The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation. (Q34141552)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11179901%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

review article

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title

The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11179901%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

main subject

endoplasmic reticulum

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4

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4 November 2019

author name string

E Chevet

1

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4 November 2019

P H Cameron

2

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4 November 2019

M F Pelletier

3

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4 November 2019

J J Bergeron

5

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4 November 2019

publication date

1 February 2001

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Current Opinion in Structural Biology

4 November 2019

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11179901%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

volume

11

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4 November 2019

issue

1

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4 November 2019

page(s)

120-124

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Expression of a gene for cyclophilin which contains an amino-terminal endoplasmic reticulum-targeting signal

4 November 2019

cites work

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7 January 2021

Protein folding in a specialized compartment: the endoplasmic reticulum

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7 January 2021

Role and regulation of the ER chaperone BiP.

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7 January 2021

The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications

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7 January 2021

The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin

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7 January 2021

Calnexin family members as modulators of genetic diseases

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7 January 2021

Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum

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7 January 2021

Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

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7 January 2021

Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation

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7 January 2021

Structure and folding of nascent polypeptide chains during protein translocation in the endoplasmic reticulum

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7 January 2021

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

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7 January 2021

Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.

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7 January 2021

The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct

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7 January 2021

Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

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7 January 2021

Setting the standards: quality control in the secretory pathway

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7 January 2021

The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase.

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7 January 2021

Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways

1 reference

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7 January 2021

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome

1 reference

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7 January 2021

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

1 reference

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7 January 2021

Cloning of mammalian Ire1 reveals diversity in the ER stress responses

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7 January 2021

Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1

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7 January 2021

A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response

1 reference

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7 January 2021

Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress

1 reference

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7 January 2021

Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans

1 reference

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7 January 2021

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

1 reference

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7 January 2021

Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress

1 reference

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7 January 2021

Perk is essential for translational regulation and cell survival during the unfolded protein response

1 reference

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7 January 2021

A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B.

1 reference

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7 January 2021

Activation of transcription factor NF-kappaB by the adenovirus E3/19K protein requires its ER retention

1 reference

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7 January 2021

Activation of NF-kappa B by ER stress requires both Ca2+ and reactive oxygen intermediates as messengers

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2800%2900168-8

7 January 2021

Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome

1 reference

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7 January 2021

Retrograde protein translocation: ERADication of secretory proteins in health and disease

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7 January 2021

Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

1 reference

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7 January 2021

Role of Cue1p in Ubiquitination and Degradation at the ER Surface

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7 January 2021

Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes.

1 reference

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7 January 2021

Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin

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7 January 2021

Glucosidase and mannosidase inhibitors mediate increased secretion of mutant alpha1 antitrypsin Z.

1 reference

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7 January 2021

Oligosaccharide trimming plays a role in the endoplasmic reticulum-associated degradation of tyrosinase

1 reference

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7 January 2021

The Chaperone Protein BiP Binds to a Mutant Prion Protein and Mediates Its Degradation by the Proteasome

1 reference

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7 January 2021

Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2800%2900168-8

7 January 2021

The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control

1 reference

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7 January 2021

Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway

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7 January 2021

A regulatory link between ER-associated protein degradation and the unfolded-protein response

1 reference

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7 January 2021

10.1016/S0959-440X(00)00168-8

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11179901%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

1 reference