RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB. - Wikidata - awgldk - TriplyDB

RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB.

RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB.

http://www.wikidata.org/entity/Q33615888

about

Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems The tmRNA ribosome-rescue system Toxin-antitoxin systems: Biology, identification, and application The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy The axe-txe complex of Enterococcus faecium presents a multilayered mode of toxin-antitoxin gene expression regulation Molecular mechanism governing ratio-dependent transcription regulation in the ccdAB operon.Three new RelE-homologous mRNA interferases of Escherichia coli differentially induced by environmental stresses.sRNA and cis-antisense sRNA identification in Staphylococcus aureus highlights an unusual sRNA gene cluster with one encoding a secreted peptide Characterization of Escherichia coli dinJ-yafQ toxin-antitoxin system using insights from mutagenesis data Integrated transcriptomic and proteomic analysis of the bile stress response in a centenarian-originated probiotic Bifidobacterium longum BBMN68 Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis The bacterial translation stress response.The three vibrio cholerae chromosome II-encoded ParE toxins degrade chromosome I following loss of chromosome II Key players in the genetic switch of bacteriophage TP901-1 Functional and structural analysis of HicA3-HicB3, a novel toxin-antitoxin system of Yersinia pestis Conditional cooperativity of toxin - antitoxin regulation can mediate bistability between growth and dormancy.A general model for toxin-antitoxin module dynamics can explain persister cell formation in E. coli.TNF Induction of NF-κB RelB Enhances RANKL-Induced Osteoclastogenesis by Promoting Inflammatory Macrophage Differentiation but also Limits It through Suppression of NFATc1 Expression One cannot rule them all: Are bacterial toxins-antitoxins druggable?Dual Role of a Biosynthetic Enzyme, CysK, in Contact Dependent Growth Inhibition in Bacteria.Conditional cooperativity in toxin-antitoxin regulation prevents random toxin activation and promotes fast translational recovery.The Escherichia coli toxin MqsR destabilizes the transcriptional repression complex formed between the antitoxin MqsA and the mqsRA operon promoter.Bacterial toxin RelE: a highly efficient ribonuclease with exquisite substrate specificity using atypical catalytic residues Regulating toxin-antitoxin expression: controlled detonation of intracellular molecular timebombs Artificial activation of toxin-antitoxin systems as an antibacterial strategy Interaction of Type IV Toxin/Antitoxin Systems in Cryptic Prophages of Escherichia coli K-12.Toxins-antitoxins: diversity, evolution and function.Chromosomal bacterial type II toxin-antitoxin systems.Toxin-antitoxin genes of the Gram-positive pathogen Streptococcus pneumoniae: so few and yet so many.mazEF-mediated programmed cell death in bacteria: "what is this?".The ClpXP protease is responsible for the degradation of the Epsilon antidote to the Zeta toxin of the streptococcal pSM19035 plasmid.Functional annotation of a novel toxin-antitoxin system Xn-RelT of Xenorhabdus nematophila; a combined in silico and in vitro approach.Hypothesis: type I toxin-antitoxin genes enter the persistence field-a feedback mechanism explaining membrane homoeostasis.Stability of the GraA Antitoxin Depends on Growth Phase, ATP Level, and Global Regulator MexT Unrelated toxin-antitoxin systems cooperate to induce persistence.Mechanisms for Differential Protein Production in Toxin-Antitoxin Systems.Association between toxin-antitoxin systems and biofilm formation Transition State Charge Stabilization and Acid-Base Catalysis of mRNA Cleavage by the Endoribonuclease RelE.

P2860

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P2860

RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB.

http://www.wikidata.org/entity/Q33615888

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

RelB and RelE of Escherichia c ...... bon-helix-helix motif in RelB.

@ast

RelB and RelE of Escherichia c ...... bon-helix-helix motif in RelB.

@en

type

label

RelB and RelE of Escherichia c ...... bon-helix-helix motif in RelB.

@ast

RelB and RelE of Escherichia c ...... bon-helix-helix motif in RelB.

@en

prefLabel

RelB and RelE of Escherichia c ...... bon-helix-helix motif in RelB.

@ast

RelB and RelE of Escherichia c ...... bon-helix-helix motif in RelB.

@en

P1433

Q33615888-A55BCCDC-363D-421C-9576-8453B6B47601

P1476

Q33615888-2B5D601A-A36F-4EF1-B49F-9F3F1A6D1B5A

P2093

Q33615888-2E364184-5470-4ECA-B1EE-F5FD3342694A

P2860

Q33615888-01BD5CB4-7C98-4C67-88F7-AACC8F3F78B1

Q33615888-09E75C5E-D5BF-4F6C-BA22-0DB67CA16D3F

Q33615888-0C7870E1-1353-4684-BB45-4C8EB944A79E

Q33615888-0CCAA087-8D93-4C8D-A506-464064F1826D

Q33615888-0D66C02F-DBEC-4199-8AC1-3222D312CF79

Q33615888-0E076141-EF1B-4E9F-A9CD-0E8E13EBEAF3

Q33615888-0E80EB2E-AD35-474D-BE6C-F79C5128863B

Q33615888-1936F322-E5DB-49B8-A75D-D0A38CB0F46B

Q33615888-1BD403E6-578E-4AAB-83C9-AC35FBF2A752

Q33615888-2514FA66-3048-4A30-A403-62B150EEA100

P304

Q33615888-D0597C56-2E83-461C-B454-04C97CEE61AF

P31

Q33615888-6DCE5B2C-59B5-467B-A656-FFEEBC3747D5

P356

Q33615888-8E2BF386-35B2-445A-832C-D87FEDCE44C5

P433

Q33615888-C042F37F-C4B6-4009-8103-FDD0F52D0B29

P478

Q33615888-85B92050-B188-4782-8548-9EAEC606A454

P50

Q33615888-2855ABA5-9D74-49F3-9708-788BF520E67C

Q33615888-E2683E91-1E49-4AEC-BE1A-B71CE33AE3E4

P577

Q33615888-52A18DD7-4B88-4786-A89E-C552ED5C6B26

P5875

Q33615888-0D821086-67A8-41A4-B8D4-BB65FD034F9E

P698

Q33615888-8476C00D-BE33-42FF-A505-B414FEBA6FDB

P921

Q33615888-B1F33007-6883-41A7-B4DC-856324CD1C73

P932

Q33615888-46C74514-59C5-43F1-B2F3-2CA1B51F18B7

P356

J.JMB.2009.09.006

P1433

Journal of Molecular Biology

P1476

RelB and RelE of Escherichia c ...... bon-helix-helix motif in RelB.

@en

P2093

Jonas Borch

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

P2860

RelE, a global inhibitor of translation, is activated during nutritional stress

An Escherichia coli chromosomal "addiction module" regulated by guanosine [corrected] 3',5'-bispyrophosphate: a model for programmed bacterial cell death

Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition

Crystal structure of the intrinsically flexible addiction antidote MazE

Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae

Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module

Nuclear magnetic resonance solution structure of the Arc repressor using relaxation matrix calculations

DNA recognition by beta-sheets in the Arc repressor-operator crystal structure

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

Percolation of the phd repressor-operator interface.

P304

183-196

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

P31

scholarly article

P356

10.1016/J.JMB.2009.09.006

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

P433

2

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

P478

394

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

P50

Martin Overgaard

P577

2009-09-08T00:00:00Z

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

P5875

26805728

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

P698

19747491

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P921

Escherichia coli

P932

2812701

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