Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer (Q24301665)

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English	Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer	scientific article

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scholarly article

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Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer (English)

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Radosław Zagożdżon

2

object named as

Radoslaw Zagozdzon

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Hava Karsenty Avraham

object named as

Hava Avraham

7

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author name string

Soyoun Kim

1

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Alan Meisler

3

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James D Baleja

4

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Yigong Fu

5

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Shalom Avraham

6

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language of work or name

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publication date

27 September 2002

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Journal of Biological Chemistry

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277

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39

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36465-70

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Association of INT2/HST1 coamplification in primary breast cancer with hormone-dependent phenotype and poor prognosis

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Inheritance of human breast cancer: evidence for autosomal dominant transmission in high-risk families

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Cancer: the rise of the genetic paradigm

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Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor

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Role of HER2 gene overexpression in breast carcinoma

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erbB-2 is a potent oncogene when overexpressed in NIH/3T3 cells

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Distinct tyrosine autophosphorylation sites negatively and positively modulate neu-mediated transformation

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The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain

1 reference

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Association of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells

1 reference

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Csk homologous kinase, a novel signaling molecule, directly associates with the activated ErbB-2 receptor in breast cancer cells and inhibits their proliferation

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Functional analysis of Csk and CHK kinases in breast cancer cells.

1 reference

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Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme family

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Ntk: a Csk-related protein-tyrosine kinase expressed in brain and T lymphocytes

1 reference

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Chk, a Csk family tyrosine protein kinase, exhibits Csk-like activity in fibroblasts, but not in an antigen-specific T-cell line.

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Mechanism-based target identification and drug discovery in cancer research

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Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

1 reference

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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

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Three-dimensional structure of the tyrosine kinase c-Src

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Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences

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Demonstration of protein-protein interaction specificity by NMR chemical shift mapping

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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

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Cellular functions regulated by Src family kinases

1 reference

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SH2 domains recognize specific phosphopeptide sequences

1 reference

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Crystal structure of the C-terminal SH2 domain of the p85alpha regulatory subunit of phosphoinositide 3-kinase: an SH2 domain mimicking its own substrate

1 reference

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Temperature-sensitive transformation by an Abelson virus mutant encoding an altered SH2 domain

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Correlation between binding and dynamics at SH2 domain interfaces

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Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase

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Six X-Linked Agammaglobulinemia-Causing Missense Mutations in the Src Homology 2 Domain of Bruton's Tyrosine Kinase: Phosphotyrosine-Binding and Circular Dichroism Analysis

1 reference

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Resolution and sensitivity gain in HCCH-TOCSY experiments by homonuclear C beta decoupling

1 reference

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7 January 2021

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10.1074/JBC.M206018200

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