메뉴 건너뛰기




Volumn 2, Issue 11, 1999, Pages 984-988

Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; FURIN; PEPTIDE DERIVATIVE;

EID: 0033352083     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/14783     Document Type: Article
Times cited : (138)

References (25)
  • 1
    • 0025316704 scopus 로고
    • Familial cerebral amyloid angiopathy with nonneuritic amyloid plaque formation
    • Plant, G. T., Revesz, T., Barnard, R. O., Harding, A. E. & Gautier-Smith, P. C. Familial cerebral amyloid angiopathy with nonneuritic amyloid plaque formation. Brain 113, 721-747 (1990).
    • (1990) Brain , vol.113 , pp. 721-747
    • Plant, G.T.1    Revesz, T.2    Barnard, R.O.3    Harding, A.E.4    Gautier-Smith, P.C.5
  • 2
    • 0001355224 scopus 로고
    • A form of familial presenile dementia with spastic paralysis (including the pathological examination of a case)
    • Worster-Drought, C., Greenfield, J. G. & McMenemey, W. H. A form of familial presenile dementia with spastic paralysis (including the pathological examination of a case). Brain 63, 237-254 (1940).
    • (1940) Brain , vol.63 , pp. 237-254
    • Worster-Drought, C.1    Greenfield, J.G.2    McMenemey, W.H.3
  • 4
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • Vidal, R. et al. A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 399, 776-781 (1999).
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1
  • 5
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama, K. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327, 625-635 (1997).
    • (1997) Biochem. J. , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 6
    • 0033059994 scopus 로고    scopus 로고
    • Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis
    • Molloy, S. S., Anderson, E. D., Jean, F. & Thomas, G. Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis. Trends Cell Biol. 9, 28-35 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 28-35
    • Molloy, S.S.1    Anderson, E.D.2    Jean, F.3    Thomas, G.4
  • 7
    • 0032517098 scopus 로고    scopus 로고
    • cDNA sequence analysis, chromosomal assignment and expression pattern of the gene coding for integral membrane protein 2B
    • Pittois, K., Deleersnijder, W. & Merregaert, J. cDNA sequence analysis, chromosomal assignment and expression pattern of the gene coding for integral membrane protein 2B. Gene 217, 141-149 (1998).
    • (1998) Gene , vol.217 , pp. 141-149
    • Pittois, K.1    Deleersnijder, W.2    Merregaert, J.3
  • 8
    • 0029742884 scopus 로고    scopus 로고
    • Isolation of markers for chondro-osteogenic differentiation using cDNA library subtraction. Molecular cloning and characterization of a gene belonging to a novel multigene family of integral membrane proteins
    • Deleersnijder, W. et al. Isolation of markers for chondro-osteogenic differentiation using cDNA library subtraction. Molecular cloning and characterization of a gene belonging to a novel multigene family of integral membrane proteins. J. Biol. Chem. 271, 19475-19482 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 19475-19482
    • Deleersnijder, W.1
  • 9
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132 (1982).
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 10
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G. & von Heijne, G. TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10, 685-686 (1994).
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 11
    • 0021800788 scopus 로고
    • Characterization of protein transport between successive compartments of the Golgi apparatus: Asymmetric properties of donor and acceptor activities in a cell free system
    • Balch, W. E. & Rothman, J. E. Characterization of protein transport between successive compartments of the Golgi apparatus: asymmetric properties of donor and acceptor activities in a cell free system. Arch. Biochem. Biophys. 240, 413-425 (1985).
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 413-425
    • Balch, W.E.1    Rothman, J.E.2
  • 12
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., Lewis, G. K., Ramsay, G. & Bishop, J. M. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Biol. 5, 3610-3616 (1985).
    • (1985) Mol. Cell Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 13
    • 0031470093 scopus 로고    scopus 로고
    • Generation of APLP2 KO mice and early postnatal lethality in APLP2/APP double KO mice
    • von Koch, C. S. et al. Generation of APLP2 KO mice and early postnatal lethality in APLP2/APP double KO mice. Neurobiol. Aging 18, 661-669 (1997).
    • (1997) Neurobiol. Aging , vol.18 , pp. 661-669
    • Von Koch, C.S.1
  • 14
    • 0026669290 scopus 로고
    • Sequence requirements for precursor cleavage within the constitutive secretory pathway
    • Watanabe, T. et al. Sequence requirements for precursor cleavage within the constitutive secretory pathway. J. Biol. Chem. 267, 8270-8274 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 8270-8274
    • Watanabe, T.1
