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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
Autor:
Kelly Tatchell, Tara Williams-Hart, Stephan N. Witt, Cheryl Clark-Dixon, Todd R. Flower, Richard M. Zweig, Lucy C. Robinson, Shaoxiao Wang, Jun Liang
Publikováno v:
Human Molecular Genetics
The mechanism by which the Parkinson's disease-related protein alpha-synuclein (alpha-syn) causes neurodegeneration has not been elucidated. To determine the genes that protect cells from alpha-syn, we used a genetic screen to identify suppressors of
Publikováno v:
Archives of Biochemistry and Biophysics. 444:61-65
ClpB and DnaK form a bi-chaperone system that reactivates strongly aggregated proteins in vivo and in vitro. Previously observed interaction between purified ClpB and DnaK suggested that one of the chaperones might recruit its partner during substrat
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:
Stephan N. Witt, Sergey V. Slepenkov
Publikováno v:
Biochemistry. 37:1015-1024
The mechanism of the ATPase cycle of the 70-kDa Escherichia coli molecular chaperone DnaK was investigated by following ATP-induced changes in the tryptophan fluorescence of DnaK. Three steps in the cycle were investigated. (i) Stopped-flow experimen
Autor:
Stephan N. Witt
How protein chaperones protect cells from neurodegenerative diseases Including contributions from leading experts, Protein Chaperones and Protection from Neurodegenerative Diseases provides an in-depth exploration of how protein chaperones are involv
Autor:
Stephan N. Witt
Publikováno v:
Molecular neurobiology. 47(2)
Parkinson’s disease (PD) is a devastating neurological condition that affects about 1 % of people older than 65 years of age. In PD, dopaminergic neurons in the mid-brain slowly accumulate cytoplasmic inclusions (Lewy bodies, LBs) of the protein al
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