(Q28303702)

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Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome

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scholarly article

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Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome (English)

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ubiquitin-proteasome system

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author name string

Y A Lam

1

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W Xu

2

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G N DeMartino

3

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R E Cohen

4

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language of work or name

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publication date

20 February 1997

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385

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737-40

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6618

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The ubiquitin-proteasome proteolytic pathway

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Ubiquitin, proteasomes, and the regulation of intracellular protein degradation

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Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates

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A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

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

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Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant

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Differential effects of ubiquitin aldehyde on ubiquitin and ATP-dependent protein degradation

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Proteolysis. The proteasome: a protein-degrading organelle?

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Structure and functions of the 20S and 26S proteasomes

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Proteasome: from structure to function

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Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes

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The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene

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Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues

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Inhibition of papain by nitriles: mechanistic studies using NMR and kinetic measurements

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Peptide aldehydes and nitriles as transition state analog inhibitors of cysteine proteases

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Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis

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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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Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting

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Degradation of monoubiquitinated alpha-globin by 26S proteasomes

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