Research graph
References from In silico analyses of isoniazid and streptomycin resistance-associated mutations in Mycobacterium tuberculosis. Local targets link to admitted publications; unresolved targets remain external evidence.
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Prevalence of antibiotic-resistant pulmonary tuberculosis in bangladesh: a systematic review and meta-analysis
2020 · External reference
Drug resistance mechanisms in mycobacterium tuberculosis
10.3390/antibiotics3030317 · 2014 · External reference
Evidence for expanding the role of streptomycin in the management of drug-resistant Mycobacterium tuberculosis
10.1128/aac.00860-20 · 2020 · External reference
Unresolved reference
External reference
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis
10.1021/bi00026a004 · 1995 · External reference
Unresolved reference
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Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate
10.1074/jbc.274.22.15582 · 1999 · External reference
The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis
10.1038/358591a0 · 1992 · External reference
New insight into the mechanism of action of and resistance to isoniazid: interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP
10.1021/ja073160k · 2007 · External reference
Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis
10.1021/bi061874m · 2006 · External reference
The software that powers scientific illustration
10.1038/d41586-020-01404-7 · 2020 · External reference
Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
10.1126/science.7886450 · 1995 · External reference
Mechanisms of isoniazid resistance in Mycobacterium tuberculosis: enzymatic characterization of enoyl reductase mutants identified in isoniazid-resistant clinical isolates
10.1086/515362 · 1998 · External reference
The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: adduct affinity and drug resistance
10.1073/pnas.2235848100 · 2003 · External reference
In vitro inhibition of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA by isoniazid
10.1128/aac.48.1.242-249.2004 · 2004 · External reference
The biosynthesis of mycolic acids in Mycobacterium tuberculosis relies on multiple specialized elongation complexes interconnected by specific protein-protein interactions
10.1016/j.jmb.2005.09.016 · 2005 · External reference
Protein-protein interactions within the fatty acid Synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability
10.1111/j.1365-2958.2004.04334.x · 2004 · External reference
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid
10.1038/nsmb1089 · 2006 · External reference
Mutations in gidB confer low-level streptomycin resistance in Mycobacterium tuberculosis
10.1128/aac.01814-10 · 2011 · External reference
Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria
10.1111/j.1365-2958.2006.05585.x · 2007 · External reference
rRNA methylation and antibiotic resistance
10.1134/s000629792011005x · 2020 · External reference
The central role of protein S12 in organizing the structure of the decoding site of the ribosome
10.1261/rna.040030.113 · 2013 · External reference
A structural basis for streptomycin-induced misreading of the genetic code
10.1038/ncomms2346 · 2013 · External reference
Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
10.1038/35030019 · 2000 · External reference
Functional role of methylation of G518 of the 16S rRNA 530 loop by GidB in Mycobacterium tuberculosis
10.1128/aac.00905-13 · 2013 · External reference
On the role of steric clashes in methylation control of restriction endonuclease activity
10.1093/nar/gkv1341 · 2016 · External reference
GidB mutation as a phylogenetic marker for Q1 cluster Mycobacterium tuberculosis isolates and intermediate-level streptomycin resistance determinant in Lisbon, Portugal
10.1111/1469-0691.12392 · 2014 · External reference
Mechanisms of streptomycin resistance: selection of mutations in the 16S rRNA gene conferring resistance
10.1128/aac.45.10.2877-2884.2001 · 2001 · External reference
SDM: a server for predicting effects of mutations on protein stability
10.1093/nar/gkx439 · 2017 · External reference
mCSM-lig: quantifying the effects of mutations on protein-small molecule affinity in genetic disease and emergence of drug resistance
10.1038/srep29575 · 2016 · External reference
AlloSigMA 2: paving the way to designing allosteric effectors and to exploring allosteric effects of mutations
10.1093/nar/gkaa338 · 2020 · External reference
AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
10.1002/jcc.21334 · 2010 · External reference
Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables
10.1093/protein/10.1.7 · 1997 · External reference
Structure-based statistical mechanical model accounts for the causality and energetics of allosteric communication
10.1371/journal.pcbi.1004678 · 2016 · External reference
Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis
10.1110/ps.062749007 · 2007 · External reference
Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis
10.1016/j.jsb.2007.04.009 · 2007 · External reference
Crystallographic and pre-steady-state kinetics studies on binding of NADH to wild-type and isoniazid-resistant enoyl-ACP(CoA) reductase enzymes from Mycobacterium tuberculosis
10.1016/j.jmb.2006.03.055 · 2006 · External reference
LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
10.1093/protein/8.2.127 · 1995 · External reference
Crystal structure of the enoyl-ACP reductase of Mycobacterium tuberculosis (InhA) in the apo-form and in complex with the active metabolite of isoniazid pre-formed by a biomimetic approach
10.1016/j.jsb.2015.04.008 · 2015 · External reference
Evaluation of gidB alterations responsible for streptomycin resistance in Mycobacterium tuberculosis
10.1093/jac/dku273 · 2014 · External reference
The protein data bank
10.1093/nar/28.1.235 · 2000 · External reference
Survey of drug resistance associated gene mutations in Mycobacterium tuberculosis, ESKAPE and other bacterial species
10.1038/s41598-020-65766-8 · 2020 · External reference
Investigating the effects of mutations on protein aggregation in the cell
10.1074/jbc.m412951200 · 2005 · External reference
Correlation of levels of folded recombinant p53 in Escherichia coli with thermodynamic stability in vitro
10.1016/j.jmb.2007.06.044 · 2007 · External reference
Stability effects of mutations and protein evolvability
10.1016/j.sbi.2009.08.003 · 2009 · External reference
Using model proteins to quantify the effects of pathogenic mutations in Ig-like proteins
10.1074/jbc.m603593200 · 2006 · External reference
The amino-acid mutational spectrum of human genetic disease
10.1186/gb-2003-4-11-r72 · 2003 · External reference
SNPs, protein structure, and disease
10.1002/humu.22 · 2001 · External reference
Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties
10.1006/jmbi.2001.5255 · 2002 · External reference
Solvent accessibility and purifying selection within proteins of Escherichia coli and Salmonella enterica
10.1093/oxfordjournals.molbev.a026310 · 2000 · External reference
UCSF Chimera--a visualization system for exploratory research and analysis
10.1002/jcc.20084 · 2004 · External reference
