Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection - Wikidata - awgldk - TriplyDB

Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection

Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection

http://www.wikidata.org/entity/Q28480875

about

The application of tetracyclineregulated gene expression systems in the validation of novel drug targets in Mycobacterium tuberculosis An essential nonredundant role for mycobacterial DnaK in native protein folding Mycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of -factor activity by proteolysis Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad Structural Basis of Mycobacterial Inhibition by Cyclomarin A Lassomycin, a Ribosomally Synthesized Cyclic Peptide, Kills Mycobacterium tuberculosis by Targeting the ATP-Dependent Protease ClpC1P1P2 Mycobacterium tuberculosis Hip1 modulates macrophage responses through proteolysis of GroEL2 Towards Selective Mycobacterial ClpP1P2 Inhibitors with Reduced Activity against the Human Proteasome.Bortezomib Warhead-Switch Confers Dual Activity against Mycobacterial Caseinolytic Protease and Proteasome and Selectivity against Human Proteasome.Enhanced specialized transduction using recombineering in Mycobacterium tuberculosis Cloning and characterization of Clp protease proteolytic subunit 2 and its implication in clinical diagnosis of tuberculosis A bacterial toxin inhibits DNA replication elongation through a direct interaction with the β sliding clamp.Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.The C-terminus of ClpC1 of Mycobacterium tuberculosis is crucial for its oligomerization and function The ClpP protease is required for the stress tolerance and biofilm formation in Actinobacillus pleuropneumoniae.Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.Regulated Expression Systems for Mycobacteria and Their Applications Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.The Mycobacterium tuberculosis Clp gene regulator is required for in vitro reactivation from hypoxia-induced dormancy.Protein-coding housekeeping gene Rv2461c can be used as an amplification target in loop-mediated isothermal amplification assay for the detection of Mycobacterium tuberculosis in sputum samples The cyclic peptide ecumicin targeting ClpC1 is active against Mycobacterium tuberculosis in vivo.Post-translational regulation via Clp protease is critical for survival of Mycobacterium tuberculosis.Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity.The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1 Target mechanism-based whole-cell screening identifies bortezomib as an inhibitor of caseinolytic protease in mycobacteria Attenuated Actinobacillus pleuropneumoniae double-deletion mutant S-8∆clpP/apxIIC confers protection against homologous or heterologous strain challenge.Mycobacterium tuberculosis ESAT-6 exhibits a unique membrane-interacting activity that is not found in its ortholog from non-pathogenic Mycobacterium smegmatis.Integration-dependent bacteriophage immunity provides insights into the evolution of genetic switches.Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis.The Protease Locus of Francisella tularensis LVS Is Required for Stress Tolerance and Infection in the Mammalian Host.Chromosomal rearrangements and protein globularity changes in Mycobacterium tuberculosis isolates from cerebrospinal fluid.Mycobacterial Caseinolytic Protease Gene Regulator ClgR Is a Substrate of Caseinolytic Protease.Virulence factors of the Mycobacterium tuberculosis complex Proteases in Mycobacterium tuberculosis pathogenesis: potential as drug targets.Genomic tools to profile antibiotic mode of action.Recently disclosed chemical entities as potential candidates for management of tuberculosis.Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Acyldepsipeptide antibiotics as a potential therapeutic agent against Clostridium difficile recurrent infections.Mycobacterium tuberculosis Prolyl Oligopeptidase Induces In vitro Secretion of Proinflammatory Cytokines by Peritoneal Macrophages.Development of new antituberculosis drugs from natural products.

P2860

Q26795478-272C8C56-3E93-414D-895D-05B6CBF63F3C Q27314706-F8BCDB07-EDBE-40CD-9263-23593E422567 Q27675886-70361A02-774B-4530-A0E2-58878DF42447 Q27678774-1BED7AD7-4102-4A92-B67A-0C7EED7ACA01 Q27679912-7501D655-8085-4DDC-BABF-9B7A5DCF580D Q27682707-1BFF7879-63F8-4C0D-A31A-FC16F0AE83EB Q28538895-B9788F9F-190D-45AA-B4C7-402CD3820D39 Q33601825-939FA51D-5558-4263-8672-6489D67CCD68 Q33607221-802EA62C-1302-408F-A3F7-8A1B81389B61 Q33709564-B9DA08AE-067B-4CC2-934C-0A6B0BFD841A Q34371280-8A30DC24-BCBA-4F63-BA77-556B3E92F5D3 Q34385523-584011F6-0200-46CC-B32F-FE603BB99D70 Q34442361-6D356C04-47BB-48E4-A05C-BAF3F141760B Q34531740-F503D3C5-E839-4FFF-8A51-24C368CB34E7 Q34551568-F454B73B-3E57-4005-9C1F-34927A2A58CB Q34624840-3CFA38D3-3253-4AA1-B256-CC13DF399BDE Q34626585-B5E28046-F031-4255-8C15-8F42ED6A1C7F Q34656348-3B8A4CED-2BE2-4F31-AE22-F63947380DDE Q35002980-F474011D-21AC-4E1A-B7B9-DA71369816DC Q35038408-243518F6-3DBF-4C3A-8F3C-33BD6B98C624 Q35106042-39B0C171-DA2E-4750-AE43-BF56F98BC333 Q35113287-1F8C992A-1393-46E6-BB25-D39A88B6A984 Q35536311-07E03C12-5E32-4FDC-925B-7E018D0176CA Q35620145-247A7DB7-297F-4E6F-96FD-0BE07EED167D Q35620201-EAC5E81D-6AE9-4EC1-9E7A-CE9AE0C0E04C Q36243182-B017D60D-CF7A-49CF-82C7-D4D3F87BAD05 Q36492775-51D74488-7799-4DB4-8609-67493B85ACEF Q36569233-EF535936-03E3-42DA-A1C1-643FAC64B089 Q36755029-1070B5BA-B38B-40EE-9614-54BABF6A6F6A Q36888447-21088B0D-A848-4F28-BBCA-6CF27F1FAE9D Q37282173-3CCCF1B1-6E6B-4842-9281-2FB163C8F08F Q37703346-98D37AA3-00E9-4D01-90FF-82454FE962AA Q38053069-143D9581-0D8A-4D86-92C9-EA7D5E497556 Q38103940-63580D15-2346-4B5A-AB5E-2D3977019A6C Q38195069-0E6A3015-C3D9-4934-BAB8-224C451D2852 Q38547127-340F3876-8DCA-420C-BBBC-E2ABF33AF94D Q38660358-7BA2F3E0-E4F7-44FA-9BAF-1B88DFBFFEAC Q38829284-B21C13BC-0B2B-4066-A1DE-22AB8352EEDF Q38949083-5B693AEC-6304-4172-BA47-347A7CF8E618 Q39019430-67326E56-F54D-4919-9BC4-464926124263

