Nogo‐B receptor is necessary for cellular dolichol biosynthesis and protein N‐glycosylation
- Kenneth D. Harrison, E. Park, W. Sessa
- Biology, ChemistryEMBO Journal
- 15 June 2011
Identification of Nogo‐B receptor (NgBR) as an essential component of the cis‐IPTase machinery yields insights into the regulation of dolichol biosynthesis.
Evidence That the wzxE Gene of Escherichia coli K-12 Encodes a Protein Involved in the Transbilayer Movement of a Trisaccharide-Lipid Intermediate in the Assembly of Enterobacterial Common Antigen*
- P. D. Rick, K. Barr, K. Sankaran, Junko Kajimura, J. Rush, C. J. Waechter
- BiologyJournal of Biological Chemistry
- 9 May 2003
Results support the conclusion that thewzxE gene encodes a membrane protein involved in the transbilayer movement of lipid III in E. coli.
Deficiency of UDP‐GlcNAc:Dolichol Phosphate N‐Acetylglucosamine‐1 Phosphate Transferase (DPAGT1) Causes a Novel Congenital Disorder of Glycosylation Type Ij
- Xiaohuai Wu, J. Rush, H. Freeze
- BiologyHuman Mutation
- 1 August 2003
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.
Requirement of the Lec35 gene for all known classes of monosaccharide-P-dolichol-dependent glycosyltransferase reactions in mammals.
- M. Anand, J. Rush, M. Lehrman
- Biology, ChemistryMolecular Biology of the Cell
- 1 February 2001
The in vitro data suggest that Lec35p controls an aspect of MPD orientation in the endoplasmic reticulum membrane that is crucial for its activity as a donor substrate and has an essential role for all known classes of monosaccharide-P-dolichol-dependent reactions in mammals.
A Novel Epimerase That Converts GlcNAc-P-P-undecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O157*
- J. Rush, C. Alaimo, Riccardo Robbiani, M. Wacker, C. J. Waechter
- Biology, ChemistryJournal of Biological Chemistry
- 18 November 2009
GalNAc-p-P-Und is synthesized reversibly by a novel GlcNAc/UDP- GalNAc epimerase after the formation of Glc NAc-P/P-und by WecA in E. coli O157.
Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy.
- Amy C Yang, B. Ng, L. Mehta
- Biology, MedicineMolecular Genetics and Metabolism
- 1 November 2013
Farnesol is utilized for isoprenoid biosynthesis in plant cells via farnesyl pyrophosphate formed by successive monophosphorylation reactions.
- L. Thai, J. Rush, C. J. Waechter
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 9 November 1999
These results document the presence of at least two CTP-mediated kinases that provide a mechanism for the utilization of F-OH and GG-OH for the biosynthesis of isoprenoid lipids and protein isopranylation.
The molecular mechanism of N-acetylglucosamine side-chain attachment to the Lancefield group A carbohydrate in Streptococcus pyogenes
- J. Rush, R. Edgar, N. Korotkova
- Biology, ChemistryJournal of Biological Chemistry
- 25 August 2017
The elucidation of GAC biosynthesis in S. pyogenes reported here enhances the understanding of how other Gram-positive bacteria produce essential components of their cell wall.
Discovery of glycerol phosphate modification on streptococcal rhamnose polysaccharides
- R. Edgar, Vincent P. van Hensbergen, N. Korotkova
- BiologyNature Chemical Biology
- 4 June 2018
Genetic, structural and biochemical analysis identifies GacH as a glycerol phosphate transferase that modifies N-acetylglucosamine components of group A carbohydrates (GAC) in streptococcal cell walls.
The LPP1 and DPP1 Gene Products Account for Most of the Isoprenoid Phosphate Phosphatase Activities inSaccharomyces cerevisiae *
- Alexander Faulkner, Xiaoming Chen, P. Sternweis
- BiologyJournal of Biological Chemistry
- 21 May 1999
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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