Aspartate decarboxylase (PanD) as a new target of pyrazinamide in Mycobacterium tuberculosis
about
A Global Perspective on Pyrazinamide Resistance: Systematic Review and Meta-AnalysisLearning from the past for TB drug discovery in the futureNew antimycobacterial agents in the pre-clinical phase or beyond: recent advances in patent literature (2001-2016).New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in MycobacteriaPyrazinamide and derivatives block ethylene biosynthesis by inhibiting ACC oxidaseA Multinational Analysis of Mutations and Heterogeneity in PZase, RpsA, and PanD Associated with Pyrazinamide Resistance in M/XDR Mycobacterium tuberculosis.In Vivo-Selected Pyrazinoic Acid-Resistant Mycobacterium tuberculosis Strains Harbor Missense Mutations in the Aspartate Decarboxylase PanD and the Unfoldase ClpC1.Uncoupling Environmental pH and Intrabacterial Acidification from Pyrazinamide Susceptibility in Mycobacterium tuberculosisThe effect of growth rate on pyrazinamide activity in Mycobacterium tuberculosis - insights for early bactericidal activity?Long-Chain Fatty Acyl Coenzyme A Ligase FadD2 Mediates Intrinsic Pyrazinamide Resistance in Mycobacterium tuberculosis.High Systemic Exposure of Pyrazinoic Acid Has Limited Antituberculosis Activity in Murine and Rabbit Models of Tuberculosis.Pyrazinamide Is Active against Mycobacterium tuberculosis Cultures at Neutral pH and Low Temperature.Validation of CoaBC as a Bactericidal Target in the Coenzyme A Pathway of Mycobacterium tuberculosis.Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosisPyrazinamide: the importance of uncovering the mechanisms of action in mycobacteria.Fighting an old disease with modern tools: characteristics and molecular detection methods of drug-resistant Mycobacterium tuberculosis.Identification of Novel Efflux Proteins Rv0191, Rv3756c, Rv3008, and Rv1667c Involved in Pyrazinamide Resistance in Mycobacterium tuberculosis.Synthesis of Novel Pyrazinamide Derivatives Based on 3-Chloropyrazine-2-carboxamide and Their Antimicrobial Evaluation.Pyrazinamide Susceptibility and pncA Mutation Profiles of Mycobacterium tuberculosis among Multidrug-Resistant Tuberculosis Patients in Bangladesh.Genetic Determinants of Drug Resistance in Mycobacterium tuberculosis and Their Diagnostic ValueTargeting Phenotypically Tolerant Mycobacterium tuberculosis.Pyrazinoic Acid Inhibits a Bifunctional Enzyme in Mycobacterium tuberculosis.Anti-tubercular Activity of Pyrazinamide is Independent of trans-Translation and RpsA.Mutation in clpC1 encoding an ATP-dependent ATPase involved in protein degradation is associated with pyrazinamide resistance in Mycobacterium tuberculosis.Half of rifampicin-resistant Mycobacterium tuberculosis complex isolated from tuberculosis patients in Sub-Saharan Africa have concomitant resistance to pyrazinamide.Non-pncA Gene-Mutated but Pyrazinamide-Resistant Mycobacterium tuberculosis: Why Is That?Using Reduced Inoculum Densities of Mycobacterium tuberculosis in MGIT Pyrazinamide Susceptibility Testing to Prevent False-Resistant Results and Improve Accuracy: A Multicenter Evaluation.Pyrazinoic Acid Inhibits Mycobacterial Coenzyme A Biosynthesis by Binding to Aspartate Decarboxylase PanD.The Forty-Sixth Euro Congress on Drug Synthesis and Analysis: Snapshot †.Design, Synthesis, Antimycobacterial Evaluation, and In Silico Studies of 3-(Phenylcarbamoyl)-pyrazine-2-carboxylic Acids.Ureidopyrazine Derivatives: Synthesis and Biological Evaluation as Anti-Infectives and Abiotic Elicitors.Update of Antitubercular Prodrugs from a Molecular Perspective: Mechanisms of Action, Bioactivation Pathways, and Associated Resistance.Pyrazinamide Resistance Is Caused by Two