메뉴 건너뛰기




Volumn 2, Issue , 2012, Pages

Computational prediction of furin cleavage sites by a hybrid method and understanding mechanism underlying diseases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84859735363     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00261     Document Type: Article
Times cited : (52)

References (29)
  • 1
    • 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 (Pt3), 625-635 (1997). (Pubitemid 27487665)
    • (1997) Biochemical Journal , vol.327 , Issue.3 , pp. 625-635
    • Nakayama, K.1
  • 2
    • 0033059994 scopus 로고    scopus 로고
    • Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis
    • DOI 10.1016/S0962-8924(98)01382-8
    • 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). (Pubitemid 29138669)
    • (1999) Trends in Cell Biology , vol.9 , Issue.1 , pp. 28-35
    • Molloy, S.S.1    Anderson, E.D.2    Jean, F.3    Thomas, G.4
  • 3
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas, G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3, 753-766 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 4
    • 77956287381 scopus 로고    scopus 로고
    • Furin targeted drug delivery for treatment of rhabdomyosarcoma in a mouse model
    • Hajdin, K., D'Alessandro, V., Niggli, F. K., Schafer, B. W. & Bernasconi, M. Furin targeted drug delivery for treatment of rhabdomyosarcoma in a mouse model. PLoS. One. 5, e10445 (2010).
    • (2010) PLoS. One , vol.5
    • Hajdin, K.1    D'Alessandro, V.2    Niggli, F.K.3    Schafer, B.W.4    Bernasconi, M.5
  • 5
    • 0028157378 scopus 로고
    • Furin has the proalbumin substrate specificity and serpin inhibitory properties of an in situ hepatic convertase
    • DOI 10.1016/0014-5793(94)80353-6
    • Brennan, S. O. & Nakayama, K. Furin has the proalbumin substrate specificity and serpin inhibitory properties of an in situ hepatic convertase. FEBS Lett. 338, 147-151 (1994). (Pubitemid 24064954)
    • (1994) FEBS Letters , vol.338 , Issue.2 , pp. 147-151
    • Brennan, S.O.1
  • 6
    • 0037830773 scopus 로고    scopus 로고
    • Furin-mediated processing of pro-C-type natriuretic peptide
    • DOI 10.1074/jbc.M301223200
    • Wu, C., Wu, F., Pan, J., Morser, J. & Wu, Q. Furin-mediated processing of Pro-Ctype natriuretic peptide. J. Biol. Chem. 278, 25847-25852 (2003). (Pubitemid 36835344)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25847-25852
    • Wu, C.1    Wu, F.2    Pan, J.3    Morser, J.4    Wu, Q.5
  • 7
    • 0032775770 scopus 로고    scopus 로고
    • The furin protease cleavage recognition sequence of Sindbis virus PE2 can mediate virion attachment to cell surface heparan sulfate
    • Klimstra, W. B., Heidner, H. W. & Johnston, R. E. The furin protease cleavage recognition sequence of Sindbis virus PE2 can mediate virion attachment to cell surface heparan sulfate. J. Virol. 73, 6299-6306 (1999). (Pubitemid 29327806)
    • (1999) Journal of Virology , vol.73 , Issue.8 , pp. 6299-6306
    • Klimstra, W.B.1    Heidner, H.W.2    Johnston, R.E.3
  • 8
    • 77649161633 scopus 로고    scopus 로고
    • A 20 Residues Motif Delineates the Furin Cleavage Site and its Physical Properties May Influence Viral Fusion
    • Sun, T. A 20 Residues Motif Delineates the Furin Cleavage Site and its Physical Properties May Influence Viral Fusion. Biochemistry Insights 2, 9-20 (2009).
    • (2009) Biochemistry Insights , vol.2 , pp. 9-20
    • Sun, T.1
  • 9
    • 77649083093 scopus 로고    scopus 로고
    • Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors
    • Sun, T. & Wu, J. Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors. Int J Biol Sci 6, 89-95 (2010).
    • (2010) Int J Biol Sci , vol.6 , pp. 89-95
    • Sun, T.1    Wu, J.2
  • 10
    • 79952257801 scopus 로고    scopus 로고
    • FurinDB: A database of 20-residue furin cleavage site motifs, substrates and their associated drugs
    • Sun, T., Huang, Q., Fang, Y. & Wu, J. FurinDB: A Database of 20-Residue Furin Cleavage Site Motifs, Substrates and Their Associated Drugs. Int. J. Mol. Sci. 12, 1060-1065 (2011).
    • (2011) Int. J. Mol. Sci , vol.12 , pp. 1060-1065
    • Sun, T.1    Huang, Q.2    Fang, Y.3    Wu, J.4
  • 11
    • 8444241860 scopus 로고    scopus 로고
    • Fast exact leave-one-out cross-validation of sparse least-squares support vector machines
    • DOI 10.1016/j.neunet.2004.07.002, PII S0893608004001431
    • Cawley, G. C. & Talbot, N. L. Fast exact leave-one-out cross-validation of sparse least-squares support vector machines. Neural Netw. 17, 1467-1475 (2004). (Pubitemid 39487142)
