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TST gene
Known as:
RDS
, THIOSULFATE SULFURTRANSFERASE
, RHODANESE
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National Institutes of Health
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Related topics
Related topics
1 relation
Thiosulfate Sulfurtransferase
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2006
Highly Cited
2006
Amino-terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-specific Protease 8 (USP8)*
G. Avvakumov
,
J. Walker
,
+4 authors
S. Dhe-Paganon
Journal of Biological Chemistry
2006
Corpus ID: 166742
Ubiquitin-specific protease 8 (USP8) hydrolyzes mono and polyubiquitylated targets such as epidermal growth factor receptors and…
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Highly Cited
2004
Highly Cited
2004
New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy*
J. Peltier
,
A. Ytterberg
,
Qi Sun
,
K. V. van Wijk
Journal of Biological Chemistry
2004
Corpus ID: 13462186
Identification of membrane proteomes remains challenging. Here, we present a simple, fast, and scalable off-line procedure based…
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Highly Cited
2004
Highly Cited
2004
Stabilization of the E3 Ubiquitin Ligase Nrdp1 by the Deubiquitinating Enzyme USP8
Xiuli Wu
,
L. Yen
,
Lisa Irwin
,
C. Sweeney
,
K. Carraway
Molecular and Cellular Biology
2004
Corpus ID: 6741488
ABSTRACT Nrdp1 is a RING finger-containing E3 ubiquitin ligase that physically interacts with and regulates steady-state cellular…
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Highly Cited
2000
Highly Cited
2000
Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.
J. Hoskins
,
Satyendra K. Singh
,
M. Maurizi
,
S. Wickner
Proceedings of the National Academy of Sciences…
2000
Corpus ID: 16310
ClpA, a bacterial member of the Clp/Hsp100 chaperone family, is an ATP-dependent molecular chaperone and the regulatory component…
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Highly Cited
1998
Highly Cited
1998
The Conserved Carboxyl Terminus and Zinc Finger-like Domain of the Co-chaperone Ydj1 Assist Hsp70 in Protein Folding*
Zhen Lu
,
D. Cyr
Journal of Biological Chemistry
1998
Corpus ID: 23388953
Ydj1 is a member of the Hsp40 (DnaJ-related) chaperone family that facilitates cellular protein folding by regulating Hsp70…
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Highly Cited
1996
Highly Cited
1996
Mechanism of chaperonin action: GroES binding and release can drive GroEL‐mediated protein folding in the absence of ATP hydrolysis.
M. Hayer-Hartl
,
Frank Weber
,
FUIrich Hartil
EMBO Journal
1996
Corpus ID: 38441957
As a basic principle, assisted protein folding by GroEL has been proposed to involve the disruption of misfolded protein…
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Highly Cited
1995
Highly Cited
1995
Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.
Jiu‐li Song
,
Chih-chen Wang
European Journal of Biochemistry
1995
Corpus ID: 7055667
Protein disulfide-isomerase (PDI) in near stoichiometric concentrations promotes reactivation and prevents aggregation of…
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Highly Cited
1995
Highly Cited
1995
Cytosolic Mercaptopyruvate Sulfurtransferase Is Evolutionarily Related to Mitochondrial Rhodanese.
N. Nagahara
,
T. Okazaki
,
T. Nishino
Journal of Biological Chemistry
1995
Corpus ID: 24950258
Rat liver mercaptopyruvate sulfurtransferase (MST) was purified to homogeneity. MST is very similar to rhodanese in…
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Highly Cited
1991
Highly Cited
1991
Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.
J. A. Mendoza
,
E. Rogers
,
G. Lorimer
,
Paul M. Horowitz
Journal of Biological Chemistry
1991
Corpus ID: 9583287
Highly Cited
1988
Highly Cited
1988
Energetics of charge–charge interactions in proteins
M. Gilson
,
B. Honig
Proteins: Structure, Function, and Bioinformatics
1988
Corpus ID: 24066386
Electrostatic interactions between pairs of atoms in proteins are calculated with a model based on the linearized Poisson…
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