The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II). (Q27939921)

From Wikidata

Jump to navigation Jump to search

scientific article

Language	Label	Description	Also known as
English	The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II).	scientific article

Statements

scholarly article

1 reference

PubMed publication ID

1 December 2016

The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II). (English)

1 reference

PubMed publication ID

1 December 2016

Saccharomyces cerevisiae

0 references

molecular chaperones

0 references

Succinate dehydrogenase iron-sulfur protein subunit SDH2 YLL041C

1 reference

GOA release 2020-03-11

Succinate dehydrogenase flavoprotein subunit SDH1 YKL148C

1 reference

GOA release 2020-03-11

Succinate dehydrogenase cytochrome b subunit SDH3 YKL141W

1 reference

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

1 reference

based on heuristic

inferred from title

author name string

E Dibrov

1

0 references

S Fu

2

0 references

B D Lemire

3

0 references

language of work or name

0 references

publication date

27 November 1998

0 references

Journal of Biological Chemistry

1 reference

PubMed publication ID

1 December 2016

273

0 references

48

0 references

32042-8

0 references

The carboxyl terminus of the Saccharomyces cerevisiae succinate dehydrogenase membrane subunit, SDH4p, is necessary for ubiquinone reduction and enzyme stability.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

The Nuclear ABC1 Gene is Essential for the Correct Conformation and Functioning of the Cytochrome bc1 Complex and the Neighbouring Complexes II and IV in the Mitochondrial Respiratory Chain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Nucleo-Mitochondrial Interactions in Mitochondrial Gene Expression

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Crosstalk between nuclear and mitochondrial genomes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

EPR studies on the respiratory chain of wild-type Saccharomyces cerevisiae and mutants with a deficiency in succinate dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

The COQ5 gene encodes a yeast mitochondrial protein necessary for ubiquinone biosynthesis and the assembly of the respiratory chain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Molecular Chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

A simple method for displaying the hydropathic character of a protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Protein import into mitochondria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Flavinylation of succinate: ubiquinone oxidoreductase from Saccharomyces cerevisiae.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Do molecular chaperones have to be proteins?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Role of the Evolutionarily Conserved Cytochrome b Tryptophan 142 in the Ubiquinol Oxidation Catalyzed by the bc1 Complex in the Yeast Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.32042

21 January 2018

Identifiers

10.1074/JBC.273.48.32042

0 references

PubMed publication ID

1 reference

PubMed publication ID

1 December 2016

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q27939921&oldid=1598796979"