A limited set of SH2 domains binds BCR through a high-affinity phosphotyrosine-independent interaction (Q24600945)

1

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A M Pendergast

2

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M H Havlik

3

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L Puil

4

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T Pawson

5

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O N Witte

Molecular and Cellular Biology

6

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language of work or name

English

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publication date

November 1992

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published in

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volume

12

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issue

11

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page(s)

5087-93

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Molecular cloning of cDNAs encoding the GAP-associated protein p190: implications for a signaling pathway from ras to the nucleus

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Multiple SH2-mediated interactions in v-src-transformed cells

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Specificity pockets for the side chains of peptide antigens in HLA-Aw68

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Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product

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BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner

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Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways

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7 April 2017

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Only site-directed antibodies reactive with the highly conserved src-homologous region of the v-abl protein neutralize kinase activity.

7 April 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias

27 September 2017

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27 September 2017

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Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor

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A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine

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27 September 2017

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27 September 2017

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30 May 2018

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30 May 2018

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30 May 2018

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