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Stephen High
Researcher at University of Manchester
Publications - 135
Citations - 8773
Stephen High is an academic researcher from University of Manchester. The author has contributed to research in topics: Endoplasmic reticulum & Membrane protein. The author has an hindex of 48, co-authored 129 publications receiving 8085 citations. Previous affiliations of Stephen High include Saarland University & Manchester Academic Health Science Centre.
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Journal ArticleDOI
Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
Andrew R. J. Young,Edmond Chan,Xiao-Wen Hu,Robert Köchl,Samuel G. Crawshaw,Stephen High,Dale W. Hailey,Jennifer Lippincott-Schwartz,Sharon A. Tooze +8 more
TL;DR: The mammalian homologue of Atg9p, a multi-spanning transmembrane protein essential in yeast for autophagy, is studied to gain a better understanding of the function of this ubiquitious protein.
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Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
TL;DR: It is likely that ERp57 functions as part of the glycoprotein-specific quality control machinery operating in the lumen of the ER.
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ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.
TL;DR: It is proposed that ERp57 forms complexes with both calnexin and calreticulin and propose that it is these complexes that can specifically modulate glycoprotein folding within the ER lumen.
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The Escherichia coli SRP and SecB targeting pathways converge at the translocon
Quido A. Valent,Pier A. Scotti,Stephen High,Jan-Willem de Gier,Gunnar von Heijne,Georg Lentzen,Wolfgang Wintermeyer,Bauke Oudega,Joen Luirink +8 more
TL;DR: It is demonstrated here that the SRP pathway delivers nascent inner membrane proteins at the membrane through a protein cross‐linking approach that delivers a variety of precursor proteins to a common membrane translocation complex of the E. coli inner membrane.
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The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence.
TL;DR: The availability of the amino acid sequence allows the interpretation of some of the many studies on the chemical and proteolytic modification of the human protein aimed at examining the structure and mechanism of this membrane transport protein.