메뉴 건너뛰기




Volumn 27, Issue 5, 2006, Pages 1087-1098

Prediction of neuropeptide prohormone cleavages with application to RFamides

Author keywords

Neuropeptides; Prohormone processing; RFamides; Statistical models

Indexed keywords

FMRFAMIDE PEPTIDE; HORMONE PRECURSOR; NEUROPEPTIDE; NEUROPEPTIDE FF; PEPTIDE; PROLACTIN RELEASING FACTOR; RFAMIDE PEPTIDE; RFAMIDE RELATED PEPTIDE; UNCLASSIFIED DRUG;

EID: 33646144688     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2005.07.026     Document Type: Article
Times cited : (38)

References (50)
  • 1
    • 14744269527 scopus 로고    scopus 로고
    • Peptidomic analysis of the larval Drosophila melangaster central nervous system by two-dimensional capillary liquid chromatography quadrupole time-of-flight mass spectrometry
    • Baggerman G., Boonen K., Verleyen P., De Loof A., and Schoofs L. Peptidomic analysis of the larval Drosophila melangaster central nervous system by two-dimensional capillary liquid chromatography quadrupole time-of-flight mass spectrometry. J Mass Spectrom 40 (2005) 250-260
    • (2005) J Mass Spectrom , vol.40 , pp. 250-260
    • Baggerman, G.1    Boonen, K.2    Verleyen, P.3    De Loof, A.4    Schoofs, L.5
  • 2
    • 0033931867 scopus 로고    scopus 로고
    • Assessing the accuracy of prediction algorithms for classification: an overview
    • Baldi P., Brunak S., Chauvin Y., Andersen C.A., and Nielsen H. Assessing the accuracy of prediction algorithms for classification: an overview. Bioinformatics 16 (2000) 412-424
    • (2000) Bioinformatics , vol.16 , pp. 412-424
    • Baldi, P.1    Brunak, S.2    Chauvin, Y.3    Andersen, C.A.4    Nielsen, H.5
  • 4
    • 0142057149 scopus 로고    scopus 로고
    • Identification of proneuropeptide FFA peptides processed in neuronal and non-neuronal cells and in nervous tissue
    • Bonnard E., Burlet-Schiltz O., Monsarrat B., Girad J., and Zajac J. Identification of proneuropeptide FFA peptides processed in neuronal and non-neuronal cells and in nervous tissue. Eur J Biochem 270 (2003) 4187-4199
    • (2003) Eur J Biochem , vol.270 , pp. 4187-4199
    • Bonnard, E.1    Burlet-Schiltz, O.2    Monsarrat, B.3    Girad, J.4    Zajac, J.5
  • 5
    • 77956712498 scopus 로고    scopus 로고
    • The enzymology of PC1 and PC2
    • Dalby R.E., and Sigman D.S. (Eds), Academic Press, San Diego
    • Cameron A., Apletalina E.V., and Lindberg I. The enzymology of PC1 and PC2. In: Dalby R.E., and Sigman D.S. (Eds). The enzymes vol. XXII (2001), Academic Press, San Diego 291-332
    • (2001) The enzymes , vol.XXII , pp. 291-332
    • Cameron, A.1    Apletalina, E.V.2    Lindberg, I.3
  • 6
    • 0036316263 scopus 로고    scopus 로고
    • Prolactin-releasing peptide in the ewe: cDNA cloning, mRNA distribution and effects on prolactin secretion in vitro and in vivo
    • Curlewis J.D., Kusters D.H., Barclay J.L., and Anderson S.T. Prolactin-releasing peptide in the ewe: cDNA cloning, mRNA distribution and effects on prolactin secretion in vitro and in vivo. J Endocrinol 174 (2002) 45-53
    • (2002) J Endocrinol , vol.174 , pp. 45-53
    • Curlewis, J.D.1    Kusters, D.H.2    Barclay, J.L.3    Anderson, S.T.4
  • 7
    • 6344272882 scopus 로고    scopus 로고
    • Cleavages within the prodomain direct intracellular trafficking and degradation of mature bone morphogenetic protein-4
