas, wild-type TFAP2A did not. FIG. 5D . Knockdown of Ubc9 or PIAS1 re-activated ERα and repressed CD44 expression in sKD-C cells. FIG. 5E . Treatment of sKD-C cells with ginkgolic acid (GA) re-activated FREM2 and ERα and repressed CD44 mRNA normalized to lowest value (top) and protein (bottom). For all panels, * indicates p<0.05 compared to normalized signal of 1.0. For CD44 expression in panel E, GA treated and untreated were also significantly different from each other, p<0.05. FIGS. 6A-6C . Sumoylation Inhibitors Cleared Cancer Stem Cell Population. FIG. 6A . Treatment of s-KD-C, BT-549, BT-20 or cells derived from a primary basal cancer (Basal Cancer) with GA or anacardic acid (AA) inhibited CD44 expression by Western blot (top row) and significantly reduced the CD44 + /CD24 −/flow population by FACS analysis (lower panels) but had no effect on the normal breast cell line MCF-10A. FIG. 6B / 6 C. Western blots showing that CD44 repression by GA and AA treatment was dependent upon expression of TFAP2A since knockdown of TFAP2A with siRNA abrogated effect of sumoylation inhibitors in sKD-C cells ( FIG. 6B ) and basal cell lines BT549 and BT20 ( FIG. 6C ). FIGS. 7A-7D . Knockdown of Sumoylation Enzymes Repressed CD44 and Blocked SUMO Conjugation of TFAP2A. Knockdown of Ubc9 and PIAS1 by siRNA repressed expression of CD44 in BT549 ( FIG. 7A ) and BT20 ( FIG. 7B ) cells showing same effect as GA and AA. FIG. 7C / 7 D. Endogenous TFAP2A was examined by western blot in BT549 (basal) ( FIG. 7C ) and MCF-7 (luminal) ( FIG. 7D ) cells. The SUMO conjugated form of TFAP2A is seen in both cell types (denoted by *) and knockdown of either Ubc9 or PIAS1 significantly reduced SUMO-conjugated TFAP2A. MW shows molecular weight markers. FIGS. 8A-8D . SUMO Inhibitors Repressed Outgrowth of Xenografts. FIG. 8A . Tumor free survival of nude mice (n=5 per group) inoculated with BT20 cells pretreated for 48 hours with either GA or AA compared to no pre-treatment; pretreated cells failed to form tumors. FIG. 8B . Tumor-free survival of nude mice (n=5 per group) inoculated with BT20 cells with animals gavaged with AA vs. vehicle. FIG. 8C . IOWA-1T cells were pre-treated with anacardic acid (AA) or vehicle and mice were followed until requiring euthanasia due to tumor size (Overall Survival). Pre-treatment with AA inhibited tumor formation, n=5 animals per group, p=0.002. FIG. 8D . Nude mice were inoculated with 1×10 6 , 5×10 5 , or 2.5×10 5 IOWA-1T cells and animals were gavaged with either vehicle or AA; vehicle-gavaged mice developed tumors in 5, 10 and 12 days, respectively. Mice gavaged with AA failed to form tumors over the course of the experiment, n=3 animals per group, p=0.025. FIG. 9A-9B . Effect of Knockdown of TFAP2C on Luminal Gene Expression. FIG. 9A . Additional data showing knockdown of TFAP2A and TFAP2C in cells from primary ERα-positive breast cancers, tumors 2 and 3, as indicated. FIG. 9B . Additional Luminal-associated genes, including the ERα-target gene, GREB1 (Ghosh et al., 2000), were repressed with knockdown of TFAP2C (C) but not TFAP2A (A). Knockdown of TFAP2A resulted in approximately 30% increase in GREB1 expression. FIG. 10 . FREM2 Expression in Breast Cancer Cell Lines and Primary Breast Cancers. FREM2 expression was characterized in a panel of cell lines by Western Blot (left) and as reported in Oncomine for FREM2 expression in primary breast cancers (right). FIGS. 11A-11F . FREM2 is a Specific TFAP2C Target Gene. FIG. 11A . ChIP-Seq of FREM2 promoter demonstrates binding of TFAP2A and TFAP2C upstream of PolII loading site. FIG. 11B . Gel shift analysis localizes AP-2 binding site in FREM2 promoter. FIG. 11C . Knock down of TFAP2C (but not TFAP2A) repressed FREM2 expression. FIG. 11D . FREM2 expression is responsive to TFAP2C in SKBR-3 ER-negative cells. FIG. 11E . FREM2 expression is not estrogen responsive as noted by Tamoxifen treatment (TAM), whereas, RET is appropriately repressed with TAM. FIG. 11F . Cloned FREM2 promoter reporter demonstrates response to TFAP2C only. FIG. 12 . ChIP-Seq Data for Select Luminal Target Genes. ChIP-seq data for six luminal target genes ESR1, MUC1, FGFR4, KRT8, RET and MYB. For each gene, the first two rows are ChIP-seq data from our laboratory. The remaining data is from publically available datasets: TFAP2C-2: GSE23852; ESR/ERα: GSE45822; FOXA1: GSE23852; FOXM1: GSE40762; H3K4me1: GSE23701; H3K4me3: GSE23701; H3K27ac: GSE45822; H3K27me3: GSE23701. The data are in agreement that TFAP2A and TFAP2C bind to the same chromosomal locations. Furthermore, the location of AP-2 peaks agrees with other datasets for TFAP2C and co-localize with FOXA1 and ERα binding sites. Histone marks are consistent with active transcription and no significant binding in these regions was identified with H3K27me3, which is associated with chromatin silencing. FIG. 13 . Additional ChIP-Seq Data for AP-2 Target Genes. ChIP-seq data for additional AP-2 target genes including the luminal target genes FOXA1, GATA3, FREM2 and XBP1. ChIP-seq data for CD44 and CDKN1A are also shown. Format and dataset sources are identical as shown in FIG. 12 . FIG. 14A-14D . Size of Sumoylated TFAP2A and TFAP2C Proteins. Images of western blots shown in FIG. 4A-4I with protein ladders demonstrate the size of the sumoylated forms of AP-2 estimated to be approximately 70 kD±5 kD. For each gel, Magic Markers XP were used; * indicates the sumoylated form of AP-2 protein. FIG. 14A . First three lanes from the blot shown in FIG. 4E for TFAP2A sumoylated in vitro. FIG. 14B . MCF-7 extract followed by first lane of blot shown in FIG. 4F demonstrating size of sumoylated TFAP2A in vivo. FIG. 14C . Last two lanes of FIG. 4G showing sumoylated TFAP2A immunoprecipitated with anti-TFAP2A antibody and blotted with SUMO2/3 antibody. FIG. 14D . First two lanes of FIG. 4I showing sumoylated form of TFAP2C in vivo with SUMO-1. FIG. 15A-15B . Sumoylated TFAP2A in Basal Cells Induced with Peroxide. Sumoylation of TFAP2A was analyzed in the basal cell line BT549 with and without treatment with peroxide. FIG. 15A . BT549 cells co-transfected with vectors for TFAP2A and either SUMO-1, -2 or -3 and treated without or with peroxide, as indicated. Induction of sumoylated TFAP2A was seen with peroxide treatment. Experiment in A was performed in the absence of the proteasome inhibitor MG-132. FIG. 15B . Similar experiments performed with MG-132 treatment either without or with peroxide. Peroxide increased the relative abundance of the base-line sumoylated form of TFAP2A and MG-132 enhanced identification of the sumoylated forms of TFAP2A. FIG. 16 . Anacardic Acid Inhibits SUMO-conjugated Proteins. Western blots were performed on protein extracts of BT549 cells treated with vehicle (V) or anacardic acid (AA) and reacted with antibodies for SUMO1, TFAP2A or GAPDH, as indicated. Equal amounts of protein were loaded in each lane. AA treatment significantly reduced the global presence of high molecular weight SUMO-conjugated proteins with similar amounts of free SUMO-1 noted. AA treatment specifically reduced the SUMO-conjugated form of TFAP2A (denoted by *). GAPDH control indicates equal loading of protein. MW indicates molecular weight markers. FIGS. 17A-17D : qPCR, CD44 downregulation after treatment of colorectal CSC with anacardic acid, 48 h. FIG. 1B : qPCR, ALCAM (activated leucocyte cell adhesion molecule) after treatment of colorectal CSC with anacardic acid, 48 h. FIG. 17C : qPCR, EPCAM (epithelial cell adhesion molecule) after treatment of colorectal CSC with anacardic acid, 48 h. FIG. 17D : Western blot, CD44 downregulation after treatment of colorectal CSC with anacardic acid, 48 h. FIG. 18 : Western blot, CD44 downregulation, Panc-1 pancreatic carcinoma was treated with ginkgolic and anacardic acids, 96 h. FIG. 19 : Western blot, CD44 downregulation, 8505c thyroid carcinoma was treated with ginkgolic and anacardic acids, 96 h. DESCRIPTION OF THE SPECIFIC EMBODIMENTS Cancer therapy is performed with sumoylation inhibitor compounds, optionally in combination with conventional cancer therapy. An effective dose of a sumoylation inhibitor is administered to a host suffering from a susceptible tumor, e.g. carcinomas, etc. Administration may be topical, localized or systemic, depending on the specific disease. The compounds are administered at a dosage that over a suitable period of time substantially reduces the tumor cell burden, while minimizing any side-effects. Sumoylation Inhibitor. The sumoylation pathway involves several steps including activation with E1 enzyme, conjugation with the E2 enzyme and ligation of the SUMO peptide with cooperative activity of the E2 and E3 ligases. Inhibitors of sumoylation can inhibit any of the steps of the sumoylation pathway. In some embodiments a sumoylation inhibitor” or “SUMO inhibitor” refers to any small molecule inhibitor that binds one or more subunit of a sumoylation enzyme, thereby inhibiting the addition of a sumo protein to a target protein. Such small molecule inhibitors may also inhibit one or more sumoylation enzymes. Preferred sumoylation inhibitors have a high level of specificity to SUMO enzymes, thereby affecting sumoylation, but do not bind or have very low level or negligible binding to proteins found in the ubiquitination pathway. In some embodiments the sumoylation inhibitor is an anacardic acid, or a derivative or analog thereof. Anacardic acid (C15:0) has the structure: Anacardic acids and derivatives thereof include, without limitation, Anacardic acid (C15:1); Anacardic acid (C15:2); Anacardic acid (C15:3); Anacardic acid (C24:1); Cardol (C12:0); N-isonicotinoyl-N′-8-[(2-carbohydroxy-3-hydroxy)phenyl]octanal hydrazine; N-isonicotinoyl-N′-8-[(2-carbohydroxy-3-hydroxy-6-nitro)phenyl]octanal hydrazine; N-(4-chloro-3-trifluoromethyl-phenyl)-2-ethoxy-6-pentadecyl-benzamide; N-(4-chloro-3-trifluoromethyl-phenyl)-2-ethoxy-benzamide; 2-isopropoxy-6-pentadecyl-N-pyridin-4-ylbenzamide; 2-ethoxy-N-(3-nitrophenyl)-6-pentadecylbenzamide; 2-ethoxy-6-pentadecyl-N-pyridin-4-ylbenzamide; 6-n-pentadecyl salicylic acid; 6-n-dodecylsalicylic acid; 6-n-heptadecylsalicylic acid; 5-[2-Ethoxy-5-(4-methylpiperazin-1-ylsulfonyl)-6-pentadecylphenyl]-1,6-dihydro-7H-pyrazolo[4, 3-d]pyrimidin-7-one; 