Geobacillus stearothermophilus
"Geobacillus stearothermophilus" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.
| Descriptor ID |
D001411
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| MeSH Number(s) |
B03.300.390.400.158.400.400 B03.353.500.100.400.400 B03.510.100.100.400.400 B03.510.415.400.158.400.400 B03.510.460.410.158.400.400
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Geobacillus stearothermophilus".
Below are MeSH descriptors whose meaning is more specific than "Geobacillus stearothermophilus".
This graph shows the total number of publications written about "Geobacillus stearothermophilus" by people in this website by year, and whether "Geobacillus stearothermophilus" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 0 | 1 |
| 1995 | 3 | 0 | 3 |
| 1999 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2008 | 1 | 0 | 1 |
| 2009 | 1 | 0 | 1 |
| 2012 | 1 | 0 | 1 |
| 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "Geobacillus stearothermophilus" by people in Profiles.
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Case BC, Hartley S, Osuga M, Jeruzalmi D, Hingorani MM. The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair. Nucleic Acids Res. 2019 05 07; 47(8):4136-4152.
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Pakotiprapha D, Samuels M, Shen K, Hu JH, Jeruzalmi D. Structure and mechanism of the UvrA-UvrB DNA damage sensor. Nat Struct Mol Biol. 2012 Feb 05; 19(3):291-8.
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Pakotiprapha D, Liu Y, Verdine GL, Jeruzalmi D. A structural model for the damage-sensing complex in bacterial nucleotide excision repair. J Biol Chem. 2009 May 08; 284(19):12837-44.
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Huang HC, Jupiter D, Qiu M, Briggs JM, Vanburen V. Cluster analysis of hydration waters around the active sites of bacterial alanine racemase using a 2-ns MD simulation. Biopolymers. 2008 Mar; 89(3):210-9.
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Pakotiprapha D, Inuzuka Y, Bowman BR, Moolenaar GF, Goosen N, Jeruzalmi D, Verdine GL. Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Mol Cell. 2008 Jan 18; 29(1):122-33.
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Zhou M, Pugmire MJ, Vuong BQ, Ealick SE. Cloning, expression and crystallization of pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. Acta Crystallogr D Biol Crystallogr. 1999 Jan; 55(Pt 1):287-90.
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Auzat I, Byrnes WM, Garel JR, Chang SH. Role of residue 161 in the allosteric transitions of two bacterial phosphofructokinases. Biochemistry. 1995 May 30; 34(21):7062-8.
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Zhu X, Byrnes M, Nelson JW, Chang SH. Role of glycine 212 in the allosteric behavior of phosphofructokinase from Bacillus stearothermophilus. Biochemistry. 1995 Feb 28; 34(8):2560-5.
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Byrnes WM, Hu W, Younathan ES, Chang SH. A chimeric bacterial phosphofructokinase exhibits cooperativity in the absence of heterotropic regulation. J Biol Chem. 1995 Feb 24; 270(8):3828-35.
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Byrnes M, Zhu X, Younathan ES, Chang SH. Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme. Biochemistry. 1994 Mar 22; 33(11):3424-31.