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The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress
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scholarly article
1 reference
stated in
PubMed
PubMed ID
18946088
retrieved
1 December 2016
title
The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress
(English)
1 reference
stated in
PubMed
PubMed ID
18946088
retrieved
1 December 2016
main subject
cell biology
0 references
molecular chaperones
0 references
Nma111p YNL123W
1 reference
stated in
GOA release 2020-03-11
author
Achim Dickmanns
series ordinal
3
0 references
Jörg B. Schulz
series ordinal
5
object named as
Jörg B Schulz
0 references
author name string
Nirmala Padmanabhan
series ordinal
1
0 references
Lars Fichtner
series ordinal
2
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Ralf Ficner
series ordinal
4
0 references
Gerhard H Braus
series ordinal
6
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language of work or name
English
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publication date
January 2009
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published in
Molecular Biology of the Cell
1 reference
stated in
PubMed
PubMed ID
18946088
retrieved
1 December 2016
volume
20
0 references
page(s)
68-77
0 references
issue
1
0 references
cites work
The inhibitor-of-apoptosis protein Bir1p protects against apoptosis in S. cerevisiae and is a substrate for the yeast homologue of Omi/HtrA2.
1 reference
stated in
PubMed Central
reference URL
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20 March 2017
Direct interaction of Saccharomyces cerevisiae Faa1p with the Omi/HtrA protease orthologue Ynm3p alters lipid homeostasis
1 reference
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reference URL
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The FK506 binding protein Fpr3 counteracts protein phosphatase 1 to maintain meiotic recombination checkpoint activity
1 reference
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reference URL
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20 March 2017
The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis
1 reference
stated in
PubMed Central
reference URL
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Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi
1 reference
stated in
PubMed Central
reference URL
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retrieved
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Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
1 reference
stated in
PubMed Central
reference URL
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HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins
1 reference
stated in
PubMed Central
reference URL
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The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif
1 reference
stated in
PubMed Central
reference URL
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A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
1 reference
stated in
PubMed Central
reference URL
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Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia
1 reference
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PubMed Central
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Yeast tom1 mutant exhibits pleiotropic defects in nuclear division, maintenance of nuclear structure and nucleocytoplasmic transport at high temperatures
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Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism
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Transformation of intact yeast cells treated with alkali cations
1 reference
stated in
PubMed Central
reference URL
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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
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PubMed Central
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1 reference
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A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
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Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression
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Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
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The HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cells
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Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
1 reference
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PubMed Central
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1 reference
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Role of the PDZ domains in Escherichia coli DegP protein
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1 reference
stated in
PubMed Central
reference URL
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Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
1 reference
stated in
PubMed Central
reference URL
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The HtrA family of serine proteases
1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613113
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29 September 2017
Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
1 reference
stated in
PubMed Central
reference URL
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The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase
1 reference
stated in
PubMed Central
reference URL
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1 reference
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PubMed Central
reference URL
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27 November 2018
A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613113
retrieved
27 November 2018
SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613113
retrieved
27 November 2018
Analysis of chaperone function using citrate synthase as nonnative substrate protein
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18946088
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
MEROPS: the peptidase database
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18946088
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1091/MBC.E08-02-0178
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1391069
OpenCitations bibliographic resource ID
1391069
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1391069
PMCID
2613113
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1391069
PubMed ID
18946088
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1391069
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