The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation (Q22010608)

GOA release 2020-03-11

magnesium ion binding

1 reference

GOA release 2020-03-11

S Bellon

1

S

Bellon

1 reference

7 February 2023

M J Fitzgibbon

2

M J

Fitzgibbon

1 reference

7 February 2023

T Fox

3

T

Fox

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7 February 2023

H M Hsiao

4

H M

Hsiao

1 reference

7 February 2023

K P Wilson

5

K P

Transcriptional regulation by MAP kinases

Wilson

1 reference

7 February 2023

language of work or name

English

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publication date

15 September 1999

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published in

Structure

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volume

7

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issue

9

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page(s)

1057-65

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cites work

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How MAP kinases are regulated

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Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation

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Three protein kinase structures define a common motif

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Phylogenetic and functional classification of mitogen- and stress-activated protein kinases

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The primary structure of p38 gamma: a new member of p38 group of MAP kinases

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Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6

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Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine

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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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A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells

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Active and inactive protein kinases: structural basis for regulation

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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

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Pyridinyl imidazole inhibitors of p38 mitogen-activated protein kinase bind in the ATP site

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A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket

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The structural basis for the specificity of pyridinylimidazole inhibitors of p38 MAP kinase

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T cell proliferation in response to interleukins 2 and 7 requires p38MAP kinase activation.

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A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase

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Crystal structure of JNK3: a kinase implicated in neuronal apoptosis

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

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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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A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility

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Crystal structure of p38 mitogen-activated protein kinase

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Human mitogen-activated protein kinase CSBP1, but not CSBP2, complements a hog1 deletion in yeast

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Mitogen-activated protein kinase pathways

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Control by phosphorylation

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Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation

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Structural basis of cyclin-dependent kinase activation by phosphorylation

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Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation

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Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death

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Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs

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Phase annealing in SHELX-90: direct methods for larger structures

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

4503842

4503842

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference