His main research concerns Cell biology, Biochemistry, Ubiquitin, Endoplasmic-reticulum-associated protein degradation and Endoplasmic reticulum. Randolph Y. Hampton combines subjects such as JUNQ and IPOD and Ubiquitin ligase with his study of Cell biology. His study in the field of Reductase, Macrophage and Cell surface receptor also crosses realms of Scavenger receptor binding and Lipid A.
His Reductase study combines topics in areas such as Integral membrane protein and Saccharomyces cerevisiae. As a member of one scientific family, Randolph Y. Hampton mostly works in the field of Endoplasmic-reticulum-associated protein degradation, focusing on Membrane protein and, on occasion, Transmembrane domain, Function, Protein ubiquitination and Ubiquitins. His Endoplasmic reticulum research is multidisciplinary, incorporating perspectives in Nucleocytoplasmic Transport Proteins, Nuclear protein, Nuclear transport, Cell nucleus and Fungal protein.
Randolph Y. Hampton spends much of his time researching Cell biology, Biochemistry, Endoplasmic reticulum, Endoplasmic-reticulum-associated protein degradation and Ubiquitin. His Cell biology study combines topics from a wide range of disciplines, such as Ubiquitin-Protein Ligases and Membrane protein. His Biochemistry study is mostly concerned with Reductase, Mevalonate pathway, Saccharomyces cerevisiae, Protein degradation and HMG-CoA reductase.
His Endoplasmic reticulum research is multidisciplinary, incorporating elements of Integral membrane protein, Sterol regulatory element-binding protein, Gene and Geranylgeranyl pyrophosphate. Randolph Y. Hampton interconnects Substrate and Sterol in the investigation of issues within Endoplasmic-reticulum-associated protein degradation. His Ubiquitin study incorporates themes from Cytosol, Plasma protein binding and Proteasome.
Randolph Y. Hampton mainly investigates Cell biology, Endoplasmic-reticulum-associated protein degradation, Protein folding, Ubiquitin and Endoplasmic reticulum. His work deals with themes such as Biochemistry, Allosteric regulation, AIM2 and Mevalonate kinase, which intersect with Cell biology. His Endoplasmic-reticulum-associated protein degradation study frequently draws connections between related disciplines such as Proteasome.
His Protein folding study integrates concerns from other disciplines, such as Sterol and Protein quality. His study in Ubiquitin is interdisciplinary in nature, drawing from both Reductase, Mutant and Cytosol. As part of one scientific family, he deals mainly with the area of Endoplasmic reticulum, narrowing it down to issues related to the Integral membrane protein, and often Transport protein and Protein degradation.
His scientific interests lie mostly in Endoplasmic-reticulum-associated protein degradation, Cell biology, Protein folding, Endoplasmic reticulum and Ubiquitin. His Endoplasmic-reticulum-associated protein degradation research entails a greater understanding of Genetics. His Cell biology research incorporates themes from Mevalonate pathway, Inflammasome, AIM2 and Cancer research.
His research integrates issues of Sterol, Protein quality, Proteostasis, Transcriptional Networks and Computational biology in his study of Protein folding. His study in the field of ERAD pathway also crosses realms of Rhomboid. His Ubiquitin study contributes to a more complete understanding of Biochemistry.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Recognition and plasma clearance of endotoxin by scavenger receptors.
Randolph Y. Hampton;Douglas T. Golenbock;Marsha Penman;Monty Krieger.
Nature (1991)
Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.
Randolph Y. Hampton;Richard G. Gardner;Jasper Rine.
Molecular Biology of the Cell (1996)
ER-associated degradation in protein quality control and cellular regulation.
Randolph Y Hampton.
Current Opinion in Cell Biology (2002)
Hrd1p/Der3p is a membrane- anchored ubiquitin ligase required for ER-associated degradation
Nathan W. Bays;Richard G. Gardner;Linda P. Seelig;Claudio A. Joazeiro.
Nature Cell Biology (2001)
HRD4/NPL4 Is Required for the Proteasomal Processing of Ubiquitinated ER Proteins
Nathan W. Bays;Sharon K. Wilhovsky;Ami Goradia;Kelley Hodgkiss-Harlow.
Molecular Biology of the Cell (2001)
Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p.
Richard G. Gardner;Gwendolyn M. Swarbrick;Nathan W. Bays;Stephen R. Cronin.
Journal of Cell Biology (2000)
Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
Jarrod W. Heck;Samantha K. Cheung;Randolph Y. Hampton.
Proceedings of the National Academy of Sciences of the United States of America (2010)
Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast.
Randolph Y. Hampton;Jasper Rine.
Journal of Cell Biology (1994)
Effects of overproduction of the catalytic domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae.
K. A. G. Donald;R. Y. Hampton;I. B. Fritz.
Applied and Environmental Microbiology (1997)
ER stress response: getting the UPR hand on misfolded proteins.
Randolph Y. Hampton.
Current Biology (2000)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below:
University of Massachusetts Medical School
University of California, Berkeley
Max Delbrück Center for Molecular Medicine
University of Michigan–Ann Arbor
University of California, San Diego
University of Michigan–Ann Arbor
University of California, San Diego
University of Cambridge
Chiba University
University of Pittsburgh
University of Pittsburgh
Brunel University London
Rice University
University of Tokyo
University of California, San Diego
University of Oulu
The Ohio State University
University of Florida
Nanjing Agricultural University
GNS Science
University of Barcelona
Chinese University of Hong Kong
Cleveland Clinic
University College London
Seoul National University
Cardiff University