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Structure of 20S proteasome from yeast at 2.4 A resolution
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1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
title
Structure of 20S proteasome from yeast at 2.4 A resolution
(English)
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
main subject
Proteasome core particle subunit beta 5 YPR103W
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit alpha 6 YMR314W
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit beta 1 YJL001W
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit alpha 4 YOL038W
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit alpha 7 YOR362C
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit beta 3 YER094C
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit beta 4 YER012W
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit alpha 3 YGR135W
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit beta 6 YBL041W
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit beta 2 YOR157C
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit beta 7 YFR050C
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit alpha 2 YML092C
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit alpha 1 YGL011C
1 reference
stated in
GOA release 2020-03-11
Proteasome core particle subunit alpha 5 YGR253C
1 reference
stated in
GOA release 2020-03-11
author
Matthias Bochtler
series ordinal
5
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
author name string
Groll M
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Ditzel L
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Löwe J
series ordinal
3
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Stock D
series ordinal
4
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Bartunik HD
series ordinal
6
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Huber R
series ordinal
7
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
language of work or name
English
0 references
publication date
1 April 1997
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
published in
Nature
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
volume
386
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
issue
6624
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
page(s)
463-471
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
cites work
Molecular cloning and functional analysis of three subunits of yeast proteasome
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Proteasomes: protein degradation machines of the cell
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New insights into proteasome function: from archaebacteria to drug development
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Proteolysis: The proteasome: a protein-degrading organelle?
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Go outside and see the proteasome. Protein degradation
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7 January 2021
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Structure and functions of the 20S and 26S proteasomes
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7 January 2021
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Proteasome: from structure to function
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7 January 2021
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Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography
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7 January 2021
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Peptide antigen production by the proteasome: complexity provides efficiency
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Crossref
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7 January 2021
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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
1 reference
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Crossref
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7 January 2021
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Proteasome from Thermoplasma acidophilum: a threonine protease
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7 January 2021
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A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
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7 January 2021
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PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core
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Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20S proteasomes. Cleavage of proteins and antigenic peptides
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Existence of a molecular ruler in proteasomes suggested by analysis of degradation products
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Incorporation of major histocompatibility complex – encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon‐γ
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20 S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins takes place in 13-16 S preproteasome complexes
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Genes encoded in the major histocompatibility complex affecting the generation of peptides for TAP transport
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Autocatalytic processing of the 20S proteasome
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Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
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Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
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MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
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MHC class I expression in mice lacking the proteasome subunit LMP-7
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Altered peptidase and viral-specific T cell response in LMP2 mutant mice.
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Penicillin acylase has a single-amino-acid catalytic centre
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Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
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7 January 2021
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Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis
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Degradation of oxidized insulin B chain by the multiproteinase complex macropain (proteasome)
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The proteasome subunit, C2, contains an important site for binding of the PA28 (11S) activator
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7 January 2021
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PA28 activator protein forms regulatory caps on proteasome stacked rings
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Antigen processing and presentation by the class I major histocompatibility complex
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The proteolytic fragments generated by vertebrate proteasomes: structural relationships to major histocompatibility complex class I binding peptides
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Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
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LMP2 proteasomes are required for the presentation of specific antigens to cytotoxic T lymphocytes.
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Structure of peptides associated with MHC class I molecules.
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20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences
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The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
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The CCP4 suite: programs for protein crystallography
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AMoRe: an automated package for molecular replacement
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A graphics model building and refinement system for macromolecules
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Accurate bond and angle parameters for X-ray protein structure refinement
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Crossref
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7 January 2021
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inferred from DOI database lookup
Identifiers
DOI
10.1038/386463A0
2 references
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
762113
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Dimensions Publication ID
1040521478
0 references
OpenCitations bibliographic resource ID
762113
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
762113
PubMed publication ID
9087403
2 references
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
762113
stated in
Europe PubMed Central
PubMed publication ID
9087403
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9087403 AND SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
ResearchGate publication ID
14129164
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