Rayees U. H. Mattoo

发表

Optical control of protein activity by fluorescent protein domains

Smriti Priya, S. Doglia, A. Natalello, 2013 .

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins

P. Goloubinoff, Rayees U. H. Mattoo, 2014, Cellular and Molecular Life Sciences.

Synthesis, characterization and anti-bacterial activity of 5-(alkenyl)-2-amino- and 2-(alkenyl)-5-phenyl-1,3,4-oxadiazoles

Rayees U. H. Mattoo, A. Rauf, M. R. Banday, 2010 .

Synthesis, Characterization and Antimicrobial Activity of Long-Chain Hydrazones

Rayees U. H. Mattoo, A. Rauf, M. R. Banday, 2008 .

Mediator structure and conformation change.

D. Bushnell, R. Kornberg, Dong-Hua Chen, 2021, Molecular cell.

Stable α-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones*

H. Lashuel, G. Dietler, P. Goloubinoff, 2010, The Journal of Biological Chemistry.

Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates*

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2013, The Journal of Biological Chemistry.

Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2010, Cell Stress and Chaperones.

Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins

P. Goloubinoff, Rayees U. H. Mattoo, 2014 .

GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP

P. De Los Rios, A. Azem, Andrija Finka, 2013, Proceedings of the National Academy of Sciences.

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes.

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2016, Annual review of biochemistry.

A recombinant chimeric protein of protective antigen and lethal factor from Bacillus anthracis in polymeric nanocapsules showed a strong immune response in mice: a potential high efficacy vaccine against anthrax.

Z. Aziziaram, Rayees U. H. Mattoo, 2022, Cellular and molecular biology.

Aggregates with Hsp 70 to Solubilize Protein Polypeptides and Reciprocally Collaborate ATP to Unfold Stable Misfolded Chaperone Using Bona Fide Hsp 110 Is a Protein Structure and Folding :

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2013 .

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins

P. Goloubinoff, Rayees U. H. Mattoo, 2014, Cellular and Molecular Life Sciences.

Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2014, Front. Mol. Biosci..

Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates.

S. Doglia, A. Natalello, P. Goloubinoff, 2013, Journal of molecular biology.

Stable -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with

P. Goloubinoff, M. Hinault, Rayees U. H. Mattoo, 2010 .