{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T09:52:45Z","timestamp":1785577965454,"version":"3.56.0"},"reference-count":47,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2013,12,1]],"date-time":"2013-12-01T00:00:00Z","timestamp":1385856000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Basic Research Program of China","doi-asserted-by":"crossref","award":["2007CB914504"],"award-info":[{"award-number":["2007CB914504"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["30973621"],"award-info":[{"award-number":["30973621"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2013,12]]},"DOI":"10.1016\/j.ejmech.2013.10.033","type":"journal-article","created":{"date-parts":[[2013,10,25]],"date-time":"2013-10-25T05:35:59Z","timestamp":1382679359000},"page":"631-639","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"special_numbering":"C","title":["Design, synthesis and evaluation of a cellular stable and detectable biotinylated fumagillin probe and investigation of cell permeability of fumagillin and its analogs to endothelial and cancer cells"],"prefix":"10.1016","volume":"70","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3145-223X","authenticated-orcid":false,"given":"Guo-Chun","family":"Zhou","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1707-5183","authenticated-orcid":false,"given":"Fang","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junting","family":"Wan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Decai","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ping","family":"Wei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pingkai","family":"Ouyang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2013.10.033_bib1","doi-asserted-by":"crossref","first-page":"1182","DOI":"10.1056\/NEJM197111182852108","article-title":"Tumor angiogenesis: therapeutic implications","volume":"285","author":"Folkman","year":"1971","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.ejmech.2013.10.033_bib2","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/S0065-230X(08)60058-5","article-title":"Tumor angiogenesis","volume":"19","author":"Folkman","year":"1974","journal-title":"Adv. Cancer Res."},{"key":"10.1016\/j.ejmech.2013.10.033_bib3","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.drup.2009.12.001","article-title":"Evading tumor evasion: current concepts and perspectives of anti-angiogenic cancer therapy","volume":"13","author":"Abdollahi","year":"2010","journal-title":"Drug Resist. Updates"},{"key":"10.1016\/j.ejmech.2013.10.033_bib4","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1038\/35025220","article-title":"Angiogenesis in cancer and other diseases","volume":"14","author":"Carmeliet","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2013.10.033_bib5","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/nrd2115","article-title":"Angiogenesis: an organizing principle for drug discovery?","volume":"6","author":"Folkman","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2013.10.033_bib6","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1126\/science.1125950","article-title":"Antiangiogenic therapy: a universal chemosensitization strategy for cancer?","volume":"312","author":"Kerbel","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2013.10.033_bib7","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1128\/JB.58.4.527-529.1949","article-title":"An antiphage agent isolated from Aspergillus sp","volume":"58","author":"Hanson","year":"1949","journal-title":"J.\u00a0Bacterial."},{"key":"10.1016\/j.ejmech.2013.10.033_bib8","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1126\/science.113.2930.202","article-title":"Fumagillin (H-3), a new antibiotic with amebicidal properties","volume":"113","author":"MdCohen","year":"1951","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2013.10.033_bib9","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1038\/348555a0","article-title":"Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumor growth","volume":"348","author":"Ingber","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2013.10.033_bib10","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1002\/hlca.19680510624","article-title":"Isolation and structure elucidation of ovalicin","volume":"51","author":"Sigg","year":"1968","journal-title":"Helv. Chim. Acta"},{"key":"10.1016\/j.ejmech.2013.10.033_bib11","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1002\/hlca.19730560303","article-title":"Structure of ovalicin","volume":"56","author":"Bollinger","year":"1973","journal-title":"Helv. Chim. Acta"},{"key":"10.1016\/j.ejmech.2013.10.033_bib12","doi-asserted-by":"crossref","first-page":"12109","DOI":"10.1021\/ja00105a084","article-title":"Enantioselective synthesis of (\u2212)-ovalicin, a potent inhibitor of angiogenesis, using substrate-enhanced catalytic asymmetric hydroxylation","volume":"116","author":"Corey","year":"1994","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2013.10.033_bib13","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1038\/bjc.1994.41","article-title":"Cytostatic inhibition of endothelial cell growth by the angiogenesis inhibitor TNP-470 (AGM-1470)","volume":"69","author":"Kusaka","year":"1994","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.ejmech.2013.10.033_bib14","first-page":"3407","article-title":"A\u00a0fumagillin derivative angiogenesis inhibitor, AGM-1470, inhibits activation of cyclin-dependent kinases and phosphorylation of retinoblastoma gene product but not protein tyrosyl phosphorylation or protooncogene expression in vascular endothelial cells","volume":"54","author":"Abe","year":"1994","journal-title":"Cancer Res."