(Q28307277)

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SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl

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title

SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl (English)

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D Baltimore

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author name string

S M Feller

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R Ren

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H Hanafusa

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language of work or name

English

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publication date

November 1994

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published in

Trends in Biochemical Sciences

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volume

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page(s)

453-8

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cites work

The nuclear tyrosine kinase c-Abl negatively regulates cell growth

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0968-0004(94)90129-5

SH2 domain specificity and activity modified by a single residue

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Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins

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Cloning of a Grb2 isoform with apoptotic properties

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Activation of phosphatidylinositol 3-kinase in cells expressing abl oncogene variants

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https://opencitations.net/index/coci/api/v1/references/10.1016/0968-0004(94)90129-5

SH2 domains recognize specific phosphopeptide sequences

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The viral and cellular forms of the Abelson (abl) oncogene

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Differential complementation of Bcr-Abl point mutants with c-Myc

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Hormone-conditional transformation by fusion proteins of c-Abl and its transforming variants

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Drosophila abl and genetic redundancy in signal transduction

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Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0968-0004(94)90129-5

A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle

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A putative modular domain present in diverse signaling proteins

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SH3--an abundant protein domain in search of a function

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Implicating the bcr/abl gene in the pathogenesis of Philadelphia chromosome-positive human leukemia

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Abl tyrosine kinase in signal transduction and cell-cycle regulation

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The structure and function of proline-rich regions in proteins

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SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

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Coupling between p210bcr-abl and Shc and Grb2 adaptor proteins in hematopoietic cells permits growth factor receptor-independent link to ras activation pathway

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Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins

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Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor

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Identification of a ten-amino acid proline-rich SH3 binding site

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Identification and Characterization of a High-Affinity Interaction Between v-Crk and Tyrosine-Phosphorylated Paxillin in CT10-Transformed Fibroblasts

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Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase

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Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho

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SH1 domain autophosphorylation of P210 BCR/ABL is required for transformation but not growth factor independence

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0968-0004(94)90129-5

c-Abl kinase regulates the protein binding activity of c-Crk

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0968-0004(94)90129-5

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

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0968-0004(94)90129-5

Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0968-0004(94)90129-5

Identifiers

DOI

10.1016/0968-0004(94)90129-5

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2281677

OpenCitations bibliographic resource ID

2281677

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2281677

PubMed publication ID

7855886

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2281677

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