  • 15
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy, S. S., Bresnahan, P. A., Leppla, S. H., Klimpel, K. R. & Thomas, G. 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. 267, 16396-16402 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 16
    • 0027474401 scopus 로고
    • Positional and additive effects of basic amino acids on processing of precursor proteins within the constitutive secretory pathway
    • Watanabe, T., Murakami, K. & Nakayama, K. Positional and additive effects of basic amino acids on processing of precursor proteins within the constitutive secretory pathway. FEBS Lett. 320, 215-218 (1993).
    • (1993) FEBS Lett. , vol.320 , pp. 215-218
    • Watanabe, T.1    Murakami, K.2    Nakayama, K.3
  • 17
    • 0028103804 scopus 로고
    • Sequence requirements for endoproteolytic processing of precursor proteins by furin: Transfection and in vitro experiments
    • Takahashi, S., Hatsuzawa, K., Watanabe, T., Murakami, K. & Nakayama, K. Sequence requirements for endoproteolytic processing of precursor proteins by furin: transfection and in vitro experiments. J. Biochem. (Tokyo) 116, 47-52 (1994).
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 47-52
    • Takahashi, S.1    Hatsuzawa, K.2    Watanabe, T.3    Murakami, K.4    Nakayama, K.5
  • 18
    • 0020561771 scopus 로고
    • Strains of CHO-K1 cells resistant to Pseudomonas exotoxin A and cross-resistant to diphtheria toxin and viruses
    • Moehring, J. M. & Moehring, T. J. Strains of CHO-K1 cells resistant to Pseudomonas exotoxin A and cross-resistant to diphtheria toxin and viruses. Infect. Immun. 41, 998-1009 (1983).
    • (1983) Infect. Immun. , vol.41 , pp. 998-1009
    • Moehring, J.M.1    Moehring, T.J.2
  • 19
    • 0027452932 scopus 로고
    • Expression of mouse furin in a Chinese hamster cell resistant to Pseudomonas exotoxin A and viruses complements the genetic lesion
    • Moehring, J. M., Inocencio, N. M., Robertson, B. J. & Moehring, T. J. Expression of mouse furin in a Chinese hamster cell resistant to Pseudomonas exotoxin A and viruses complements the genetic lesion. J. Biol. Chem. 268, 2590-2594 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 2590-2594
    • Moehring, J.M.1    Inocencio, N.M.2    Robertson, B.J.3    Moehring, T.J.4
  • 20
    • 0029066531 scopus 로고
    • Analysis of mutations in alleles of the fur gene from an endoprotease-deficient Chinese hamster ovary cell strain
    • Spence, M. J., Sucic, J. F., Foley, B. T. & Moehring, T. J. Analysis of mutations in alleles of the fur gene from an endoprotease-deficient Chinese hamster ovary cell strain. Somat. Cell Mol. Genet. 21, 1-18 (1995).
    • (1995) Somat. Cell Mol. Genet. , vol.21 , pp. 1-18
    • Spence, M.J.1    Sucic, J.F.2    Foley, B.T.3    Moehring, T.J.4
  • 21
    • 0030969770 scopus 로고    scopus 로고
    • Processing of wild-type and mutant proinsulin-like growth factor-IA by subtilisin-related proprotein convertases
    • Duguay, S. J., Milewski, W. M., Young, B. D., Nakayama, K. & Steiner, D. F. Processing of wild-type and mutant proinsulin-like growth factor-IA by subtilisin-related proprotein convertases. J. Biol. Chem. 272, 6663-6670 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 6663-6670
    • Duguay, S.J.1    Milewski, W.M.2    Young, B.D.3    Nakayama, K.4    Steiner, D.F.5
  • 22
    • 0025373508 scopus 로고
    • Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing
    • Sisodia, S. S., Koo, E. H., Beyreuther, K., Unterbeck, A. & Price, D. L. Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 248, 492-495 (1990).
    • (1990) Science , vol.248 , pp. 492-495
    • Sisodia, S.S.1    Koo, E.H.2    Beyreuther, K.3    Unterbeck, A.4    Price, D.L.5
  • 23
    • 0031028166 scopus 로고    scopus 로고
    • The transmembrane domain of a carboxyl-terminal anchored protein determines localization to the endoplasmic reticulum
    • Yang, M., Ellenberg, J., Bonicacino, J. S. & Weissman, A. M. The transmembrane domain of a carboxyl-terminal anchored protein determines localization to the endoplasmic reticulum. J. Biol. Chem. 272, 1970-1975 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 1970-1975
    • Yang, M.1    Ellenberg, J.2    Bonicacino, J.S.3    Weissman, A.M.4
  • 24
    • 0032513057 scopus 로고    scopus 로고
    • Transmembrane topology of glucose-6-phosphatase
    • Pan, C. J., Lin, B. & Chou, J. Y. Transmembrane topology of glucose-6-phosphatase. J. Biol. Chem. 273, 6144-6148 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 6144-6148
    • Pan, C.J.1    Lin, B.2    Chou, J.Y.3
  • 25
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry
    • Wang, R., Sweeney, D., Gandy, S. E. & Sisodia, S. S. The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry. J. Biol. Chem. 271, 31894-31902 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31894-31902
    • Wang, R.1    Sweeney, D.2    Gandy, S.E.3    Sisodia, S.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.