Interactions of the Rad51 inhibitor DIDS with human and bovine serum albumins: Optical spectroscopy and isothermal calorimetry approaches-Reference-Cited by-同舟云学术

Interactions of the Rad51 inhibitor DIDS with human and bovine serum albumins: Optical spectroscopy and isothermal calorimetry approaches

Published:2019-12 Issue: Volume:167 Page:187-197
ISSN:0300-9084
Container-title:Biochimie
language:en
Short-container-title:Biochimie

Author:

Velic Denis,Charlier Cathy,Popova Milena,Jaunet-Lahary Titouan,Bouchouireb Zakaria,Henry Sébastien,Weigel Pierre,Masson Jean-Yves,Laurent Adèle,Nabiev Igor^ORCID,Fleury Fabrice^ORCID

Funder

Ligue Contre le Cancer

Program Samuel-De-Champlain

MES-TransMed Pari Scientifique

GENCI-CINES/IDRIS

CCIPL

Ministry of Education and Science of the Russian Federation

Publisher

Elsevier BV

Subject

General Medicine,Biochemistry

Reference42 articles.

1. New light on the "old" chloride channel blocker DIDS;Wulff;ACS Chem. Biol.,2008

2. DIDS, a chemical compound that inhibits RAD51-mediated homologous pairing and strand exchange;Ishida;Nucleic Acids Res.,2009

3. Design of potent inhibitors of human RAD51 recombinase based on BRC motifs of BRCA2 protein: modeling and experimental validation of a chimera peptide;Nomme;J. Med. Chem.,2010

4. Systematic screen identifies miRNAs that target RAD51 and RAD51D to enhance chemosensitivity;Huang;Mol. Cancer Res.,2013

5. RAD51 as a potential biomarker and therapeutic target for pancreatic cancer;Nagathihalli;Biochim. Biophys. Acta,2011

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