    • Degnin C., Jean F., Thomas G., and Christian J.L. Cleavages within the prodomain direct intracellular trafficking and degradation of mature bone morphogenetic protein-4. Mol Biol Cell 15 (2004) 5012-5020
    • (2004) Mol Biol Cell , vol.15 , pp. 5012-5020
    • Degnin, C.1    Jean, F.2    Thomas, G.3    Christian, J.L.4
  • 8
    • 12344302029 scopus 로고    scopus 로고
    • Significance of prohormone convertase 2, PC2, mediated initial cleavage at the proglucagon interdomain site, Lys70-Arg71, to generate glucagon
    • Dey A., Lipkind G.M., Rouille Y., Norrbom C., Stein J., Zhang C., et al. Significance of prohormone convertase 2, PC2, mediated initial cleavage at the proglucagon interdomain site, Lys70-Arg71, to generate glucagon. Endocrinology 146 (2005) 713-727
    • (2005) Endocrinology , vol.146 , pp. 713-727
    • Dey, A.1    Lipkind, G.M.2    Rouille, Y.3    Norrbom, C.4    Stein, J.5    Zhang, C.6
  • 9
    • 2442675424 scopus 로고    scopus 로고
    • The expanding family of -RFamide peptides and their effects on feeding behaviour
    • Dockray G.J. The expanding family of -RFamide peptides and their effects on feeding behaviour. Exp Physiol 89 (2004) 229-235
    • (2004) Exp Physiol , vol.89 , pp. 229-235
    • Dockray, G.J.1
  • 10
    • 0043126911 scopus 로고    scopus 로고
    • Logistic regression and artificial neural network classification models: a methodology review
    • Dreiseitl S., and Ohno-Machado L. Logistic regression and artificial neural network classification models: a methodology review. J Biomed Inform 35 (2002) 352-359
    • (2002) J Biomed Inform , vol.35 , pp. 352-359
    • Dreiseitl, S.1    Ohno-Machado, L.2
  • 11
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert P., Brunak S., and Blom N. Prediction of proprotein convertase cleavage sites. Protein Eng Des Sel 17 (2004) 107-112
    • (2004) Protein Eng Des Sel , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 14
    • 0037743535 scopus 로고    scopus 로고
    • The crystal structure of the proprotein processing proteinase furin explains its stringent specificity
    • Henrich S., Cameron A., Bourenkov G.P., Kiefersauer R., Huber R., Lindberg I., et al. The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nat Struct Biol 10 (2003) 520-526
    • (2003) Nat Struct Biol , vol.10 , pp. 520-526
    • Henrich, S.1    Cameron, A.2    Bourenkov, G.P.3    Kiefersauer, R.4    Huber, R.5    Lindberg, I.6
  • 15
    • 9644281041 scopus 로고    scopus 로고
    • Proportion convertase models based on the crystal structures of furin and kexin: Explanation of their specificity
    • Henrich S., Lindberg I., Bode W., and Than M.E. Proportion convertase models based on the crystal structures of furin and kexin: Explanation of their specificity. J Mol Biol 345 (2005) 211-227
    • (2005) J Mol Biol , vol.345 , pp. 211-227
    • Henrich, S.1    Lindberg, I.2    Bode, W.3    Than, M.E.4
  • 17
    • 0034306368 scopus 로고    scopus 로고
    • New neuropeptides containing carboxy-terminal RFamide and their receptor in mammals
    • Hinuma S., Shintani Y., Fukusumi S., Iijima N., Matsumoto Y., Hosoya M., et al. New neuropeptides containing carboxy-terminal RFamide and their receptor in mammals. Nat Cell Biol 2 (2000) 703-708
    • (2000) Nat Cell Biol , vol.2 , pp. 703-708
    • Hinuma, S.1    Shintani, Y.2    Fukusumi, S.3    Iijima, N.4    Matsumoto, Y.5    Hosoya, M.6
  • 18
    • 0037647026 scopus 로고    scopus 로고
