Cargando…

In vivo evaluation of Clostridioides difficile enoyl-ACP reductase II (FabK) Inhibition by phenylimidazole unveils a promising narrow-spectrum antimicrobial strategy

Clostridioides difficile infection (CDI) is a leading cause of hospital-acquired diarrhea, which often stem from disruption of the gut microbiota by broad-spectrum antibiotics. The increasing prevalence of antibiotic-resistant C. difficile strains, combined with disappointing clinical trials results...

Descripción completa

Detalles Bibliográficos
Autores principales:	Dureja, Chetna, Rutherford, Jacob T., Pavel, Fahad B. A., Norseeda, Krissada, Prah, Isaac, Sun, Dianqing, Hevener, Kirk E., Hurdle, Julian G.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Cold Spring Harbor Laboratory 2023
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10543012/ https://www.ncbi.nlm.nih.gov/pubmed/37790427 http://dx.doi.org/10.1101/2023.09.22.559005

Ejemplares similares

1233. Identification of Novel Inhibitors of Clostridioides difficile Enoyl-Reductase II (FabK) by High-Throughput Virtual and Experimental Screening
por: Wahrmund, Rebecca D, et al.
Publicado: (2020)

Determination of the Crystal Structure and Active Residues of FabV, the Enoyl-ACP Reductase from Xanthomonas oryzae
por: Li, He, et al.
Publicado: (2011)

Pharmacophore and Molecular Docking Guided 3D-QSAR Study of Bacterial Enoyl-ACP Reductase (FabI) Inhibitors
por: Lu, Xiaoyun, et al.
Publicado: (2012)

Correlating drug–target kinetics and in vivo pharmacodynamics: long residence time inhibitors of the FabI enoyl-ACP reductase
por: Daryaee, Fereidoon, et al.
Publicado: (2016)

380. A molecular epidemiological exploration of reduced vancomycin susceptibility in Clostridioides difficile
por: Eubank, Taryn A, et al.
Publicado: (2022)

Bacterial Enoyl-Reductases: The Ever-Growing List of Fabs, Their Mechanisms and Inhibition
por: Hopf, Fernanda S. M., et al.
Publicado: (2022)

Pyrrolyl Pyrazoline Carbaldehydes as Enoyl-ACP Reductase Inhibitors: Design, Synthesis and Antitubercular Activity
por: Dixit, Sheshagiri R., et al.
Publicado: (2017)

Unsaturated fatty acid synthesis in Enterococcus faecalis requires a specific enoyl‐ACP reductase
por: Dong, Huijuan, et al.
Publicado: (2022)

Structure-based identification of novel inhibitors targeting the enoyl-ACP reductase enzyme of Acinetobacter baumannii
por: Khan, Shama, et al.
Publicado: (2023)

2-Phenylimidazole dihydrogen phosphate phosphoric acid
por: Xia, Dao-Cheng, et al.
Publicado: (2010)

Shewanella oneidensis FabB: A β-ketoacyl-ACP Synthase That Works with C16:1-ACP
por: Luo, Qixia, et al.
Publicado: (2016)

Decoding a cryptic mechanism of metronidazole resistance among globally disseminated fluoroquinolone-resistant Clostridioides difficile
por: Olaitan, Abiola O., et al.
Publicado: (2023)

Removal of p-Nitrophenol by Adsorption with 2-Phenylimidazole-Modified ZIF-8
por: Zhao, Yu, et al.
Publicado: (2023)

QSAR and Molecular Docking Studies of Oxadiazole-Ligated Pyrrole Derivatives as Enoyl-ACP (CoA) Reductase Inhibitors
por: Asgaonkar, Kalyani D., et al.
Publicado: (2014)

A Structural and Energetic Model for the Slow-Onset Inhibition of the Mycobacterium tuberculosis Enoyl-ACP Reductase InhA
por: Li, Huei-Jiun, et al.
Publicado: (2014)

In Silico Repositioning of Cannabigerol as a Novel Inhibitor of the Enoyl Acyl Carrier Protein (ACP) Reductase (InhA)
por: Pinzi, Luca, et al.
Publicado: (2019)

Functional Characterization of Triclosan-Resistant Enoyl-acyl-carrier Protein Reductase (FabV) in Pseudomonas aeruginosa
por: Huang, Yong-Heng, et al.
Publicado: (2016)

Functional, thermodynamics, structural and biological studies of in silico-identified inhibitors of Mycobacterium tuberculosis enoyl-ACP(CoA) reductase enzyme
por: Martinelli, Leonardo K. B., et al.
Publicado: (2017)

