Results 141 to 150 of about 5,166 (218)

Repurposing the angiotensin II receptor blocker valsartan to inhibit penicillin-binding protein 3 and its mutants in Haemophilus influenzae: a comprehensive in silico approach

Frontiers in Bioinformatics
IntroductionAmpicillin-resistant Haemophilus influenzae (H. influenzae) has been recently designated as a medium-priority bacterial pathogen in 2024 by the World Health Organization (WHO).
Srujal Kacha, Srujal Kacha, Janani Arun, Neelu Nargund, Tushar Joshi, Shalini Mathpal, Sudha Ramaiah, Sudha Ramaiah, Anand Anbarasu, Anand Anbarasu   +9 more
doaj   +1 more source

Additional file 17: of Stationary phase persister formation in Escherichia coli can be suppressed by piperacillin and PBP3 inhibition

, 2019
Table S2. DNA oligonucleotides. (DOCX 17 kb)
Aedo, Sandra, Orman, Mehmet, Brynildsen, Mark   +2 more
openaire   +1 more source

Prevalence and molecular characteristics of β-lactam resistance in non-typeable Haemophilus influenzae isolates in Korea

Annals of Clinical Microbiology
Background: Haemophilus influenzae is the causative pathogen for various infectious diseases, such as respiratory infections, otitis media, sinusitis, and meningitis.
Eun-Young Kim, Yeon Chan Choi, Hyeon Jin Choi, Si Hyun Kim, Jihyun Cho, Seok Hoon Jeong, Dokyun Kim, Hyun Soo Kim, Soo Hyun Kim, Young Ah Kim, Young Ree Kim, Nam Hee Ryoo, Jong Hee Shin, Kyeong Seob Shin, Young Uh, Jeong Hwan Shin   +15 more
doaj   +1 more source

Characterization of Haemophilus influenzae Strains with Non-Enzymatic Resistance to β-Lactam Antibiotics Caused by Mutations in the PBP3 Gene in the Czech Republic in 2010–2018 [PDF]

, 2021
Vladislav Jakubů, Lucia Mališová, Martin Musílek, Katarína Pomorská, Helena Žemličková   +4 more
openalex   +1 more source

The role of GpsB in Staphylococcus aureus cell morphogenesis

mBio
For decades, cells of the Gram-positive bacterial pathogen Staphylococcus aureus were thought to lack a dedicated elongation machinery. However, S.
Sara F. Costa, Bruno M. Saraiva, Helena Veiga, Leonor B. Marques, Simon Schäper, Marta Sporniak, Daniel E. Vega, Ana M. Jorge, Andreia M. Duarte, António D. Brito, Andreia C. Tavares, Patricia Reed, Mariana G. Pinho   +12 more
doaj   +1 more source

Additional file 11: of Stationary phase persister formation in Escherichia coli can be suppressed by piperacillin and PBP3 inhibition

, 2019
Sandra Aedo, Mehmet A. Orman, Mark P. Brynildsen   +2 more
openalex   +1 more source

Biophysical and biochemical studies of penicillin binding proteins and novel PBP3 inhibitors [PDF]

Antimicrobial resistance presents a worrying and growing threat to modern medicine. Combatting this challenge requires the discovery of new antimicrobial compounds, which are insensitive to current resistance pathways. One of the most important classes of antibiotics, β-lactams, target penicillin binding proteins (PBPs), a family of enzymes that ...
openaire  

Identifikasi Interaksi Molekuler Peptida Antimikrobial dari Lendir Kulit Ikan Lele Kuning (Pelteobagrus fulvidraco) terhadap Penicillin-Binding Protein 3 (PBP3) pada Escherichia coli secara In silico

, 2020
Taufik Muhammad Fakih, Mentari Luthfika Dewi   +1 more
openalex   +1 more source

In-vitro and In-silico Study of Bioactive Compounds from Coccocarpia erythroxyli as Inhibitors Targeting PBP3 (6ILE) for Antibacterial Applications

Trends in Sciences
Lichens are recognized as sources of diverse bioactive metabolites with potential antibacterial properties. This study evaluated the antibacterial activity of Coccocarpia erythroxyli (Spreng.) Swinscow & Krog and its interaction with Penicillin-Binding Protein 3 (PBP3, PDB ID: 6I1E). Methanol extracts of C.
Oky Kusuma Atni, Erman Munir, Nursahara Pasaribu   +2 more
openaire   +1 more source

Usual and unusual antibacterial effects of quinolones [PDF]

, 2017
Recently documented antibacterial effects of quinolones are reviewed. DNA gyrase is most likely to be the primary target site for these agents. Quinolones rapidly kill susceptible bacteria; the mechanisms of the bactericidal activity, still poorly ...
Furet, Y. X., Pechère, J.-C
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