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pro vyhledávání: '"Stephan N Witt"'
Autor:
Stephan N. Witt
Publikováno v:
Biopolymers. 93:218-228
Because over expression of Hsp70 molecular chaperones suppresses the toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, and various polyQ-diseases (Huntington's dise
Autor:
Stephan N. Witt
Publikováno v:
Protein & Peptide Letters. 16:631-634
This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 A from the emerging nascent chain has an effective concentration of 1 x 10(-1) M, which is 4-5 orders of magnitude larger than the con
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:
Stephan N. Witt
Publikováno v:
Current proteinpeptide science. 10(5)
In a Nature article published in 1993, Anthony L. Fink and colleagues reported how Hsp70 chaperones use ATP binding in the presence of K+, rather than hydrolysis, to accelerate substrate release. As of the summer of 2008, his article had received 297
Autor:
Sergey V, Slepenkov, Stephan N, Witt
Publikováno v:
Molecular microbiology. 45(5)
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 compare two distinctly different global mechanisms of action--holding ve
Publikováno v:
Biochemistry. 41(26)
In this study, the effect of pH on the conformation and the reactivity of the Escherichia coli Hsp70 molecular chaperone DnaK was investigated using spectroscopic and chemical assays. DnaK exhibits negligible binding of the hydrophobic dye 1-anilino-