New insights into proteasome function: from archaebacteria to drug development (Q28255512)

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scientific article published on August 1, 1995

Language	Label	Description	Also known as
English	New insights into proteasome function: from archaebacteria to drug development	scientific article published on August 1, 1995

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scholarly article

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1 reference

Europe PubMed Central

New insights into proteasome function: from archaebacteria to drug development (English)

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author name string

A. L. Goldberg

1

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9383453

26 November 2024

R. Stein

2

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9383453

26 November 2024

J. Adams

3

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9383453

26 November 2024

language of work or name

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publication date

August 1995

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full work available at URL

https://doi.org/10.1016/1074-5521(95)90182-5

online access status

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9383453

26 November 2024

https://api.elsevier.com/content/article/PII:1074552195901825?httpAccept=text/xml

1 reference

10.1016/1074-5521(95)90182-5

https://api.crossref.org/works/10.1016/1074-5521(95)90182-5

26 November 2024

https://api.elsevier.com/content/article/PII:1074552195901825?httpAccept=text/plain

1 reference

10.1016/1074-5521(95)90182-5

https://api.crossref.org/works/10.1016/1074-5521(95)90182-5

26 November 2024

Chemistry and Biology

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2

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8

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503-8

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The ubiquitin-proteasome proteolytic pathway

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10.1016/1074-5521(95)90182-5

https://api.crossref.org/works/10.1016/1074-5521(95)90182-5

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Functions of the proteasome: the lysis at the end of the tunnel

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10.1016/1074-5521(95)90182-5

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Proteasomes: protein degradation machines of the cell

3

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10.1016/1074-5521(95)90182-5

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The mechanism and functions of ATP-dependent proteases in bacterial and animal cells

4

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Proteasomes: multicatalytic proteinase complexes

5

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Proteasomes: protein and gene structures

6

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Proteolysis: The proteasome: a protein-degrading organelle?

8

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Critical elements in proteasome assembly

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Conformational constraints in protein degradation by the 20S proteasome

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

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PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core

19

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Existence of a molecular ruler in proteasomes suggested by analysis of degradation products

20

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Proteasome from Thermoplasma acidophilum: a threonine protease

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Penicillin acylase has a single-amino-acid catalytic centre

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

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A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B

24

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p34Cdc28-mediated control of Cln3 cyclin degradation

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Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy

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Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation

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Proteolysis, proteasomes and antigen presentation

29

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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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Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes

31

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MHC-linked LMP gene products specifically alter peptidase activities of the proteasome

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Interferon-gamma induces different subunit organizations and functional diversity of proteasomes

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Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins

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TAP1-dependent peptide translocation in vitro is ATP dependent and peptide selective

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MHC class I expression in mice lacking the proteasome subunit LMP-7

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Altered peptidase and viral-specific T cell response in LMP2 mutant mice.

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The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B

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A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B

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Function and activation of NF-kappa B in the immune system

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NF-kappa B: a lesson in family values

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Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway

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The proteasome pathway is required for cytokine-induced endothelial-leukocyte adhesion molecule expression

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