A M Roseman
Overview
Explore the profile of A M Roseman 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
15
Citations
951
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
11.
White H, Chen S, Roseman A, Yifrach O, Horovitz A, Saibil H
Nat Struct Biol
. 1997 Sep;
4(9):690-4.
PMID: 9302993
No abstract available.
12.
Lee G, Roseman A, Saibil H, Vierling E
EMBO J
. 1997 Feb;
16(3):659-71.
PMID: 9034347
The small heat shock proteins (sHSPs) recently have been reported to have molecular chaperone activity in vitro; however, the mechanism of this activity is poorly defined. We found that HSP18.1,...
13.
Roseman A, Chen S, White H, Braig K, Saibil H
Cell
. 1996 Oct;
87(2):241-51.
PMID: 8861908
Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two back-to-back seven-membered rings of GroEL...
14.
Chen S, Roseman A, Hunter A, Wood S, Burston S, Ranson N, et al.
Nature
. 1994 Sep;
371(6494):261-4.
PMID: 7915827
Protein folding mediated by the molecular chaperone GroEL occurs by its binding to non-native polypeptide substrates and is driven by ATP hydrolysis. Both of these processes are influenced by the...
15.
Saibil H, Zheng D, Roseman A, Hunter A, Watson G, Chen S, et al.
Curr Biol
. 1993 May;
3(5):265-73.
PMID: 15335746
Background: The chaperonins, a family of molecular chaperones, are large oligomeric proteins that bind nonnative intermediates of protein folding. They couple the release and correct folding of their ligands to...