Occurrence of an HIV‐1 gp160 endoproteolytic activity in low‐density vesicles and evidence for a distinct density distribution from endogenously expressed furin and PC7/LPC convertases
暂无分享,去创建一个
N. Seidah | P. Courtoy | J. Ruysschaert | E. Decroly | M. Vandenbranden | R. Fuchs | V. Morel | M. Leruth | S. Wouters | D. Shober | Jean-Marie Ruysschaert | Michel Vandenbranden | Daniela Shober | Valérie Morel | Michèle Leruth
[1] Shai Cohen,et al. Bartonella henselae Endocarditis: An Usual Presentation of an Unusual Disease , 2019, European journal of case reports in internal medicine.
[2] P. Courtoy,et al. Furin and proprotein convertase 7 (PC7)/lymphoma PC endogenously expressed in rat liver can be resolved into distinct post-Golgi compartments. , 1998, Biochemical Journal.
[3] P. Marynen,et al. Inhibition of intracellular proteolytic processing of soluble proproteins by an engineered alpha 2-macroglobulin containing a furin recognition sequence in the bait region. , 1997, The Biochemical journal.
[4] H. Nagamune,et al. A novel human PACE4 isoform, PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus. , 1997, Journal of biochemistry.
[5] N. Seidah,et al. Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160 , 1997, FEBS letters.
[6] M. Spence,et al. Endoprotease Activities Other Than Furin and PACE4 with a Role in Processing of HIV-I gp160 Glycoproteins in CHO-K1 Cells* , 1997, The Journal of Biological Chemistry.
[7] R. Angeletti,et al. Localization of Endogenous Furin in Cultured Cell Lines , 1997, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.
[8] N. Seidah,et al. The isoforms of proprotein convertase PC5 are sorted to different subcellular compartments , 1996, The Journal of cell biology.
[9] C Di Bello,et al. Identification of the Paired Basic Convertases Implicated in HIV gp160 Processing Based on in Vitro Assays and Expression in CD4+ Cell Lines* , 1996, The Journal of Biological Chemistry.
[10] J. Bonifacino,et al. Protein targeting by tyrosine- and di-leucine-based signals: evidence for distinct saturable components , 1996, The Journal of cell biology.
[11] N. Seidah,et al. cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[12] N. Seidah,et al. Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases. , 1996, The Biochemical journal.
[13] O. Bakke,et al. Physiological functions of endosomal proteolysis. , 1995, The Biochemical journal.
[14] T. Moehring,et al. Furin activates Pseudomonas exotoxin A by specific cleavage in vivo and in vitro. , 1994, The Journal of biological chemistry.
[15] M. Hamaguchi,et al. A furin-defective cell line is able to process correctly the gp160 of human immunodeficiency virus type 1 , 1994, Journal of virology.
[16] J. Ruysschaert,et al. The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM). , 1994, The Journal of biological chemistry.
[17] L. Montagnier,et al. Effects of calcium ions on proteolytic processing of HIV‐1 gp160 precursor and on cell fusion , 1994, FEBS letters.
[18] N. Katunuma,et al. Processing protease for gp160 human immunodeficiency virus type I envelope glycoprotein precursor in human T4+ lymphocytes. Purification and characterization. , 1993, The Journal of biological chemistry.
[19] H. Klenk,et al. Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60 , 1992, Nature.
[20] E. Fenouillet,et al. Immunological analysis of human immunodeficiency virus type 1 envelope glycoprotein proteolytic cleavage. , 1992, Virology.
[21] K. Howell,et al. Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38). , 1990, The Biochemical journal.
[22] E. Engleman,et al. Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex. , 1990, The Journal of biological chemistry.
[23] R. Pal,et al. Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[24] I. Mellman,et al. Acidification and ion permeabilities of highly purified rat liver endosomes. , 1989, The Journal of biological chemistry.
[25] J. Bonifacino,et al. Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[26] C. Bordier. Phase separation of integral membrane proteins in Triton X-114 solution. , 1981, The Journal of biological chemistry.
[27] F. Leighton,et al. THE LARGE-SCALE SEPARATION OF PEROXISOMES, MITOCHONDRIA, AND LYSOSOMES FROM THE LIVERS OF RATS INJECTED WITH TRITON WR-1339 , 1968, The Journal of cell biology.
[28] J. Farber,et al. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. , 1999, Annual review of immunology.
[29] N. Seidah,et al. The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. , 1994, Biochimie.