5-[2-Methoxy-5-(4-methylpiperazin-1-ylsulfonyl)-6-pentadecylphenyl]-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one; 2-hydroxy-6-[(8Z,11Z)-pentadeca-8,11,14-trienyl]benzoic acid. A derivative of particular interest is gingkolic acid, (Z)-6-(Pentadec-8-enyl)-2-hydroxybenzoic acid. Analogues of interest include those of Formula I: Where R is an aliphatic or aromatic moiety, for example CH 2 (CH 2 ) n CH 3 ; where n is from 1-10; benzyl; etc. Examples of sumoylation inhibitors are described, for example in US 20130245032 A1, Hemshekhar et al. (2012) Basic and Clinical Pharmacology & Toxocology 110(2):122-132; Ghizzoni et al. (2010) Bioorg. Med. Chem 18(16):5826-34; Kusio-Kobialka et al. (2013) Anticancer Agents Med Chem 13(5):762-7; Zhang et al. (2011 Molecules 16: 4059-4069; each herein specifically incorporated by reference. An effective dose of a sumoylation inhibitor is a dose that reduces the concentration of SUMO-conjugated form of TFAP2A in a cancer cell, e.g. reduces by about 10%, by about 20%, by about 30%, by about 40%, by about 50%, by about 60%, by about 70%, by about 80%, by about 80%, by about 90%, or more. The effective dose can also be monitored by the effect of down-regulating sumoylation of TFAP2A in a population of cancer cells, where in a population of cell the expression of CD44 is down-regulated, such that the number of CD44 + cells in the population is reduced by about 10%, by about 20%, by about 30%, by about 40%, by about 50%, by about 60%, by about 70%, by about 80%, by about 80%, by about 90%, or more. Where the population of cancer cells is a population of basal-type breast carcinoma cells, the effective dose may be monitored by the phenotypic change from basal-type to luminal type, for example as exemplified by expression of ERα, wherein in a population of basal-type breast carcinoma cells, treatment with an effective dose of a sumoylation inhibitor increased the number of ERα + cells at least about 2-fold, at least about 3-fold, at least about 5-fold, at least about 10-fold, or more. Alternatively, an effective dose of a sumoylation inhibitor can be measured as the dose that results in killing of cancer cells. In some embodiments, the dose of sumoylation inhibitor as a single agent is effective to kill at least about 25% of the cancer cells present in a population, more usually at least about 50% killing, and may be about 90% or greater of the cells present in a population. In other embodiments the effective dose of a sumoylation inhibitor can be measured as the dose that results in altering the phenotype of a cancer cell to be susceptible to chemotherapy or radiation therapy, where the number of cells in a population susceptible to a conventional dose of chemotherapy or radiation is increased at least about 2-fold, at least about 3-fold, at least about 5-fold, at least about 10-fold, or more, relative to an untreated population. In some embodiments, a population of cells is monitored for one or more of the above activities, i.e. alteration of phenotype, decrease of CD44 + cells, increase in susceptibility to chemotherapy or radiation, etc. The susceptibility of a particular tumor cell population to killing with the combined therapy may be determined by in vitro testing, as detailed in the experimental section. Typically a culture of the tumor cell is combined with a combination of a chemotherapeutic or radiation therapy and a sumoylation inhibitor at varying concentrations for a period of time sufficient to allow the active agents to work, usually between about one hour and one week. For in vitro testing, cultured cells from a biopsy sample of the tumor may be used. The viable cells left after treatment are then counted. In some embodiments of the invention, a combination therapy is provided. The combined used of sumoylation inhibitors and chemotherapeutics agent has the advantages that the required dosages for the individual drugs is lower, and the effect of the different drugs complementary. Depending on the patient and condition being treated and on the administration route, the sumoylation inhibitors may be administered in dosages of 0.001 mg to 5 mg/kg body weight per day. The range is broad, since in general the efficacy of a therapeutic effect for different mammals varies widely with doses typically being 20, 30 or even 40 times smaller (per unit body weight) in man than in the rat. Similarly the mode of administration can have a large effect on dosage. Thus for example oral dosages in the rat may be ten times the injection dose. The dosage for the chemotherapeutic agent will be equal to, or less than the conventional dosage for that agent. A typical dosage may be a solution suitable for intravenous administration; a tablet taken from two to six times daily, or one time-release capsule or tablet taken once a day and containing a proportionally higher content of active ingredient, etc. The time-release effect may be obtained by capsule materials that dissolve at different pH values, by capsules that release slowly by osmotic pressure, or by any other known means of controlled release. Those of skill will