A food-grade enzyme preparation with modest gluten detoxification properties. [PDF]
PLoS ONE, 2009 Celiac sprue is a life-long disease characterized by an intestinal inflammatory response to dietary gluten. A gluten-free diet is an effective treatment for most patients, but accidental ingestion of gluten is common, leading to incomplete recovery or ...
Jennifer Ehren +5 more
doaj +1 more source
Molecules, 2023 Ochratoxin A (OTA) is considered one of the main mycotoxins responsible for health problems and considerable economic losses in the feed industry.
Pablo César Orozco-Cortés +4 more
semanticscholar +1 more source
Structural modeling and functional analysis of the essential ribosomal processing protease Prp from Staphylococcus aureus [PDF]
, 2017 In Firmicutes and related bacteria, ribosomal large subunit protein L27 is encoded with a conserved N-terminal extension that is removed to expose residues critical for ribosome function. Bacteria encoding L27 with this N-terminal extension also encode a
Christie, Gail E. +3 more
core +2 more sources
The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer
International Journal of Molecular Sciences, 2023 Papain-like cysteine proteases are composed of 11 human cysteine cathepsins, originally located in the lysosomes. They exhibit broad specificity and act as endopeptidases and/or exopeptidases.
V. Stoka +3 more
semanticscholar +1 more source
A biotechnology perspective of fungal proteases [PDF]
, 2015 Proteases hydrolyze the peptide bonds of proteins into peptides and amino acids, being found in all living organisms, and are essential for cell growth and differentiation.
Almeida, Renata Paula Coppini de +9 more
core +1 more source
Papain-like peptidases: structure, function, and evolution
Biomolecular Concepts, 2013 Papain-like cysteine peptidases are a diverse family of peptidases found in most known organisms. In eukaryotes, they are divided into multiple evolutionary groups, which can be clearly distinguished on the basis of the structural characteristics of the ...
Novinec Marko, Lenarčič Brigita
doaj +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
Asparaginyl endopeptidases: enzymology, applications and limitations
Organic and biomolecular chemistry, 2021 Asparaginyl endopeptidases (AEP) are cysteine proteases found in mammalian and plant cells. Several AEP isoforms from plant species were found to exhibit transpeptidase activity which is integral for the key head-to-tail cyclisation reaction during the ...
T. Tang, Louis Y. P. Luk
semanticscholar +1 more source
The calpastatin-derived calpain inhibitor CP1B reduces mRNA expression of matrix metalloproteinase-2 and-9 and invasion by leukemic THP-1 cells [PDF]
, 2003 The ubiquitous proteases μ- and m-calpain are Ca2+-dependent cysteine endopeptidases. Besides involvement in a variety of physio(patho)logical processes, recent studies suggest a pivotal role of calpains in differentiation of hematopoietic cells and ...
Croall D. E. +8 more
core +1 more source
Kinetic Characterization of Cerium and Gallium Ions as Inhibitors of Cysteine Cathepsins L, K, and S
International Journal of Molecular Sciences, 2022 Heavy metal ions can disrupt biological functions via multiple molecular mechanisms, including inhibition of enzymes. We investigate the interactions of human papain-like cysteine endopeptidases cathepsins L, K, and S with gallium and cerium ions, which ...
Marko Novinec +5 more
semanticscholar +1 more source