Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase.
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Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †Structural biology of copper traffickingInteractions of Cu(I) with selenium-containing amino acids determined by NMR, XAS, and DFT studies.Stable Cu(II) and Cu(I) mononuclear intermediates in the assembly of the CuA center of Thermus thermophilus cytochrome oxidase.Trapping intermediates in metal transfer reactions of the CusCBAF export pump of
P2860
Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on December 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Selenocysteine positional vari ...... rone for superoxide dismutase.
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Selenocysteine positional vari ...... rone for superoxide dismutase.
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type
label
Selenocysteine positional vari ...... rone for superoxide dismutase.
@en
Selenocysteine positional vari ...... rone for superoxide dismutase.
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prefLabel
Selenocysteine positional vari ...... rone for superoxide dismutase.
@en
Selenocysteine positional vari ...... rone for superoxide dismutase.
@nl
P2093
P2860
P356
P1433
P1476
Selenocysteine positional vari ...... erone for superoxide dismutase
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P2093
Adenike Otoikhian
Kevin M Clark
Ninian J Blackburn
P2860
P304
13074-13083
P356
10.1021/BI801438G
P407
P577
2008-12-01T00:00:00Z