readily appreciate that dose levels can vary as a function of the specific compound, the severity of the symptoms and the susceptibility of the subject to side effects. Some of the specific compounds are more potent than others. Preferred dosages for a given compound are readily determinable by those of skill in the art by a variety of means. A preferred means is to measure the physiological potency of a given compound. For use in the subject methods, sumoylation inhibitors may be formulated with other pharmaceutically active agents, particularly other anti-metastatic, anti-tumor or anti-angiogenic agents. Angiostatic compounds of interest include angiostatin, endostatin, carboxy terminal peptides of collagen alpha (XV), etc. Cytotoxic and cytostatic agents of interest include adriamycin, alkeran, Ara-C, BICNU, busulfan, CNNU, cisplatinum, cytoxan, daunorubicin, DTIC, 5-FU, hydrea, ifosfamide, methotrexate, mithramycin, mitomycin, mitoxantrone, nitrogen mustard, velban, vincristine, vinblastine, VP-16, carboplatinum, fludarabine, gemcitabine, idarubicin, irinotecan, leustatin, navelbine, taxol, taxotere, topotecan, etc. It is contemplated that the composition will be obtained and used under the guidance of a physician for in vivo use. To provide a synergistic effect in a combined therapy, a chemotherapeutic agent, or radiation therapy, and the sumoylation inhibitor can be delivered together or separately, and simultaneously or at different times within the day. The dose will vary depending on the specific cytotoxic agent utilized, type of tumor, patient status, etc., at a dose sufficient to substantially ablate the tumor cell population, while maintaining patient viability. Treatment will generally be continued until there is a substantial reduction, e.g. at least about 50%, decrease in the tumor burden, and may be continued until there are essentially no tumor cells detected in the body. Tumors of interest for treatment include carcinomas, e.g. breast, colon, colorectal, prostate, pancreatic, melanoma, ductal, endometrial, stomach, dysplastic oral mucosa, invasive oral cancer, non-small cell lung carcinoma, thyroid, transitional and squamous cell urinary carcinoma, etc.; neurological malignancies, e.g. neuroblastoma, gliomas, etc.; hematological malignancies, e.g. childhood acute leukemia, non-Hodgkin's lymphomas, chronic lymphocytic leukemia, malignant cutaneous T-cells, mycosis fungoides, non-MF cutaneous T-cell lymphoma, lymphomatoid papulosis, T-cell rich cutaneous lymphoid hyperplasia, bullous pemphigoid, discoid lupus erythematosus, lichen planus, etc.; and the like. Breast cancer is of particular interest. The majority of breast cancers are adenocarcinoma subtypes. Ductal carcinoma in situ is the most common type of noninvasive breast cancer. In DCIS, the malignant cells have not metastasized through the walls of the ducts into the fatty tissue of the breast. Infiltrating (or invasive) ductal carcinoma (IDC) has metastasized through the wall of the duct and invaded the fatty tissue of the breast. Infiltrating (or invasive) lobular carcinoma (ILC) is similar to IDC, in that it has the potential metastasize elsewhere in the body. About 10% to 15% of invasive breast cancers are invasive lobular carcinomas. Of interest in the treatment of breast cancer are the various types of breast cancer, e.g. luminal A; luminal B; HER2-type; and basal-type, triple negative carcinomas. Luminal A cancers are ER + and/or PR + , HER2 − , low Ki67e. Luminal B cancers are ER + and/or PR + , HER2 + (or HER2 − with high Ki67). Basal-type cancers are triple negative, i.e. ER − , PR − , HER2 − and are typically resistant to conventional chemotherapy or radiation. Her2 type are ER − , PR − , HER2+. The host, or patient, may be from any mammalian species, e.g. primate sp., particularly humans; rodents, including mice, rats and hamsters; rabbits; equines, bovines, canines, felines; etc. Animal models are of interest for experimental investigations, providing a model for treatment of human disease. Pharmaceutical Formulations: sumoylation inhibitors can be incorporated into a variety of formulations for therapeutic administration. More particularly, the compounds of the present invention can be formulated into pharmaceutical compositions by combination with appropriate pharmaceutically acceptable carriers or diluents, and may be formulated into preparations in solid, semi-solid, liquid or gaseous forms, such as tablets, capsules, powders, granules, ointments, solutions, suppositories, injections, inhalants, gels, microspheres, and aerosols. As such, administration of the compounds can be achieved in various ways, including oral, buccal, rectal, parenteral, intraperitoneal, intradermal, transdermal, intracheal, etc., administration. The active agent may be systemic after administration or may be localized by the use of regional administration, intramural administration, or use of an implant that acts to retain the active dose at the site of implantation. In pharmaceutical dosage forms, the compounds may be administered in the form of their pharmaceutically acceptable salts. They