about
Establishment of the chloroplast genetic system in rice during early leaf development and at low temperaturesPotassium Acts as a GTPase-Activating Element on Each Nucleotide-Binding Domain of the Essential Bacillus subtilis EngAMetal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPasesStructural and Functional Insights into the Mode of Action of a Universally Conserved Obg GTPaseHflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditionsHost Matters: Medicinal Leech Digestive-Tract Symbionts and Their Pathogenic PotentialThe Neisseria gonorrhoeae Obg protein is an essential ribosome-associated GTPase and a potential drug targetTypA is involved in virulence, antimicrobial resistance and biofilm formation in Pseudomonas aeruginosaMutations in GTP binding protein Obg of Mycoplasma synoviae vaccine strain MS-H: implications in temperature-sensitivity phenotypeTargeting an Essential GTPase Obg for the Development of Broad-Spectrum AntibioticsGTP-binding protein Era: a novel gene target for biofuel productionReactive oxygen species do not contribute to ObgE*-mediated programmed cell deathCharacterization of the autophosphorylation property of HflX, a ribosome-binding GTPase from Escherichia coliThe Escherichia coli GTPase ObgE modulates hydroxyl radical levels in response to DNA replication fork arrest.Identification of novel small RNAs and characterization of the 6S RNA of Coxiella burnetii.Structural insights into the function of a unique tandem GTPase EngA in bacterial ribosome assembly.Evidence for lateral gene transfer (LGT) in the evolution of eubacteria-derived small GTPases in plant organelles.High-resolution melting-curve analysis of obg gene to differentiate the temperature-sensitive Mycoplasma synoviae vaccine strain MS-H from non-temperature-sensitive strains.The evolutionary and functional diversity of classical and lesser-known cytoplasmic and organellar translational GTPases across the tree of lifePredicting the minimal translation apparatus: lessons from the reductive evolution of mollicutes.Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.OLA1 regulates protein synthesis and integrated stress response by inhibiting eIF2 ternary complex formation.Exceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome.A universally conserved ATPase regulates the oxidative stress response in Escherichia coliRedox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1.Conserved bacterial RNase YbeY plays key roles in 70S ribosome quality control and 16S rRNA maturationMycobacterium fluoroquinolone resistance protein B, a novel small GTPase, is involved in the regulation of DNA gyrase and drug resistance.Obg-like ATPase 1 regulates global protein serine/threonine phosphorylation in cancer cells by suppressing the GSK3β-inhibitor 2-PP1 positive feedback loop.OLA1 contributes to epithelial-mesenchymal transition in lung cancer by modulating the GSK3β/snail/E-cadherin signaling.Coexpression of Escherichia coli obgE, Encoding the Evolutionarily Conserved Obg GTPase, with Ribosomal Proteins L21 and L27TaTypA, a Ribosome-Binding GTPase Protein, Positively Regulates Wheat Resistance to the Stripe Rust Fungus.Ribosome recycling defects modify the balance between the synthesis and assembly of specific subunits of the oxidative phosphorylation complexes in yeast mitochondriaOLA1, a Translational Regulator of p21, Maintains Optimal Cell Proliferation Necessary for Developmental Progression.Identification of YbeY-Protein Interactions Involved in 16S rRNA Maturation and Stress Regulation in Escherichia coliDER containing two consecutive GTP-binding domains plays an essential role in chloroplast ribosomal RNA processing and ribosome biogenesis in higher plants.Thymineless death is inhibited by CsrA in Escherichia coli lacking the SOS response.Bacterial Obg proteins: GTPases at the nexus of protein and DNA synthesis.The paradox of elongation factor 4: highly conserved, yet of no physiological significance?Histidine 114 Is Critical for ATP Hydrolysis by the Universally Conserved ATPase YchF.Bacterial ferrous iron transport: the Feo system.
P2860
Q26829420-0A47E419-9DAC-47F8-89AC-E15B588C7C4AQ27674429-6CED826A-5576-47BB-9201-136A6107BF71Q27681423-F2222A67-5F43-40B9-BC94-C512F4CBA450Q27683859-E4547554-43E8-41DB-BE17-1D30E9CF4CC9Q27702284-EEE75B91-1436-40C7-A2AF-3E0D6C6E3A18Q28077266-FFF996A3-2C11-4FBD-8D35-B54294086393Q28485125-0488B2CB-A537-4048-99AF-6BB6F7768D85Q28492591-F325EFE4-0C9A-4E7F-8DC3-ECE3E8FB9E13Q28533534-D9740E77-0108-45F9-81A1-CE985A5CDBB4Q28553171-D06207D5-E599-4D90-ADEB-9595C70E987AQ28650826-A5E9E1D4-7C3E-44BF-9F35-C84F2173895FQ28829944-4FFEEFD6-031F-4D14-B3A3-2913BB5D6226Q28831340-30D6D0E4-01BE-4FF1-BF16-C7BA77E06A77Q34366109-0BD9F7D4-B1B0-457A-B671-979411D9C6B5Q34425836-C04807FA-3592-4BB5-9D0E-C9A0BFCB3E60Q34579765-D2F7631C-C995-4247-BEC6-DE97DD0CD481Q34677440-3C70CFD8-B3C9-4919-BA4D-BAF62C2B1C14Q35124251-C17BBD70-0AED-48EE-BD58-0BF30F5BEBC4Q35127797-EA96A2BF-3447-4237-9D98-491923FFA6C3Q35165320-28E39011-E8AA-48AE-A82C-399E0711CA42Q35796219-04E0F677-AF82-4CB2-8ABC-19CF5697E323Q35964463-77A335EB-7622-4D10-9B72-038206F9AE96Q36206202-35E5BB3C-13EB-46D2-8CC8-6B3A9EFDD791Q36481799-2F53360B-3EFE-4A77-AD7F-C223DE13DFE9Q36549318-1C4C8991-3081-4396-B74E-BBE9C7096654Q36604911-45DB8891-8260-4239-944D-DEC591353CE6Q36619820-89306871-F528-461F-ABAB-E84EADA2A909Q36772158-A353B989-96FA-4E06-9D3E-E384A35E1FB6Q36962983-5D7797C1-F18D-4509-8A87-3C7E3E4E7F1BQ37002216-7C2FB168-659F-4DB3-9C0D-EFD420FA5E80Q37022990-9A9CA753-D946-4154-86FB-3F34C06CFBDEQ37076349-87CFC7D6-B1F9-4DF0-B126-C55B0BAAA4EDQ37287406-2F285F01-43E1-4CF7-AD0E-CA2ED01BE43AQ37402292-5393C080-5237-494F-80C2-BD410957C07FQ37443517-57F77D2D-5C76-4DB7-B1D7-F48346A17EC0Q37504337-005B32A0-F6FB-453B-A873-CF31835920F0Q38093857-895C6CB6-D013-48EC-9C6D-7A961FA58137Q38105598-B1EB5A8B-37A3-4305-BCBC-39700E15CD51Q38410850-C562CD0C-86A5-48B0-A059-CA0F15A9FB84Q38673867-EF156BB4-C825-4BCB-8640-B7AACEC19D27
P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The universally conserved prokaryotic GTPases
@ast
The universally conserved prokaryotic GTPases
@en
The universally conserved prokaryotic GTPases
@nl
type
label
The universally conserved prokaryotic GTPases
@ast
The universally conserved prokaryotic GTPases
@en
The universally conserved prokaryotic GTPases
@nl
prefLabel
The universally conserved prokaryotic GTPases
@ast
The universally conserved prokaryotic GTPases
@en
The universally conserved prokaryotic GTPases
@nl
P2093
P2860
P50
P3181
P356
P1476
The universally conserved prokaryotic GTPases
@en
P2093
J. Michiels
M. Fauvart
N. Verstraeten
W. Versees
P2860
P304
507-42, second and third pages of table of content
P3181
P356
10.1128/MMBR.00009-11
P407
P577
2011-09-01T00:00:00Z