Unfolded protein response-induced BiP/Kar2p production protects cell growth against accumulation of misfolded protein aggregates in the yeast endoplasmic reticulum. (Q52537062)

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scientific article published in October 1999

Language	Label	Description	Also known as
English	Unfolded protein response-induced BiP/Kar2p production protects cell growth against accumulation of misfolded protein aggregates in the yeast endoplasmic reticulum.	scientific article published in October 1999

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

Unfolded protein response-induced BiP/Kar2p production protects cell growth against accumulation of misfolded protein aggregates in the yeast endoplasmic reticulum. (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

endoplasmic reticulum

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based on heuristic

inferred from title

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author name string

Umebayashi K

1

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

Hirata A

2

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

Horiuchi H

3

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

Ohta A

4

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

Takagi M

5

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

publication date

1 October 1999

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

European Journal of Cell Biology

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Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

78

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Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

10

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Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

726-738

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.

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SEC11 is required for signal peptide processing and yeast cell growth

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Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

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7 January 2021

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A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

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The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane

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A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors

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SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum

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The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

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Degradation of Rhizopus niveus aspartic proteinase-I with mutated prosequences occurs in the endoplasmic reticulum of Saccharomyces cerevisiae.

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

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Cer1p, a novel Hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeast

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Active Site Mutations in Yeast Protein Disulfide Isomerase Cause Dithiothreitol Sensitivity and a Reduced Rate of Protein Folding in the Endoplasmic Reticulum

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Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus

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In vivo reactivation of heat-denatured protein in the endoplasmic reticulum of yeast

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Endoplasmic Reticulum Stress-induced mRNA Splicing Permits Synthesis of Transcription Factor Hac1p/Ern4p That Activates the Unfolded Protein Response

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The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum

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Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast

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Inducible Membranes in Yeast: Relation to the Unfolded-Protein-Response Pathway

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A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus

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Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway

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IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae

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Saccharomyces cerevisiae IRE2/HAC1 is involved in IRE1-mediated KAR2 expression

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Proliferation of intracellular membrane structures upon homologous overproduction of cytochrome P-450 in Candida maltosa

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Endoplasmicreticulum-induced signal transduction and gene expression

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The FKB2 gene of Saccharomyces cerevisiae, encoding the immunosuppressant-binding protein FKBP-13, is regulated in response to accumulation of unfolded proteins in the endoplasmic reticulum

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Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum

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The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates

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A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s

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Getting started with yeast

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tRNA ligase is required for regulated mRNA splicing in the unfolded protein response

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Identifiers

10.1016/S0171-9335(99)80041-7

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 May 2018

http://europepmc.org/abstract/MED/10569245

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