The SH3 domain of Eps8 exists as a novel intertwined dimer-Reference-Cited by-同舟云学术

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The SH3 domain of Eps8 exists as a novel intertwined dimer

Published:1997-09 Issue:9 Volume:4 Page:739-743
ISSN:1072-8368
Container-title:Nature Structural Biology
language:
Short-container-title:Nat Struct Mol Biol

Author:

Radha Kishan K.V.,Scita Giorgio,Wong William T.,Di Fiore Pier Paolo,Newcomer Marcia E.

Publisher

Springer Science and Business Media LLC

Subject

Genetics,Biochemistry,Structural Biology

Reference35 articles.

1. Solution structure and peptide binding of the SH3 domain from human Fyn

2. Structural basis for the binding of proline-rich peptides to SH3 domains

3. Backwards and forwards binding

4. Two Binding Orientations for Peptides to the Src SH3 Domain: Development of a General Model for SH3-Ligand Interactions

5. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides

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1. Targeting of microvillus protein Eps8 by the NleH effector kinases from enteropathogenic E. coli;Proceedings of the National Academy of Sciences;2022-08-17

2. Structural insights into the substrate-binding proteins Mce1A and Mce4A from Mycobacterium tuberculosis;IUCrJ;2021-07-28

3. EPS8 phosphorylation by Src modulates its oncogenic functions;British Journal of Cancer;2020-07-09

4. Small molecule AX-024 reduces T cell proliferation independently of CD3ϵ/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain;Journal of Biological Chemistry;2020-06

5. Novel Nuclear Partnering Role of EPS8 With FOXM1 in Regulating Cell Proliferation;Frontiers in Oncology;2019-03-19

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