K
Keith K. Stanley
Researcher at University of New South Wales
Publications - 8
Citations - 282
Keith K. Stanley is an academic researcher from University of New South Wales. The author has contributed to research in topics: Secretory protein & Kinase. The author has an hindex of 5, co-authored 8 publications receiving 272 citations.
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Journal ArticleDOI
The propeptide of macrophage inhibitory cytokine (MIC‐1), a TGF‐β superfamily member, acts as a quality control determinant for correctly folded MIC‐1
Asne R. Bauskin,Hong Ping Zhang,W. Douglas Fairlie,Xiao Yan He,Patricia K Russell,Anthony G. Moore,David Brown,Keith K. Stanley,Samuel N. Breit +8 more
TL;DR: This is the first demonstration, to the authors' knowledge, of a quality control function in a propeptide domain of a secretory protein and represents an additional mechanism to ensure correct folding of proteins leaving the ER.
Journal ArticleDOI
A novel gene family induced by acute inflammation in endothelial cells.
TL;DR: It is proposed that NLF1 and NLF2 belong to a novel gene family encoding nuclear factors with a role in regulating genes which control cellular architecture which might increase vascular permeability in acute inflammation.
Journal ArticleDOI
Src family kinase activation in glycosphingolipid-rich membrane domains of endothelial cells treated with oxidised low density lipoprotein.
Simon J. Myers,Keith K. Stanley +1 more
TL;DR: It is concluded that 7-ketocholesterol and possibly other components of oxLDL can equilibrate into glycosphingolipid-rich membranes and increase the activity of src kinases, possibly by interaction with caveolin.
Journal ArticleDOI
N-glycans are not a universal signal for apical sorting of secretory proteins
TL;DR: The results indicate that not all cell lines recognise N‐glycans as a signal for apical sorting and raises the possibility of using ECV304 cells as a model system for analysis of apicals sorting molecules.
Journal ArticleDOI
ROLE OF PHOSPHORYLATION OF THE CYTOPLASMIC DOMAIN OF THE α2‐MACROGLOBULIN RECEPTOR (LRP)
TL;DR: It is shown that LDLR/LRP was rapidly turned over by proteasomal degradation but that this turnover was also not a consequence of phosphorylation, and thatosphorylation is exclusive to the cytoplasmic domain.