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Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors.
scientific article
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scholarly article
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
title
Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors
(English)
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
author
Tamim M Nazif
series ordinal
1
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
author name string
Bogyo M
series ordinal
2
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
language of work or name
English
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publication date
1 March 2001
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Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
number of pages
6
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Proceedings of the National Academy of Sciences of the United States of America
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Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
volume
98
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
issue
6
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
page(s)
2967-2972
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
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ImageQuant
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Europe PubMed Central
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11 June 2022
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/PMC30590/fullTextXML
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inferred from PubMed Central ID database lookup
cites work
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Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes
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The proteasome
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Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants
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Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes
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Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
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Bovine spleen multicatalytic proteinase complex (proteasome). Replacement of X, Y, and Z subunits by LMP7, LMP2, and MECL1 and changes in properties and specificity
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Structure and functions of the 20S and 26S proteasomes
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Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
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Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
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Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex
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Peptide libraries: determination of relative reaction rates of protected amino acids in competitive couplings
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Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex
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Evidence that the nature of amino acid residues in the P3 position directs substrates to distinct catalytic sites of the pituitary multicatalytic proteinase complex (proteasome).
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Towards subunit-specific proteasome inhibitors: synthesis and evaluation of peptide alpha',beta'-epoxyketones.
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A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome.
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MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
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Identifiers
DOI
10.1073/PNAS.061028898
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
ADS bibcode
2001PNAS...98.2967N
0 references
PMC publication ID
30590
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
PubMed publication ID
11248015
1 reference
stated in
Europe PubMed Central
PMC publication ID
30590
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248015%20AND%20SRC:MED&resulttype=core&format=json
retrieved
5 November 2019
ResearchGate publication ID
12084394
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