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Biochemical and physiological characterization of the GTP-binding protein Obg of Mycobacterium tuberculosis
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scholarly article
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PubMed
PubMed ID
21352546
retrieved
24 January 2017
title
Biochemical and physiological characterization of the GTP-binding protein Obg of Mycobacterium tuberculosis
(English)
1 reference
stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
main subject
Mycobacterium tuberculosis
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author
Subramanian Dhandayuthapani
series ordinal
4
object named as
Subramanian Dhandayuthapani
1 reference
stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
author name string
Smitha J. Sasindran
series ordinal
1
1 reference
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PubMed
PubMed ID
21352546
retrieved
24 January 2017
Sankaralingam Saikolappan
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
Virginia L. Scofield
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
publication date
25 February 2011
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stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
published in
BMC Microbiology
1 reference
stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
volume
11
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stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
page(s)
43
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stated in
PubMed
PubMed ID
21352546
retrieved
24 January 2017
exact match
https://scigraph.springernature.com/pub.10.1186/1471-2180-11-43
0 references
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Structural and biochemical analysis of the Obg GTP binding protein
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The GTPase superfamily: conserved structure and molecular mechanism
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Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae
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The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase
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The Caulobacter crescentus CgtAC protein cosediments with the free 50S ribosomal subunit
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Macrophage-induced genes of Legionella pneumophila: protection from reactive intermediates and solute imbalance during intracellular growth
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Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase
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The Bacillus subtilis GTP binding protein obg and regulators of the sigma(B) stress response transcription factor cofractionate with ribosomes
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The Caulobacter crescentus CgtA protein displays unusual guanine nucleotide binding and exchange properties
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Molecular cloning and characterization of the obg gene of Streptomyces griseus in relation to the onset of morphological differentiation
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29 September 2017
Biochemical characterization of the essential GTP-binding protein Obg of Bacillus subtilis
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PubMed Central
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29 September 2017
Effects on Bacillus subtilis of a conditional lethal mutation in the essential GTP-binding protein Obg
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29 September 2017
Possible role for the essential GTP-binding protein Obg in regulating the initiation of sporulation in Bacillus subtilis
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PubMed Central
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29 September 2017
Restricting conformational flexibility of the switch II region creates a dominant-inhibitory phenotype in Obg GTPase Nog1.
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2 June 2018
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Survey for g-proteins in the prokaryotic genomes: prediction of functional roles based on classification
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Human small G proteins, ObgH1, and ObgH2, participate in the maintenance of mitochondria and nucleolar architectures.
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The GTP binding protein Obg homolog ObgE is involved in ribosome maturation.
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21 January 2018
A Vibrio harveyi insertional mutant in the cgtA (obg, yhbZ) gene, whose homologues are present in diverse organisms ranging from bacteria to humans and are essential genes in many bacterial species.
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27 November 2018
Deficiency of essential GTP-binding protein ObgE in Escherichia coli inhibits chromosome partition
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Biochemical properties of Ha-ras encoded p21 mutants and mechanism of the autophosphorylation reaction
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21352546
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12 December 2020
based on heuristic
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An essential GTP-binding protein functions as a regulator for differentiation in Streptomyces coelicolor
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21352546
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12 December 2020
based on heuristic
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Identifiers
DOI
10.1186/1471-2180-11-43
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
963747
Dimensions Publication ID
1049795749
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OpenCitations bibliographic resource ID
963747
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
963747
PMCID
3056739
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
963747
PubMed ID
21352546
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
963747
ResearchGate publication ID
50212343
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