(Q37104965)

English

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

scientific article published on December 2008

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

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

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

molecular chaperones

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L-selenocysteine

1 reference

based on heuristic

inferred from title

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1

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

Wilfred van der Donk

4

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Europe PubMed Central

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17 January 2020

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Kevin M Clark

2

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17 January 2020

Adenike Otoikhian

3

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

Ninian J Blackburn

5

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Europe PubMed Central

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17 January 2020

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publication date

1 December 2008

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Europe PubMed Central

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17 January 2020

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

47

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

49

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

13074-13083

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

Studies on deprotection of cysteine and selenocysteine side-chain protecting groups

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Activation of superoxide dismutases: putting the metal to the pedal

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Function, structure, and mechanism of intracellular copper trafficking proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-dimer model of LYS7-SOD association and copper delivery

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Crystal structure of the second domain of the human copper chaperone for superoxide dismutase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Crystal structure of the copper chaperone for superoxide dismutase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

The copper chaperone for superoxide dismutase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

27 June 2018

A selenocysteine variant of the human copper chaperone for superoxide dismutase. A Se-XAS probe of cluster composition at the domain 3-domain 3 dimer interface

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

3 September 2018

Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

3 September 2018

Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

3 September 2018

Ligand substitution in cubic clusters: surprising isolation of the cocrystallization products of Cu8(mu8-Se)[S2P(OEt)2]6 and Cu6[S2P(OEt)2]6.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

3 September 2018

Copper-selenium interactions: influence of alkane spacer and halide anion in the synthesis of unusual polynuclear copper(I) complexes with bis(diphenylselenophosphinyl)alkanes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

3 September 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2645929

3 September 2018

Ferrocenyldiselenolate-stabilized copper-selenium clusters

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structure-function analyses of the ATX1 metallochaperone

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Synthesis of a selenocysteine-containing peptide by native chemical ligation

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Domains I and III of the human copper chaperone for superoxide dismutase interact via a cysteine-bridged Dicopper(I) cluster

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Major changes in copper coordination accompany reduction of peptidylglycine monooxygenase: implications for electron transfer and the catalytic mechanism

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Heterodimer formation between superoxide dismutase and its copper chaperone

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

State-of-the-Art Analysis of Whole X-ray Absorption Spectra

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Copper delivery by metallochaperone proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structures of the Cuprous-Thiolate Clusters of the Mac1 and Ace1 Transcriptional Activators

1 reference

https://pubmed.ncbi.nlm.nih.gov/19007184

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI801438G

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19007184%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

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