(Q43984163)

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PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity.

scientific article published in May 2002

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10 December 2019

PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity (English)

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11997009%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

Rhodobacter sphaeroides

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Rhodobacter sphaeroides

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inferred from title

Alastair G McEwan

1

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10 December 2019

6

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10 December 2019

Geoffrey Robert Moore

8

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Geoffrey R Moore

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10 December 2019

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Allison Lewin

2

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10 December 2019

Sharon L Davy

3

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10 December 2019

Ruth Boetzel

4

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10 December 2019

Andrew Leech

5

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10 December 2019

Tania Wood

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10 December 2019

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1 May 2002

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10 December 2019

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10 December 2019

518

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10 December 2019

1-3

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10 December 2019

10-16

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The superfamily of heme-copper respiratory oxidases

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Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å

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Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

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The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidase

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Cloning and characterization of senC, a gene involved in both aerobic respiration and photosynthesis gene expression in Rhodobacter capsulatus

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Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: a mutant histidine kinase

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An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae

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Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase

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Redox signaling: globalization of gene expression

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Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes.

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Reassessment of Ellman's reagent

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Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase

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21 January 2018

Copper chaperones: function, structure and copper-binding properties.

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A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae

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21 January 2018

Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae.

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21 January 2018

Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein.

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21 January 2018

Metal ion chaperone function of the soluble Cu(I) receptor Atx1.

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21 January 2018

Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase

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Bridge over troubled waters: sensing stress by disulfide bond formation

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Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity

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Generalized approach to the regulation and integration of gene expression

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The 2.2 Å Crystal Structure of Hsp33

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Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step Mechanism

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21 January 2018

From redox flow to gene regulation: role of the PrrC protein of Rhodobacter sphaeroides 2.4.1.

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7 January 2021

SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae

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7 January 2021

Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase

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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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NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9

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Copper delivery by metallochaperone proteins

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Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase

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Redox switch of hsp33 has a novel zinc-binding motif

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10.1016/S0014-5793(02)02532-2

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11997009%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

PubMed publication ID

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Europe PubMed Central

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10 December 2019

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