منابع مشابه
Eukaryotic Chaperonins: Lubricating the Folding of WD-repeat Proteins
For most proteins of the eukaryotic cytosol, the folding pathways are still largely a mystery, even though many cytosolic chaperones have been identified, including multiple members of the heat shock protein (Hsp) 70 family, Hsp90 and the chaperonin, CCT/TRiC. Particularly puzzling has been the role of CCT, a distant cousin of the prokaryotic chaperonin GroEL, found in eukaryotes and archea. Gr...
متن کاملEukaryotic Chaperonins: Lubricating the Folding of WD-repeat Proteins Dispatch
For most proteins of the eukaryotic cytosol, the folding pathways are still largely a mystery, even though many cytosolic chaperones have been identified, including multiple members of the heat shock protein (Hsp) 70 family, Hsp90 and the chaperonin, CCT/TRiC. Particularly puzzling has been the role of CCT, a distant cousin of the prokaryotic chaperonin GroEL, found in eukaryotes and archea. Gr...
متن کاملEditorial: Signaling through WD-Repeat Proteins in Plants
Plants are sessile organisms that rely on appropriate signal-transduction responses in order to cope with the challenges imposed by their environment, and must be able to recognize potential damage or benefit to respond accordingly. These response mechanisms are mediated by specific sets of signal receptors, effector proteins interacting through scaffolding assemblies, second messengers, and tr...
متن کاملGemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins.
The survival of motor neurons (SMN) protein is the product of the disease gene of spinal muscular atrophy and is found both in the cytoplasm and the nucleus, where it is concentrated in gems. SMN is part of a multi-protein complex that includes Gemin2, Gemin3, and Gemin4. The SMN complex plays an important role in the cytoplasmic assembly of small nuclear ribonucleoproteins (snRNPs) and likely ...
متن کاملA novel WD repeat protein component of the methylosome binds Sm proteins.
We have recently described a large (20 S) protein arginine methyltransferase complex, termed the methylosome, that contains the methyltransferase JBP1 (PRMT5) and the pICln protein. The methylosome functions to modify specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins, and this modification targets these proteins to the survival...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2004
ISSN: 0108-7673
DOI: 10.1107/s0108767304097363