Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly (Q27931608)

Proteasome core particle subunit beta 4 YER012W

GOA release 2020-03-11

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The role of pro regions in protein folding.

GOA release 2020-03-11

author name string

P Chen

series ordinal

1

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M Hochstrasser

series ordinal

2

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language of work or name

English

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publication date

20 September 1996

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1 December 2016

86

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page(s)

961-72

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issue

6

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cites work

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

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Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor

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The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo

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Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin

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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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New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites

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Ubiquitin, proteasomes, and the regulation of intracellular protein degradation

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The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo

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The DOA pathway: studies on the functions and mechanisms of ubiquitin-dependent protein degradation in the yeast Saccharomyces cerevisiae

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Evidence indicating that the human proteasome is a complex dimer

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The human proteasome subunit HsN3 is located in the inner rings of the complex dimer.

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

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Proteasomes: protein degradation machines of the cell

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Proteasome from Thermoplasma acidophilum: a threonine protease

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In vivo assembly of the proteasomal complexes, implications for antigen processing

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Critical elements in proteasome assembly

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