Removal of Phosphate by Adsorption with 2-Phenylimidazole-Modified Porous ZIF-8: Powder and Chitosan Spheres
por: Zhao, Yu, et al.
Publicado: (2023)

Observed crowding effects on Mycobacterium tuberculosis 2-trans-enoyl-ACP (CoA) reductase enzyme activity are not due to excluded volume only
por: Rotta, Mariane, et al.
Publicado: (2017)

Review of Platensimycin and Platencin: Inhibitors of β-Ketoacyl-acyl Carrier Protein (ACP) Synthase III (FabH)
por: Shang, Ruofeng, et al.
Publicado: (2015)

Aqueous Molecular Dynamics Simulations of the M. tuberculosis Enoyl-ACP Reductase-NADH System and Its Complex with a Substrate Mimic or Diphenyl Ethers Inhibitors
por: da Silva Lima, Camilo Henrique, et al.
Publicado: (2015)

Synthesis and Antimicrobial Activity Screening of Piperazines Bearing N,N′-Bis(1,3,4-thiadiazole) Moiety as Probable Enoyl-ACP Reductase Inhibitors
por: Omar, Alaa Z., et al.
Publicado: (2022)

A novel 3‐oxoacyl‐ACP reductase (FabG3) is involved in the xanthomonadin biosynthesis of Xanthomonas campestris pv. campestris
por: Yu, Yonghong, et al.
Publicado: (2019)

Escherichia coli FabG 3-ketoacyl-ACP reductase proteins lacking the assigned catalytic triad residues are active enzymes
por: Hu, Zhe, et al.
Publicado: (2021)

Improved chemical and isotopic labeling of biomembranes in Bacillus subtilis by leveraging CRISPRi inhibition of beta-ketoacyl-ACP synthase (fabF)
por: Nickels, Jonathan D., et al.
Publicado: (2022)

Crystal structure of FabZ-ACP complex reveals a dynamic seesaw-like catalytic mechanism of dehydratase in fatty acid biosynthesis
por: Zhang, Lin, et al.
Publicado: (2016)

Modulation of Medium-Chain Fatty Acid Synthesis in Synechococcus sp. PCC 7002 by Replacing FabH with a Chaetoceros Ketoacyl-ACP Synthase
por: Gu, Huiya, et al.
Publicado: (2016)

ACP basic statistics = ACP, statistiques de base.
Publicado: (1985)

A novel circuit overrides Adr 1p control during expression of Saccharomyces cerevisiae 2-trans-enoyl-ACP reductase Etr 1p of mitochondrial type 2 fatty acid synthase
por: Gurvitz, Aner
Publicado: (2009)

Single chain Fab (scFab) fragment
por: Hust, Michael, et al.
Publicado: (2007)

GCNCPR-ACPs: a novel graph convolution network method for ACPs prediction
por: Wu, Xiujin, et al.
Publicado: (2022)

Fractionation of Fab glycosylated immunoglobulin G with concanavalin A chromatography unveils new structural properties of the molecule
por: Huang, Tao, et al.
Publicado: (2016)

Identification of 2-Aminothiazole-4-Carboxylate Derivatives Active against Mycobacterium tuberculosis H(37)R(v) and the β-Ketoacyl-ACP Synthase mtFabH
por: Al-Balas, Qosay, et al.
Publicado: (2009)

Progress in the Discovery of Treatments for C. difficile Infection: A Clinical and Medicinal Chemistry Review
por: Tsutsumi, Lissa S., et al.
Publicado: (2014)

Genetic Mechanisms of Vancomycin Resistance in Clostridioides difficile: A Systematic Review
por: Eubank, Taryn A., et al.
Publicado: (2022)

DLFF-ACP: prediction of ACPs based on deep learning and multi-view features fusion
por: Cao, Ruifen, et al.
Publicado: (2021)

Synthesis, Molecular Docking Study, and Biological Evaluation of New 4-(2,5-Dimethyl-1H-pyrrol-1-yl)-N’-(2-(substituted)acetyl)benzohydrazides as Dual Enoyl ACP Reductase and DHFR Enzyme Inhibitors
por: Mahnashi, Mater H., et al.
Publicado: (2023)

ACP medicine : a publication of the American College of Physicians /
Publicado: (2004)

Interrogation of Essentiality in the Reconstructed Haemophilus influenzae Metabolic Network Identifies Lipid Metabolism Antimicrobial Targets: Preclinical Evaluation of a FabH β-Ketoacyl-ACP Synthase Inhibitor
por: López-López, Nahikari, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_87h4po42ma82jvjtu44avm4k96