Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein (Q24318588)

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Language	Label	Description	Also known as
English	Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein	scientific article

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scholarly article

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Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein (English)

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author name string

D Dowbenko

1

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S Spencer

2

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C Quan

3

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L A Lasky

4

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language of work or name

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publication date

9 January 1998

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Journal of Biological Chemistry

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273

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2

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989-96

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Protein modules and signalling networks

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Signalling through SH2 and SH3 domains

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

SH2 and SH3 domains

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

The WW domain: a signalling site in dystrophin?

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Towards prediction of cognate complexes between the WW domain and proline-rich ligands

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Characterization of the WW domain of human yes-associated protein and its polyproline-containing ligands

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Identification of novel human WW domain-containing proteins by cloning of ligand targets

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B

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https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Protein tyrosine phosphatases in signal transduction.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

WW domains and retrovirus budding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

Alpha-helical coiled coils: more facts and better predictions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

21 January 2018

PTP-PEST: a protein tyrosine phosphatase regulated by serine phosphorylation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

7 January 2021

based on heuristic

inferred from DOI database lookup

Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

7 January 2021

based on heuristic

inferred from DOI database lookup

WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.2.989

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1074/JBC.273.2.989

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