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

Functional characterization of peanut serine/threonine/tyrosine protein kinase: molecular docking and inhibition kinetics with tyrosine kinase inhibitors.

Biochemistry - 28 Sept 2004

Rudrabhatla Parvathi, Rajasekharan Ram

Abstract excerpt

Serine/threonine/tyrosine (STY) protein kinase from peanut is developmentally regulated and is induced by abiotic stresses. In addition, STY protein kinase activity is regulated by tyrosine phosphorylation. Kinetic mechanism of plant dual specificity protein kinases is not studied so far. Recombinant STY protein kinase occurs as a monomer in solution as shown by gel filtration chromatography. The relative...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Arachis
Share to Chromatography, Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genistein

Share to Protein Structure, Quaternary

Share to Protein-Tyrosine Kinases

Share to Staurosporine

Share to Tyrphostins

Source

Identifiers

PMID: 15379551
DOI: 10.1021/bi0497042

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional characterization of peanut serine/threonine/tyrosine protein kinase: molecular docking and inhibition kinetics with tyrosine kinase inhibitors.PMID 15379551Read ↗

Mutational analysis of stress-responsive peanut dual specificity protein kinase. Identification of tyrosine residues involved in regulation of protein kinase activity.Semantic proximity Read ↗

Autophosphorylation of gatekeeper tyrosine by symbiosis receptor kinase.Semantic proximity Read ↗

Autoinhibitory mechanisms in receptor tyrosine kinases.Semantic proximity Read ↗

Autophosphorylation Affects Substrate-Binding Affinity of Tobacco Ca2+-Dependent Protein Kinase1.Semantic proximity Read ↗

A tumor suppressor homolog, AtPTEN1, is essential for pollen development in Arabidopsis.Semantic proximity Read ↗

Phosphorylation analysis of plant viral proteins.Semantic proximity Read ↗

Serine/threonine/tyrosine protein kinase from Arabidopsis thaliana is dependent on serine residues for its activity.Semantic proximity Read ↗

Arabidopsis serine/threonine/tyrosine protein kinase phosphorylates oil body proteins that regulate oil content in the seeds.Semantic proximity Read ↗

Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase.Semantic proximity Read ↗

Alteration of substrate specificity: the variable N-terminal domain of tobacco Ca(2+)-dependent protein kinase is important for substrate recognition.Semantic proximity Read ↗

Biochemical properties of two protein kinases involved in disease resistance signaling in tomato.Semantic proximity Read ↗

The major site of the pti1 kinase phosphorylated by the pto kinase is located in the activation domain and is required for pto-pti1 physical interaction.Semantic proximity Read ↗

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