Rayees U H Mattoo
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Explore the profile of Rayees U H Mattoo including associated specialties, affiliations and a list of published articles.
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10
Citations
402
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Recent Articles
1.
Aziziaram Z, Mattoo R
Cell Mol Biol (Noisy-le-grand)
. 2022 Aug;
68(3):1-8.
PMID: 35988177
Anthrax is a serious infectious disease caused by Bacillus anthracis, rod-shaped gram-positive bacteria. The disease infects both humans and animals and causes severe illness. Many vaccines have been developed for...
2.
Zhang H, Chen D, Mattoo R, Bushnell D, Wang Y, Yuan C, et al.
Mol Cell
. 2021 Feb;
81(8):1781-1788.e4.
PMID: 33571424
Mediator is a universal adaptor for transcription control. It serves as an interface between gene-specific activator or repressor proteins and the general RNA polymerase II (pol II) transcription machinery. Previous...
3.
Finka A, Mattoo R, Goloubinoff P
Annu Rev Biochem
. 2016 Apr;
85:715-42.
PMID: 27050154
Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989, groundbreaking experiments demonstrated that a purified chaperone can bind and prevent...
4.
Mattoo R, Farina Henriquez Cuendet A, Subanna S, Finka A, Priya S, Sharma S, et al.
Front Mol Biosci
. 2015 May;
1:7.
PMID: 25988148
The role of bacterial Hsp40, DnaJ, is to co-chaperone the binding of misfolded or alternatively folded proteins to bacterial Hsp70, DnaK, which is an ATP-fuelled unfolding chaperone. In addition to...
5.
Mattoo R, Goloubinoff P
Cell Mol Life Sci
. 2014 Apr;
71(17):3311-25.
PMID: 24760129
By virtue of their general ability to bind (hold) translocating or unfolding polypeptides otherwise doomed to aggregate, molecular chaperones are commonly dubbed "holdases". Yet, chaperones also carry physiological functions that...
6.
Mattoo R, Sharma S, Priya S, Finka A, Goloubinoff P
J Biol Chem
. 2013 Jun;
288(29):21399-21411.
PMID: 23737532
Structurally and sequence-wise, the Hsp110s belong to a subfamily of the Hsp70 chaperones. Like the classical Hsp70s, members of the Hsp110 subfamily can bind misfolding polypeptides and hydrolyze ATP. However,...
7.
Priya S, Kumar Sharma S, Sood V, Mattoo R, Finka A, Azem A, et al.
Proc Natl Acad Sci U S A
. 2013 Apr;
110(18):7199-204.
PMID: 23584019
Chaperonins are cage-like complexes in which nonnative polypeptides prone to aggregation are thought to reach their native state optimally. However, they also may use ATP to unfold stably bound misfolded...
8.
Natalello A, Mattoo R, Priya S, Sharma S, Goloubinoff P, Doglia S
J Mol Biol
. 2013 Jan;
425(7):1158-71.
PMID: 23306033
Misfolded polypeptide monomers may be regarded as the initial species of many protein aggregation pathways, which could accordingly serve as primary targets for molecular chaperones. It is therefore of paramount...
9.
Hinault M, Farina Henriquez Cuendet A, Mattoo R, Mensi M, Dietler G, Lashuel H, et al.
J Biol Chem
. 2010 Sep;
285(49):38173-82.
PMID: 20847048
α-Synuclein aggregation and accumulation in Lewy bodies are implicated in progressive loss of dopaminergic neurons in Parkinson disease and related disorders. In neurons, the Hsp70s and their Hsp40-like J-domain co-chaperones...
10.
Finka A, Mattoo R, Goloubinoff P
Cell Stress Chaperones
. 2010 Aug;
16(1):15-31.
PMID: 20694844
Molecular chaperones are central to cellular protein homeostasis. In mammals, protein misfolding diseases and aging cause inflammation and progressive tissue loss, in correlation with the accumulation of toxic protein aggregates...