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Mechanism of CuA assembly
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title
Mechanism of CuA assembly
(English)
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main subject
cell biology
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author
Lucia Banci
series ordinal
2
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Simone Ciofi-Baffoni
series ordinal
4
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Ivano Bertini
series ordinal
3
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Shenlin Wang
object named as
Shenlin Wang
series ordinal
8
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Georgios A. Spyroulias
series ordinal
6
object named as
Georgios A Spyroulias
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author name string
Luciano A Abriata
series ordinal
1
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Petros Gkazonis
series ordinal
5
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Alejandro J Vila
series ordinal
7
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publication date
October 2008
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published in
Nature Chemical Biology
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volume
4
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issue
10
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page(s)
599-601
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cites work
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Human Sco1 and Sco2 function as copper-binding proteins
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27 November 2018
Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase
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27 November 2018
Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p
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27 November 2018
Identification of a disulfide switch in BsSco, a member of the Sco family of cytochrome c oxidase assembly proteins
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27 November 2018
PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity.
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Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/18758441
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Cytochrome c oxidase
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18758441
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The CuACenter of a Soluble Domain fromThermusCytochromeba3. An NMR Investigation of the Paramagnetic Protein
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reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1038/NCHEMBIO.110
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Dimensions Publication ID
1047312266
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PMC publication ID
2596924
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PubMed publication ID
18758441
0 references
ResearchGate publication ID
23224772
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