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

P Rudrabhatla, R Rajasekharan - Biochemistry, 2004 - ACS Publications
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 …

Mutational analysis of stress-responsive peanut dual specificity protein kinase: identification of tyrosine residues involved in regulation of protein kinase activity

P Rudrabhatla, R Rajasekharan - Journal of biological chemistry, 2003 - ASBMB
We recently reported thatArachis hypogaea serine/threonine/tyrosine (STY) protein kinase is
developmentally regulated and is induced by abiotic stresses (Rudrabhatla, P., and …

Developmentally regulated dual-specificity kinase from peanut that is induced by abiotic stresses

P Rudrabhatla, R Rajasekharan - Plant physiology, 2002 - academic.oup.com
Tyrosine (Tyr) phosphorylation represents an important biochemical mechanism to regulate
many cellular processes. No Tyr kinase has been cloned so far in plants. Dual-specificity …

Serine/threonine/tyrosine protein kinase from Arabidopsis thaliana is dependent on serine residues for its activity

MM Reddy, R Rajasekharan - Archives of biochemistry and biophysics, 2007 - Elsevier
Genome-wide analysis of Arabidopsis thaliana with tyrosine kinase motif from animals
predicted that tyrosine phosphorylation could be brought about only by dual-specificity …

Isolation and Characterization of GmSTY1, a Novel Gene Encoding a Dual‐Specificity Protein Kinase in Soybean (Glycine max L.)

ZS Xu, YZ Ma, XG Cheng, LX Cao… - Journal of Integrative …, 2006 - Wiley Online Library
Phosphorylation of protein kinases has profound effects on their activity and interaction with
other proteins. Tyrosine phosphorylation was reported to be involved in various …

Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine.

N Ali, U Halfter, NH Chua - Journal of Biological Chemistry, 1994 - ASBMB
Phosphorylation of proteins on serine, threonine, or tyrosine residues represents an
important biochemical mechanism to regulate the activity of enzymes and is used in many …

Genome-wide analysis and experimentation of plant serine/threonine/tyrosine-specific protein kinases

P Rudrabhatla, MM Reddy, R Rajasekharan - Plant molecular biology, 2006 - Springer
Protein tyrosine phosphorylation plays an important role in cell growth, development and
oncogenesis. No classical protein tyrosine kinase has hitherto been cloned from plants …

[PDF][PDF] Characterization of dual specificity protein kinase from maize seedlings.

J Trojanek, M Klimecka, A Fraser… - Acta Biochimica …, 2004 - bibliotekanauki.pl
A protein kinase of 57 kDa, able to phosphorylate tyrosine in synthetic substrates pol (Glu4,
Tyr1) and a fragment of Src tyrosine kinase, was isolated and partly purified from maize …

Role of threonine residues in the regulation of manganese-dependent Arabidopsis serine/threonine/tyrosine protein kinase activity

MM Reddy, R Rajasekharan - Archives of biochemistry and biophysics, 2006 - Elsevier
Tyrosine phosphorylation in plants could be performed only by dual-specificity kinases.
Arabidopsis thaliana dual-specificity protein kinase (AtSTYPK) exhibited strong preference …

Role of protein tyrosine phosphatases in plants

A Shankar, N Agrawal, M Sharma, A Pandey… - Current …, 2015 - ingentaconnect.com
Reversible protein phosphorylation is a crucial regulatory mechanism that controls many
biological processes in eukaryotes. In plants, phosphorylation events primarily occur on …