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A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity

publié dans: Journal of Molecular Biology

date de publication: 2006-10-26

langue: anglais

Articles cités 37

Date

Titre

Auteur·ices

2006-01-01

Relating protein motion to catalysis

Sharon Hammes-Schiffer
2005-09-01

C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)--endogenous negative regulators of Src-family protein kinases

Heung-Chin Cheng, Terrence D. Mulhern
2005-09-08

Coupling phosphoryl transfer and substrate interactions in protein kinases
2005-06-01

The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation
2005-02-01

Probing the communication between the regulatory and catalytic domains of a protein tyrosine kinase, Csk.
2005-08-01

Coupled motions in the SH2 and kinase domains of Csk control Src phosphorylation

Kjetil Taskén
2004-10-05

Protein thiol modifications visualized in vivo

Lars Ingo Ole Leichert
2004-03-01

Oxidative stress activates both Src-kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk: caveolin-1 and paxillin

Cynthia Corley Mastick
2004-07-01

Dynamic coupling between the SH2 domain and active site of the COOH terminal Src kinase, Csk.
2003-10-17

Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins

Peter Guy Wolynes
2003-04-09

Functions of the activation loop in Csk protein-tyrosine kinase
2002-03-07

Structure of the carboxyl-terminal Src kinase, Csk

Yoshiharu Takayama, Atsushi Nakagawa
2002-12-01

1H, 13C and 15N chemical shift assignments of the SH2 domain of the Csk homologous kinase

Terrence D. Mulhern, Heung-Chin Cheng
2001-11-01

Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR.
2001-06-04

Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src kinase (Csk) from lipid rafts

Kjetil Taskén
2000-04-27

Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases

Yoshinori Satomi
2000-05-01

Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation

Karel Drbal, Tomáš Brdička
2000-10-01

Catalytic assessment of the glycine-rich loop of the v-Fps oncoprotein using site-directed mutagenesis
2000-10-01

Building-block approach for determining low-frequency normal modes of macromolecules.
1999-10-01

600 ps molecular dynamics reveals stable substructures and flexible hinge points in cAMP dependent protein kinase
1999-08-01

Domain interactions in protein tyrosine kinase Csk.
1999-07-01

Mutations in the N-terminal regulatory region reduce the catalytic activity of Csk, but do not affect its recognition of Src.
1999-04

Automated analysis of interatomic contacts in proteins
1998-05-01

Kinetic analyses of mutations in the glycine-rich loop of cAMP-dependent protein kinase.
1997

Cellular functions regulated by Src family kinases
1997-12-01

Structures of Src-family tyrosine kinases
1996-01-01

Redox modulation of tyrosine phosphorylation-dependent signal transduction pathways
1996-08-26

Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis
1995-11

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Stephan Grzesiek, Ad Bax
1995-07

Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
1994-01-01

Structure and function of SH2 domains
1993-10-01

Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations

Article - wd:Q42551167

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