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CCS gene
Known as:
CCS
, COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE
National Institutes of Health
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Related topics
Related topics
1 relation
Calcarine sulcus
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2019
Highly Cited
2019
Osa‐miR398b boosts H2O2 production and rice blast disease‐resistance via multiple superoxide dismutases
Yan Li
,
Xiao-Long Cao
,
+17 authors
Wenming Wang
The New phytologist
2019
Corpus ID: 58591234
Summary miRNAs contribute to plant resistance against pathogens. Previously, we found that the function of miR398b in immunity in…
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Highly Cited
2018
Highly Cited
2018
In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation.
E. Luchinat
,
L. Banci
Accounts of chemical research
2018
Corpus ID: 46930201
Cellular structural biology methods are needed to characterize biological processes at atomic resolution in the physiological…
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Highly Cited
2010
Highly Cited
2010
Regulation of the Copper Chaperone CCS by XIAP-Mediated Ubiquitination
Graham F. Brady
,
S. Galbán
,
+5 authors
C. Duckett
Molecular and Cellular Biology
2010
Corpus ID: 35001746
ABSTRACT In order to balance the cellular requirements for copper with its toxic properties, an elegant set of mechanisms has…
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2008
2008
Variable response of selected cuproproteins in rat choroid plexus and cerebellum following perinatal copper deficiency
A. A. Gybina
,
J. Prohaska
Genes & Nutrition
2008
Corpus ID: 25019031
Recent immunohistochemical characterization of the copper transport protein, Ctr1, reported enriched levels in mouse choroid…
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2008
2008
Present situation of biomarkers for copper status.
M. Olivares
,
M. Méndez
,
P. Astudillo
,
F. Pizarro
The American journal of clinical nutrition
2008
Corpus ID: 4480587
Serum or plasma copper and ceruloplasmin concentrations are the most widely used laboratory indicators to evaluate copper status…
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Highly Cited
2006
Highly Cited
2006
Mechanisms of the Copper-dependent Turnover of the Copper Chaperone for Superoxide Dismutase*
Amy Caruano-Yzermans
,
T. Bartnikas
,
J. Gitlin
Journal of Biological Chemistry
2006
Corpus ID: 22401638
The copper chaperone for superoxide dismutase (CCS) is an intracellular metallochaperone required for incorporation of copper…
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Highly Cited
2001
Highly Cited
2001
Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
A. Lamb
,
A. S. Torres
,
T. O’Halloran
,
A. Rosenzweig
Nature Structural Biology
2001
Corpus ID: 31920386
The copper chaperone for superoxide dismutase (CCS) activates the eukaryotic antioxidant enzyme copper, zinc superoxide dismutase…
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2001
2001
Copper Stabilizes a Heterodimer of the yCCS Metallochaperone and Its Target Superoxide Dismutase*
A. S. Torres
,
V. Petri
,
T. Rae
,
T. O’Halloran
The Journal of Biological Chemistry
2001
Corpus ID: 8750460
The copper chaperone for superoxide dismutase (CCS) activates the antioxidant enzyme Cu,Zn-SOD (SOD1) by directly inserting the…
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Highly Cited
2000
Highly Cited
2000
Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase.
P. Wong
,
D. Waggoner
,
+6 authors
J. Gitlin
Proceedings of the National Academy of Sciences…
2000
Corpus ID: 25282366
Recent studies in Saccharomyces cerevisiae suggest that the delivery of copper to Cu/Zn superoxide dismutase (SOD1) is mediated…
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Highly Cited
2000
Highly Cited
2000
Heterodimer formation between superoxide dismutase and its copper chaperone.
A. Lamb
,
A. S. Torres
,
T. O’Halloran
,
A. Rosenzweig
Biochemistry
2000
Corpus ID: 18691031
Copper, zinc superoxide dismutase (SOD1) is activated in vivo by the copper chaperone for superoxide dismutase (CCS). The…
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