Results 1 to 10 of about 43,515 (179)
Histidine and Aspartic Acid Residues Important for Immunoglobulin G Endopeptidase Activity of the Group AStreptococcusOpsonophagocytosis-Inhibiting Mac Protein [PDF]
Infection and Immunity, 2003 ABSTRACTThe secreted Mac protein made by serotype M1 group AStreptococcus(GAS) (designated Mac5005) inhibits opsonophagocytosis and killing of GAS by human polymorphonuclear neutrophils. This protein also has cysteine endopeptidase activity against human immunoglobulin G (IgG).
Benfang, Lei +5 more
openaire +3 more sources
Catalysis Letters, 2021 Aspartic proteases (E.C.3.4.23.) are endopeptidases with molecular masses ranging between 30–45 kDa. They depend on aspartic acid residues for their catalytic activity and show maximal activity at low pH.
Jermen Mamo +5 more
semanticscholar +1 more source
Phosphorylated acidic serine–aspartate-rich MEPE-associated motif peptide from matrix extracellular phosphoglycoprotein inhibits phosphate regulating gene with homologies to endopeptidases on the X-chromosome enzyme activity [PDF]
Journal of Endocrinology, 2007 Inactivating PHEX (phosphate regulating gene with homologies to endopeptidases on the X chromosome) mutations cause X-linked hypophosphatemia in humans and mice (Hyp) through overproduction of fibroblast growth factor 23 (FGF23) a phosphaturic factor, by osteocytes.
Shiguang, Liu +4 more
openaire +2 more sources
Frontiers in Immunology, 2023 Glioblastoma is the most common primary malignant tumor of the central nervous system, which has the characteristics of strong invasion, frequent recurrence, and rapid progression.
Hao Liu +8 more
semanticscholar +1 more source
Novel strategy for the demulsification of isolated sesame oil bodies by endogenous proteases
Journal of the American Oil Chemists Society, 2021 Oleosins are mandatory to avoid coalescence of oil bodies (OBs), so commercial proteases are used to efficiently demulsify OBs into food oil. However, the commercial proteases and pH regulators (acid and alkali) greatly restrict this method in industry ...
Yeming Chen +4 more
semanticscholar +1 more source
bioRxiv, 2020 Aspartic proteases (E.C.3.4.23.) are endopeptidases with molecular masses ranging between 30–45 kDa. They depend on aspartic acid residues for their catalytic activity and show maximal activity at low pH.
Jermen Mamo +5 more
semanticscholar +1 more source
Yeast as a tool to explore cathepsin D function [PDF]
, 2015 Cathepsin D has garnered increased attention in recent years, mainly since it has been associated with several human pathologies. In particular, cathepsin D is often overexpressed and hypersecreted in cancer cells, implying it may constitute a ...
Castro, L. +5 more
core +7 more sources
The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries
Journal of Food Quality, 2018 Proteases represent one of the three largest groups of industrial enzymes and account for about 60% of the total global enzymes sale. According to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, proteases are ...
Jermen Mamo, F. Assefa
semanticscholar +1 more source
Aspartic Acid in Health and Disease
Nutrients, 2023 Aspartic acid exists in L- and D-isoforms (L-Asp and D-Asp). Most L-Asp is synthesized by mitochondrial aspartate aminotransferase from oxaloacetate and glutamate acquired by glutamine deamidation, particularly in the liver and tumor cells, and ...
M. Holeček
semanticscholar +1 more source
Presence and expression of hydrogenase specific C-terminal endopeptidases in cyanobacteria [PDF]
, 2003 BACKGROUND: Hydrogenases catalyze the simplest of all chemical reactions: the reduction of protons to molecular hydrogen or vice versa. Cyanobacteria can express an uptake, a bidirectional or both NiFe-hydrogenases.
Batur, Mehtap +2 more
core +3 more sources