may also be used in appropriate association with other pharmaceutically active compounds. The following methods and excipients are merely exemplary and are in no way limiting. For oral preparations, the compounds can be used alone or in combination with appropriate additives to make tablets, powders, granules or capsules, for example, with conventional additives, such as lactose, mannitol, corn starch or potato starch; with binders, such as crystalline cellulose, cellulose derivatives, acacia, corn starch or gelatins; with disintegrators, such as corn starch, potato starch or sodium carboxymethylcellulose; with lubricants, such as talc or magnesium stearate; and if desired, with diluents, buffering agents, moistening agents, preservatives and flavoring agents. The compounds can be formulated into preparations for injections by dissolving, suspending or emulsifying them in an aqueous or nonaqueous solvent, such as vegetable or other similar oils, synthetic aliphatic acid glycerides, esters of higher aliphatic acids or propylene glycol; and if desired, with conventional additives such as solubilizers, isotonic agents, suspending agents, emulsifying agents, stabilizers and preservatives. The compounds can be utilized in aerosol formulation to be administered via inhalation. The compounds of the present invention can be formulated into pressurized acceptable propellants such as dichlorodifluoromethane, propane, nitrogen and the like. Furthermore, the compounds can be made into suppositories by mixing with a variety of bases such as emulsifying bases or water-soluble bases. The compounds of the present invention can be administered rectally via a suppository. The suppository can include vehicles such as cocoa butter, carbowaxes and polyethylene glycols, which melt at body temperature, yet are solidified at room temperature. Unit dosage forms for oral or rectal administration such as syrups, elixirs, and suspensions may be provided wherein each dosage unit, for example, teaspoonful, tablespoonful, tablet or suppository, contains a predetermined amount of the composition containing one or more compounds of the present invention. Similarly, unit dosage forms for injection or intravenous administration may comprise the compound of the present invention in a composition as a solution in sterile water, normal saline or another pharmaceutically acceptable carrier. Implants for sustained release formulations are well-known in the art. Implants are formulated as microspheres, slabs, etc. with biodegradable or non-biodegradable polymers. For example, polymers of lactic acid and/or glycolic acid form an erodible polymer that is well-tolerated by the host. The implant containing sensitizer is placed in proximity to the site of the tumor, so that the local concentration of active agent is increased relative to the rest of the body. The term “unit dosage form”, as used herein, refers to physically discrete units suitable as unitary dosages for human and animal subjects, each unit containing a predetermined quantity of compounds of the present invention calculated in an amount sufficient to produce the desired effect in association with a pharmaceutically acceptable diluent, carrier or vehicle. The specifications for the novel unit dosage forms of the present invention depend on the particular compound employed and the effect to be achieved, and the pharmacodynamics associated with each compound in the host. The pharmaceutically acceptable excipients, such as vehicles, adjuvants, carriers or diluents, are readily available to the public. Moreover, pharmaceutically acceptable auxiliary substances, such as pH adjusting and buffering agents, tonicity adjusting agents, stabilizers, wetting agents and the like, are readily available to the public. Drug screening methods are used to identify agents that inhibit sumoylation for use in the methods of the invention. Of particular interest are screening assays for agents that have a low toxicity for human cells. A wide variety of assays may be used for this purpose, including labeled in vitro protein-protein binding assays, electrophoretic mobility shift assays, immunoassays for protein binding, and the like. For example, the effect of an agent on tumor cell phenotype with respect to susceptibility to conventional chemotherapeutic agents, expression of CD44, expression of estrogen receptor in breast carcinoma cells, expression of reporters based on response genes, etc. can be measured in a screening assay. A reduction on the sumo conjugated form of TFAP2A in a cancer cell can be measured. The susceptibility of a particular tumor cell population to killing with the combined therapy may be determined by in vitro testing, as detailed in the experimental section. Typically a culture of the tumor cell is combined with a combination of a chemotherapeutic or radiation therapy and a sumoylation inhibitor at varying concentrations for a period of time sufficient to allow the active agents to work, usually between about one hour and one week. For in vitro testing, cultured cells from a biopsy sample of the tumor may be used. The viable