Results 31 to 40 of about 20,933 (225)
BMC Evolutionary Biology, 2011 Background Omptins are a family of outer membrane proteases that have spread by horizontal gene transfer in Gram-negative bacteria that infect vertebrates or plants.
Westerlund-Wikström Benita +3 more
doaj +1 more source
Proteolytic processing and activation of Clostridium perfringens epsilon toxin by caprine small intestinal contents. [PDF]
, 2014 Epsilon toxin (ETX), a pore-forming toxin produced by type B and D strains of Clostridium perfringens, mediates severe enterotoxemia in livestock and possibly plays a role in human disease.
Freedman, John C +3 more
core +2 more sources
Using the SUBcellular database for Arabidopsis proteins to localize the Deg protease family
Frontiers in Plant Science, 2014 Sub-functionalization during the expansion of gene families in eukaryotes has occurred in part through specific subcellular localization of different family members.
Sandra Karin Tanz +7 more
doaj +1 more source
Biotechnology for Biofuels and Bioproducts, 2023 Background Keratin, the main component of chicken feather, is the third most abundant material after cellulose and chitin. Keratin can be converted into high-value compounds and is considered a potential high-quality protein supplement; However, its ...
Yuhong Lai +4 more
doaj +1 more source
Proteomes, 2018 The recent identification of catalytically active peptidylglycine α-amidating monooxygenase (PAM) in Chlamydomonas reinhardtii, a unicellular green alga, suggested the presence of a PAM-like gene and peptidergic signaling in the last eukaryotic ...
Raj Luxmi +6 more
doaj +1 more source
Recombinant expression and functional analysis of proteases from Streptococcus pneumoniae, Bacillus anthracis, and Yersinia pestis [PDF]
, 2011 Background Uncharacterized proteases naturally expressed by bacterial pathogens represents important topic in infectious disease research, because these enzymes may have critical roles in pathogenicity and cell physiology.
Keehwan Kwon +7 more
core +1 more source
Proteases that degrade the biofilm matrix
Zdorovʹe Rebenka, 2020 Biofilms protect bacteria from the action of antibacterial drugs and are one of the mechanisms of antibiotic resistance of infections. Destruction of the bacterial biofilm matrix leads to the release of bacteria and they again become vulnerable to ...
А.Е. Abaturov
doaj +1 more source
Proteases and caspase-like activity in the yeast Saccharomyces cerevisiae. [PDF]
, 2013 addresses: Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter EX4 4QD, UK.types: Journal Article; Research Support, Non-U.S.
Ramsdale, M, Wilkinson, D
core +1 more source
Sensitive substrates for neprilysin (neutral endopeptidase) and thermolysin that are highly resistant to serine proteases [PDF]
FEBS Letters, 1996 Tripeptide derivatives like 3‐carboxypropanoylalanyl‐alanyl‐leucine 4‐nitroanilide or 3‐carboxypropanoylalanyl‐alanyl‐phenylalanine 4‐nitroanilide are very sensitive substrates for neprilysin (k cat > 102 s−1; k cat/K m ≥ 106 s−1 · M−1) and are widely employed in investigations of the enzyme. However, these compounds are also good substrates for the
Spungin-Bialik, Anya +4 more
openaire +2 more sources
Veterinary Research, 2019 Yersinia ruckeri is the causative agent of enteric redmouth disease in salmonids. In fish, the intestine represents an important site of nutrient uptake, host–pathogen interactions, and defense.
Gokhlesh Kumar +3 more
doaj +1 more source