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Jeffrey S. Rush

Researcher at University of Kentucky

Publications -  67
Citations -  2351

Jeffrey S. Rush is an academic researcher from University of Kentucky. The author has contributed to research in topics: Endoplasmic reticulum & Dolichol. The author has an hindex of 27, co-authored 66 publications receiving 2198 citations.

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Erythroglycan, a high molecular weight glycopeptide with the repeating structure [galactosyl-(1 leads to 4)-2-deoxy-2-acetamido-glucosyl(1 leads to 3)] comprising more than one-third of the protein-bound carbohydrate of human erythrocyte stroma.

TL;DR: Erythroglycan may have the same type of keratan-like core structure as the long chain blood group glycolipids from human erythrocytes and could be a protein-bound carrier of the ABO determinants.
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Deficiency of UDP‐GlcNAc:Dolichol Phosphate N‐Acetylglucosamine‐1 Phosphate Transferase (DPAGT1) Causes a Novel Congenital Disorder of Glycosylation Type Ij

TL;DR: A novel CDG type, CDG‐Ij, is identified, resulting from deficiency in UDP‐GlcNAc: dolichol phosphate N‐acetyl‐glucosamine‐1 phosphate transferase (GPT) activity encoded by DPAGT1, which is concluded to be responsible for the CDG symptoms in this patient.
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The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae.

TL;DR: Results indicate that LPP1 and DPP1 account for most of the hydrolytic activities toward isoprenoid pyrophosphates, dolichyl-P-P, farnesyl-F-P -P, and geranylgeranyl-p-P but also suggest that yeast contain other enzymes capable of dephosphorylating these essential isopranoid intermediates.
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Nogo‐B receptor is necessary for cellular dolichol biosynthesis and protein N‐glycosylation

TL;DR: Identification of Nogo‐B receptor (NgBR) as an essential component of the cis‐IPTase machinery yields insights into the regulation of dolichol biosynthesis.