},{"key":"10.1016\/j.ejmech.2013.10.033_bib15","first-page":"1","article-title":"Significant inhibition of endothelial cell growth in tumor vasculature by an angiogenesis inhibitor, TNP-470 (AGM-1470)","volume":"14","author":"Yamamoto","year":"1994","journal-title":"Anticancer Res."},{"key":"10.1016\/j.ejmech.2013.10.033_bib16","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/S1074-5521(99)80129-X","article-title":"Selective inhibition of amino-terminal methionine processing by TNP-470 and ovalicin in endothelial cells","volume":"6","author":"Turk","year":"1999","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ejmech.2013.10.033_bib17","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1111\/j.1440-1827.2009.02393.x","article-title":"Fumagillin inhibits colorectal cancer growth and metastasis in mice: in\u00a0vivo and in\u00a0vitro study of anti-angiogenesis","volume":"59","author":"Hou","year":"2009","journal-title":"Pathol. Int."},{"key":"10.1016\/j.ejmech.2013.10.033_bib18","doi-asserted-by":"crossref","first-page":"771","DOI":"10.3748\/wjg.v11.i6.771","article-title":"Fumagillin treatment of hepatocellular carcinoma in rats: an in\u00a0vivo study of antiangiogenesis","volume":"11","author":"Sheen","year":"2005","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.ejmech.2013.10.033_bib19","first-page":"4262","article-title":"Inhibition of tumor growth and metastasis of rodent tumors by the angiogenesis inhibitor O-(chloroacetyl-carbamoyl)fumagillol (TNP-470; AGM-1470)","volume":"53","author":"Yamaoka","year":"1993","journal-title":"Cancer Res."},{"key":"10.1016\/j.ejmech.2013.10.033_bib20","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1126\/science.284.5415.808","article-title":"Effects of angiogenesis inhibitors on multistage carcinogenesis in mice","volume":"284","author":"Bergers","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2013.10.033_bib21","first-page":"1201","article-title":"Survival benefit of KRN7000 immune therapy in combination with TNP470 in hamster liver metastasis model of pancreatic cancer","volume":"10","author":"Matsumoto","year":"2003","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.ejmech.2013.10.033_bib22","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1056\/NEJM199804023381412","article-title":"Complete remission of metastatic cervical cancer with the angiogenesis inhibitor TNP-470","volume":"338","author":"Kudelka","year":"1998","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.ejmech.2013.10.033_bib23","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.1016\/S0959-8049(96)00388-7","article-title":"TNP-470 (AGM-1470): mechanisms of action and early clinical development","volume":"32A","author":"Castronovo","year":"1996","journal-title":"Eur. J. Cancer"},{"key":"10.1016\/j.ejmech.2013.10.033_bib24","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1023\/A:1018301031580","article-title":"New anti-angiogenesis agents: review of the clinical experience with carboxyamido-triazole (CAI), thalidomide, TNP-470 and interleukin-12","volume":"1","author":"Masiero","year":"1997","journal-title":"Angiogenesis"},{"key":"10.1016\/j.ejmech.2013.10.033_bib25","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1073\/pnas.89.2.539","article-title":"The eukaryotic initiation factor 2-associated 67-kDa polypeptide (p67) plays a critical role in regulation of protein synthesis initiation in animal cells","volume":"89","author":"Ray","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2013.10.033_bib26","doi-asserted-by":"crossref","first-page":"7714","DOI":"10.1073\/pnas.92.17.7714","article-title":"Eukaryotic methionyl aminopeptidases: two classes of cobalt- dependent enzymes","volume":"92","author":"Arfin","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2013.10.033_bib27","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0968-0004(98)01227-4","article-title":"N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families","volume":"23","author":"Bradshaw","year":"1998","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.ejmech.2013.10.033_bib28","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/S1074-5521(97)90198-8","article-title":"Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin","volume":"4","author":"Griffith","year":"1997","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ejmech.2013.10.033_bib29","doi-asserted-by":"crossref","first-page":"6099","DOI":"10.1073\/pnas.94.12.6099","article-title":"The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2","volume":"94","author":"Sin","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2013.10.033_bib30","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1126\/science.282.5392.1324","article-title":"Structure of human methionine aminopeptidase-2 complexed with fumagillin","volume":"282","author":"Liu","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2013.10.033_bib31","doi-asserted-by":"crossref","first-page":"15183","DOI":"10.1073\/pnas.95.26.15183","article-title":"Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2","volume":"95","author":"Griffith","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2013.10.033_bib32","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1016\/S0968-0896(98)00078-9","article-title":"Synthetic