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Novel inhibitors of Mycobacterium tuberculosis GuaB2 identified by a target based high-throughput phenotypic screen
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Flexible protein–ligand docking by global energy optimization in internal coordinates
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Flexible protein–ligand docking by global energy optimization in internal coordinates
inferredcites →https://doi.org/10.1002/cmdc.201200428openalex-snapshot
Fueling Open‐Source Drug Discovery: 177 Small‐Molecule Leads against Tuberculosis
inferredcites →https://doi.org/10.1002/med.20104openalex-snapshot
Inosine monophosphate dehydrogenase (IMPDH) as a target in drug discovery
inferredcites →https://doi.org/10.1007/s10822-012-9547-0openalex-snapshot
Docking and scoring with ICM: the benchmarking results and strategies for improvement
inferredcites →https://doi.org/10.1016/j.drudis.2010.08.004openalex-snapshot
Ligand efficiency indices for an effective mapping of chemico-biological space: the concept of an atlas-like representation
inferredcites →https://doi.org/10.1016/s0140-6736(98)04022-7openalex-snapshot
Randomised controlled trial of self-supervised and directly observed treatment of tuberculosis
inferredcites →https://doi.org/10.1021/acsinfecdis.6b00102openalex-snapshot
The Inosine Monophosphate Dehydrogenase, GuaB2, Is a Vulnerable New Bactericidal Drug Target for Tuberculosis
inferredcites →https://doi.org/10.1021/acsinfecdis.6b00103openalex-snapshot
Essential but Not Vulnerable: Indazole Sulfonamides Targeting Inosine Monophosphate Dehydrogenase as Potential Leads againstMycobacterium tuberculosis
inferredcites →https://doi.org/10.1021/cr900021wopenalex-snapshot
IMP Dehydrogenase: Structure, Mechanism, and Inhibition
inferredcites →https://doi.org/10.1038/256331a0openalex-snapshot
IMP dehydrogenase, an enzyme linked with proliferation and malignancy
inferredcites →https://doi.org/10.1038/31159openalex-snapshot
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
inferredcites →https://doi.org/10.1038/513481aopenalex-snapshot
Chemistry: Chemical con artists foil drug discovery
inferredcites →https://doi.org/10.1038/nrd4001openalex-snapshot
Advances in the development of new tuberculosis drugs and treatment regimens
inferredcites →https://doi.org/10.1042/bj1830481openalex-snapshot
Inosine 5′-monophosphate dehydrogenase of Escherichia coli. Purification by affinity chromatography, subunit structure and inhibition by guanosine 5′-monophosphate
inferredcites →https://doi.org/10.1073/pnas.231275498openalex-snapshot
Comprehensive identification of conditionally essential genes in mycobacteria
inferredcites →https://doi.org/10.1074/jbc.m808541200openalex-snapshot
A Regulatory Role of the Bateman Domain of IMP Dehydrogenase in Adenylate Nucleotide Biosynthesis
inferredcites →https://doi.org/10.1093/cid/cir889openalex-snapshot
Totally Drug-Resistant Tuberculosis in India
inferredcites →https://doi.org/10.1093/nar/gkt1180openalex-snapshot
PDBe: Protein Data Bank in Europe
inferredcites →https://doi.org/10.1093/nar/gku397openalex-snapshot
PRISM: a web server and repository for prediction of protein–protein interactions and modeling their 3D complexes
inferredcites →https://doi.org/10.1099/mic.0.042549-0openalex-snapshot
Identification of novel diphenyl urea inhibitors of Mt-GuaB2 active against Mycobacterium tuberculosis
inferredcites →https://doi.org/10.1126/science.1106753openalex-snapshot
A Diarylquinoline Drug Active on the ATP Synthase of Mycobacterium tuberculosis
inferredcites →https://doi.org/10.1371/journal.pone.0033886openalex-snapshot
Identification of Novel Mt-Guab2 Inhibitor Series Active against M. tuberculosis
inferredcites →https://doi.org/10.1371/journal.pone.0138976openalex-snapshot
Mycobacterium tuberculosis IMPDH in Complexes with Substrates, Products and Antitubercular Compounds
inferredcites →https://doi.org/10.1378/chest.08-2427openalex-snapshot
Emergence of New Forms of Totally Drug-Resistant Tuberculosis Bacilli
inferredcites →https://doi.org/10.2217/fmb.10.50openalex-snapshot
Tmc207: the First Compound of A New class of Potent Anti-Tuberculosis Drugs
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4765237openalex-extracted
New Synergistic Benzoquinone Scaffolds as Inhibitors of Mycobacterial Cytochrome Bc1 Complex to Treat Multi-Drug Resistant Tuberculosis
inferred← citeshttps://doi.org/10.1002/asia.202200125openalex-snapshot
Mutants of Helicobacter pylori IMPDH: Kinetics and in silico Studies to Determine the Structural and Functional Role of Key Amino Acids
inferred← citeshttps://doi.org/10.1007/978-3-030-05282-9_5openalex-snapshot
In Silico Structure-Based Prediction of Receptor–Ligand Binding Affinity: Current Progress and Challenges
inferred← citeshttps://doi.org/10.1007/978-981-95-3957-4_28openalex-snapshot
Synthetic Biology for Drug Discovery
inferred← citeshttps://doi.org/10.1016/j.bmcl.2018.04.045openalex-snapshot
Hit discovery of Mycobacterium tuberculosis inosine 5′-monophosphate dehydrogenase, GuaB2, inhibitors
