(Q27930979)

1 December 2016

title

The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation (English)

1 reference

Proteasome regulatory particle base subunit RPN2 YIL075C

PubMed

PubMed publication ID

1 December 2016

1 reference

GOA release 2020-03-11

1 reference

Proteasome core particle subunit beta 7 YFR050C

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

António J Marques

1

0 references

Christoph Glanemann

2

0 references

Paula C Ramos

3

0 references

R Jürgen Dohmen

Journal of Biological Chemistry

4

0 references

language of work or name

English

0 references

publication date

30 November 2007

0 references

published in

1 reference

PubMed

PubMed publication ID

17911101

The proteasome: paradigm of a self-compartmentalizing protease

1 December 2016

volume

282

0 references

issue

48

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page(s)

34869-76

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cites work

1 reference

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A proteasome for all occasions

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Structure of 20S proteasome from yeast at 2.4 A resolution

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The structure of the mammalian 20S proteasome at 2.75 A resolution

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Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation

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

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A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

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Proteasomes: machines for all reasons

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PA200, a nuclear proteasome activator involved in DNA repair

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The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle

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Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes.

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Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly

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beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint

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20S proteasome biogenesis

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

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Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly.

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Role of C-terminal extensions of subunits beta2 and beta7 in assembly and activity of eukaryotic proteasomes.

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Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme

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Essential problems in quantification of proteins following colloidal staining with coomassie brilliant blue dyes in polyacrylamide gels, and their solution.

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20 S proteasomes are imported as precursor complexes into the nucleus of yeast

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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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Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast

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Biting the hand that feeds: Rpn4-dependent feedback regulation of proteasome function

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RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit

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Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome

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Widespread aneuploidy revealed by DNA microarray expression profiling.

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Multiple associated proteins regulate proteasome structure and function

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Structural basis for the activation of 20S proteasomes by 11S regulators

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Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits

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Proteasome assembly triggers a switch required for active-site maturation.

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Rearrangement of the 16S precursor subunits is essential for the formation of the active 20S proteasome

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Nucleotide excision repair and the ubiquitin proteasome pathway--do all roads lead to Rome?

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Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes

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20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals.

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