analogues of TNP-470 and ovalicin reveal a common molecular basis for inhibition of angiogenesis and immunosuppression","volume":"6","author":"Turk","year":"1998","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib33","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0960-894X(99)00577-6","article-title":"Design and synthesis of highly potent fumagillin analogues from homology modeling for a human MetAP-2","volume":"10","author":"Han","year":"2000","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2013.10.033_bib34","doi-asserted-by":"crossref","first-page":"3452","DOI":"10.1021\/jm0341103","article-title":"Fumagalone, a reversible inhibitor of type 2 methionine aminopeptidase and angiogenesis","volume":"46","author":"Zhou","year":"2003","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib35","doi-asserted-by":"crossref","first-page":"10768","DOI":"10.1073\/pnas.0404105101","article-title":"A\u00a0methionine aminopeptidase-2 inhibitor, PPI-2458, for the treatment of rheumatoid arthritis","volume":"101","author":"Bernier","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2013.10.033_bib36","doi-asserted-by":"crossref","first-page":"5645","DOI":"10.1021\/jm060559v","article-title":"Fumarranol, a rearranged fumagillin analogue that inhibits angiogenesis in\u00a0vivo","volume":"49","author":"Lu","year":"2006","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib37","doi-asserted-by":"crossref","first-page":"3772","DOI":"10.1002\/anie.200600757","article-title":"Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases","volume":"45","author":"Hu","year":"2006","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.ejmech.2013.10.033_bib38","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1021\/cb600362d","article-title":"Inhibition of angiogenesis by the antifungal drug itraconazole","volume":"2","author":"Chong","year":"2007","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.ejmech.2013.10.033_bib39","doi-asserted-by":"crossref","first-page":"3832","DOI":"10.1021\/jm0601001","article-title":"Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding","volume":"49","author":"Sheppard","year":"2006","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib40","doi-asserted-by":"crossref","first-page":"3777","DOI":"10.1021\/jm061182w","article-title":"Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore","volume":"50","author":"Marino","year":"2007","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib41","doi-asserted-by":"crossref","first-page":"5644","DOI":"10.1021\/jm050408c","article-title":"4-Aryl-1,2,3-triazole: a novel template for a reversible methionine aminopeptidase 2 inhibitor, optimized to inhibit angiogenesis in\u00a0vivo","volume":"48","author":"Kallander","year":"2005","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib42","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1002\/(SICI)1097-4644(20000601)77:3<465::AID-JCB11>3.0.CO;2-M","article-title":"Selective inhibition of endothelial cell proliferation by fumagillin is not due to differential expression of methionine aminopeptidases","volume":"77","author":"Wang","year":"2000","journal-title":"J.\u00a0Cell. Biochem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib43","doi-asserted-by":"crossref","first-page":"52964","DOI":"10.1074\/jbc.M309039200","article-title":"Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors","volume":"278","author":"Towbin","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib44","first-page":"699","article-title":"Synthesis and in\u00a0vitro test of a biotinylated fumagillin derivative","volume":"32","author":"Liu","year":"2010","journal-title":"World Sci-Tech R & D"},{"key":"10.1016\/j.ejmech.2013.10.033_bib45","doi-asserted-by":"crossref","first-page":"2549","DOI":"10.1021\/ja00762a080","article-title":"A\u00a0total synthesis of (\u00b1)-fumagillin","volume":"94","author":"Corey","year":"1972","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2013.10.033_bib46","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1021\/bc950094f","article-title":"Synthesis of norbiotinamine and its derivatives","volume":"7","author":"Szalecki","year":"1996","journal-title":"Bioconjug. Chem."},{"key":"10.1016\/j.ejmech.2013.10.033_bib48","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/nchembio748","article-title":"Actin is the primary cellular receptor of bistramide A","volume":"1","author":"Statsuk","year":"2005","journal-title":"Nat. Chem. Biol."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523413006740?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523413006740?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,8,6]],"date-time":"2020-08-06T18:42:41Z","timestamp":1596739361000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523413006740"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,12]]},"references-count":47,"alternative-id":["S0223523413006740"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2013.10.033","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2013,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Design, synthesis and evaluation of a cellular stable and detectable biotinylated fumagillin probe and investigation of cell permeability of fumagillin and its analogs to endothelial and cancer cells","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2013.10.033","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2013 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}