Derived structure of the putative sialic acid transporter from Escherichia coli predicts a novel sugar permease domain.
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Identification of a novel sialic acid transporter in Haemophilus ducreyiMajor facilitator superfamilyDiversity of microbial sialic acid metabolismNontypeable Haemophilus influenzae: the role of N-acetyl-5-neuraminic acid in biologyCharacterization of the N-acetyl-5-neuraminic acid-binding site of the extracytoplasmic solute receptor (SiaP) of nontypeable Haemophilus influenzae strain 2019Structural insights into the regulation of sialic acid catabolism by the Vibrio vulnificus transcriptional repressor NanRSialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporterMetabolic incorporation of unnatural sialic acids into Haemophilus ducreyi lipooligosaccharides.Insights into the evolution of sialic acid catabolism among bacteria.Metabolism of sialic acid by Bifidobacterium breve UCC2003.Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli.An infant-associated bacterial commensal utilizes breast milk sialyloligosaccharides.Unified theory of bacterial sialometabolism: how and why bacteria metabolize host sialic acidsSialic acid (N-acetyl neuraminic acid) utilization by Bacteroides fragilis requires a novel N-acetyl mannosamine epimerase.Sialic acid catabolism confers a competitive advantage to pathogenic vibrio cholerae in the mouse intestine.Biosynthesis and production of polysialic acids in bacteria.Host Sialic Acids: A Delicacy for the Pathogen with Discerning Taste.Cloning, sequence, and transcriptional regulation of the operon encoding a putative N-acetylmannosamine-6-phosphate epimerase (nanE) and sialic acid lyase (nanA) in Clostridium perfringens.The membrane proteins SiaQ and SiaM form an essential stoichiometric complex in the sialic acid tripartite ATP-independent periplasmic (TRAP) transporter SiaPQM (VC1777-1779) from Vibrio cholerae.YjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-acetylneuraminic acidSialic acid metabolism's dual function in Haemophilus influenzae.Characterization of a novel sialic acid transporter of the sodium solute symporter (SSS) family and in vivo comparison with known bacterial sialic acid transporters.Enhanced production of N-acetyl-D-neuraminic acid by multi-approach whole-cell biocatalyst.N-Acetylneuraminic acid uptake in Pasteurella (Mannheimia) haemolytica A2 occurs by an inducible and specific transport system.Distant cis-active sequences and sialic acid control the expression of fimB in Escherichia coli K-12.The first committed step in the biosynthesis of sialic acid by Escherichia coli K1 does not involve a phosphorylated N-acetylmannosamine intermediate.Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity."Just a spoonful of sugar...": import of sialic acid across bacterial cell membranes.Sialic acid utilization by the soil bacterium Corynebacterium glutamicum.
P2860
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P2860
Derived structure of the putative sialic acid transporter from Escherichia coli predicts a novel sugar permease domain.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
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1995年學術文章
@zh-hant
name
Derived structure of the putat ...... a novel sugar permease domain.
@en
Derived structure of the putat ...... a novel sugar permease domain.
@nl
type
label
Derived structure of the putat ...... a novel sugar permease domain.
@en
Derived structure of the putat ...... a novel sugar permease domain.
@nl
prefLabel
Derived structure of the putat ...... a novel sugar permease domain.
@en
Derived structure of the putat ...... a novel sugar permease domain.
@nl
P2093
P2860
P1476
Derived structure of the putat ...... a novel sugar permease domain.
@en
P2093
P2860
P304
P356
10.1128/JB.177.20.6005-6010.1995
P577
1995-10-01T00:00:00Z