Distinct Mechanisms: Prevention of Coenzyme A Depletion and Loss of Virulence Factor Synthesis.Identification of novel mutations in LprG (rv1411c), rv0521,rv3630, rv0010c, ppsC,cyp128 associated with pyrazinoic acid/pyrazinamide resistance in Mycobacterium tuberculosis.Comparing and Validating Machine Learning Models for Mycobacterium tuberculosis Drug Discovery.Targeting the Proteostasis Network for Mycobacterial Drug Discovery.Molecular Targets Related Drug Resistance Mechanisms in MDR-, XDR-, and TDR-Mycobacterium tuberculosis Strains.Drug-resistance patterns of Mycobacterium tuberculosis strains and associated risk factors among multi drug-resistant tuberculosis suspected patients from Ethiopia.Insight into novel clinical mutants of RpsA-S324F, E325K, and G341R of associated with pyrazinamide resistanceDesign, Synthesis and Evaluation of -pyrazinylbenzamides as Potential Antimycobacterial Agents
P2860
Q27011264-1BB52F63-7E33-4DDC-9C95-D5C3A5362097Q27485405-57FAD565-01FE-4346-870C-DDE63948D1DFQ30243915-137A9411-2507-4D82-8319-CF5EA1272419Q33600161-7DA13BEB-D7DE-469F-9E08-AB1F1C48BF80Q33804763-95DCDD4E-98B0-4AB5-A921-67BC02151582Q33812455-2932D89F-DA3A-4E7A-BA3B-4476E06DC1B0Q33912749-F5153EBC-9EBD-4705-BE97-295A40C54393Q34494098-FB44207C-2287-4F24-BAAD-8604907C8481Q36019139-1EED91E6-2566-43CB-9417-AB0535B477DCQ36194929-149E8586-C831-49F3-837A-E36C3AE742E6Q37023104-8241CA65-2485-49CB-AE31-99BBFD4FDEEDQ37120038-1E82CD1C-9189-414F-9BBC-C79412A3D4EFQ37497737-85EAD844-1BCE-4B65-A4D3-4AD80CEAC24AQ37612920-378108B3-CD4D-4378-8A98-238E2098FBFEQ38368943-D4A46999-21D4-403B-869C-573B20E8FF3FQ38545953-5E262A8E-0E51-4B8F-A103-FEFEDB2E90A3Q38674445-F572C96D-D124-42F6-9E8B-EFFC32AC79F3Q38718136-C7562A8C-7986-414E-9904-ED5FD31DBE78Q38718396-B6C2270C-EA67-4AF8-AAF8-92B297DE49D1Q38999525-1BD9D53F-E60E-43FC-B0EB-C443D0C29430Q39149038-6EC04909-22E2-46EE-A5D6-CF7C5B3E5FD6Q40239350-677ED147-1A0D-4D7D-863E-18DC93B68F2EQ41094161-93643540-6C77-454F-AD93-1257E12D6173Q42320288-EABA8561-F403-4605-AD30-6390E5E4E3B1Q43923911-85CA18F8-2E2D-4158-95BE-C3DDD647CEB5Q45223094-6E54FE71-6A44-4FAB-9DD8-D7E0CBBA8FA8Q46765284-4BAE6C8F-9D57-4DA7-B080-A3345EA0BDC9Q47099741-13F08E64-15BE-4532-94F7-59AE053D9847Q47215879-40417503-0F53-4F35-9D42-D60565FD22C8Q48113518-6C6FACDD-0F1C-48C6-9D6C-F44871CADA8FQ48135432-F73596FB-D328-4689-9469-C60E40DF7665Q48331193-794EE1B9-E3C5-4C4A-AC74-614C1493AE97Q49174862-9552ECFB-E36E-4684-8A7B-7CEE87E5609FQ52568630-E1B6A6BB-3401-4968-9B21-5E410F365EB2Q52578227-E77D700E-0E99-48FB-85ED-F6244F8949C2Q52692190-59C80E44-0142-400A-8529-53828729529BQ55091455-2E3779CB-2517-493D-92FE-8D792BB9CF84Q55240979-32AC9C79-FC32-439A-95D8-3E9EB90D38EFQ58583416-D36526C3-F04F-443C-8D0A-B0CC963F41BAQ58691665-2EC31524-A863-461F-8134-B1B23B642A0F
P2860
Aspartate decarboxylase (PanD) as a new target of pyrazinamide in Mycobacterium tuberculosis
description
2014 nî lūn-bûn
@nan
2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Aspartate decarboxylase (PanD) ...... in Mycobacterium tuberculosis
@ast
Aspartate decarboxylase (PanD) ...... in Mycobacterium tuberculosis
@en
Aspartate decarboxylase
@nl
type
label
Aspartate decarboxylase (PanD) ...... in Mycobacterium tuberculosis
@ast
Aspartate decarboxylase (PanD) ...... in Mycobacterium tuberculosis
@en
Aspartate decarboxylase
@nl
prefLabel
Aspartate decarboxylase (PanD) ...... in Mycobacterium tuberculosis
@ast
Aspartate decarboxylase (PanD) ...... in Mycobacterium tuberculosis
@en
Aspartate decarboxylase
@nl
P2093
P2860
P356
P1476
Aspartate decarboxylase (PanD) ...... in Mycobacterium tuberculosis
@en
P2093
Jiazhen Chen
Shuo Zhang
Wanliang Shi
Wenhong Zhang
Xinhua Weng
Ying Zhang
P2860
P356
10.1038/EMI.2014.61
P577
2014-08-13T00:00:00Z