Results 91 to 100 of about 6,528 (248)

Mechanism of lantibiotic-induced pore-formation [PDF]

open access: yesAntonie van Leeuwenhoek, 1996
Nisin and other lantibiotics have a bacteriocidal effect against Gram-positive bacteria, and also inhibit the outgrowth of bacterial spores. The bacteriocidal effect appears to be due to the formation of pores in the bacterial membrane. In the absence of anionic membrane phospholipids, the lantibiotic nisin acts as an anion selective carrier.
Moll, Gert N.   +3 more
openaire   +3 more sources

Hijacking the Electron Train: Menaquinone‐Binding Antimicrobial Peptides

open access: yesChemBioChem, Volume 26, Issue 18, September 18, 2025.
Menaquinone is an emerging target for antimicrobial peptides. Could it be the new Achilles’ Heel of bacteria? The rise of antibiotic resistance threatens to undermine modern medicine, making the development of new antibiotics and novel targets an urgent priority.
Eilidh J. Matheson, Stephen A. Cochrane
wiley   +1 more source

An association between peptidoglycan synthesis and organization of the Streptococcus pyogenes ExPortal [PDF]

open access: yes, 2013
The ExPortal of Streptococcus pyogenes is a focal microdomain of the cytoplasmic membrane that clusters the translocons of the general secretory pathway with accessory factors to facilitate the maturation of secreted polypeptides.
Caparon, Michael G   +2 more
core   +2 more sources

Photoaffinity labeling coupled to MS to identify peptide biological partners: Secondary reactions, for better or for worse?

open access: yesMass Spectrometry Reviews, Volume 44, Issue 5, Page 715-756, September/October 2025.
Abstract Affinity photolabeling is a smart method to study noncovalent and transient interactions and provide a submolecular picture of the contacts between interacting partners. In this review, we will focus on the identification of peptide partners using photoaffinity labeling coupled to mass spectrometry in different contexts such as in vitro with a
Astrid Walrant, Emmanuelle Sachon
wiley   +1 more source

SppI Forms a Membrane Protein Complex with SppA and Inhibits Its Protease Activity in Bacillus subtilis

open access: yesmSphere, 2020
The membrane protease SppA of Bacillus subtilis was first described as a signal peptide peptidase and later shown to confer resistance to lantibiotics. Here, we report that SppA forms octameric complexes with YteJ, a membrane protein of thus-far-unknown ...
Gabriela Henriques   +9 more
doaj   +1 more source

The Skin Microbiome, Microbial Metabolites and the Epidermal Response to Ultraviolet Radiation—Towards Next Generation Suncare

open access: yesExperimental Dermatology, Volume 34, Issue 7, July 2025.
ABSTRACT Ultraviolet radiation (UVR) presents one of the greatest challenges to human skin, with numerous studies documenting its effects on skin physiology. Recently, growing recognition of the microbiome's crucial role in skin health has led to investigations on how UVR influences skin‐microbiome interactions.
Steven D. Mercer   +2 more
wiley   +1 more source

Relatedness between the two-component lantibiotics lacticin 3147 and staphylococcin C55 based on structure, genetics and biological activity [PDF]

open access: yes, 2007
peer-reviewedBackground: Two component lantibiotics, such as the plasmid-encoded lacticin 3147 produced by Lactococcus lactis DPC3147 and staphylococcin C55 produced by Staphylococcus aureus C55, represent an emerging subgroup of bacteriocins.
Colin Hill   +6 more
core   +2 more sources

Antimicrobial peptides as novel anti-tuberculosis therapeutics [PDF]

open access: yes, 2016
"Available online 24 May 2016"Tuberculosis (TB), a disease caused by the human pathogen Mycobacterium tuberculosis, has recently joined HIV/AIDS as the world's deadliest infectious disease, affecting around 9.6 million people worldwide in 2014. Of those,
Agerberth   +208 more
core   +1 more source

First evidence of production of the lantibiotic nisin P [PDF]

open access: gold, 2020
Enriqueta García-Gutiérrez   +8 more
openalex   +1 more source

Salivaricin G32, a Homolog of the Prototype Streptococcus pyogenes Nisin-Like Lantibiotic SA-FF22, Produced by the Commensal Species Streptococcus salivarius

open access: yesInternational Journal of Microbiology, 2012
Salivaricin G32, a 2667 Da novel member of the SA-FF22 cluster of lantibiotics, has been purified and characterized from Streptococcus salivarius strain G32.
Philip A. Wescombe   +8 more
doaj   +1 more source

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