Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity (Q28278276)

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English	Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity	scientific article

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scholarly article

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Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity (English)

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author name string

A Charest

1

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J Wagner

2

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S Jacob

3

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C J McGlade

4

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M L Tremblay

5

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language of work or name

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publication date

5 April 1996

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Journal of Biological Chemistry

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271

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14

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8424-9

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An alternative to SH2 domains for binding tyrosine-phosphorylated proteins

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PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine

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A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides

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Shc Binding to Nerve Growth Factor Receptor Is Mediated by the Phosphotyrosine Interaction Domain

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Binding of Shc to the NPXY Motif Is Mediated by Its N-terminal Domain

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Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor

1 reference

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Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains

1 reference

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The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif

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'Zip codes' direct intracellular protein tyrosine phosphatases to the correct cellular 'address'.

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A phosphotyrosine interaction domain

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Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis

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Signal transduction in bacteria

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