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Items: 1 to 20 of 115

1.

Cu(I) affinities of the domain 1 and 3 sites in the human metallochaperone for Cu,Zn-superoxide dismutase.

Allen S, Badarau A, Dennison C.

Biochemistry. 2012 Feb 21;51(7):1439-48. doi: 10.1021/bi201370r. Epub 2012 Feb 9.

PMID:
22320662
2.

Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface.

Stasser JP, Eisses JF, Barry AN, Kaplan JH, Blackburn NJ.

Biochemistry. 2005 Mar 8;44(9):3143-52.

PMID:
15736924
3.

A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase.

Stasser JP, Siluvai GS, Barry AN, Blackburn NJ.

Biochemistry. 2007 Oct 23;46(42):11845-56. Epub 2007 Sep 29.

PMID:
17902702
4.

Copper trafficking mechanism of CXXC-containing domains: insight from the pH-dependence of their Cu(I) affinities.

Badarau A, Dennison C.

J Am Chem Soc. 2011 Mar 9;133(9):2983-8. doi: 10.1021/ja1091547. Epub 2011 Feb 16.

PMID:
21323310
5.

Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase.

Torres AS, Petri V, Rae TD, O'Halloran TV.

J Biol Chem. 2001 Oct 19;276(42):38410-6. Epub 2001 Jul 25.

6.

X-ray absorption investigation of a unique protein domain able to bind both copper(I) and copper(II) at adjacent sites of the N-terminus of Haemophilus ducreyi Cu,Zn superoxide dismutase.

D'Angelo P, Pacello F, Mancini G, Proux O, Hazemann JL, Desideri A, Battistoni A.

Biochemistry. 2005 Oct 4;44(39):13144-50.

PMID:
16185082
7.

Metal binding affinities of Arabidopsis zinc and copper transporters: selectivities match the relative, but not the absolute, affinities of their amino-terminal domains.

Zimmermann M, Clarke O, Gulbis JM, Keizer DW, Jarvis RS, Cobbett CS, Hinds MG, Xiao Z, Wedd AG.

Biochemistry. 2009 Dec 15;48(49):11640-54. doi: 10.1021/bi901573b.

PMID:
19883117
8.

Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase.

Schmidt PJ, Rae TD, Pufahl RA, Hamma T, Strain J, O'Halloran TV, Culotta VC.

J Biol Chem. 1999 Aug 20;274(34):23719-25.

9.

Copper and zinc binding properties of the N-terminal histidine-rich sequence of Haemophilus ducreyi Cu,Zn superoxide dismutase.

Paksi Z, Jancs├│ A, Pacello F, Nagy N, Battistoni A, Gajda T.

J Inorg Biochem. 2008 Sep;102(9):1700-10. doi: 10.1016/j.jinorgbio.2008.04.007. Epub 2008 May 6.

PMID:
18565588
10.

Binding of copper(I) by the Wilson disease protein and its copper chaperone.

Wernimont AK, Yatsunyk LA, Rosenzweig AC.

J Biol Chem. 2004 Mar 26;279(13):12269-76. Epub 2004 Jan 6.

11.

Cu(I) binding and transfer by the N terminus of the Wilson disease protein.

Yatsunyk LA, Rosenzweig AC.

J Biol Chem. 2007 Mar 23;282(12):8622-31. Epub 2007 Jan 17.

12.

A histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning.

Battistoni A, Pacello F, Mazzetti AP, Capo C, Kroll JS, Langford PR, Sansone A, Donnarumma G, Valenti P, Rotilio G.

J Biol Chem. 2001 Aug 10;276(32):30315-25. Epub 2001 May 21.

13.

Metallochaperone for Cu,Zn-superoxide dismutase (CCS) protein but not mRNA is higher in organs from copper-deficient mice and rats.

Prohaska JR, Broderius M, Brokate B.

Arch Biochem Biophys. 2003 Sep 15;417(2):227-34.

PMID:
12941305
14.

Mechanism of Cu,Zn-superoxide dismutase activation by the human metallochaperone hCCS.

Rae TD, Torres AS, Pufahl RA, O'Halloran TV.

J Biol Chem. 2001 Feb 16;276(7):5166-76. Epub 2000 Oct 3.

15.

The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1.

Walker JM, Huster D, Ralle M, Morgan CT, Blackburn NJ, Lutsenko S.

J Biol Chem. 2004 Apr 9;279(15):15376-84. Epub 2004 Jan 30.

17.

Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.

Wernimont AK, Huffman DL, Lamb AL, O'Halloran TV, Rosenzweig AC.

Nat Struct Biol. 2000 Sep;7(9):766-71.

PMID:
10966647
18.

Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase.

Fan B, Rosen BP.

J Biol Chem. 2002 Dec 6;277(49):46987-92. Epub 2002 Sep 25.

19.

Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase.

Barry AN, Clark KM, Otoikhian A, van der Donk WA, Blackburn NJ.

Biochemistry. 2008 Dec 9;47(49):13074-83. doi: 10.1021/bi801438g.

20.

A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1.

Schmidt PJ, Ramos-Gomez M, Culotta VC.

J Biol Chem. 1999 Dec 24;274(52):36952-6.

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