Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.

Oncogene | Sep 6, 2001

http://www.ncbi.nlm.nih.gov/pubmed/11571652

The ubiquitin pathway is involved in the proteolytic turnover of many short-lived cellular regulatory proteins. Since selective degradation of substrates of this system requires the covalent attachment of a polyubiquitin chain to the substrates, degradation could be counteracted by de-ubiquitinating enzymes (or isopeptidases) which selectively remove the polyubiquitin chain. Unp is a human isopeptidase with still poorly understood biological functions. Here, we show that cellular Unp specifically interacts with the retinoblastoma gene product (pRb).

Pubmed ID: 11571652 RIS Download

Mesh terms: Amino Acid Motifs | Antibodies | Cell Cycle | Cell Line | Humans | Jurkat Cells | Oncogene Proteins | Retinoblastoma Protein | Tumor Cells, Cultured | Ubiquitin Thiolesterase | Ubiquitins

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NCI NIH HHS, Id: 5RO1-CA81755
  • Agency: NCI NIH HHS, Id: P30-CA16087
  • Agency: NCI NIH HHS, Id: R01-CA76584
  • Agency: NIGMS NIH HHS, Id: R01-GM57587
  • Agency: NCI NIH HHS, Id: R21-CA66229

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.