cells left after treatment are then counted. The purified protein may also be used for determination of three-dimensional crystal structure, which can be used for modeling intermolecular interactions. The sumoylation pathway involves several steps including activation with E1 enzyme, conjugation with the E2 enzyme and ligation of the SUMO peptide with cooperative activity of the E2 and E3 ligases. Inhibitors of sumoylation can involve screening to inhibit any of the steps of the sumoylation pathway. The term “agent”, for example a candidate agent tested in a screening assay, as used herein describes any molecule, e.g. protein or pharmaceutical, with the capability of inhibiting sumoylation, particularly inhibiting sumoylation of TFAP2A in a cancer cell. Generally a plurality of assay mixtures are run in parallel with different agent concentrations to obtain a differential response to the various concentrations. Typically, one of these concentrations serves as a negative control, i.e. at zero concentration or below the level of detection. Candidate agents encompass numerous chemical classes, though typically they are organic molecules, preferably small organic compounds having a molecular weight of more than 50 and less than about 2,500 daltons. Candidate agents comprise functional groups necessary for structural interaction with proteins, particularly hydrogen bonding, and typically include at least an amine, carbonyl, hydroxyl or carboxyl group, preferably at least two of the functional chemical groups. The candidate agents often comprise cyclical carbon or heterocyclic structures and/or aromatic or polyaromatic structures substituted with one or more of the above functional groups. Candidate agents are also found among biomolecules including peptides, saccharides, fatty acids, steroids, purines, pyrimidines, derivatives, structural analogs or combinations thereof. In some embodiments the candidate agent is a derivative or analog of anacardic acid. Candidate agents are obtained from a wide variety of sources including libraries of synthetic or natural compounds. For example, numerous means are available for random and directed synthesis of a wide variety of organic compounds and biomolecules, including expression of randomized oligonucleotides and oligopeptides. Alternatively, libraries of natural compounds in the form of bacterial, fungal, plant and animal extracts are available or readily produced. Additionally, natural or synthetically produced libraries and compounds are readily modified through conventional chemical, physical and biochemical means, and may be used to produce combinatorial libraries. Known pharmacological agents may be subjected to directed or random chemical modifications, such as acylation, alkylation, esterification, amidification, etc. to produce structural analogs. Where the screening assay is a binding assay, one or more of the molecules may be joined to a label, where the label can directly or indirectly provide a detectable signal. Various labels include radioisotopes, fluorescers, chemiluminescers, enzymes, specific binding molecules, particles, e.g. magnetic particles, and the like. Specific binding molecules include pairs, such as biotin and streptavidin, digoxin and antidigoxin etc. For the specific binding members, the complementary member would normally be labeled with a molecule that provides for detection, in accordance with known procedures. A variety of other reagents may be included in the screening assay. These include reagents like salts, neutral proteins, e.g. albumin, detergents, etc. that are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Reagents that improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, anti-microbial agents, etc. may be used. The mixture of components are added in any order that provides for the requisite binding. Incubations are performed at any suitable temperature, typically between 4 and 40° C. Incubation periods are selected for optimum activity, but may also be optimized to facilitate rapid high-throughput screening. Typically between 0.1 and 1 hours will be sufficient. The compounds having the desired pharmacological activity may be administered in a physiologically acceptable carrier to a host for treatment of cancer, etc., or to otherwise enhance function. The agents may be administered in a variety of ways, orally, topically, parenterally e.g. subcutaneously, intraperitoneally, by viral infection, intravascularly, etc. Topical treatments are of particular interest. Depending upon the manner of introduction, the compounds may be formulated in a variety of ways. The concentration of therapeutically active compound in the formulation may vary from about 0.1-100 wt. %. The pharmaceutical compositions can be prepared in various forms, such as granules, tablets, pills, suppositories, capsules, suspensions, salves, lotions and the like. Pharmaceutical grade organic or inorganic carriers and/or diluents suitable for oral and topical use can be used to make up compositions containing the therapeutically-active compounds. Diluents known to the art include aqueous media, vegetable