Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown (Q73075592)

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1 November 2019

title

Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown (English)

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1 November 2019

author name string

A F Kisselev

1

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1 November 2019

T N Akopian

2

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1 November 2019

V Castillo

3

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1 November 2019

A L Goldberg

4

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1 November 2019

publication date

1 September 1999

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1 November 2019

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1 November 2019

volume

4

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1 November 2019

issue

3

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1 November 2019

page(s)

395-402

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Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum

1 November 2019

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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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A 3,4-dichloroisocoumarin-resistant component of the multicatalytic proteinase complex

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Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly

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Structure and functions of the 20S and 26S proteasomes

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Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation

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Degradation of oxidized insulin B chain by the multiproteinase complex macropain (proteasome)

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Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants

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Peptidylglutamyl-peptide hydrolase activity of the multicatalytic proteinase complex: evidence for a new high-affinity site, analysis of cooperative kinetics, and the effect of manganese ions

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Structure of 20S proteasome from yeast at 2.4 A resolution

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The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing

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Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes

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The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation

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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-gamma

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Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae

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Kinetic studies of the branched chain amino acid preferring peptidase activity of the 20S proteasome: development of a continuous assay and inhibition by tripeptide aldehydes and clasto-lactacystin beta-lactone

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Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1.

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Regulation of the peptidylglutamyl-peptide hydrolyzing activity of the pituitary multicatalytic proteinase complex

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7 January 2021

Degradation of cell proteins and the generation of MHC class I-presented peptides

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7 January 2021

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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A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10518220%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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