David J R Pugh

Summary

Affiliation: University of the Western Cape
Country: South Africa

Publications

  1. pmc DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways
    David J R Pugh
    Biotechnology Department, University of the Western Cape, Modderdam Road, Bellville 7535, South Africa
    BMC Struct Biol 6:1. 2006
  2. pmc Solution structure of RING finger-like domain of retinoblastoma-binding protein-6 (RBBP6) suggests it functions as a U-box
    Mautin A Kappo
    Biotechnology Department, University of the Western Cape, Bellville 7535, South Africa
    J Biol Chem 287:7146-58. 2012
  3. doi request reprint RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1
    Moredreck Chibi
    Biotechnology Department, University of the Western Cape, Bellville, South Africa
    J Mol Biol 384:908-16. 2008

Collaborators

  • Moredreck Chibi
  • Mautin A Kappo
  • D Jasper G Rees
  • Andrew Faro
  • Takalani Mulaudzi
  • Eiso Ab
  • Joanna C Moolman-Smook
  • Victor Muleya
  • John O Poole
  • Jean M McKenzie
  • Faqeer Hassem
  • R Andrew Atkinson
  • Mervin Meyer
  • Johanna C Moolman-Smook
  • Amanda Skepu

Detail Information

Publications3

  1. pmc DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways
    David J R Pugh
    Biotechnology Department, University of the Western Cape, Modderdam Road, Bellville 7535, South Africa
    BMC Struct Biol 6:1. 2006
    ..RBBP6 has recently been shown to be highly up-regulated in oesophageal cancer, and to be a promising target for immunotherapy against the disease...
  2. pmc Solution structure of RING finger-like domain of retinoblastoma-binding protein-6 (RBBP6) suggests it functions as a U-box
    Mautin A Kappo
    Biotechnology Department, University of the Western Cape, Bellville 7535, South Africa
    J Biol Chem 287:7146-58. 2012
    ..Taken together with the structural similarities to U-box-containing proteins, our data suggest that RBBP6 plays a role in chaperone-mediated ubiquitination and possibly in protein quality control...
  3. doi request reprint RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1
    Moredreck Chibi
    Biotechnology Department, University of the Western Cape, Bellville, South Africa
    J Mol Biol 384:908-16. 2008
    ..In the light of the important role that YB-1 appears to play in tumourigenesis, our results suggest that RBBP6 may be a relevant target for therapeutic drugs aimed at modifying the activity of YB-1...