Targeting Tubulin-colchicine Site for Cancer Therapy: Inhibitors, Antibody- Drug Conjugates and Degradation Agents
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Published:2019-09-03
Issue:15
Volume:19
Page:1289-1304
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ISSN:1568-0266
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Container-title:Current Topics in Medicinal Chemistry
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language:en
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Short-container-title:CTMC
Author:
Duan Yongtao1, Liu Wei1, Tian Liang1, Mao Yanna1, Song Chuanjun2
Affiliation:
1. Henan Provincial Key Laboratory of Children's Genetics and Metabolic Diseases, Children's Hospital Affiliated to Zhengzhou University, Henan Children's Hospital, Zhengzhou Children's Hospital, Zhengzhou, 450018, China 2. College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou, 450001, China
Abstract
Microtubules are essential for the mitotic division of cells and have been an attractive target
for antitumour drugs due to the increased incidence of cancer and significant mitosis rate of tumour cells.
In the past few years, tubulin-colchicine binding site, as one of the three binding pockets including taxol-,
vinblastine- and colchicine-binding sites, has been focused on to design tubulin-destabilizing agents including
inhibitors, antibody-drug conjugates and degradation agents. The present review is the first to
cover a systemic and recent synopsis of tubulin-colchicine binding site agents. We believe that it would
provide an increase in our understanding of receptor-ligand interaction pattern and consciousness of a
series of challenges about tubulin target druggability.
Funder
Henan Medical Science and Technology Program Henan Province Postdoctoral Science Foundation National Natural Science Foundation of China
Publisher
Bentham Science Publishers Ltd.
Subject
Drug Discovery,General Medicine
Reference154 articles.
1. Smith R.A.; Manassaram-Baptiste D.; Brooks D.; Doroshenk M.; Fedewa S.; Saslow D.; Brawley O.W.; Wender R.; Cancer screening in the United States, 2015: A review of current American cancer society guidelines and current issues in cancer screening. CA Cancer J Clin [http://dx.doi.org/10.3322/caac.21261]. [PMID: 25581023].2015,65(1),30-54 2. Fitzmaurice C.; Akinyemiju T.F.; Al Lami F.H.; Alam T.; Alizadeh-Navaei R.; Allen C.; Alsharif U.; Alvis-Guzman N.; Amini E.; Anderson B.O.; Aremu O.; Artaman A.; Asgedom S.W.; Assadi R.; Atey T.M.; Avila-Burgos L.; Awasthi A.; Ba Saleem H.O.; Barac A.; Bennett J.R.; Bensenor I.M.; Bhakta N.; Brenner H.; Cahuana-Hurtado L.; Castañeda-Orjuela C.A.; Catalá-López F.; Choi J.J.; Christopher D.J.; Chung S.C.; Curado M.P.; Dandona L.; Dandona R.; das Neves, J.; Dey, S.; Dharmaratne, S.D.; Doku, D.T.; Driscoll, T.R.; Dubey, M.; Ebrahimi, H.; Edessa, D.; El-Khatib, Z.; Endries, A.Y.; Fischer, F.; Force, L.M.; Foreman, K.J.; Gebrehiwot, S.W.; Gopalani, S.V.; Grosso, G.; Gupta, R.; Gyawali, B.; Hamadeh, R.R.; Hamidi, S.; Harvey, J.; Hassen, H.Y.; Hay, R.J.; Hay, S.I.; Heibati, B.; Hiluf, M.K.; Horita, N.; Hosgood, H.D.; Ilesanmi, O.S.; Innos, K.; Islami, F.; Jakovljevic, M.B.; Johnson, S.C.; Jonas, J.B.; Kasaeian, A.; Kassa, T.D.; Khader, Y.S.; Khan, E.A.; Khan, G.; Khang, Y.H.; Khosravi, M.H.; Khubchandani, J.; Kopec, J.A.; Kumar, G.A.; Kutz, M.; Lad, D.P.; Lafranconi, A.; Lan, Q.; Legesse, Y.; Leigh, J.; Linn, S.; Lunevicius, R.; Majeed, A.; Malekzadeh, R.; Malta, D.C.; Mantovani, L.G.; McMahon, B.J.; Meier, T.; Melaku, Y.A.; Melku, M.; Memiah, P.; Mendoza, W.; Meretoja, T.J.; Mezgebe, H.B.; Miller, T.R.; Mohammed, S.; Mokdad, A.H.; Moosazadeh, M.; Moraga, P.; Mousavi, S.M.; Nangia, V.; Nguyen, C.T.; Nong, V.M.; Ogbo, F.A.; Olagunju, A.T.; Pa, M.; Park, E.K.; Patel, T.; Pereira, D.M.; Pishgar, F.; Postma, M.J.; Pourmalek, F.; Qorbani, M.; Rafay, A.; Rawaf, S.; Rawaf, D.L.; Roshandel, G.; Safiri, S.; Salimzadeh, H.; Sanabria, J.R.; Santric Milicevic, M.M.; Sartorius, B.; Satpathy, M.; Sepanlou, S.G.; Shackelford, K.A.; Shaikh, M.A.; Sharif-Alhoseini, M.; She, J.; Shin, M.J.; Shiue, I.; Shrime, M.G.; Sinke, A.H.; Sisay, M.; Sligar, A.; Sufiyan, M.B.; Sykes, B.L.; Tabarés-Seisdedos, R.; Tessema, G.A.; Topor-Madry, R.; Tran, T.T.; Tran, B.X.; Ukwaja, K.N.; Vlassov, V.V.; Vollset, S.E.; Weiderpass, E.; Williams, H.C.; Yimer, N.B.; Yonemoto, N.; Younis, M.Z.; Murray, C.J.L.; Naghavi, M. Global burden of disease cancer collaboration. Global, regional, and national cancer incidence, mortality, years of life lost, years lived with disability, and disability-adjusted life-years for 29 cancer groups, 1990 to 2016: A systematic analysis for the global burden of disease study. JAMA Oncol [http://dx.doi.org/10.1001/jamaoncol.2018.2706]. [PMID: 29860482].2018,4(11),1553-1568 3. Brouhard G.J.; Rice L.M.; The contribution of αβ-tubulin curvature to microtubule dynamics. J Cell Biol [http://dx.doi.org/10.1083/jcb.201407095]. [PMID: 25385183].2014,207(3),323-334 4. McIntosh J.R.; Hays T.; A brief history of research on mitotic mechanisms. Biology (Basel) [http://dx.doi.org/10.3390/biology5040055]. [PMID: 28009830].2016,5(4),E55 5. Petry S.; Mechanisms of mitotic spindle assembly. Annu Rev Biochem [http://dx.doi.org/10.1146/annurev-biochem-060815-014528]. [PMID: 27145846].2016,85,659-683
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