Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Active mutants of the TCR-mediated p38α alternative activation site show changes in the phosphorylation lip and DEF site formation.

Journal of molecular biology - 4 Feb 2011

Tzarum Netanel, Diskin Ron, Engelberg David, Livnah Oded

Abstract excerpt

The p38α mitogen-activated protein kinase is commonly activated by dual (Thr and Tyr) phosphorylation catalyzed by mitogen-activated protein kinase kinases. However, in T-cells, upon stimulation of the T-cell receptor, p38α is activated via an alternative pathway, involving its phosphorylation by zeta-chain-associated protein kinase 70 on Tyr323, distal from the phosphorylation lip. Tyr323-phosphorylated p38α is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Enzyme Activation

Share to Molecular Sequence Data

Share to Phosphorylation

Share to Protein Conformation

Share to Receptors, Antigen, T-Cell

Source

Identifiers

PMID: 21146537
DOI: 10.1016/j.jmb.2010.11.023

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Active mutants of the TCR-mediated p38α alternative activation site show changes in the phosphorylation lip and DEF site formation.PMID 21146537Read ↗

Structures of p38alpha active mutants reveal conformational changes in L16 loop that induce autophosphorylation and activation.Semantic proximity Read ↗

DEF pocket in p38α facilitates substrate selectivity and mediates autophosphorylation.Semantic proximity Read ↗

p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180.Semantic proximity Read ↗

Active mutants of the human p38alpha mitogen-activated protein kinase.Semantic proximity Read ↗

Intrinsically active variants of all human p38 isoforms.Semantic proximity Read ↗

A conserved arginine within the αC-helix of Erk1/2 is a latch of autoactivation and of oncogenic capabilities.Semantic proximity Read ↗

A novel lipid binding site formed by the MAP kinase insert in p38 alpha.Semantic proximity Read ↗

Identification of two distinct regions of p38 MAPK required for substrate binding and phosphorylation.Semantic proximity Read ↗

Characterization of Ser338 phosphorylation for Raf-1 activation.Semantic proximity Read ↗

Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K.Semantic proximity Read ↗

MAP-quest: could we produce constitutively active variants of MAP kinases?Semantic proximity Read ↗

A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.