A potential proteasome-interacting motif within the ubiquitin-like domain of parkin and other proteins (Q35162573)

6 August 2017

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title

A potential proteasome-interacting motif within the ubiquitin-like domain of parkin and other proteins (English)

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6 August 2017

Sudarshan C Upadhya

1

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PubMed ID

12826399

6 August 2017

Ashok N Hegde

series ordinal

2

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6 August 2017

1 June 2003

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6 August 2017

4

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Trends in Biochemical Sciences

inferred from page(s)

published in

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6 August 2017

28

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6 August 2017

6

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6 August 2017

280-283

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

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Rad23 links DNA repair to the ubiquitin/proteasome pathway

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Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome

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Multiple associated proteins regulate proteasome structure and function

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Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a

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Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis.

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The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome

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The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway

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MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function

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Proteasome subunit Rpn1 binds ubiquitin-like protein domains

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Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

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Transferring substrates to the 26S proteasome.

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New mutation (R42P) of the parkin gene in the ubiquitinlike domain associated with parkinsonism

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Emerging roles of ubiquitin in transcription regulation

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Identifiers

DOI

1 reference

6 August 2017

1 reference

PubMed ID

12826399