Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

Rayees U H Mattoo

Showing results (1-10 of 11) with videos related to

Pageof 2
Sort By:
Cellular and Molecular Biology (Noisy-Le-Grand, France)|August 21, 2022
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 anthraxZahra Aziziaram, Rayees U H Mattoo
Cellular and Molecular Life Sciences : CMLS|April 25, 2014
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteinsRayees U H Mattoo, Pierre Goloubinoff
Annual Review of Biochemistry|April 7, 2016
Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding EnzymesAndrija Finka, Rayees U H Mattoo, Pierre Goloubinoff
Cell Stress & Chaperones|August 10, 2010
Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cellsAndrija Finka, Rayees U H Mattoo, Pierre Goloubinoff
The Journal of Biological Chemistry|June 6, 2013
Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregatesRayees U H Mattoo, Sandeep K Sharma, Smriti Priya, et al.
Molecular Cell|November 19, 2025
Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase moduleRayees U H Mattoo, Dong-Hua Chen, David A Bushnell, et al.
Journal of Molecular Biology|January 12, 2013
Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substratesAntonino Natalello, Rayees U H Mattoo, Smriti Priya, et al.
Frontiers in Molecular Biosciences|May 20, 2015
Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaKRayees U H Mattoo, America Farina Henriquez Cuendet, Sujatha Subanna, et al.
The Journal of Biological Chemistry|September 18, 2010
Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperonesMarie-Pierre Hinault, America Farina Henriquez Cuendet, Rayees U H Mattoo, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 16, 2013
GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATPSmriti Priya, Sandeep Kumar Sharma, Vishal Sood, et al.
Pageof 2

Showing results (1-10 of 11) with videos related to

Sort By:
Pageof 2
Cellular and Molecular Biology (Noisy-Le-Grand, France)|August 21, 2022
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 anthraxZahra Aziziaram, Rayees U H Mattoo
Cellular and Molecular Life Sciences : CMLS|April 25, 2014
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteinsRayees U H Mattoo, Pierre Goloubinoff
Annual Review of Biochemistry|April 7, 2016
Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding EnzymesAndrija Finka, Rayees U H Mattoo, Pierre Goloubinoff
Cell Stress & Chaperones|August 10, 2010
Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cellsAndrija Finka, Rayees U H Mattoo, Pierre Goloubinoff
The Journal of Biological Chemistry|June 6, 2013
Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregatesRayees U H Mattoo, Sandeep K Sharma, Smriti Priya, et al.
Molecular Cell|November 19, 2025
Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase moduleRayees U H Mattoo, Dong-Hua Chen, David A Bushnell, et al.
Journal of Molecular Biology|January 12, 2013
Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substratesAntonino Natalello, Rayees U H Mattoo, Smriti Priya, et al.
Frontiers in Molecular Biosciences|May 20, 2015
Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaKRayees U H Mattoo, America Farina Henriquez Cuendet, Sujatha Subanna, et al.
The Journal of Biological Chemistry|September 18, 2010
Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperonesMarie-Pierre Hinault, America Farina Henriquez Cuendet, Rayees U H Mattoo, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 16, 2013
GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATPSmriti Priya, Sandeep Kumar Sharma, Vishal Sood, et al.
Pageof 2