and animal oils and fats. Stabilizing agents, wetting and emulsifying agents, salts for varying the osmotic pressure or buffers for securing an adequate pH value, and skin penetration enhancers can be used as auxiliary agents. The agents can be used in native form or can be modified to form a chemical derivative. As used herein, a molecule is said to be a “chemical derivative” of another molecule when it contains additional chemical moieties not normally a part of the molecule. Such moieties may improve the molecule's solubility, absorption, biological half life, etc. The moieties may alternatively decrease the toxicity of the molecule, eliminate or attenuate any undesirable side effect of the molecule, etc. Moieties capable of present invention can be administered concurrently with, prior to, or following the administration of the other agent. The agents are administered to the mammal in a pharmaceutically acceptable form and in a therapeutically effective concentration. A composition is said to be “pharmacologically acceptable” if its administration can be tolerated by a recipient patient. Such an agent is said to be administered in a “therapeutically effective amount” if the amount administered is physiologically significant. An agent is physiologically significant if its presence results in a detectable change in the physiology of a recipient patient. The agents of the present invention can be formulated according to known methods to prepare pharmaceutically useful compositions, whereby these materials, or their functional derivatives, are combined in admixture with a pharmaceutically acceptable carrier vehicle. Suitable vehicles and their formulation, inclusive of other human proteins, e.g., human serum albumin, are described, for example, in Remington's Pharmaceutical Sciences (16th ed., Osol, A., Ed., Mack, Easton Pa. (1980)). In order to form a pharmaceutically acceptable composition suitable for effective administration, such compositions will contain an effective amount of one or more of the agents of the present invention, together with a suitable amount of carrier vehicle. Additional pharmaceutical methods may be employed to control the duration of action. Control release preparations may be achieved through the use of polymers to complex or absorb one or more of the agents of the present invention. The controlled delivery may be exercised by selecting appropriate macromolecules (for example polyesters, polyamino acids, polyvinyl, pyrrolidone, ethylenevinylacetate, methylcellulose, carboxymethylcellulose, or protamine, sulfate) and the concentration of macromolecules as well as the methods of incorporation in order to control release. Another possible method to control the duration of action by controlled release preparations is to incorporate agents of the present invention into particles of a polymeric material such as polyesters, polyamino acids, hydrogels, poly(lactic acid) or ethylene vinylacetate copolymers. Alternatively, instead of incorporating these agents into polymeric particles, it is possible to entrap these materials in microcapsules prepared, for example, by coacervation techniques or by interfacial polymerization, for example, hydroxymethylcellulose or gelatine microcapsules; and poly(methylmethacylate) microcapsules, respectively, or in colloidal drug delivery systems, for example, liposomes, albumin microspheres, microemulsions, nanoparticles, and nanocapsules or in macroemulsions. The following examples are offered by way of illustration and not by way of limitation. EXPERIMENTAL The following examples are put forth so as to provide those of ordinary skill in the art with a complete disclosure and description of how to make and use the subject invention, and are not intended to limit the scope of what is regarded as the invention. Efforts have been made to ensure accuracy with respect to the numbers used (e.g. amounts, temperature, concentrations, etc.) but some experimental errors and deviations should be allowed for. Unless otherwise indicated, parts are parts by weight, molecular weight is average molecular weight, temperature is in degrees centigrade; and pressure is at or near atmospheric. The TFAP2C/AP-2γ transcription factor is required to maintain the luminal mammary phenotype. Functional specificity of TFAP2C was mapped to the activation domain and a non-selective screen identified the requirement of the sumoylation pathway to maintain TFAP2C-specific gene regulation. Disruption of the sumoylation pathway by knockdown of sumoylation enzymes, mutation of the SUMO-target lysine of TFAP2A, or treatment with sumoylation inhibitors induced a basal to luminal transition. Sumoylation inhibitors cleared the cancer stem cell population characterizing basal cancers but had no effect on normal mammary epithelial cells. These findings establish a critical role for sumoylation in regulating the transcriptional mechanisms that maintain the basal cancer phenotype. Sumoylation inhibitors offer a novel therapeutic approach for the treatment of aggressive basal breast cancer. Clinical breast cancer subtypes are characterized