The Effects of One-Point Mutation on the New Delhi Metallo Beta-Lactamase-1 Resistance toward Carbapenem Antibiotics and β-Lactamase Inhibitors: An In Silico …

VT Tran, VH Tran, DN Nguyen, TGS Do, TP Vo… - International Journal of …, 2022 - mdpi.com
Antibiotic resistance has been becoming more and more critical due to bacteria's evolving
hydrolysis enzymes. The NDM-1 enzyme could hydrolyze not only carbapenems but also …

Molecular and computational approaches to understand resistance of New Delhi metallo β-lactamase variants (NDM-1, NDM-4, NDM-5, NDM-6, NDM-7)-producing …

A Ali, D Gupta, G Srivastava, A Sharma… - Journal of Biomolecular …, 2019 - Taylor & Francis
The discovery of NDM-1 and its variants has caused the emergence of antibiotic resistance
in the community and hospital setting, causing major concern for health care across the …

[HTML][HTML] Molecular Modeling and simulation-based identification of inhibitors against new Delhi Metallo-Lactamase 1: Implications for bacterial antibiotic resistance

S Haque, DM Mathkor, AK Johargy, H Faidah… - Journal of King Saud …, 2024 - Elsevier
Abstract Objectives Bacterial infections expressing New Delhi metallo-lactamase-1 (NDM-1)
pose an escalating global threat to healthcare systems. NDM-1 is an enzyme that renders β …

Identification of a potential inhibitor (MCULE-8777613195-0-12) of New Delhi Metallo-β-Lactamase-1 (NDM-1) using in silico and in vitro approaches

G Muteeb, MT Rehman, MF AlAjmi, M Aatif, M Farhan… - Molecules, 2022 - mdpi.com
New Delhi metallo-β-lactamase-1 (NDM-1), expressed in different Gram-negative bacteria,
is a versatile enzyme capable of hydrolyzing β-lactam rings containing antibiotics such as …

[HTML][HTML] Binding selectivity analysis of new delhi metallo-beta-lactamase-1 inhibitors using molecular dynamics simulations: Exploring possibilities for decoding …

S Haque, F Ahmad, DM Mathkor, H Makhdoom… - Journal of Infection and …, 2024 - Elsevier
Abstract Background New Delhi metallo-beta-lactamase-1 (NDM1) confers resistance to
several bacterial species against a broad range of beta-lactam antibiotics and turning them …

Cracking the Code of Antibiotic Resistance OF Klebsiella pneumoniae ST16: A Computational Exploration of Whole Genome Sequences for Beta-lactam Resistance …

AI Faleti, TA Ibisanmi - 2023 - researchsquare.com
Antibiotic resistance is a growing concern in the field of healthcare and medicine. This
research project involves an exploration of the whole genome sequences of Klebsiella …

Identification of a potential inhibitor for New Delhi metallo-β-lactamase 1 (NDM-1) from FDA approved chemical library-a drug repurposing approach to combat …

A Fasim, SS More - Journal of Biomolecular Structure & Dynamics, 2022 - europepmc.org
Superbugs producing New Delhi metallo-β-lactamase 1 (NDM-1) enzyme is a growing
crisis, that is adversely affecting the global health care system. NDM-1 empowers the …

Role of non-active site residues in maintaining New Delhi metallo-β-lactamase-1 (NDM-1) function: an approach of site-directed mutagenesis and docking

A Ali, D Gupta, AU Khan - FEMS microbiology letters, 2021 - academic.oup.com
New Delhi metallo-β-lactamase-1 (NDM-1) has been known to hydrolyze nearly all β-lactam
antibiotics, leading to a multidrug-resistant state. Hence, it is important to study its structure …

[PDF][PDF] An in silico approach to discover potential inhibitors against multi-drug resistant bacteria producing New-Delhi metallo-β-Lactamase 1 (NDM-1) enzyme

H Chetia, DK Sharma, R Sarma… - Int. J. Pharm. Pharm …, 2014 - researchgate.net
ABSTRACT New Delhi Metallo-β-lactamase 1 (NDM-1) is a monomeric, plasmid-encoded
enzyme that can hydrolyze β-lactam antibiotics over a wide range. Presence of this enzyme …

E152A substitution drastically affects NDM-5 activity

G Kumar, B Issa, D Kar, S Biswal… - FEMS Microbiology …, 2017 - academic.oup.com
Abstract New Delhi Metallo beta-lactamase (NDM) is of significant public health concern due
to its enormous potential to hydrolyse all major beta-lactams including carbapenems. Amino …