P2860

Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection

http://www.wikidata.org/entity/Q28480875

description

2012 nî lūn-bûn

@nan

2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

name

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@ast

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@en

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@nl

type

label

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@ast

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@en

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@nl

prefLabel

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@ast

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@en

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@nl

P1433

Q28480875-BE0CD9EB-FD57-4CE6-9C36-C6B40B8778DB

P1476

Q28480875-9B058344-F296-470D-92C2-C4375C048F17

P2093

Q28480875-10EB30DF-D248-45B2-B6E6-3BDB5A16CDD4

Q28480875-3027702D-A140-4F5E-865F-867277CDD602

Q28480875-4D0A2C3B-8331-49F6-AB1A-9641304E1754

Q28480875-71791DE1-7FC3-4B82-A2C9-FF341718652B

Q28480875-8C57C081-89C6-4B26-ABBD-2E9CE358DF43

Q28480875-8FED99EB-188B-4628-AE3F-B1CEDE68EF8C

Q28480875-B8199262-1E0A-4602-9995-1FA0A13F4EEA

P2860

Q28480875-0DE4932E-D7DC-48E5-8DA7-5741C843187E

Q28480875-142E7A98-5E1F-4F94-BE35-4654DF6776C8

Q28480875-1D2731B0-CE71-4DDD-8023-3176BEF54C32

Q28480875-2DBBA206-534D-41F6-98BF-C1F60FBA932F

Q28480875-3A0F3848-CCB2-4127-A852-A342D752D0BE

Q28480875-431CC6B8-00B9-4222-9452-994105D0C75E

Q28480875-46E2A9E4-F072-4175-89BE-46CCD0AEF021

Q28480875-4CCB76AB-34FE-4F29-9EBE-A2A2451D8E27

Q28480875-4E8C064A-0C7D-4945-9B91-179A6A5FA81A

Q28480875-4EA951C0-D30C-4ABA-9FF8-976F9CE83CEF

P304

Q28480875-BD5B4C23-4427-41D4-A394-C2F3B835E9DF

P31

Q28480875-354229F2-1237-4A5F-BD7E-57C7C5F69D1B

P3181

Q28480875-46CA9E3F-E756-479D-8DDF-A4EE19C12F3C

P356

Q28480875-490A0FD5-AEA5-4BC6-8FAA-8C284B845A6B

P407

Q28480875-97027818-18D3-4BD9-838B-1244EE7FCA29

P433

Q28480875-8315E92A-90C8-4572-AA07-A5F68EDB28FE

P478

Q28480875-9BEEFAD6-9B86-4AC5-B2ED-F5044F2C1E15

P50

Q28480875-D3E62F6F-069E-457C-AB9F-F372706CC673

P577

Q28480875-68F9668D-2F40-4BD1-BF3C-C10BE9CFD594

P5875

Q28480875-0E1E64AC-3BC1-4E20-A0E8-DE590A389AAB

P698

Q28480875-FD34BDA5-2CAF-47FC-B80E-4CF5EAB34671

P921

Q28480875-D54FD645-1674-4025-A07B-5E2CAB117A22

P932

Q28480875-3F3D56E3-73DB-4735-93A8-341B6072DA9C

P3181

P356

JOURNAL.PPAT.1002511

P1433

P1476

Mycobacterium tuberculosis Clp ...... in vitro and during infection

@en

P2093

Alfred L Goldberg

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

Daniel H F Rubin

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

Eric J Rubin

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

Olga Kandror

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

Ravikiran M Raju

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

Tatos N Akopian

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

Vidhya Krishnamoorthy

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

P2860

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1

The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

Genes required for mycobacterial growth defined by high density mutagenesis

Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis

ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage

Mycobacterium tuberculosis ftsH expression in response to stress and viability

Characterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosis

The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide

Cell cycle control by an essential bacterial two-component signal transduction protein.

P304

e1002511

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

P31

scholarly article

P3181

3415418

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

P356

10.1371/JOURNAL.PPAT.1002511

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

P407

P433

2

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

P478

8

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

P50

Meera Unnikrishnan

P577

2012-02-16T00:00:00Z

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

P5875

221855992

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

P698

22359499

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

P921

Mycobacterium tuberculosis

P932

3280978

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