inferred← citeshttps://doi.org/10.1016/j.bmcl.2024.130026openalex-snapshot
Discovery of potent dihydro-oxazinoquinolinone inhibitors of GuaB for the treatment of tuberculosis
inferred← citeshttps://doi.org/10.1016/j.copbio.2017.03.023openalex-snapshot
Novel and revisited approaches in antituberculosis drug discovery
inferred← citeshttps://doi.org/10.1016/j.ejmech.2019.04.027openalex-snapshot
Synthesis and Structure–Activity relationship of 1-(5-isoquinolinesulfonyl)piperazine analogues as inhibitors of Mycobacterium tuberculosis IMPDH
inferred← citeshttps://doi.org/10.1016/j.ejmech.2024.116479openalex-snapshot
New synergistic benzoquinone scaffolds as inhibitors of mycobacterial cytochrome bc1 complex to treat multi-drug resistant tuberculosis
inferred← citeshttps://doi.org/10.1016/j.mib.2017.11.017openalex-snapshot
Host–pathogen systems for early drug discovery against tuberculosis
inferred← citeshttps://doi.org/10.1017/s0031182017002037openalex-snapshot
Microbial protein targets: towards understanding and intervention
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.7b01622openalex-snapshot
Fragment-Based Approach to Targeting Inosine-5′-monophosphate Dehydrogenase (IMPDH) from Mycobacterium tuberculosis
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.7b01839openalex-snapshot
Expanding Benzoxazole-Based Inosine 5′-Monophosphate Dehydrogenase (IMPDH) Inhibitor Structure–Activity As Potential Antituberculosis Agents
inferred← citeshttps://doi.org/10.1021/acsinfecdis.3c00463openalex-snapshot
Identification of Chemical Scaffolds Targeting Drug-Resistant and Latent Mycobacterium tuberculosis through High-Throughput Whole-Cell Screening
inferred← citeshttps://doi.org/10.1021/acsinfecdis.6c00350openalex-snapshot
Development of GuaB Inhibitors to Treat Mycobacterium tuberculosis Infection
inferred← citeshttps://doi.org/10.1038/s41467-024-50933-6openalex-snapshot
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase
inferred← citeshttps://doi.org/10.1038/s41557-024-01516-xopenalex-snapshot
Discovery of isoquinoline sulfonamides as allosteric gyrase inhibitors with activity against fluoroquinolone-resistant bacteria
inferred← citeshttps://doi.org/10.1038/s41586-025-09177-7openalex-snapshot
Targeting de novo purine biosynthesis for tuberculosis treatment
inferred← citeshttps://doi.org/10.1038/s41598-017-09642-yopenalex-snapshot
Inhibiting mycobacterial tryptophan synthase by targeting the inter-subunit interface
inferred← citeshttps://doi.org/10.1038/s41598-018-22228-6openalex-snapshot
Antimycobacterial drug discovery using Mycobacteria-infected amoebae identifies anti-infectives and new molecular targets
inferred← citeshttps://doi.org/10.1038/s41598-018-31157-3openalex-snapshot
Identification and characterization of aspartyl-tRNA synthetase inhibitors against Mycobacterium tuberculosis by an integrated whole-cell target-based approach
inferred← citeshttps://doi.org/10.1038/s41598-018-37490-xopenalex-snapshot
Identification of selective inhibitors of Helicobacter pylori IMPDH as a targeted therapy for the infection
inferred← citeshttps://doi.org/10.1080/14756366.2025.2598479openalex-snapshot
Substrate cooperativity shapes competitive inhibitor responses in mycobacterial inosine 5′-monophosphate dehydrogenase
inferred← citeshttps://doi.org/10.1101/2021.08.05.455185openalex-snapshot
The mycobacterial guaB1 gene encodes a guanosine 5’-monophosphate reductase with a cystathione-β-synthase domain
inferred← citeshttps://doi.org/10.1111/febs.16448openalex-snapshot
The mycobacterial guaB1 gene encodes a guanosine 5′‐monophosphate reductase with a cystathionine‐β‐synthase domain
inferred← citeshttps://doi.org/10.1128/jb.00102-24openalex-snapshot
Differential effects of inosine monophosphate dehydrogenase (IMPDH/GuaB) inhibition in Acinetobacter baumannii and Escherichia coli
inferred← citeshttps://doi.org/10.1128/jb.00477-21openalex-snapshot
Union Is Strength: Target-Based and Whole-Cell High-Throughput Screens in Antibacterial Discovery
inferred← citeshttps://doi.org/10.1128/mbio.00897-24openalex-snapshot
Discovery of GuaB inhibitors with efficacy against Acinetobacter baumannii infection
inferred← citeshttps://doi.org/10.3389/fphar.2024.1329011openalex-snapshot
A journey into the regulatory secrets of the de novo purine nucleotide biosynthesis
inferred← citeshttps://doi.org/10.3390/ijms231810669openalex-snapshot
Fragment-Based Drug Discovery against Mycobacteria: The Success and Challenges
inferred← citeshttps://doi.org/10.3390/ijms27114829openalex-snapshot
The Spermidine Synthase Gene as a Reporter of Transcription Inhibition in Escherichia coli
inferred← citeshttps://doi.org/10.5772/intechopen.82374openalex-snapshot
Computational Deorphaning of Mycobacterium tuberculosis Targets
inferred← citeshttps://doi.org/10.70675/2db6eaa8z1907z4401z9f4bzd077bc99bdebopenalex-snapshot
Enzymes de la voie de biosynthèse de novo des nucléotides puriques chez les bactéries : caractérisation et rôle physiologique
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