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The Unique Amino-Terminal Domain of p56lckRegulates Interactions with Tyrosine Protein Phosphatases in T Lymphocytes

Data up to Jan 2025

Published1995
Citations35
References57

Total Citations Per Year

Abstract

References (57)

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The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain

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Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins.

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Short Related Sequences in the Cytoplasmic Domains of CD4 and CD8 Mediate Binding to the Amino-Terminal Domain of the p56lck Tyrosine Protein Kinase

1990 • 245 citations

Neoplastic transformation induced by an activated lymphocyte-specific protein tyrosine kinase (pp56lck).

1988 • 232 citations

CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck.

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p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain.

1992 • 212 citations

Mutation of a site of tyrosine phosphorylation in the lymphocyte-specific tyrosine protein kinase, p56lck, reveals its oncogenic potential in fibroblasts.

1988 • 208 citations

Regulation of Lymphocyte Function by Protein Phosphorylation

1993 • 203 citations

Correlation between Src family member regulation by the protein-tyrosine-phosphatase CD45 and transmembrane signaling through the T-cell receptor.

1993 • 202 citations

The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP.

1993 • 199 citations

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1987 • 132 citations

Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation.

1990 • 129 citations

CD8+ T-cell clones deficient in the expression of the CD45 protein tyrosine phosphatase have impaired responses to T-cell receptor stimuli.

1991 • 109 citations

A functional complex is formed in human T lymphocytes between the protein tyrosine phosphatase CD45, the protein tyrosine kinase p56lck and pp32, a possible common substrate

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Post-translational alterations of the tyrosine kinase p56lck in response to activators of protein kinase C.

1988 • 103 citations

CD45 regulation of tyrosine phosphorylation and enzyme activity of src family kinases.

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Phosphorylation of Ser-42 and Ser-59 in the N-terminal region of the tyrosine kinase p56lck.

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Phosphorylation of serine 59 of p56lck in activated T cells.

1993 • 85 citations

Regulation of the enzymatic function of the lymphocyte-specific tyrosine protein kinase p56lck by the non-catalytic SH2 and SH3 domains.

1992 • 82 citations

The CD45 tyrosine phosphatase regulates phosphotyrosine homeostasis and its loss reveals a novel pattern of late T cell receptor-induced Ca2+ oscillations.

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The lymphocyte-specific tyrosine protein kinase p56lck.

1991 • 60 citations

CD45-associated kinase activity requires lck but not T cell receptor expression in the Jurkat T cell line.

1993 • 54 citations

Anti-CD3 and phorbol ester induce distinct phosphorylated sites in the SH2 domain of p56lck.

1993 • 54 citations

Insulin‐specific T cell hybridomas derived from (H‐2b × H‐2k)F1 mice preferably employ F1unique restriction elements for antigen recognition

1985 • 44 citations

The SH2 Domain is Required for Stable Phosphorylation of p561ck at Tyrosine 505, the Negative Regulatory Site

1993 • 44 citations

Oncogenic activation of p59fyn tyrosine protein kinase by mutation of its carboxyl-terminal site of tyrosine phosphorylation, tyrosine 528.

1994 • 43 citations

Interactions of the SH2 domain of lymphocyte-specific tyrosine protein kinase p56lck with phosphotyrosine-containing proteins.

1993 • 43 citations

Analysis of the sites in p56lck whose phosphorylation is induced by tetradecanoyl phorbol acetate.

1990 • 35 citations

Use of the Escherichia coli gene for asparagine synthetase as a selective marker in a shuttle vector capable of dominant transfection and amplification in animal cells.

1987 • 33 citations

Intramolecular and extramolecular mechanisms repress the catalytic function of p56lck in resting T-lymphocytes.

1994 • 19 citations

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The Unique Amino-Terminal Domain of p56lckRegulates Interactions with Tyrosine Protein… (1995) – Molecular and Cellular Biology | Metascience Observatory Explorer