Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Sergey V. Slepenkov"'
Autor:
Nirjhar M. Aloy, Michael W. Graner, Christina Coughlan, Sergey V. Slepenkov, Sahar Shekoohi, Stephan N. Witt
Publikováno v:
Cancer Research. 82:1575-1575
The purpose of this study is to understand the role of α-synuclein in the regulation of the trafficking and release of modulators of metastasis in melanoma. Metastasis causes melanoma-induced death and 5-year survival rates, subsequent to metastasis
Autor:
Sergey V. Slepenkov, William F. Marzluff, Marcin Ziemniak, Wei Su, Edward Darzynkiewicz, Robert E. Rhoads, Shawn M. Lyons, Jacek Jemielity, Joanna Kowalska, Michael K. Slevin
Publikováno v:
RNA. 19:1-16
Metazoan replication-dependent histone mRNAs are only present in S-phase, due partly to changes in their stability. These mRNAs end in a unique stem–loop (SL) that is required for both translation and cell-cycle regulation. Previous studies showed
Autor:
Robert E. Rhoads, David J. McGee, Carolyn Conant, Sergey V. Slepenkov, James G. Traylor, Traci L. Testerman, Viktoriya Ekshyyan, Olga Senkovich, Jun Yin, Patrick Adegboyega
Publikováno v:
Infection and Immunity. 79:3106-3116
Helicobacter pylori persistently colonizes humans, causing gastritis, ulcers, and gastric cancer. Adherence to the gastric epithelium has been shown to enhance inflammation, yet only a few H. pylori adhesins have been paired with targets in host tiss
Publikováno v:
Journal of Biological Chemistry. 281:14927-14938
Recruitment of eukaryotic mRNA to the 48 S initiation complex is rate-limiting for protein synthesis under normal conditions. Binding of the 5' -terminal cap structure of mRNA to eIF4E is a critical event during this process. Mammalian eIF4E is phosp
Publikováno v:
FEBS Letters. 565:65-69
Recent reports have indicated that insect antimicrobial peptides kill bacteria by inhibiting the molecular chaperone DnaK. It was proposed that the antimicrobial peptide, all-l-pyrrhocoricin (l-PYR), binds to two sites on DnaK, the conventional subst
Publikováno v:
Biochemistry. 42:5867-5876
The C-terminal domain of the molecular chaperone DnaK is a compact lid-like structure made up of five alpha-helices (alphaA-alphaE) (residues 508-608) that is followed by a 30-residue disordered, flexible region (609-638). The lid encapsulates the pe
Autor:
Sergey V. Slepenkov, Stephan N. Witt
Publikováno v:
Biochemistry. 41:12224-12235
DnaK, the Escherichia coli Hsp70, possesses two functional domains, the N- and C-terminal ATPase and peptide-binding domains, respectively. Elucidation of the mechanism of allosteric coupling between the two domains is key to understanding how Hsp70
Autor:
Sergey V. Slepenkov, Stephan N. Witt
Publikováno v:
Molecular Microbiology. 45:1197-1206
Summary We discuss recent experiments that have illuminated individual steps in the reaction cycle of the Escherichia coli Hsp70 molecular chaperone DnaK. Using this new information, we comparetwo distinctly different global mechanisms of action –
Publikováno v:
Journal of Biological Chemistry. 276:27231-27236
The C-terminal, polypeptide binding domain of the 70-kDa molecular chaperone DnaK is composed of a unique lidlike subdomain that appears to hinder steric access to the peptide binding site. We have expressed, purified, and characterized a lidless for
Autor:
Stephan N. Witt, Sergey V. Slepenkov
Publikováno v:
Journal of Fluorescence. 9:281-293
This article reviews the recent progress in unraveling the kinetic mechanism of the 70-kDa molecular chaperones by the use of fluorescence spectroscopic methods. Dissecting the kinetics of the individual steps in the 70-kDa chaperone reaction cycle i