Donghong Ju

Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and -independent.

Homeostatic regulation of the proteasome via an Rpn4-dependent feedback circuit.

Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.

Roles of tyrosine phosphorylation and cleavage of protein kinase Cdelta in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis.

A synthetic defect in protein degradation caused by loss of Ufd4 and Rad23.

Identification of the preferential ubiquitination site and ubiquitin-dependent degradation signal of Rpn4.

The armadillo repeats of the Ufd4 ubiquitin ligase recognize ubiquitin-fusion proteins.

Diminished feedback regulation of proteasome expression and resistance to proteasome inhibitors in breast cancer cells.

Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal.

Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.

Disruption of Rpn4-induced proteasome expression in Saccharomyces cerevisiae reduces cell viability under stressed conditions.

Dyclonine and alverine citrate enhance the cytotoxic effects of proteasome inhibitor MG132 on breast cancer cells.

Disruption of actin cytoskeleton mediates loss of tensile stress induced early phenotypic modulation of vascular smooth muscle cells in organ culture.

The transcription activation domain of Rpn4 is separate from its degrons.

Proteasomal degradation of Rpn4 in Saccharomyces cerevisiae is critical for cell viability under stressed conditions.

Disruption of SM22 promotes inflammation after artery injury via nuclear factor kappaB activation.

Inhibition of proteasomal degradation of rpn4 impairs nonhomologous end-joining repair of DNA double-strand breaks.

Resveratrol induces p53 and suppresses myocardin-mediated vascular smooth muscle cell differentiation.

Arterial injury promotes medial chondrogenesis in Sm22 knockout mice.

The CCAAT box-binding transcription factor NF-Y regulates basal expression of human proteasome genes.

The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits.

Challenging paradigms: long non-coding RNAs in breast ductal carcinoma in situ (DCIS).

Nuclear import factor Srp1 and its associated protein Sts1 couple ribosome-bound nascent polypeptides to proteasomes for cotranslational degradation.

Dyclonine enhances the cytotoxic effect of proteasome inhibitor bortezomib in multiple myeloma cells.

Rapidly Translated Polypeptides Are Preferred Substrates for Cotranslational Protein Degradation.