Salivary gland development: its mediation by a subtilisin-like proprotein convertase, PACE4
Tetsuya Akamatsu+5 more
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The Furin Protease Dependence and Antiviral GBP2 Sensitivity of Murine Leukemia Virus Infection Are Determined by the Amino Acid Sequence at the Envelope Glycoprotein Cleavage Site. [PDF]
Kubo Y, Hans MB, Nakamura T, Hayashi H.
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The Diverse Pathways for Cell Surface MT1-MMP Localization in Migratory Cells. [PDF]
Kelly H, Inada M, Itoh Y.
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The link between the trans-Golgi network and tumour progression. [PDF]
Jahangiri L.
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PCSK7, a potential target for the treatment of age-related macular degeneration: inhibition of retinal epithelial cell death. [PDF]
Zhang X, Zhao X, Xin X.
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Identification of Furin Protease Small-Molecule Inhibitor with a 1,3-Thiazol-2-ylaminosulfonyl Scaffold. [PDF]
Kolarič A+4 more
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The Inhibitory Effects of Alpha 1 Antitrypsin on Endosomal TLR Signaling Pathways. [PDF]
Elshikha AS+4 more
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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
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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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