    • (2004) Neural Networks , vol.17 , Issue.10 , pp. 1467-1475
    • Cawley, G.C.1    Talbot, N.L.C.2
  • 13
    • 64149123778 scopus 로고    scopus 로고
    • Next-generation sequencing: From basic research to diagnostics
    • Voelkerding, K. V., Dames, S. A. & Durtschi, J. D. Next-generation sequencing: from basic research to diagnostics. Clin. Chem. 55, 641-658 (2009).
    • (2009) Clin. Chem , vol.55 , pp. 641-658
    • Voelkerding, K.V.1    Dames, S.A.2    Durtschi, J.D.3
  • 14
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. Three-dimensional structure of membrane and surface proteins. Annu. Rev. Biochem. 53, 595-623 (1984).
    • (1984) Annu. Rev. Biochem , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 15
    • 78650584621 scopus 로고    scopus 로고
    • Biological functions of the genes in the mammaprint breast cancer profile reflect the hallmarks of cancer
    • Sun, T. et al. Biological functions of the genes in the mammaprint breast cancer profile reflect the hallmarks of cancer. Biomark. Insights. 5, 129-138 (2010).
    • (2010) Biomark. Insights , vol.5 , pp. 129-138
    • Sun, T.1
  • 17
    • 77952988108 scopus 로고    scopus 로고
    • A new generation of homology search tools based on probabilistic inference
    • Eddy, S. R. A new generation of homology search tools based on probabilistic inference. Genome Inform. 23, 205-211 (2009).
    • (2009) Genome Inform , vol.23 , pp. 205-211
    • Eddy, S.R.1
  • 19
    • 0032892577 scopus 로고    scopus 로고
    • AAindex: Amino acid index database
    • DOI 10.1093/nar/27.1.368
    • Kawashima, S., Ogata, H. & Kanehisa, M. AAindex: Amino Acid Index Database. Nucleic Acids Res. 27, 368-369 (1999). (Pubitemid 29209488)
    • (1999) Nucleic Acids Research , vol.27 , Issue.1 , pp. 368-369
    • Kawashima, S.1    Ogata, H.2    Kanehisa, M.3
  • 21
    • 0034981134 scopus 로고    scopus 로고
    • Mutational spectrum of the ED1 gene in X-linked hypohidrotic ectodermal dysplasia
    • DOI 10.1038/sj.ejhg.5200635
    • Vincent, M. C., Biancalana, V., Ginisty, D., Mandel, J. L. & Calvas, P. Mutational spectrum of the ED1 gene in X-linked hypohidrotic ectodermal dysplasia. Eur. J. Hum. Genet. 9, 355-363 (2001). (Pubitemid 32499452)
    • (2001) European Journal of Human Genetics , vol.9 , Issue.5 , pp. 355-363
    • Vincent, M.C.1    Biancalana, V.2    Ginisty, D.3    Mandel, J.L.4    Calvas, P.5
  • 24
    • 0028881825 scopus 로고
    • Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A alpha 20 Val-.Asp)
    • Brennan, S. O., Hammonds, B. & George, P. M. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A alpha 20 Val-. Asp).J. Clin. Invest 96, 2854-2858 (1995).
    • (1995) J. Clin. Invest , vol.96 , pp. 2854-2858
    • Brennan, S.O.1    Hammonds, B.2    George, P.M.3
  • 25
    • 0014349825 scopus 로고
    • The characterization of amino acid sequences in proteins by statistical methods
    • Zimmerman, J. M., Eliezer, N. & Simha, R. The characterization of amino acid sequences in proteins by statistical methods. J. Theor. Biol. 21, 170-201 (1968).
    • (1968) J. Theor. Biol , vol.21 , pp. 170-201
    • Zimmerman, J.M.1    Eliezer, N.2    Simha, R.3
  • 27
    • 0023731964 scopus 로고
    • Amino acid side chain parameters for correlation studies in biology and pharmacology
    • Fauchere, J. L., Charton, M., Kier, L. B., Verloop, A. & Pliska, V. Amino acid side chain parameters for correlation studies in biology and pharmacology. Int. J. Pept. Protein Res. 32, 269-278 (1988).
    • (1988) Int. J. Pept. Protein Res , vol.32 , pp. 269-278
    • Fauchere, J.L.1    Charton, M.2    Kier, L.B.3    Verloop, A.4    Pliska, V.5
  • 28
    • 0016192651 scopus 로고
    • Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues
    • Bull, H. B. & Breese, K. Surface tension of amino acid solutions: a hydrophobicity scale of the amino acid residues. Arch. Biochem. Biophys. 161, 665-670 (1974).
    • (1974) Arch. Biochem. Biophys , vol.161 , pp. 665-670
    • Bull, H.B.1    Breese, K.2
  • 29
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins. A tool for the selection of peptide antigens
    • DOI 10.1007/BF01195768
    • Karplus, P. A. & Schulz, G. E. Prediction of Chain Flexibility in Proteins-A Tool for the Selection of Peptide Antigens. Naturwissenschaften 72, 212-213 (1985). (Pubitemid 15094544)
    • (1985) Naturwissenschaften , vol.72 , Issue.4 , pp. 212-213
    • Karplus, P.A.1    Schulz, G.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.