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Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum
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Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
title
Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum
(English)
1 reference
stated in
Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
main subject
endoplasmic reticulum
0 references
Heat shock protein 90 beta family member 1
1 reference
stated in
GOA release 2020-03-11
protein transport
1 reference
stated in
GOA release 2020-03-11
author
Béla Z Schmidt
series ordinal
1
1 reference
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Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
author name string
David H Perlmutter
series ordinal
2
1 reference
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Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
language of work or name
English
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publication date
21 April 2005
1 reference
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Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
published in
American Journal of Physiology - Gastrointestinal and Liver Physiology
1 reference
stated in
Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
volume
289
1 reference
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Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
issue
3
1 reference
stated in
Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
page(s)
G444-55
1 reference
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Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
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UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates
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A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency
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Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
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Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state
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The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
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Glucosidase and mannosidase inhibitors mediate increased secretion of mutant alpha1 antitrypsin Z.
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A naturally occurring nonpolymerogenic mutant of alpha 1-antitrypsin characterized by prolonged retention in the endoplasmic reticulum
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Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates
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Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation
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Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways
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1 reference
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inferred from DOI database lookup
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Coordinated activation of Hsp70 chaperones
1 reference
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Crossref
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https://api.crossref.org/works/10.1152%2FAJPGI.00237.2004
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based on heuristic
inferred from DOI database lookup
Alpha1-antitrypsin deficiency. 4: Molecular pathophysiology
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1152%2FAJPGI.00237.2004
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7 January 2021
based on heuristic
inferred from DOI database lookup
Protein glucosylation and its role in protein folding
1 reference
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Crossref
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https://api.crossref.org/works/10.1152%2FAJPGI.00237.2004
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7 January 2021
based on heuristic
inferred from DOI database lookup
Fasting in alpha1-antitrypsin deficient liver: constitutive [correction of consultative] activation of autophagy.
1 reference
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Crossref
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7 January 2021
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Role of ubiquitin in proteasomal degradation of mutant alpha(1)-antitrypsin Z in the endoplasmic reticulum
1 reference
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Crossref
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https://api.crossref.org/works/10.1152%2FAJPGI.00237.2004
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The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1152%2FAJPGI.00237.2004
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7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1152/AJPGI.00237.2004
2 references
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3660878
stated in
Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
OpenCitations bibliographic resource ID
3660878
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3660878
PubMed publication ID
15845869
2 references
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3660878
stated in
Europe PubMed Central
PubMed publication ID
15845869
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15845869%20AND%20SRC:MED&resulttype=core&format=json
retrieved
11 January 2020
ResearchGate publication ID
7891517
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