ArticleBiomolecules2019
Comparative Structural Analysis of Different Mycobacteriophage-Derived Mycolylarabinogalactan Esterases (Lysin B).
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- Exploring the molecular properties and bactericidal potential of Lysin B from mycobacteriophage WXIN.BMC microbiology · 2026Article
- Functional and Structural Insights into Lipases Associated with Fruit Lipid Accumulation inBiomolecules · 2026Article
- Combined experimental and in silico elucidation of KP27 endolysin reveals a phage derived antibacterial with pH and thermal robustness.Scientific reports · 2025Article
- Next-generation antimicrobials: A review of phage lysins as precision weapons against drug-resistant pathogens.Virulence · 2025Review
- Mining versatile feruloyl esterases: phylogenetic classification, structural features, and deep learning model.Bioresources and bioprocessing · 2025Article
- Discovery and characterization of a novel LysinB from F2 sub-cluster mycobacteriophage RitSun.Scientific reports · 2024Article
- Exploring the Enzymatic and Antibacterial Activities of Novel Mycobacteriophage Lysin B Enzymes.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacteriophage endolysins have emerged as a potential alternative to the current antimycobacterial agents. This study focuses on mycolylarabinogalactan hydrolase (LysB) enzymes of the α/β-hydrolase family, which disrupt the unique mycolic acid layer of mycobacterium cell wall. Multiple sequence alignment and structural analysis studies showed LysB-D29, the only enzyme with a solved three-dimensional structure, to share several common features with esterases (lacking lid domain) and lipases (acting on long chain lipids). Sequence and structural comparisons of 30 LysB homology models showed great variation in domain organizations and total protein length with major differences in the loop-5 motif harboring the catalytic histidine residue. Docking of different
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Registered trials
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