Combined In-Solution Fragment Screening and Crystallographic Binding-Mode Analysis with a Two-Domain Hsp70 Construct-Reference-Cited by-同舟云学术

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Combined In-Solution Fragment Screening and Crystallographic Binding-Mode Analysis with a Two-Domain Hsp70 Construct

Published:2024-02-05 Issue: Volume: Page:
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Zehe Markus¹^ORCID,Kehrein Josef¹^ORCID,Schollmayer Curd¹,Plank Christina¹²,Kovacs Helena³,Merino Asumendi Eduardo¹^ORCID,Holzgrabe Ulrike¹^ORCID,Grimm Clemens²,Sotriffer Christoph¹^ORCID

Affiliation:

1. University of Würzburg, Institute of Pharmacy and Food Chemistry, Am Hubland, DE-97074 Würzburg, Germany

2. University of Würzburg, Department of Biochemistry and Cancer Therapy Research Center (CTRC), Theodor-Boveri-Institute, Am Hubland, DE-97074 Würzburg, Germany

3. Bruker Switzerland AG, Industriestrasse 26, CH-8117 Fällanden, Switzerland

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.3c00589

Reference67 articles.

1. Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target

2. Targeting Hsp70: A possible therapy for cancer

3. Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries

4. Hsp70- and Hsp90-Mediated Regulation of the Conformation of p53 DNA Binding Domain and p53 Cancer Variants

5. HSP70 and HSP90 in Cancer: Cytosolic, Endoplasmic Reticulum and Mitochondrial Chaperones of Tumorigenesis

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