- CCS (gene)
Copper chaperone for superoxide dismutase, also known as CCS, is a human
gene .cite web | title = Entrez Gene: CCS copper chaperone for superoxide dismutase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9973| accessdate = ]PBB_Summary
section_title =
summary_text = Copper chaperone for superoxide dismutase specifically delivers Cu to copper/zinc superoxide dismutase and may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.cite web | title = Entrez Gene: CCS copper chaperone for superoxide dismutase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9973| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Culotta VC, Klomp LW, Strain J, "et al." |title=The copper chaperone for superoxide dismutase. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23469–72 |year= 1997 |pmid= 9295278 |doi=
*cite journal | author=Casareno RL, Waggoner D, Gitlin JD |title=The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 23625–8 |year= 1998 |pmid= 9726962 |doi=
*cite journal | author=Rothstein JD, Dykes-Hoberg M, Corson LB, "et al." |title=The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain. |journal=J. Neurochem. |volume=72 |issue= 1 |pages= 422–9 |year= 1999 |pmid= 9886096 |doi=
*cite journal | author=Rae TD, Schmidt PJ, Pufahl RA, "et al." |title=Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. |journal=Science |volume=284 |issue= 5415 |pages= 805–8 |year= 1999 |pmid= 10221913 |doi=
*cite journal | author=Lamb AL, Wernimont AK, Pufahl RA, "et al." |title=Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. |journal=Biochemistry |volume=39 |issue= 7 |pages= 1589–95 |year= 2000 |pmid= 10677207 |doi=
*cite journal | author=Moore SD, Chen MM, Cox DW |title=Cloning and mapping of murine superoxide dismutase copper chaperone (Ccsd) and mapping of the human ortholog. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 1-2 |pages= 35–7 |year= 2000 |pmid= 10773661 |doi=
*cite journal | author=Bartnikas TB, Waggoner DJ, Casareno RL, "et al." |title=Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase. |journal=Mamm. Genome |volume=11 |issue= 5 |pages= 409–11 |year= 2000 |pmid= 10790544 |doi=
*cite journal | author=Rae TD, Torres AS, Pufahl RA, O'Halloran TV |title=Mechanism of Cu,Zn-superoxide dismutase activation by the human metallochaperone hCCS. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 5166–76 |year= 2001 |pmid= 11018045 |doi= 10.1074/jbc.M008005200
*cite journal | author=McLoughlin DM, Standen CL, Lau KF, "et al." |title=The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9303–7 |year= 2001 |pmid= 11115513 |doi= 10.1074/jbc.M010023200
*cite journal | author=Silahtaroglu AN, Brondum-Nielsen K, Gredal O, "et al." |title=Human CCS gene: genomic organization and exclusion as a candidate for amyotrophic lateral sclerosis (ALS). |journal=BMC Genet. |volume=3 |issue= |pages= 5 |year= 2002 |pmid= 11991808 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Bertinato J, L'Abbé MR |title=Copper modulates the degradation of copper chaperone for Cu,Zn superoxide dismutase by the 26 S proteosome. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35071–8 |year= 2003 |pmid= 12832419 |doi= 10.1074/jbc.M302242200
*cite journal | author=Silahtaroglu AN, Jensen LR, Harboe TL, "et al." |title=Sequencing and mapping of the porcine CCS gene. |journal=Anim. Genet. |volume=35 |issue= 4 |pages= 353–4 |year= 2004 |pmid= 15265083 |doi= 10.1111/j.1365-2052.2004.01150.x
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Stasser JP, Eisses JF, Barry AN, "et al." |title=Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface. |journal=Biochemistry |volume=44 |issue= 9 |pages= 3143–52 |year= 2005 |pmid= 15736924 |doi= 10.1021/bi0478392
*cite journal | author=Duquesne AE, Ruijter M, Brouwer J, "et al." |title=Solution structure of the second PDZ domain of the neuronal adaptor X11alpha and its interaction with the C-terminal peptide of the human copper chaperone for superoxide dismutase. |journal=J. Biomol. NMR |volume=32 |issue= 3 |pages= 209–18 |year= 2005 |pmid= 16132821 |doi= 10.1007/s10858-005-7333-1
*cite journal | author=Caruano-Yzermans AL, Bartnikas TB, Gitlin JD |title=Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase. |journal=J. Biol. Chem. |volume=281 |issue= 19 |pages= 13581–7 |year= 2006 |pmid= 16531609 |doi= 10.1074/jbc.M601580200PBB_Controls
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