The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing (Q27939678)

Proteasome core particle subunit beta 1 YJL001W

GOA release 2020-03-11

1 reference

Proteasome core particle subunit beta 2 YOR157C

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

W Heinemeyer

1

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M Fischer

2

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T Krimmer

3

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U Stachon

4

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D H Wolf

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

3 October 1997

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published in

1 reference

1 December 2016

272

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issue

40

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page(s)

25200-9

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cites work

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Proteolysis: The proteasome: a protein-degrading organelle?

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Proteasomes: protein degradation machines of the cell

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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

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Peptide antigen production by the proteasome: complexity provides efficiency

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The multicatalytic proteinase complex, a major extralysosomal proteolytic system

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PRE3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity.

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Proteasome from Thermoplasma acidophilum: a threonine protease

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A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

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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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Subunit arrangement in the human 20S proteasome

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A homolog of the proteasome-related RING10 gene is essential for yeast cell growth

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Mutations in PRG1, a yeast proteasome-related gene, cause defects in nuclear division and are suppressed by deletion of a mitotic cyclin gene

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Identifiers

DOI

10.1074/JBC.272.40.25200

1 reference

Consolidated OpenCitations Corpus – April 2017

93682

93682

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference