HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions - Test2 - elhamkhani - TriplyDB

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

http://www.wikidata.org/entity/Q27702284

about

Characterization of the autophosphorylation property of HflX, a ribosome-binding GTPase from Escherichia coli Chemical and structural characterization of a model Post-Termination Complex (PoTC) for the ribosome recycling reaction: Evidence for the release of the mRNA by RRF and EF-G.ppGpp negatively impacts ribosome assembly affecting growth and antimicrobial tolerance in Gram-positive bacteria Biological cryo-electron microscopy in China Genetic Selection of Peptide Aptamers That Interact and Inhibit Both Small Protein B and Alternative Ribosome-Rescue Factor A of Aeromonas veronii C4.The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome.Disassembly of the Staphylococcus aureus hibernating 100S ribosome by an evolutionarily conserved GTPase.The kinetic mechanism of bacterial ribosome recycling.NOVEL ANTIBIOTIC RESISTANCE DETERMINANTS FROM AGRICULTURAL SOIL EXPOSED TO ANTIBIOTICS WIDELY USED IN HUMAN MEDICINE AND ANIMAL FARMING.Survival of the drowsiest: the hibernating 100S ribosome in bacterial stress management.Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged ribosomes

P2860

Q28831340-6A30264E-E361-4200-BC2E-571E11CC64D7 Q33724909-8D3CEA4C-125E-4D82-B3E6-1008E1BC5D9F Q35948392-80E950B0-978C-4FFE-9983-D92A878503A0 Q36106092-0AFD1298-0ACB-48F5-B3DD-CC045E606A9B Q36121221-2F9612C8-E314-4D8A-A83B-51B28EFD306C Q38667794-1937B533-23A3-4688-8FAC-A4FE00E4AF62 Q42284102-A8AC47DE-4F42-46E7-B322-467C271EDB35 Q47100996-4D757E4E-E061-4ED4-8C26-654FECF5CDD4 Q47207035-EEBB6ABB-BDD4-4864-8E50-541E9F5AFEDA Q48113261-A44626A3-23C8-41FE-9530-891E41570435 Q57291551-3AE65707-8DAE-4D9F-A5DA-AB0121D5FFFE Q57753732-A9970D81-ADF9-4886-9699-9C51847B2D1E

P2860

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

http://www.wikidata.org/entity/Q27702284

description

2015 nî lūn-bûn

@nan

2015 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@ast

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@en

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@nl

type

label

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@ast

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@en

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@nl

prefLabel

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@ast

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@en

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@nl

P1433

Q27702284-F79F30BC-3E14-4D63-8E3B-9652336D5569

P1476

Q27702284-4EC50A22-D848-48E6-B762-23FD17BE6685

P2093

Q27702284-1EA8E28A-98EF-4917-9134-8B1E07A7E74C

Q27702284-508921A1-42F7-47A2-93A1-1072302E839F

Q27702284-62E754AD-4EFB-48D4-AA7B-987DF02357C3

Q27702284-664F11B7-29B1-4C22-8744-148DA84D6B8D

Q27702284-9636798C-246C-424D-AAD0-319814E7D55C

Q27702284-B0D0F347-F2D5-4045-9CB0-6F2C1EB8C581

Q27702284-C41608C8-CF5B-406F-BDFE-10A030810870

Q27702284-E38CFC98-6FF8-45EF-9841-9E11BF2629FE

Q27702284-E7710238-80B2-4052-A3FF-54933D924142

Q27702284-FB0EE97E-C2C5-4DE5-9E84-956FDE7397BF

P2860

Q27702284-04C1D2E1-60C1-45AB-AA0F-84CF660E4FC6

Q27702284-05558C2F-A186-4052-AD19-BA908D3CF253

Q27702284-0E216A44-5127-460A-8E89-0EBA31982678

Q27702284-165C3A4A-0E60-4E57-999D-6071AA1E05D5

Q27702284-1D5405F3-3114-42E9-93D3-BB438634F514

Q27702284-1F1F2CF7-D508-40C2-BFD8-D9C39E17A07C

Q27702284-21A176DF-50AD-4BD8-BC9B-F1457BDD6F39

Q27702284-22333D42-65C6-45CE-8133-0D38EAC8DEBE

Q27702284-258C69A2-0A89-474B-A65F-3A2DAE03519F

Q27702284-2E4354C1-A9E9-4B98-9EBF-72E0B99E32BC

P2888

Q27702284-908B228A-4F57-4848-A99C-3663C67C0223

P304

Q27702284-093B5F46-7AD6-41C7-A580-BC7BCE6C57C5

P31

Q27702284-FA1F0827-AA5B-4CDC-8059-88EB42DFD8FC

P3181

Q27702284-DCD2EA32-08BC-4386-A270-E964E30733E1

P356

Q27702284-B652E09D-1B83-45F0-8086-FB732D58B131

P433

Q27702284-6EB2B808-D49F-468F-B895-A776E387BF3B

P478

Q27702284-5F29CD25-5EFA-44A1-9B79-C564B912EB57

P50

Q27702284-21A51432-1D92-4CE4-AAD6-87B186BCFCBB

Q27702284-A03CAD53-16CD-406F-B493-8426A05953D2

P577

Q27702284-EAF85C1C-6CBA-4C59-BC63-E32FCF8043ED

P5875

Q27702284-AAA460AC-87F0-43E2-9E37-C63B5DBB3A79

P6179

Q27702284-14107A3E-40E0-454D-B23A-2445550D6114

P698

Q27702284-CEF28EAD-E380-4FA0-ABD0-6369B41F21EB

P3181

P356

P1433

Nature Structural & Molecular Biology

P1476

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

@en

P2093

Chandra Sekhar Mandava

http://www.w3.org/2001/XMLSchema#string

Dejiu Zhang

http://www.w3.org/2001/XMLSchema#string

Jianlin Lei

http://www.w3.org/2001/XMLSchema#string

Kaixia Mi

http://www.w3.org/2001/XMLSchema#string

Ningning Li

http://www.w3.org/2001/XMLSchema#string

Wei Cao

http://www.w3.org/2001/XMLSchema#string

Xiaojing Li

http://www.w3.org/2001/XMLSchema#string

Xiaoxiao Zhang

http://www.w3.org/2001/XMLSchema#string

Yan Qin

http://www.w3.org/2001/XMLSchema#string

Yanqing Zhang

http://www.w3.org/2001/XMLSchema#string

P2860

Conformational flexibility and molecular interactions of an archaeal homologue of the Shwachman-Bodian-Diamond syndrome protein.

Experimental Determination and System Level Analysis of Essential Genes in Escherichia coli MG1655

Genome-wide expression profiling in Escherichia coli K-12

I-TASSER: a unified platform for automated protein structure and function prediction

Structures of the bacterial ribosome in classical and hybrid states of tRNA binding

Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome.

Ribosome formation from subunits studied by stopped-flow and rayleigh light scattering

The universally conserved prokaryotic GTPases

Locking and unlocking of ribosomal motions

Crystal structure of the ribosome recycling factor bound to the ribosome

P2888

P304

906-913

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

963722

http://www.w3.org/2001/XMLSchema#string

P356

10.1038/NSMB.3103

http://www.w3.org/2001/XMLSchema#string

P433

11

http://www.w3.org/2001/XMLSchema#string

P478

22

http://www.w3.org/2001/XMLSchema#string

P50

P577

2015-10-12T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

282816028

http://www.w3.org/2001/XMLSchema#string

P6179

1007709677

http://www.w3.org/2001/XMLSchema#string

P698

26458047

http://www.w3.org/2001/XMLSchema#string