Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Susan K. Lyman"'
Autor:
Chatanika Stoop-Myer, Robin Pedersen, Vic E. Myer, Sena Jong, Yuji Mishina, Brent L. Kreider, Susan K. Lyman, Chris Wilson, Jesse J. Smith, Linda Bruett, Lizabeth P. Amaral, Craig M. Thompson
Publikováno v:
SLAS Discovery. 9:196-207
G protein-coupled receptors (GPCRs) are a superfamily of proteins that include some of the most important drug targets in the pharmaceutical industry. Despite the success of this group of drugs, there remains a need to identify GPCR-targeted drugs wi
Publikováno v:
The Journal of Cell Biology
Previous work has shown that the transport of some small protein cargoes through the nuclear pore complex (NPC) can occur in vitro in the absence of nucleoside triphosphate hydrolysis. We now demonstrate that in the importin α/β and transportin imp
Autor:
Larry Gerace, Susan K. Lyman
Publikováno v:
Journal of Cell Biology. 154:17-20
In vivo studies on the dynamics of the nuclear pore complex (NPC) in yeast suggested that NPCs are highly mobile in the nuclear envelope. However, new evidence indicates that in mammalian cells NPCs are stably attached to a flexible lamina framework,
Publikováno v:
RNA. 5:1597-1604
We have identified an apparent human homolog of the yeast Nop5/Nop58 protein. hNop5/Nop58 codes for a protein of predicted molecular weight 59.6 kDa and is 46.8% identical to Saccharomyces cerevisiae Nop5/Nop58. Immunofluorescent staining with antibo
Autor:
Leanne H. Goon, Suzanne C. Crawley, Jana Vaclavikova, Joanne I. Adamkewicz, Garth Joseph Mcgrath, Scott A. Detmer, Robert A. Blake, Jason Y. Chew, Jennifer Choi, Susan K. Lyman, Mary E. Gerritsen, Ruoyu Gong, Charles R. Holst
Publikováno v:
PLoS ONE, Vol 6, Iss 3, p e17692 (2011)
PLoS ONE
PLoS ONE
BackgroundMany proteins that are dysregulated or mutated in cancer cells rely on the molecular chaperone HSP90 for their proper folding and activity, which has led to considerable interest in HSP90 as a cancer drug target. The diverse array of HSP90
Publikováno v:
Proceedings of the National Academy of Sciences. 89:12108-12111
Initiation of DNA replication by phage lambda requires the ordered assembly and disassembly of a specialized nucleoprotein structure at the origin of replication. In the disassembly pathway, a set of Escherichia coli heat shock proteins termed the Hs
Publikováno v:
The Journal of biological chemistry. 278(20)
SR proteins and related RS domain-containing polypeptides are an important class of splicing regulators in higher eukaryotic cells. The RS domain facilitates nuclear import of SR proteins and mediates protein-protein interactions during spliceosome a
Autor:
Randy Schekman, Susan K. Lyman
Publikováno v:
The Journal of Cell Biology
To clarify the roles of Kar2p (BiP) and Sec63p in translocation across the ER membrane in Saccharomyces cerevisiae, we have utilized mutant alleles of the essential genes that encode these proteins: kar2-203 and sec63-1. Sanders et al. (Sanders, S. L
Autor:
Randy Schekman, Susan K. Lyman
Publikováno v:
Cell. (1):85-96
The translocation of a secretory precursor protein across the ER membrane comprises three phases: docking of the precursor at the membrane, insertion into the translocation pore, and exit from the pore into the ER lumen. We demonstrate that Sec62p, S