VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
about
Emerging Roles of Toxin-Antitoxin Modules in Bacterial PathogenesisToxin-Antitoxin systems: their role in persistence, biofilm formation, and pathogenicityStructure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic BacteriaAnalysis of non-typeable Haemophilous influenzae VapC1 mutations reveals structural features required for toxicity and flexibility in the active siteWake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancyToxin inhibition in C. crescentus VapBC1 is mediated by a flexible pseudo-palindromic protein motif and modulated by DNA binding.Comprehensive classification of the PIN domain-like superfamilyVapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA.Dormant non-culturable Mycobacterium tuberculosis retains stable low-abundant mRNA.Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectorsRNA damage in biological conflicts and the diversity of responding RNA repair systemsGrowth-regulating Mycobacterium tuberculosis VapC-mt4 toxin is an isoacceptor-specific tRNase.tRNAs taking charge.Mechanism of endonuclease cleavage by the HigB toxinStructural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.Functional Studies of Five Toxin-Antitoxin Modules in Mycobacterium tuberculosis H37Rv.VapCs of Mycobacterium tuberculosis cleave RNAs essential for translation.Multiple toxin-antitoxin systems in Mycobacterium tuberculosis.23S rRNA as an a-Maz-ing new bacterial toxin target.Post-transcriptional regulation of gene expression in bacterial pathogens by toxin-antitoxin systems.tRNA-targeting ribonucleases: molecular mechanisms and insights into their physiological roles.Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes.Identification of a VapBC toxin-antitoxin system in a thermophilic bacterium Thermus thermophilus HB27.VapC toxins drive cellular dormancy under uranium stress for the extreme thermoacidophile Metallosphaera prunae.Toxins of Prokaryotic Toxin-Antitoxin Systems with Sequence-Specific Endoribonuclease Activity.Structural conservation of the PIN domain active site across all domains of life.The Mycobacterium tuberculosis relBE toxin:antitoxin genes are stress-responsive modules that regulate growth through translation inhibition.MazF ribonucleases promote Mycobacterium tuberculosis drug tolerance and virulence in guinea pigs.Crystal structure of Mycobacterium tuberculosis VapC20 toxin and its interactions with cognate antitoxin, VapB20, suggest a model for toxin-antitoxin assembly.Toxins MazF and MqsR cleave Escherichia coli rRNA precursors at multiple sites.Structural insights into species-specific features of the ribosome from the human pathogen Mycobacterium tuberculosis.Diversity and functionality of plasmid-borne VagCD toxin-antitoxin systems of Klebsiella pneumoniae.Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.Homologous VapC Toxins Inhibit Translation and Cell Growth by Sequence-Specific Cleavage of tRNAfMet.Messing up translation from the start: how AtaT inhibits translation initiation in E. coli.HicA toxin of Escherichia coli derepresses hicAB transcription to selectively produce HicB antitoxin.AtaT blocks translation initiation by N-acetylation of the initiator tRNAfMet.The VapBC1 toxin-antitoxin complex from Mycobacterium tuberculosis: purification, crystallization and X-ray diffraction analysis.The toxin GraT inhibits ribosome biogenesis.Substrate specificity of human MCPIP1 endoribonuclease.
P2860
Q26744373-3D78B62B-AEF3-45DB-92E2-9179BED4B7B7Q26822986-65EBB3B7-B735-4E96-A96D-D7305A3D8B69Q28066978-1A28BF09-5F1C-4D21-9E41-35B37B51D7AEQ28544904-941665C9-C9DD-42E8-B0FF-65998D27F40CQ28601184-C628F062-6C33-44D1-858A-BB650599A03FQ33558196-CE67E776-1571-4FA2-80F3-43A5855B486AQ33878209-3A5C7492-A54F-489C-A5C1-B1359D415B6EQ33927697-818507AF-FFE2-425F-B1CA-2C810BC8A61CQ35842990-962C43D3-BBA4-41AF-8AA6-999764E399BCQ35984251-DDC74DBD-831E-40E9-ADBB-68C7CC9ACC17Q36106467-E93B1610-1AEE-470C-B9EF-FDF41958DA64Q36207778-60B263AD-B96D-4676-A8E5-EFB53B097581Q36443829-2AD4199D-DE61-461D-B624-6BDF1F3A522FQ37264379-FC56003E-FBD4-4559-99CA-C866805E65F0Q37425410-CAF972CB-D9F2-4CC1-B908-BFDC038AE52DQ37522465-78E160D4-42FB-4CBA-8D11-52E6D6EE9520Q37522982-85F2168C-6A4F-4431-86EE-24F7A6DA7A8CQ37670036-44BB8FEF-31E5-4973-A0E0-FA068F687421Q37681030-5A1933C4-81E8-4014-B38E-381BFC2D62AEQ38187662-10A03DE5-6542-46AF-A3C0-0E4C5C814B7CQ38770150-F328CFE8-4493-4E3B-9CDB-0FB816C97C92Q39167588-E5A58A71-DAB7-47BB-A9DF-936DD88FBF7DQ39181653-B070C323-AE24-417C-89C2-D8ABE8369AC9Q39190958-ADD3114E-FABA-4202-BAA2-4070EE67A64AQ39248956-C7670CC4-74F5-4D42-9F6E-FA17656BB7D5Q39309154-AC9F1268-3C09-442D-A245-E6BE70EDB619Q40936733-26A82E32-F8FB-4647-B85D-C23B99D06A19Q41530127-F7819CCB-3970-419D-9134-34956EDE8682Q41990179-1BB07278-9C21-40C7-ACEB-930945033A0CQ45765080-C244859C-74D1-4D22-8F4A-8823038762A1Q46295002-5A1EFAB0-2360-44F6-A3C7-4F149A5AA340Q46428157-754099A9-2A87-4F0E-9FD9-9756656568F8Q47120991-4C4ECB72-9959-4997-836B-7C34CB7747FFQ47434080-EF70D6A2-B08B-4DEB-BC51-B2F736F709D2Q47445659-C89352B1-ADA3-46B4-BCA9-F4F5EBFE0BAFQ48156817-038DB3CB-A912-43C3-B447-ECB76580B2DEQ48336528-F7043D7B-8149-44CE-B375-21DB2956CF68Q51702108-F57E87DA-2020-4AF6-BB06-F1942FAC0BBAQ54251773-5E3656B4-1773-45AD-A367-073C877C5BADQ55075630-E5428751-F4CF-4BDA-82D2-A8806256A4E1
P2860
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
description
2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
@hy
article publié dans Nature Communications
@fr
artículu científicu espublizáu en 2013
@ast
im Januar 2013 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2013/01/01)
@sk
vědecký článek publikovaný v roce 2013
@cs
wetenschappelijk artikel (gepubliceerd op 2013/01/01)
@nl
наукова стаття, опублікована в січні 2013
@uk
name
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@ast
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@en
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@nl
type
label
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@ast
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@en
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@nl
prefLabel
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@ast
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@en
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@nl
P2860
P50
P3181
P356
P1476
VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA
@en
P2093
Alistair K. Brown
P2860
P2888
P3181
P356
10.1038/NCOMMS3796
P407
P577
2013-01-01T00:00:00Z
P5875
P6179
1051963560