Results 201 to 210 of about 25,303 (250)
Some of the next articles are maybe not open access.
Proprotein convertases as therapeutic targets
Expert Opinion on Therapeutic Targets, 2008Limited endoproteolysis of precursor proteins is a common mechanism of production of functional proteins and peptides. In the secretory pathway of eukaryotic cells, this endoproteolysis is principally mediated by a family of calcium-dependent serine proteases, generically known as proprotein convertases.
Michel, Chrétien +3 more
openaire +2 more sources
Proprotein Convertases in Health and Disease
New England Journal of Medicine, 2011Proteases that process larger precursor proteins into smaller functional proteins are involved in a wide range of physiologic processes. Derangements in the function of these enzymes play a role in many diseases.
Andrew W, Artenstein, Steven M, Opal
openaire +2 more sources
Current Opinion in Chemical Biology, 1998
The major endoproteolytic processing enzymes of the secretory pathway are the subtilisin-like proprotein convertases (SPCs). Furin (SPC1) has emerged as one of the major processing enzymes of the constitutive secretory pathway and its localization in the trans-Golgi network and mechanism of autoactivation have been studied in considerable detail ...
openaire +2 more sources
The major endoproteolytic processing enzymes of the secretory pathway are the subtilisin-like proprotein convertases (SPCs). Furin (SPC1) has emerged as one of the major processing enzymes of the constitutive secretory pathway and its localization in the trans-Golgi network and mechanism of autoactivation have been studied in considerable detail ...
openaire +2 more sources
Inhibitors of proprotein convertases
Journal of Molecular Medicine, 2005The discovery of mammalian subtilases, proprotein convertases (PCs) or subtilisin-like proprotein convertases (SPCs), in 1990 was a result of sustained efforts in searching for enzyme/s responsible for maturation of inactive protein precursors. Since then, seven PCs have so far been discovered that cleave at the carboxy-terminal of a basic amino acid ...
openaire +2 more sources
Proprotein convertases in atherogenesis
Current Opinion in Lipidology, 2015The proprotein convertases subtilisin/kexin (PCSKs) are endoproteases identified as activators of precursors from hormones and peptides. On the basis of the variety of substrates and regulation in disease, they have been recognized as mediators in atherogenesis.
openaire +2 more sources
The activation and physiological functions of the proprotein convertases
The International Journal of Biochemistry & Cell Biology, 2008The mammalian secretory proprotein convertases are part of a family of nine serine proteinases of the subtilisin-type. Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7. The two other convertases SKI-1/S1P and PCSK9 are implicated in cholesterol and/or fatty acid metabolism.
Nabil G, Seidah +7 more
openaire +2 more sources
The biology and therapeutic targeting of the proprotein convertases
Nature Reviews Drug Discovery, 2012The mammalian proprotein convertases constitute a family of nine secretory serine proteases that are related to bacterial subtilisin and yeast kexin. Seven of these (proprotein convertase 1 (PC1), PC2, furin, PC4, PC5, paired basic amino acid cleaving enzyme 4 (PACE4) and PC7) activate cellular and pathogenic precursor proteins by cleavage at single or
Nabil G, Seidah, Annik, Prat
openaire +2 more sources
Characterization of proADAMTS5 processing by proprotein convertases
The International Journal of Biochemistry & Cell Biology, 2009ADAMTS5 (aggrecanase-2), a key metalloprotease mediating cartilage destruction in arthritis, is synthesized as a zymogen, proADAMTS5. We report a detailed characterization of the propeptide excision mechanism and demonstrate that it is a major regulatory step with unusual characteristics. Using furin-deficient cells and a furin inhibitor, we found that
Jean-Michel, Longpré +5 more
openaire +2 more sources
Proprotein Convertase PC3 Is Not a Transmembrane Protein
Biochemistry, 2005Proprotein convertase PC3 (also known as PC1) is an endopeptidase involved in proteolytic processing of peptide hormone precursors in granules of the regulated secretory pathway of endocrine cells. Lacking any extended hydrophobic segments, PC3 was considered to be a secretory protein only peripherally attached to the granule membrane.
Stettler, H., Suri, G., Spiess, M.
openaire +3 more sources
FGF23 is processed by proprotein convertases but not by PHEX
Bone, 2004X-linked hypophosphatemia (XLH) and autosomal dominant hypophosphatemic rickets (ADHR) are characterized by renal phosphate wasting, rickets, and osteomalacia. ADHR is caused by gain of function mutations in the fibroblast growth factor 23 gene (FGF23). During secretion, FGF23 is processed at the C-terminus between amino acids 179 and 180. The cleavage
Anna, Benet-Pagès +5 more
openaire +2 more sources