Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases [PDF]
, 2011 Phytocystatins are inhibitors of cysteine-proteases from plants putatively involved in plant defence based on their capability of inhibit heterologous enzymes.
A Kiggundu +49 more
core +2 more sources
Iron-binding fragments from the N-Terminal and C-Terminal regions of human lactoferrin [PDF]
, 1978 Digestion of lactoferrin with pepsin at pH 3.0 gave an iron-binding half-molecule that represents the C-terminal part of the native protein. Tryptic or chymotryptic digestion of 30%/-iron-saturated lactoferrin yielded the N- and C-terminal half ...
Bluard-Deconinck, JM +5 more
core +1 more source
Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA [PDF]
, 2009 HGF (hepatocyte growth factor) is a pleiotropic cytokine homologous to the serine protease zymogen plasminogen that requires canonical proteolytic cleavage to gain functional activity.
Andrew M. Schumacher +47 more
core +3 more sources
Changes in arginine carboxypeptidase (CPR) activity in stressed rats
Pathophysiology, 1994 Abstract An arginine carboxypeptidase (CPR) is generated from its precursor (ProCPR) by proteolytic enzyme and may function in vivo in the removal of C-terminal arginine from inflammatory peptides such as C3a and C5a. We studied changes in this enzyme activity in rats submitted to liver cirrhois, hepatectomy, splenectomy, burning or endotoxin ...
Katsumi Kato +5 more
openaire +1 more source
Kinin-generating cellular model obtained from human glioblastoma cell line U-373 [PDF]
, 2013 Kinins, a group of important pro-inflammatory peptides, are abundantly found in tissues and biological fluids of cancer patients. Bradykinin, the major representative of kinins, induces vascular permeability and, in consequence, promotes tumor expansion.
Błońska, Beata +3 more
core +1 more source
The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids [PDF]
, 2014 The posttranslational modification of carboxy-terminal tails of tubulin plays an important role in the regulation of the microtubule cytoskeleton. Enzymes responsible for deglutamylating tubulin have been discovered within a novel family of mammalian ...
Andrieux, Annie +10 more
core +5 more sources
The location of the arginine-specific carboxypeptidase in the membrane of Mycoplasma salivarium and its physiological functions [PDF]
FEMS Microbiology Letters, 1992 A non-penetrating probe, 2,4,6-trinitrobenzenesulfonate, inhibited the activity of the carboxypeptidase purified from the cell membranes of Mycoplasma salivarium and the same enzymatic activity of intact Mycoplasma cells as well. Growth of the organism in medium containing benzoylglycyl-L-arginine resulted in a higher pH and higher turbidity than ...
K, Shibata, T, Watanabe
openaire +2 more sources
Mutational replacement of methionine by arginine in the S′1 substrate binding site of yeast carboxypeptidase [PDF]
Carlsberg Research Communications, 1986 Alkylation of Met-398 in the S′1 binding site of carboxypeptidase Y drastically reduces kcat for hydrolysis of peptides, presumably due to introduction of a positively charged sulfonium ion. In the present work a positive charge has been introduced by means of site-directed mutagenesis, exchanging Met-398 with the cationic arginyl residue.
BECH, LM +4 more
openaire +2 more sources
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
Mechanisms of Action and Cell Death Associated with Clostridium perfringens Toxins. [PDF]
, 2018 Clostridium perfringens uses its large arsenal of protein toxins to produce histotoxic, neurologic and intestinal infections in humans and animals. The major toxins involved in diseases are alpha (CPA), beta (CPB), epsilon (ETX), iota (ITX), enterotoxin (
McClane, Bruce A +2 more
core +3 more sources