Umesh K Bageshwar
Overview
Explore the profile of Umesh K Bageshwar including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
14
Citations
211
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Bageshwar U, Dattagupta A, Musser S
PLoS One
. 2021 Sep;
16(9):e0256715.
PMID: 34499687
The twin-arginine translocation (Tat) pathway transports folded proteins across energetic membranes. Numerous Tat substrates contain co-factors that are inserted before transport with the assistance of redox enzyme maturation proteins (REMPs),...
2.
Hamsanathan S, Anthonymuthu T, Bageshwar U, Musser S
Biophys J
. 2017 Dec;
113(12):2650-2668.
PMID: 29262359
The Tat machinery catalyzes the transport of folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane in plants. Using fluorescence quenching and cross-linking approaches, we demonstrate that the...
3.
Bageshwar U, Srivastava M, Pardha-Saradhi P, Paul S, Gothandapani S, Jaat R, et al.
Appl Environ Microbiol
. 2017 May;
83(15).
PMID: 28550063
In our endeavor to improve the nitrogen fixation efficiency of a soil diazotroph that would be unaffected by synthetic nitrogenous fertilizers, we have deleted a part of the negative regulatory...
4.
Bageshwar U, VerPlank L, Baker D, Dong W, Hamsanathan S, Whitaker N, et al.
PLoS One
. 2016 Feb;
11(2):e0149659.
PMID: 26901445
The twin arginine translocation (Tat) pathway transports fully-folded and assembled proteins in bacteria, archaea and plant thylakoids. The Tat pathway contributes to the virulence of numerous bacterial pathogens that cause...
5.
Liang F, Bageshwar U, Musser S
J Biol Chem
. 2012 Feb;
287(16):12703-14.
PMID: 22367204
The bacterial Sec protein translocation system catalyzes the transport of unfolded precursor proteins across the cytoplasmic membrane. Using a recently developed real time fluorescence-based transport assay, the effects of the...
6.
Whitaker N, Bageshwar U, Musser S
J Biol Chem
. 2012 Feb;
287(14):11252-60.
PMID: 22315217
The Escherichia coli twin-arginine translocation (Tat) system transports fully folded and assembled proteins across the inner membrane into the periplasmic space. Traditionally, in vitro protein translocation studies have been performed...
7.
Bageshwar U, Whitaker N, Liang F, Musser S
Mol Microbiol
. 2009 Sep;
74(1):209-226.
PMID: 19732346
Signal peptides target protein cargos for secretion from the bacterial cytoplasm. These signal peptides contain a tri-partite structure consisting of a central hydrophobic domain (h-domain), and two flanking polar domains....
8.
Liang F, Bageshwar U, Musser S
Mol Biol Cell
. 2009 Aug;
20(19):4256-66.
PMID: 19656854
An in vitro real-time single turnover assay for the Escherichia coli Sec transport system was developed based on fluorescence dequenching. This assay corrects for the fluorescence quenching that occurs when...
9.
Bageshwar U, Musser S
J Cell Biol
. 2007 Oct;
179(1):87-99.
PMID: 17908913
The twin-arginine translocation (Tat) pathway in Escherichia coli transports fully folded and assembled proteins across the energy-transducing periplasmic membrane. In chloroplasts, Tat transport requires energy input only from the proton...
10.
Premkumar L, Greenblatt H, Bageshwar U, Savchenko T, Gokhman I, Sussman J, et al.
Proc Natl Acad Sci U S A
. 2005 May;
102(21):7493-8.
PMID: 15894606
Protein molecular adaptation to drastically shifting salinities was studied in dCA II, an alpha-type carbonic anhydrase (EC 4.2.1.1) from the exceptionally salt-tolerant unicellular green alga Dunaliella salina. The salt-inducible, extracellular...