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SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
17441508
retrieved
1 December 2016
title
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
17441508
retrieved
1 December 2016
main subject
cell biology
0 references
Saccharomyces cerevisiae
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molecular chaperones
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Mdy2p YOL111C
1 reference
stated in
GOA release 2020-03-11
Type I HSP40 co-chaperone YDJ1 YNL064C
1 reference
stated in
GOA release 2020-03-11
Sgt2p YOR007C
1 reference
stated in
GOA release 2020-03-11
author name string
Shen-Ting Liou
series ordinal
1
0 references
Ming-Yuan Cheng
series ordinal
2
0 references
Chung Wang
series ordinal
3
0 references
language of work or name
English
0 references
publication date
2007
0 references
published in
Cell Stress & Chaperones
1 reference
stated in
PubMed
PubMed ID
17441508
retrieved
1 December 2016
volume
12
0 references
page(s)
59-70
0 references
issue
1
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exact match
https://scigraph.springernature.com/pub.10.1379/csc-220r.1
0 references
cites work
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Mdy2, a ubiquitin-like (UBL)-domain protein, is required for efficient mating in Saccharomyces cerevisiae
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Cns1 is an activator of the Ssa1 ATPase activity
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Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae
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Sti1 Is a Novel Activator of the Ssa Proteins
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Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
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20 March 2017
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
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A comprehensive two-hybrid analysis to explore the yeast protein interactome
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The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
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20 March 2017
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
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20 March 2017
Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing
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PubMed Central
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Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
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PubMed Central
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20 March 2017
The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation
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PubMed Central
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20 March 2017
Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo
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PubMed Central
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20 March 2017
Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae
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MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import
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PubMed Central
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20 March 2017
YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1852894
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Regulation of Hsp70 function by a eukaryotic DnaJ homolog
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Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
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Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
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Molecular chaperones in the cytosol: from nascent chain to folded protein
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Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats
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Isolation and characterization of human SGT and identification of homologues in Saccharomyces cerevisiae and Caenorhabditis elegans
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PubMed Central
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20 March 2017
Tetratrico peptide repeat interactions: to TPR or not to TPR?
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PubMed Central
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20 March 2017
Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions
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PubMed Central
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20 March 2017
TPR proteins: the versatile helix
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PubMed Central
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7 April 2017
The Hsp70 and Hsp60 chaperone machines
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7 April 2017
Pathways of chaperone-mediated protein folding in the cytosol
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PubMed Central
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7 April 2017
Characterization of the G alpha(s) regulator cysteine string protein
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PubMed Central
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29 September 2017
Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity
1 reference
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PubMed Central
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Hsp104 interacts with Hsp90 cochaperones in respiring yeast
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29 September 2017
Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins
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PubMed Central
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29 September 2017
A trimeric protein complex functions as a synaptic chaperone machine.
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29 September 2017
Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
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PubMed Central
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29 September 2017
The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
1 reference
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PubMed Central
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2 June 2018
Experimental evolution of mating discrimination in budding yeast.
1 reference
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PubMed Central
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27 November 2018
Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/17441508
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/17441508
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Functional specificity among Hsp70 molecular chaperones
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/17441508
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1379/CSC-220R.1
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
336024
Dimensions Publication ID
1002440724
0 references
OpenCitations bibliographic resource ID
336024
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
336024
PMCID
1852894
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
336024
PubMed ID
17441508
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
336024
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