Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis. - sprookjes - yvandenbroek - TriplyDB

Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis.

Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis.

http://www.wikidata.org/entity/Q27646579

about

targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis Striking the Right Balance Determines TB or Not TB Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly Rv2969c, essential for optimal growth inMycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases Evidence that phosphorylation of threonine in the GT motif triggers activation of PknA, a eukaryotic-type serine/threonine kinase from Mycobacterium tuberculosis Proteins with complex architecture as potential targets for drug design: a case study of Mycobacterium tuberculosis Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G Mycobacterium tuberculosis protein kinase K enables growth adaptation through translation control Insights into protein kinase regulation and inhibition by large scale structural comparison Exploring prospects of novel drugs for tuberculosis.RNA interference in J774 macrophages reveals a role for coronin 1 in mycobacterial trafficking but not in actin-dependent processes.8-pCPT-cGMP stimulates alphabetagamma-ENaC activity in oocytes as an external ligand requiring specific nucleotide moieties PknG senses amino acid availability to control metabolism and virulence of Mycobacterium tuberculosis.Biochemical and spatial coincidence in the provisional Ser/Thr protein kinase interaction network of Mycobacterium tuberculosis.Functional and genomic analyses of alpha-solenoid proteins.Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe-S center Insights from the molecular docking of withanolide derivatives to the target protein PknG from Mycobacterium tuberculosis.A redox regulatory system critical for mycobacterial survival in macrophages and biofilm development.Distinct Responses of Mycobacterium smegmatis to Exposure to Low and High Levels of Hydrogen Peroxide An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase Molecular mechanisms of host-pathogen interactions and their potential for the discovery of new drug targets Differential expression of a virulence factor in pathogenic and non-pathogenic mycobacteria.Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host.The Gewald multicomponent reaction.Eukaryote-like serine/threonine kinases and phosphatases in bacteria.Role of mycobacteria effectors in phagosome maturation blockage and new drug targets discovery.Elimination of intracellularly residing Mycobacterium tuberculosis through targeting of host and bacterial signaling mechanisms.Tetratricopeptide repeat motifs in the world of bacterial pathogens: role in virulence mechanisms.Bacterial cell division regulation by Ser/Thr kinases: a structural perspective New insights into the interaction of Mycobacterium tuberculosis and human macrophages.Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G.An insight into future antibacterial therapy.Protein Kinase G confers survival advantage to Mycobacterium tuberculosis during latency like conditions.Thiol-based redox modulation of a cyanobacterial eukaryotic-type serine/threonine kinase required for oxidative stress tolerance.New Test System for Serine/Threonine Protein Kinase Inhibitors Screening: E. coli APHVIII/Pk25 design Biochemical and functional characterizations of tyrosine phosphatases from pathogenic and nonpathogenic mycobacteria: indication of phenyl cyclopropyl methyl-/phenyl butenyl azoles as tyrosine phosphatase inhibitors.Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G.

P2860

Q21202793-03259088-5DE4-44C2-A90D-AB142DFA234E Q27001010-6BA3297B-B649-4740-BC5C-5F75314D8A94 Q27652901-E3535678-9749-4945-8937-EF57B19C978F Q27670972-15E3C6D2-A58A-49D5-8B34-0E560EAAFA38 Q27680167-DE41E57C-34E5-4D4B-9FCF-51EF361F339D Q27697968-6EB615FE-89A1-4F4F-A76F-2841172D421A Q28479221-379FB1E7-5961-4AF3-ACD6-BD93F71BE082 Q28487492-CD5F9CA9-D124-4209-8E36-D461E2566728 Q28487634-1CC76BE6-236B-4C82-82BD-2B45F207D91E Q30381908-DAA665DB-96CB-4908-837E-A17A2A1F30DA Q30421213-F5F318D0-B567-4F07-8F6B-4A6E34CC431A Q30481387-B93B532D-88A9-4637-ABCD-A0EDAAC827B7 Q33655686-CC9F8EC5-4B0F-4B3A-84EE-8F9B5CF4053C Q33739457-D5D5C9A1-B612-40F5-A6E2-030D13A7BC26 Q33946952-BB215DC8-D705-4792-B8ED-3A6E5E6B34B1 Q34039121-1C0EAE4E-B716-4BCE-BF88-1367D99E8F01 Q34565203-608D0B12-15C1-4AB2-BE15-D3C072AB7615 Q34781265-E46C80F0-18A9-4232-A76D-3A6E880E9E1A Q35202985-04773D2B-8581-4D3C-A798-EA4C106B7541 Q35605459-BDD8E65A-279D-4138-9802-09268A28B83D Q35725724-8FA80C21-2C83-40DE-B55B-5B6D3EDBF975 Q35860669-73C457A1-9019-465D-9B05-9DAB86E7A624 Q36283574-DC79ED45-28F2-48C9-826F-6F46E610B806 Q37089988-E7BFF7B1-2338-45D6-98BB-A17BF90FAB7A Q37444940-747B40FB-89D4-445E-BA6E-503217F40130 Q37448076-9B48BF73-7DAF-45FA-BF22-D518D89170B2 Q37700274-8F10DBED-78A3-4957-9064-34261AFE5EE2 Q37849482-0AD97CCB-D94B-46C4-9251-A6AD3CAB6B73 Q37890318-C3FDF9E7-015C-419F-BEE6-ECFC9EA29E2C Q38056148-53351A32-83CF-4C63-8FAD-903795FE0E96 Q38069528-9FBC2DB0-5A15-4C25-8F2F-68C91822706B Q38072994-8D04952C-3321-4E22-A1BC-31CCC17AAFFB Q38206868-2C12A6C4-082F-4137-ACF7-9981C5E1EEC3 Q39218676-E7171CE0-FD17-4076-B2B7-68CC3473983A Q39528561-BE496DF8-F5B9-4515-A153-E4B59D10FF28 Q40087605-10695DEF-7BE4-452C-AE1F-62562AAF032D Q41821032-D9C9D4A8-D42C-402A-BFF2-E9D785CE6B0E Q42153115-FCA2AFB9-2B51-4D9B-89E3-F7D49EBDDD60 Q46762736-1CA11D7C-B6FC-4677-8A2B-E3B4ACA68154 Q48353158-703D18ED-134C-4C5D-91DE-5844C345CE85

