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CYS1 gene
Known as:
CYS1
, cystin 1
National Institutes of Health
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2012
2012
Intramolecular disulfide bond between catalytic cysteines in an intein precursor.
Wen Chen
,
Lingyun Li
,
+5 authors
Chunyu Wang
Journal of the American Chemical Society
2012
Corpus ID: 20548965
Protein splicing is a self-catalyzed and spontaneous post-translational process in which inteins excise themselves out of…
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2007
2007
Oxidation and Nitrosylation of Cysteines Proximal to the Intermediate Filament (IF)-binding Site of Plectin
R. Spurny
,
Kamaran K. Abdoulrahman
,
+4 authors
G. Wiche
Journal of Biological Chemistry
2007
Corpus ID: 20541428
As an intermediate filament (IF)-based cytolinker protein, plectin plays a key role in the maintenance of cellular…
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2007
2007
Solution structure of an M‐1 conotoxin with a novel disulfide linkage
W. Du
,
Yuhong Han
,
Fei-Juan Huang
,
Juan-Qin Li
,
C. Chi
,
W. Fang
The FEBS Journal
2007
Corpus ID: 25708290
The M‐superfamily of conotoxins has a typical Cys framework (‐CC‐C‐C‐CC‐), and is one of the eight major superfamilies found in…
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2006
2006
Enhanced stability of recombinant keratinocyte growth factor by mutagenesis.
E. Hsu
,
T. Osslund
,
+5 authors
L. Narhi
Protein engineering, design & selection : PEDS
2006
Corpus ID: 24496054
Native sequence keratinocyte growth factor (KGF) is fairly unstable, as manifested by the loss of the monomeric native protein…
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1999
1999
Role of the Cysteine-rich Domain of the t-SNARE Component, SYNDET, in Membrane Binding and Subcellular Localization*
Darshan K. Koticha
,
Stephen J. Huddleston
,
J. Witkin
,
G. Baldini
Journal of Biological Chemistry
1999
Corpus ID: 22845667
Wild-type syndet is efficiently recruited at the plasma membrane in transfected AtT-20 cells. A deletion at the cysteine-rich…
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Highly Cited
1999
Highly Cited
1999
The N-terminal Disulfide Linkages of Human Insulin-like Growth Factor-binding Protein-6 (hIGFBP-6) and hIGFBP-1 Are Different as Determined by Mass Spectrometry*
G. Neumann
,
L. Bach
Journal of Biological Chemistry
1999
Corpus ID: 22037459
The actions of insulin-like growth factors (IGFs) are modulated by a family of six high affinity binding proteins (IGFBPs 1–6…
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Highly Cited
1996
Highly Cited
1996
Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of…
M. Isupov
,
G. Obmolova
,
+5 authors
A. Teplyakov
Structure
1996
Corpus ID: 43068954
1992
1992
Identification of a Saccharomyces cerevisiae homolog of the SNF2 transcrioptional regulator in the DNA sequence of an 8·6 kb region in the LTE1‐CYS1 interval on the left arm of chormosome I
M. W. Clark
,
W. Zhong
,
+4 authors
H. Bussey
Yeast
1992
Corpus ID: 36094872
The DNA sequence of an 8·6 kb region of the left arm of chromosome I has been determined. This region, between the LTEL and CYS1…
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Highly Cited
1989
Highly Cited
1989
A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases.
B. Mei
,
H. Zalkin
Journal of Biological Chemistry
1989
Corpus ID: 25288892
A family of four glutamine amidotransferases has a homologous glutamine amide transfer domain, designated purF-type, that is…
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Highly Cited
1975
Highly Cited
1975
Structure-function relationships and site of action of apamin, a neurotoxic polypeptide of bee venom with an action on the central nervous system.
J. Vincent
,
H. Schweitz
,
M. Lazdunski
Biochemistry
1975
Corpus ID: 23967334
Specific chemical modifications of apamin have been used to study the residues involved in its toxic action. Transformation of…
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