Arylthioindole Inhibitors of Tubulin Polymerization. 3. Biological Evaluation, Structure−Activity Relationships and Molecular Modeling Studies-Reference-Cited by-同舟云学术

Arylthioindole Inhibitors of Tubulin Polymerization. 3. Biological Evaluation, Structure−Activity Relationships and Molecular Modeling Studies

Published:2007-05-12 Issue:12 Volume:50 Page:2865-2874
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

La Regina Giuseppe¹,Edler Michael C.¹,Brancale Andrea¹,Kandil Sahar¹,Coluccia Antonio¹,Piscitelli Francesco¹,Hamel Ernest¹,De Martino Gabriella¹,Matesanz Ruth¹,Díaz José Fernando¹,Scovassi Anna Ivana¹,Prosperi Ennio¹,Lavecchia Antonio¹,Novellino Ettore¹,Artico Marino¹,Silvestri Romano¹

Affiliation:

1. Istituto Pasteur − Fondazione Cenci Bolognetti, Dipartimento di Studi Farmaceutici, Sapienza Università di Roma, Piazzale Aldo Moro 5, I-00185 Roma, Italy, Welsh School of Pharmacy, Cardiff University, King Edward VII Avenue, Cardiff, CF10 3XF, United Kingdom, Toxicology and Pharmacology Branch, Developmental Therapeutics Program, Division of Cancer Treatment and Diagnosis, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland 21702, Dipartimento di Chimica...

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm061479u

Reference36 articles.

1. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain

2. High-Resolution Model of the Microtubule

3. The Binding Mode of Epothilone A on α,ß-Tubulin by Electron Crystallography

4. The length of a junction between the B and Z conformations in DNA is three base pairs or less

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