Regions outside of conserved PxxPxR motifs drive the high affinity interaction of GRB2 with SH3 domain ligands-Reference-Cited by-同舟云学术

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Regions outside of conserved PxxPxR motifs drive the high affinity interaction of GRB2 with SH3 domain ligands

Published:2015-10 Issue:10 Volume:1853 Page:2560-2569
ISSN:0167-4889
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Author:

Bartelt Rebekah R.,Light Jonathan,Vacaflores Aldo,Butcher Alayna,Pandian Madhana,Nash Piers,Houtman Jon C.D.

Funder

American Heart Association

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference44 articles.

1. The SH3 domain—a family of versatile peptide- and protein-recognition module;Kaneko;Front. Biosci.,2008

2. SH3 domain ligand binding: what's the consensus and where's the specificity?;Saksela;FEBS Lett.,2012

3. Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction;Li;Biochem. J.,2005

4. Searching for specificity in SH domains;Ladbury;Chem. Biol.,2000

5. A high-affinity Arg-X-X-Lys SH3 binding motif confers specificity for the interaction between Gads and SLP-76 in T Cell signaling;Berry;Curr. Biol.,2002

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1. Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy;ELIFE;2024

2. Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy;eLife;2024-07-12

3. Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy;eLife;2024-07-12

4. Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy;2024-06-21

5. GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production;Scientific Reports;2023-03-02

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