Furin

[1]. Kornelia Hardes, et al. Novel Furin Inhibitors with Potent Anti-infectious Activity. ChemMedChem. 2015 Jul;10(7):1218-31. [Content Brief]

[2]. Sven O Dahms, et al. X-ray structures of human furin in complex with competitive inhibitors. ACS Chem Biol. 2014 May 16;9(5):1113-8. [Content Brief]

[3]. M Tsuneoka, et al. Evidence for involvement of furin in cleavage and activation of diphtheria toxin. J Biol Chem. 1993 Dec 15;268(35):26461-5. [Content Brief]

[4]. C M Dubois, et al. Processing of transforming growth factor beta 1 precursor by human furin convertase. J Biol Chem. 1995 May 5;270(18):10618-24. [Content Brief]

[5]. Alexander G Semenov, et al. Processing of pro-B-type natriuretic peptide: furin and corin as candidate convertases. Clin Chem. 2010 Jul;56(7):1166-76. [Content Brief]

[6]. Jianhao Peng, et al. Glycosylation and processing of pro-B-type natriuretic peptide in cardiomyocytes. Biochem Biophys Res Commun. 2011 Aug 5;411(3):593-8. [Content Brief]

[7]. Ayako Ueo, et al. Lysosome-Associated Membrane Proteins Support the Furin-Mediated Processing of the Mumps Virus Fusion Protein. J Virol. 2020 Jun 1;94(12):e00050-20. [Content Brief]

[8]. R Leduc, et al. Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage. J Biol Chem. 1992 Jul 15;267(20):14304-8. [Content Brief]

[9]. Markus Hoffmann, et al. A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells. Mol Cell. 2020 May 21;78(4):779-784.e5. [Content Brief]

[10]. P J Barr, et al. cDNA and gene structure for a human subtilisin-like protease with cleavage specificity for paired basic amino acid residues. DNA Cell Biol. 1991 Jun;10(5):319-28. [Content Brief]

[11]. S Takahashi, et al. A mutation of furin causes the lack of precursor-processing activity in human colon carcinoma LoVo cells. Biochem Biophys Res Commun. 1993 Sep 15;195(2):1019-26. [Content Brief]

[12]. E D Anderson, et al. Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage. EMBO J. 1997 Apr 1;16(7):1508-18. [Content Brief]

[13]. Tim Schulte, et al. The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. Sci Rep. 2016 Sep 1;6:32371. [Content Brief]

[14]. Eric D Anderson, et al. The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation. J Biol Chem. 2002 Apr 12;277(15):12879-90. [Content Brief]

[15]. R J Wise, et al. Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9378-82. [Content Brief]

[16]. K R Klimpel, et al. Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10277-81. [Content Brief]

[17]. S Takahashi, et al. A second mutant allele of furin in the processing-incompetent cell line, LoVo. Evidence for involvement of the homo B domain in autocatalytic activation. J Biol Chem. 1995 Nov 3;270(44):26565-9. [Content Brief]

[18]. S S Molloy, et al. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J Biol Chem. 1992 Aug 15;267(23):16396-402. [Content Brief]