Department of Surgery
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Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and -independent.
The Journal of biological chemistry Jun, 2004 | Pubmed ID: 15090546
Homeostatic regulation of the proteasome via an Rpn4-dependent feedback circuit.
Biochemical and biophysical research communications Aug, 2004 | Pubmed ID: 15358214
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
The Journal of biological chemistry Dec, 2004 | Pubmed ID: 15504724
Roles of tyrosine phosphorylation and cleavage of protein kinase Cdelta in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis.
The Journal of biological chemistry Jun, 2005 | Pubmed ID: 15774464
A synthetic defect in protein degradation caused by loss of Ufd4 and Rad23.
Biochemical and biophysical research communications Mar, 2006 | Pubmed ID: 16430867
Identification of the preferential ubiquitination site and ubiquitin-dependent degradation signal of Rpn4.
The Journal of biological chemistry Apr, 2006 | Pubmed ID: 16492666
The armadillo repeats of the Ufd4 ubiquitin ligase recognize ubiquitin-fusion proteins.
FEBS letters Jan, 2007 | Pubmed ID: 17204268
Diminished feedback regulation of proteasome expression and resistance to proteasome inhibitors in breast cancer cells.
Breast cancer research and treatment Jan, 2008 | Pubmed ID: 17431761
Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal.
Biochimica et biophysica acta Nov, 2007 | Pubmed ID: 17532487
Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.
Molecular and cellular biology Feb, 2008 | Pubmed ID: 18070918
Disruption of Rpn4-induced proteasome expression in Saccharomyces cerevisiae reduces cell viability under stressed conditions.
Genetics Dec, 2008 | Pubmed ID: 18832351
Dyclonine and alverine citrate enhance the cytotoxic effects of proteasome inhibitor MG132 on breast cancer cells.
International journal of molecular medicine Feb, 2009 | Pubmed ID: 19148544
Disruption of actin cytoskeleton mediates loss of tensile stress induced early phenotypic modulation of vascular smooth muscle cells in organ culture.
Experimental and molecular pathology Feb, 2010 | Pubmed ID: 19874818
The transcription activation domain of Rpn4 is separate from its degrons.
The international journal of biochemistry & cell biology Feb, 2010 | Pubmed ID: 19914394
Proteasomal degradation of Rpn4 in Saccharomyces cerevisiae is critical for cell viability under stressed conditions.
Genetics Feb, 2010 | Pubmed ID: 19933873
Disruption of SM22 promotes inflammation after artery injury via nuclear factor kappaB activation.
Circulation research Apr, 2010 | Pubmed ID: 20224039
Inhibition of proteasomal degradation of rpn4 impairs nonhomologous end-joining repair of DNA double-strand breaks.
PloS one , 2010 | Pubmed ID: 20376190
Resveratrol induces p53 and suppresses myocardin-mediated vascular smooth muscle cell differentiation.
Toxicology letters Nov, 2010 | Pubmed ID: 20797428
Arterial injury promotes medial chondrogenesis in Sm22 knockout mice.
Cardiovascular research Apr, 2011 | Pubmed ID: 21183509
The CCAAT box-binding transcription factor NF-Y regulates basal expression of human proteasome genes.
Biochimica et biophysica acta Apr, 2012 | Pubmed ID: 22285817
The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits.
Biochemical and biophysical research communications Mar, 2012 | Pubmed ID: 22349505
Challenging paradigms: long non-coding RNAs in breast ductal carcinoma in situ (DCIS).
Frontiers in genetics , 2013 | Pubmed ID: 23577021
Nuclear import factor Srp1 and its associated protein Sts1 couple ribosome-bound nascent polypeptides to proteasomes for cotranslational degradation.
The Journal of biological chemistry Jan, 2014 | Pubmed ID: 24338021
Dyclonine enhances the cytotoxic effect of proteasome inhibitor bortezomib in multiple myeloma cells.
Molecular medicine reports Nov, 2014 | Pubmed ID: 25174315
Rapidly Translated Polypeptides Are Preferred Substrates for Cotranslational Protein Degradation.
The Journal of biological chemistry Apr, 2016 | Pubmed ID: 26961882
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