The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin. (Q34172330)

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English	The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin.	scientific article

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16 February 2020

The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin (English)

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16 February 2020

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16 February 2020

Anandhi Anandan

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16 February 2020

Keith A. Stubbs

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16 February 2020

Martin J. Scanlon

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16 February 2020

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16 February 2020

Charlene M Kahler

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16 February 2020

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Susannah Piek

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16 February 2020

Zhirui Wang

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16 February 2020

Adam M Lakey

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16 February 2020

Stephanie N Bartley

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16 February 2020

Shakeel Mowlaboccus

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16 February 2020

Parastoo Azadi

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16 February 2020

Russell W Carlson

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16 February 2020

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12 September 2014

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16 February 2020

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16 February 2020

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16 February 2020

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16 February 2020

e106513

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16 February 2020

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Creative Commons Attribution 4.0 International

12 September 2014

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0 references

Lipid A's structure mediates Neisseria gonorrhoeae fitness during experimental infection of mice and men.

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The structure of the neisserial lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin

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The Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA Enzymes

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Phosphoethanolamine substitution of lipid A and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum

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5 July 2018

Modification of lipooligosaccharide with phosphoethanolamine by LptA in Neisseria meningitidis enhances meningococcal adhesion to human endothelial and epithelial cells

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A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2+ hypersensitivity of an eptB deletion mutant.

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Phosphorylation of the Lipid A Region of Meningococcal Lipopolysaccharide: Identification of a Family of Transferases That Add Phosphoethanolamine to Lipopolysaccharide

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KpsF is the arabinose-5-phosphate isomerase required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression in Neisseria meningitidis

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Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family

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Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells

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Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: effects on bacterial growth and biogenesis of functional type IV pili

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Genetic basis for biosynthesis, structure, and function of meningococcal lipooligosaccharide (endotoxin)

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12 December 2020

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inferred from PubMed ID database lookup

Reduced DNA binding and uptake in the absence of DsbA1 and DsbA2 of Neisseria meningitidis due to inefficient folding of the outer-membrane secretin PilQ

1 reference

https://pubmed.ncbi.nlm.nih.gov/25215579

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The membrane phospholipids of Neisseria meningitidis and Neisseria gonorrhoeae as characterized by fast atom bombardment mass spectrometry

1 reference

https://pubmed.ncbi.nlm.nih.gov/25215579

12 December 2020

based on heuristic

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First Neisseria gonorrhoeae strain with resistance to cefixime causing gonorrhoea treatment failure in Austria, 2011

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https://pubmed.ncbi.nlm.nih.gov/25215579

12 December 2020

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10.1371/JOURNAL.PONE.0106513

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16 February 2020

2014PLoSO...9j6513P

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16 February 2020

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16 February 2020

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