Results 221 to 230 of about 8,088 (248)
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Proprotein convertases: lessons from knockouts
The FASEB Journal, 2006The physiological role of the subtilisin/kexin‐like proprotein convertases (PCs) in rodents has been examined through the use of knockout mice. This review will summarize the major in vivo defects that result from the disruption of the expression of their genes.
Nathalie, Scamuffa +4 more
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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
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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 ...
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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 ...
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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 ...
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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.
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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
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Proprotein Convertases in Gynecological Cancers
Colloquium Series on Protein Activation and Cancer, 2012ABSTRACT Gynecological cancers include neoplasias of internal female genital organs, mainly ovarian, endometrial and cervical tumors, and cancers of the external female genital structures. Current scientific evidence indicates that both up- and down-regulation of the expression of PCs are part of the multiple changes occurring in these gynecological ...
Andres J.P. Klein-Szanto +2 more
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Proprotein convertase subtilisin/kexin type 9 inhibition
Current Opinion in Lipidology, 2012There are now ample data that demonstrate that inhibition of PCSK9 (proprotein convertase subtilisin/kexin type 9) can safely lower LDL cholesterol synergistically with statins. Considering that PCSK9 was first identified less than a decade ago, the last few years have shown rapid and remarkable advancements in our understanding and knowledge of the ...
David A, Marais +4 more
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Viral envelope glycoprotein processing by proprotein convertases
Antiviral Research, 2013The proprotein convertases (PCs) are a family of nine mammalian enzymes that play key roles in the maintenance of cell homeostasis by activating or inactivating proteins via limited proteolysis under temporal and spatial control. A wide range of pathogens, including major human pathogenic viruses can hijack cellular PCs for their own purposes.
Pasquato Antonella +4 more
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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
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