P2860

Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis.

http://www.wikidata.org/entity/Q27646579

description

2007 nî lūn-bûn

@nan

2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Structural basis for the speci ...... of Mycobacterium tuberculosis

@nl

Structural basis for the speci ...... of Mycobacterium tuberculosis.

@ast

Structural basis for the speci ...... of Mycobacterium tuberculosis.

@en

type

label

Structural basis for the speci ...... of Mycobacterium tuberculosis

@nl

Structural basis for the speci ...... of Mycobacterium tuberculosis.

@ast

Structural basis for the speci ...... of Mycobacterium tuberculosis.

@en

prefLabel

Structural basis for the speci ...... of Mycobacterium tuberculosis

@nl

Structural basis for the speci ...... of Mycobacterium tuberculosis.

@ast

Structural basis for the speci ...... of Mycobacterium tuberculosis.

@en

P1433

Q27646579-3F1FAC9B-C3AF-46DA-A337-CA44AE52742A

P1476

Q27646579-36BCCE37-3A28-4731-96D0-3D4F5F317034

P2093

Q27646579-37371E85-8CBD-4A4D-B50D-DE66EBEA47AE

Q27646579-49EE65E7-65CA-47EB-A96F-AAA89053D35E

Q27646579-6307D610-C256-45C8-BE76-856083972A97

Q27646579-B84ED578-084A-4E3A-921C-D97E29BBC847

Q27646579-D014A1D7-02DE-4443-9C9B-43CF739ECAE6

Q27646579-E5DC00C4-60A3-49C7-A225-669B4504085F

P2860

Q27646579-0C5E16C9-C752-45F7-B4BB-472F5A29CB17

Q27646579-1D265A5E-94B6-42DD-A34A-F4E1B9F48967

Q27646579-2BB20038-250F-432C-8618-73F036D0D33B

Q27646579-2FB08C0F-BBEF-4A09-A339-ED7B8B0EC0AE

Q27646579-3DB4ADE2-A326-42A8-A65A-42656ECF5DED

Q27646579-410FB5ED-3A9B-4064-830F-A67F5068ABF8

Q27646579-5128A3B3-6651-4BFD-9F5A-1FD7AB073289

Q27646579-51531B7E-365A-48FC-B58C-6065A4584AEC

Q27646579-5AE841EE-7607-4E66-8661-309CFC336818

Q27646579-5B1ACD62-FBDA-4940-A3D2-825543E13283

P304

Q27646579-92F945DE-82BF-48DE-A513-3D65E40EB5BA

P31

Q27646579-31B0C390-33C6-4C04-B11A-18B5264D2463

P356

Q27646579-53B03DCE-A623-4B60-9CB5-453C44CD49D7

P407

Q27646579-6DCC534C-32E0-4FD5-8472-E3C7DDAFDF46

P433

Q27646579-36ECCB8A-D000-4B2B-89D4-30D6D054C820

P478

Q27646579-B51DC3F3-7797-484B-8BCD-AA0C9AE179ED

P50

Q27646579-492CD109-E253-44FF-99C5-E9377FC49F95

Q27646579-FDDE8919-80ED-4A63-8A1E-220E11A70BAB

P577

Q27646579-9CE37766-608B-43DE-B42F-5BED29BEA138

P5875

Q27646579-5A82F1FF-4F0F-4A84-A020-6DCB6E863F15

P698

Q27646579-1546A375-9851-4736-ABE3-C758E2C27709

P921

Q27646579-1042CEA5-E4B0-48FB-B5C7-0AAE744ACE9D

Q27646579-2159EDC1-2412-4462-B194-DEE5F1CD357E

P932

Q27646579-E32CCCBF-4A39-4A46-8779-74498151BE3E

P356

PNAS.0702842104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structural basis for the speci ...... of Mycobacterium tuberculosis.

@en

P2093

Fritz Winkler

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

Gabriele Kunz

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

Nicole Scherr

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

Philipp Mueller

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

Rajesh Jayachandran

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

Srinivas Honnappa

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

P2860

Massive gene decay in the leprosy bacillus

The protein kinase complement of the human genome

Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases

Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis

Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

The conformational plasticity of protein kinases

Protein kinase G from pathogenic mycobacteria promotes survival within macrophages

TPR proteins: the versatile helix

Active and inactive protein kinases: structural basis for regulation

Mycobacterium tuberculosis: here today, and here tomorrow

P304

12151-12156

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

P31

scholarly article

P356

10.1073/PNAS.0702842104

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

P407

P433

29

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

P478

104

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

P50

Michel O Steinmetz

P577

2007-07-06T00:00:00Z

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

P5875

6220487

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

P698

17616581

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

P921

Mycobacterium tuberculosis

P932

1924570

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