PM534, an Optimized Target-Protein Interaction Strategy through the Colchicine Site of Tubulin-Reference-Cited by-同舟云学术

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PM534, an Optimized Target-Protein Interaction Strategy through the Colchicine Site of Tubulin

Published:2024-01-31 Issue: Volume: Page:
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Lucena-Agell Daniel¹,Guillén María José²,Matesanz Ruth¹,Álvarez-Bernad Beatriz¹,Hortigüela Rafael¹,Avilés Pablo²,Martínez-Díez Marta²,Santamaría-Núñez Gema²,Contreras Julia³,Plaza-Menacho Iván³,Giménez-Abián Juan F.¹,Oliva María A.¹^ORCID,Cuevas Carmen²,Díaz J. Fernando¹^ORCID

Affiliation:

1. Unidad BICS. Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, 28040 Madrid, Spain

2. PharmaMar S.A., Avda de los Reyes 1, Colmenar Viejo, 28770 Madrid, Spain

3. Centro Nacional de Investigaciones Oncológicas (CNIO), Melchor Fernández Almagro 3, 28029 Madrid, Spain

Funder

Ministerio de Ciencia e InnovaciÃ³n

European Commission

FundaciÃ³n Tatiana PÃ©rez de GuzmÃ¡n el Bueno

PharmaMar

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.3c01775

Reference71 articles.

1. Microtubules as a target for anticancer drugs

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

3. Structural basis for the regulation of tubulin by vinblastine

4. A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs

5. Pironetin Binds Covalently to αCys316 and Perturbs a Major Loop and Helix of α-Tubulin to Inhibit Microtubule Formation

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