ArticleMicrobial drug resistance (Larchmont, N.Y.)2016
LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions.
Article in Microbial drug resistance (Larchmont, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Novel endopeptidase overcoming lysostaphin resistance.Scientific reports · 2026Article
- Enhancing stability and safety of chimeric peptidoglycan hydrolases by linker engineering.Applied microbiology and biotechnology · 2026Article
- An antibiotic-free antimicrobial combination of bacteriocins and a peptidoglycan hydrolase:Applied and environmental microbiology · 2025Article
- From discovery to potential application: engineering a novel M23 peptidase to combat Listeria monocytogenes.Scientific reports · 2025Article
- Engineering of chimeric enzymes with expanded tolerance to ionic strength.Microbiology spectrum · 2024Article
- Staphylococcus aureus sacculus mediates activities of M23 hydrolases.Nature communications · 2023Article
- Bacteriophage Endolysin: A Powerful Weapon to Control Bacterial Biofilms.The protein journal · 2023Review
- Influence of NaCl and pH on lysostaphin catalytic activity, cell binding, and bacteriolytic activity.Applied microbiology and biotechnology · 2022Article
- Electrostatic Interaction with the Bacterial Cell Envelope Tunes the Lytic Activity of Two Novel Peptidoglycan Hydrolases.Microbiology spectrum · 2022Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Structural Characterization of EnpA D,L-Endopeptidase fromInternational journal of molecular sciences · 2021Article
- Article
- Identification of Biomarkers for Systemic Distribution of Nanovesicles FromFrontiers in immunology · 2021Article
- Two New M23 Peptidoglycan Hydrolases With Distinct Net Charge.Frontiers in microbiology · 2021Article
- LytU-SH3b fusion protein as a novel and efficient enzybiotic against methicillin-resistantMolecular biology research communications · 2019Article
- Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.Scientific reports · 2019Article
- Antimicrobial activity of bacteriophage derived triple fusion protein againstAIMS microbiology · 2019Article
- Structural and Functional Insights Into Lysostaphin-Substrate Interaction.Frontiers in molecular biosciences · 2018Article
- Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity in extended environmental conditions. Our results exemplify the possibility of exploring autolytic enzymes in engineering lysins with desired features. Moreover, they suggest a possible mechanism of autolysin physiological activity regulation by local ionic environments in the cell wall.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.