by patterns of gene expression that predict outcome and response to therapy. Luminal breast cancers express steroid hormone receptors and tend to be hormone responsive. By comparison, basal breast cancers are not hormone responsive, display an expansion of cancer stem cells and have a worse prognosis. Herein, we show that TFAP2C has a unique role compared to other AP-2 family members in maintaining patterns of gene expression that characterize luminal cancers. We report the novel finding that the sumoylation pathway is required to maintain TFAP2C specific gene regulation of the luminal expression cluster. Sumoylation inhibitors induce a transition from the basal towards a luminal breast cancer phenotype thus forming the basis for new treatment strategies. Breast cancer has an incidence of 226,000 and accounts for approximately 40,000 deaths annually in the US. There has been an improvement in survival for women with breast cancer, though patients with locally advanced or metastatic disease continue to have a poor prognosis. The clinical subtypes of breast cancer are defined by the expression of estrogen receptor-alpha (ERα), progesterone receptor (PgR) and amplification and overexpression of c-ErbB2/HER2. The four common molecular subtypes of breast cancers include the Luminal A (ERα/PgR+, HER2−), Luminal B (ERα/PgR+, HER2+), HER2 (ERcontacting a cancer cell population with a sumoylation inhibitor in a dose effective to reduce the number of cancer cells in the population."],"number":1,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the dose of sumoylation inhibitor is effective to reduce levels of sumo-conjugated TFAP2A."],"number":2,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 2, wherein the method reduces the number of cancer stem cells, and reduction of cancer stem cells is monitored by determining the expression of CD44+ cells in the population."],"number":3,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, further comprising contacting the cancer cell population with one or more chemotherapeutic agents, wherein the population of cells has increased responsiveness to chemotherapeutic agents following contacting with a sumoylation inhibitor."],"number":4,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, further comprising treating the cancer cell population with radiation therapy, wherein the population of cells has increased responsiveness to radiation therapy following contacting with a sumoylation inhibitor."],"number":5,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the cancer cell population is a human cell population."],"number":6,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 6, wherein said cancer is a solid tumor."],"number":7,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 6, wherein said tumor is a carcinoma."],"number":8,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 8, wherein said tumor is a breast carcinoma."],"number":9,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 9, wherein the cancer cell population is a basal-type breast carcinoma, and wherein following contacting with the sumoylation inhibitor the basal-type carcinoma cells are induced to a luminal-type breast carcinoma phenotype."],"number":10,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 10, further comprising the step of monitoring expression of at least one marker indicative of the breast carcinoma phenotype."],"number":11,"annotation":false,"title":false,"claim":true},{"lines":["The method of any one of claims 1-11, wherein the sumoylation inhibitor is anacardic acid or a derivative or analog thereof."],"number":12,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 12, wherein the sumoylation inhibitor is gingkolic acid."],"number":13,"annotation":false,"title":false,"claim":true},{"lines":["A method of screening for a candidate agent that is a sumoylation inhibitor useful in treatment of cancer, the method comprising:\n
contacting a cancer cell with the candidate agent; and\n
determining the concentration of sumo-conjugated TFAP2A, wherein a reduction in sumo-conjugated TFAP2A is indicative that the candidate agent is useful in cancer treatment."],"number":14,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 14, further comprising:\n
contacting a population of cancer cells with the candidate agent; and\n
determining the concentration of cancer stem cells, wherein a reduction in the number of cancer stem cells is indicative that the candidate agent is useful in cancer treatment."],"number":15,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 15, wherein the cancer stem cells are monitored by expression of CD44."],"number":16,"annotation":false,"title":false,"claim":true}]}},"filters":{"npl":[],"notNpl":[],"applicant":[],"notApplicant":[],"inventor":[],"notInventor":[],"owner":[],"notOwner":[],"tags":[],"dates":[],"types":[],"notTypes":[],"j":[],"notJ":[],"fj":[],"notFj":[],"classIpcr":[],"notClassIpcr":[],"classNat":[],"notClassNat":[],"classCpc":[],"notClassCpc":[],"so":[],"notSo":[],"sat":[]},"sequenceFilters":{"s":"SEQIDNO","d":"ASCENDING","p":0,"n":10,"sp":[],"si":[],"len":[],"t":[],"loc":[]}}