L B Poole
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Explore the profile of L B Poole including associated specialties, affiliations and a list of published articles.
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29
Citations
973
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Recent Articles
1.
Ritz D, Lim J, Reynolds C, Poole L, Beckwith J
Science
. 2001 Oct;
294(5540):158-60.
PMID: 11588261
Pathways for the reduction of protein disulfide bonds are found in all organisms and are required for the reductive recycling of certain enzymes including the essential protein ribonucleotide reductase. An...
2.
Reynolds C, Poole L
Biochemistry
. 2001 Apr;
40(13):3912-9.
PMID: 11300770
AhpF, the flavoprotein reductase component of the Salmonella typhimurium alkyl hydroperoxide reductase system, catalyzes the reduction of an intersubunit disulfide bond in the peroxidatic active site of the system's other...
3.
Wood Z, Poole L, Karplus P
Biochemistry
. 2001 Apr;
40(13):3900-11.
PMID: 11300769
AhpF, a homodimer of 57 kDa subunits, is a flavoenzyme which catalyzes the NADH-dependent reduction of redox-active disulfide bonds in the peroxidase AhpC, a member of the recently identified peroxiredoxin...
4.
Baker L, Raudonikiene A, Hoffman P, Poole L
J Bacteriol
. 2001 Feb;
183(6):1961-73.
PMID: 11222594
Helicobacter pylori, an oxygen-sensitive microaerophile, contains an alkyl hydroperoxide reductase homologue (AhpC, HP1563) that is more closely related to 2-Cys peroxiredoxins of higher organisms than to most other eubacterial AhpC...
5.
Poole L, Reynolds C, Wood Z, Karplus P, ELLIS H, Li Calzi M
Eur J Biochem
. 2000 Sep;
267(20):6126-33.
PMID: 11012664
A group of bacterial flavoproteins related to thioredoxin reductase contain an additional approximately 200-amino-acid domain including a redox-active disulfide center at their N-termini. These flavoproteins, designated NADH:peroxiredoxin oxidoreductases, catalyze the...
6.
Reynolds C, Poole L
Biochemistry
. 2000 Jul;
39(30):8859-69.
PMID: 10913298
AhpF of Salmonella typhimurium, the flavoprotein reductase required for catalytic turnover of AhpC with hydroperoxide substrates in the alkyl hydroperoxide reductase system, is a 57 kDa protein with homology to...
7.
Yamamoto Y, Higuchi M, Poole L, Kamio Y
Biosci Biotechnol Biochem
. 2000 Jul;
64(5):1106-9.
PMID: 10879495
Alkyl hydroperoxide reductase in Streptococcus mutans consists of two components, Nox-1 and AhpC. Deletion of nox-1 and ahpC in a double mutant as well as the wild-type of Streptococcus mutans...
8.
Yamamoto Y, Higuchi M, Poole L, Kamio Y
J Bacteriol
. 2000 Jun;
182(13):3740-7.
PMID: 10850989
We have previously identified and characterized the alkyl hydroperoxide reductase of Streptococcus mutans, which consists of two components, Nox-1 and AhpC. Deletion of both nox-1 and ahpC had no effect...
9.
Poole L, Godzik A, Nayeem A, SCHMITT J
Biochemistry
. 2000 Jun;
39(22):6602-15.
PMID: 10828978
AhpF, the flavin-containing component of the Salmonella typhimurium alkyl hydroperoxide reductase system, catalyzes the NADH-dependent reduction of an active-site disulfide bond in the other component, AhpC, which in turn reduces...
10.
Poole L, Higuchi M, Shimada M, Calzi M, Kamio Y
Free Radic Biol Med
. 2000 Feb;
28(1):108-20.
PMID: 10656297
Nox-1 from Streptococcus mutans, the bacteria which cause dental caries, was previously identified as an H2O2-forming reduced nicotinamide adenine dinucleotide (NADH) oxidase. Nox-1 is homologous with the flavoprotein component, AhpF,...