Uma Kota

Works (4)

Updated: July 5th, 2023 15:54

2011 review

Advances in qualitative and quantitative plant membrane proteomics

[Review of ]. PHYTOCHEMISTRY, 72(10), 1040–1060.

By: U. Kota n & M. Goshe n

author keywords: Membrane proteomics; Liquid chromatography; Mass spectrometry; Quantitation; Quantification; Stable isotope-coded; Label-free
MeSH headings : Cell Membrane / chemistry; Cell Membrane / metabolism; Organelles / chemistry; Organelles / metabolism; Plant Proteins / analysis; Plant Proteins / metabolism; Protein Processing, Post-Translational; Proteomics
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2009 journal article

Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 106(2), 658–663.

By: M. Oh *, X. Wang n, U. Kota n, M. Goshe n, S. Clouse n & S. Huber *

MeSH headings : Arabidopsis; Arabidopsis Proteins / genetics; Arabidopsis Proteins / metabolism; Mutation; Phosphorylation; Plant Leaves; Protein Kinases / genetics; Protein Kinases / metabolism; Protein Serine-Threonine Kinases / metabolism; Signal Transduction; Tyrosine / metabolism
TL;DR: It is reported that recombinant cytoplasmic domains of BRI1 and BAK1 also autophosphorylate on tyrosine residues and thus are dual-specificity kinases, suggesting that tyosine signaling should be considered with other plant receptor kinases as well. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
2. Zero Hunger (Web of Science)
13. Climate Action (Web of Science)
Source: Web Of Science
Added: August 6, 2018

2008 journal article

Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling

DEVELOPMENTAL CELL, 15(2), 220–235.

By: X. Wang n, U. Kota n, K. He *, K. Blackburn  n, J. Li *, M. Goshe n, S. Huber*, S. Clouse n

MeSH headings : Amino Acid Sequence; Arabidopsis / drug effects; Arabidopsis / enzymology; Arabidopsis Proteins / chemistry; Arabidopsis Proteins / metabolism; Brassinosteroids; Cholestanols / metabolism; Cholestanols / pharmacology; Chromatography, Liquid; Flagellin / metabolism; Mass Spectrometry; Models, Biological; Molecular Sequence Data; Mutation / genetics; Phosphorylation / drug effects; Protein Kinases / chemistry; Protein Kinases / metabolism; Protein Serine-Threonine Kinases / chemistry; Protein Serine-Threonine Kinases / metabolism; Protein Structure, Tertiary; Signal Transduction / drug effects; Steroids, Heterocyclic / metabolism; Steroids, Heterocyclic / pharmacology; Substrate Specificity / drug effects
TL;DR: A sequential transphosphorylation model in which BRI1 controls signaling specificity by direct BR binding followed by substrate phosphorylation is proposed, which suggests both conservation and distinct differences between the molecular mechanisms regulating phosphorylated-dependent kinase activation in plant and animal receptor kinases. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
2. Zero Hunger (Web of Science)
13. Climate Action (Web of Science)
Source: Web Of Science
Added: August 6, 2018

2007 journal article

Characterization of a new family of protein kinases from Arabidopsis containing phosphoinositide 3/4-kinase and ubiquitin-like domains

BIOCHEMICAL JOURNAL, 409, 117–127.

By: R. Galvao n, U. Kota n, E. Soderblom n, M. Goshe n & W. Boss n

author keywords: phosphoinositide kinase (PIK); phosphorylation; proteasome regulatory particle non-ATPase 10 subunit (proteasome RPN10 subunit); protein kinase; ubiquitin fusion degradation (UFD); ubiquitin-like domain (UBL domain)
MeSH headings : Adaptor Proteins, Signal Transducing / chemistry; Arabidopsis / metabolism; Arabidopsis Proteins / chemistry; Arabidopsis Proteins / metabolism; Catalysis; Class Ia Phosphatidylinositol 3-Kinase; Cloning, Molecular; DNA, Complementary / metabolism; Genetic Vectors; Humans; Phosphatidylinositol 3-Kinases / chemistry; Phosphatidylinositol 3-Kinases / metabolism; Phosphorylation; Phylogeny; Protein Kinases / chemistry; Protein Kinases / classification; Protein Structure, Tertiary; Recombinant Proteins / chemistry; Ubiquitin / chemistry; Ubiquitin / metabolism
TL;DR: In vitro analysis of AtPI4Kgamma4 indicates that it interacts directly with, and phosphorylates, two proteins involved in the ubiquitin-proteasome system, namely UFD1 (ubiquitin fusion degradation 1) and RPN10 (regulatory particle non-ATPase 10). (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2025) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.