Results 31 to 40 of about 260,045 (204)

Cyclotides: Disulfide-rich peptide toxins in plants [PDF]

open access: yesToxicon, 2019
Cyclotides are a plant-derived family of peptides that comprise approximately 30 amino acid residues, a cyclic backbone and a cystine knot. Due to their unique structure, cyclotides are exceptionally stable to heat or proteolytic degradation and are tolerant to amino acid substitutions in their backbone loops between conserved cysteine residues.
Yen-Hua Huang   +2 more
openaire   +3 more sources

Dramatic expansion of the black widow toxin arsenal uncovered by multi-tissue transcriptomics and venom proteomics. [PDF]

open access: yes, 2014
BackgroundAnimal venoms attract enormous interest given their potential for pharmacological discovery and understanding the evolution of natural chemistries.
Ayoub, Nadia A   +4 more
core   +2 more sources

Current status and future directions of botulinum neurotoxins for targeting pain processing. [PDF]

open access: yes, 2015
Current evidence suggests that botulinum neurotoxins (BoNTs) A1 and B1, given locally into peripheral tissues such as skin, muscles, and joints, alter nociceptive processing otherwise initiated by inflammation or nerve injury in animal models and humans.
Pellett, Sabine   +2 more
core   +5 more sources

Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin

open access: yesCommunications Biology, 2021
Watanabe-Takahashi, Tamada, Senda et al. identify a tetravalent peptide that inhibits Shiga toxin (Stx), a major virulence factor of enterohemorrhagic Escherichia coli, by targeting its receptor-binding.
Miho Watanabe-Takahashi   +8 more
doaj   +1 more source

A novel RRGW derived peptide is a promising inhibitor of BoNT/A

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2023
Clostridium botulinum neurotoxin type A (BoNT/A) is one of the most potent biotoxins ever known. Its entry into neurons could block vesicle exocytosis to abolish the release of neurotransmitters from nerve terminals, thus leading to muscle paralysis ...
Wantong Ma   +10 more
doaj   +1 more source

The isolation and characterisation of temperature-dependent Ricin A chain molecules in Saccharomyces cerevisiae. [PDF]

open access: yes, 2007
Ricin is a heterodimeric plant protein that is potently toxic to mammalian cells. Toxicity results from the catalytic depurination of eukaryotic ribosomes by ricin A chain (RTA) that follows toxin endocytosis to, and translocation across, the ...
Allen   +41 more
core   +1 more source

Toxins and antimicrobial peptides: interactions with membranes [PDF]

open access: yesSPIE Proceedings, 2009
The innate immunity to pathogenic invasion of organisms in the plant and animal kingdoms relies upon cationic antimicrobial peptides (AMPs) as the first line of defense. In addition to these natural peptide antibiotics, similar cationic peptides, such as the bee venom toxin melittin, act as nonspecific toxins. Molecular details of AMP and peptide toxin
Diana E, Schlamadinger   +2 more
openaire   +2 more sources

Cationic Antimicrobial Peptides Inactivate Shiga Toxin-Encoding Bacteriophages [PDF]

open access: yesFrontiers in Chemistry, 2017
Shiga toxin (Stx) is the principal virulence factor during Shiga toxin-producing Escherichia coli (STEC) infections. We have previously reported the inactivation of bacteriophage encoding Stx after treatment with chitosan, a linear polysaccharide polymer with cationic properties.
Manuel E. Del Cogliano   +13 more
openaire   +5 more sources

Cyanobacterial Toxins and Peptides in Lake Vegoritis, Greece [PDF]

open access: yesToxins, 2021
Cyanotoxins (CTs) produced by cyanobacteria in surface freshwater are a major threat for public health and aquatic ecosystems. Cyanobacteria can also produce a wide variety of other understudied bioactive metabolites such as oligopeptides microginins (MGs), aeruginosins (AERs), aeruginosamides (AEGs) and anabaenopeptins (APs). This study reports on the
Sevasti-Kiriaki Zervou   +8 more
openaire   +3 more sources

The signal peptide of yeast killer toxin K2 confers producer self-protection and allows conversion into a modular toxin-immunity system

open access: yesCell Reports
Summary: Some microbial toxins also target the producer species itself, necessitating a means of self-protection. The M2 double-stranded RNA (dsRNA) killer virus in Saccharomyces cerevisiae contains a single open reading frame (ORF) encoding both the ...
Rianne C. Prins, Sonja Billerbeck
doaj   +1 more source

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