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Crystal structure of JNK3: a kinase implicated in neuronal apoptosis
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scholarly article
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title
Crystal structure of JNK3: a kinase implicated in neuronal apoptosis
(English)
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main subject
apoptotic process
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crystal structure
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author name string
X Xie
series ordinal
1
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Y Gu
series ordinal
2
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T Fox
series ordinal
3
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J T Coll
series ordinal
4
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M A Fleming
series ordinal
5
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W Markland
series ordinal
6
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P R Caron
series ordinal
7
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K P Wilson
series ordinal
8
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M S Su
series ordinal
9
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publication date
15 August 1998
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published in
Structure
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volume
6
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page(s)
983-91
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issue
8
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cites work
How MAP kinases are regulated
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Selective interaction of JNK protein kinase isoforms with transcription factors
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Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
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Integration of MAP kinase signal transduction pathways at the serum response element
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Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway
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p53 is phosphorylated in vitro and in vivo by an ultraviolet radiation-induced protein kinase characteristic of the c-Jun kinase, JNK1.
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A splicing variant of a death domain protein that is regulated by a mitogen-activated kinase is a substrate for c-Jun N-terminal kinase in the human central nervous system
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p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system
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Developmental expression in the mouse nervous system of the p493F12 SAP kinase
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Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
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Crystal structure of p38 mitogen-activated protein kinase
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Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase
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Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
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2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor.
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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
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JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation
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Activity of the MAP kinase ERK2 is controlled by a flexible surface loop
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Regulation of the activity of the transcription factors AP-1 and NFAT during differentiation of precursor CD4+ T-cells into effector cells
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Regulation of AP-1 and NFAT transcription factors during thymic selection of T cells
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Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
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Cardiac hypertrophy induced by mitogen-activated protein kinase kinase 7, a specific activator for c-Jun NH2-terminal kinase in ventricular muscle cells
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AMoRe: an automated package for molecular replacement
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PROCHECK: a program to check the stereochemical quality of protein structures
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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
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ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
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Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase
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The protein kinase family: conserved features and deduced phylogeny of the catalytic domains
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JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
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Signal transduction by tumor necrosis factor mediated by JNK protein kinases
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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
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Identifiers
DOI
10.1016/S0969-2126(98)00100-2
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PubMed ID
9739089
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ResearchGate publication ID
13546943
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