    • 2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor
    • Holyoak T., Wilson M.A., Fenn T.D., Kettner C.A., Petsko G.A., Fuller R.S., et al. 2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor. Biochemistry 42 (2003) 6709-6718
    • (2003) Biochemistry , vol.42 , pp. 6709-6718
    • Holyoak, T.1    Wilson, M.A.2    Fenn, T.D.3    Kettner, C.A.4    Petsko, G.A.5    Fuller, R.S.6
  • 19
    • 1542297713 scopus 로고    scopus 로고
    • Structural basis for differences in substrate selectivity in Kex2 and Furin protein convertases
    • Holyoak T., Kettner C.A., Petsko G.A., Fuller R.S., and Ringe D. Structural basis for differences in substrate selectivity in Kex2 and Furin protein convertases. Biochemistry 43 (2004) 2412-2421
    • (2004) Biochemistry , vol.43 , pp. 2412-2421
    • Holyoak, T.1    Kettner, C.A.2    Petsko, G.A.3    Fuller, R.S.4    Ringe, D.5
  • 21
    • 0346251363 scopus 로고    scopus 로고
    • From precursor to final peptides: a statistical sequence-based approach to predicting prohormone processing
    • Hummon A.B., Hummon N.P., Corbin R.W., Li L., Vilim F.S., Weiss K.R., et al. From precursor to final peptides: a statistical sequence-based approach to predicting prohormone processing. J Proteome Res 2 (2003) 650-656
    • (2003) J Proteome Res , vol.2 , pp. 650-656
    • Hummon, A.B.1    Hummon, N.P.2    Corbin, R.W.3    Li, L.4    Vilim, F.S.5    Weiss, K.R.6
  • 23
    • 0036157791 scopus 로고    scopus 로고
    • A novel amphibian hypothalamic neuropeptide: isolation, localization and biological activity
    • Koda A., Ukena K., Teranishi H., Ohta S., Yamamoto K., Kikuyama, et al. A novel amphibian hypothalamic neuropeptide: isolation, localization and biological activity. Endocrinology 143 (2002) 411-419
    • (2002) Endocrinology , vol.143 , pp. 411-419
    • Koda, A.1    Ukena, K.2    Teranishi, H.3    Ohta, S.4    Yamamoto, K.5    Kikuyama6
  • 24
    • 0000605787 scopus 로고    scopus 로고
    • Dalby R.E., and Sigman D.S. (Eds), Academic Press, San Diego
    • Molloy S.S., and Furin T.G. In: Dalby R.E., and Sigman D.S. (Eds). The enzymes vol. XXII (2001), Academic Press, San Diego 199-235
    • (2001) The enzymes , vol.XXII , pp. 199-235
    • Molloy, S.S.1    Furin, T.G.2
  • 25
    • 0030725756 scopus 로고    scopus 로고
    • Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing a wide variety of precursor proteins
    • Nakayama K. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing a wide variety of precursor proteins. Biochem J 327 (1997) 625-635
    • (1997) Biochem J , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 26
    • 0036768383 scopus 로고    scopus 로고
    • A neuropeptide FF-related gene is expressed selectively in neurons of the terminal nerve in Danio rerio
    • Oehlmann V.D., Korte H., Sterner C., and Korsching S.I. A neuropeptide FF-related gene is expressed selectively in neurons of the terminal nerve in Danio rerio. Mech Dev 117 (2002) 357-361
    • (2002) Mech Dev , vol.117 , pp. 357-361
    • Oehlmann, V.D.1    Korte, H.2    Sterner, C.3    Korsching, S.I.4
  • 27
    • 4043069259 scopus 로고    scopus 로고
    • Gonadotropin-inhibitory hormone in Gambel's white-crowned sparrow (Zonotrichia leucophrys gambelii): cDNA identification, transcript localization and functional effects in laboratory and field experiments
    • Osugi T., Ukena K., Bentley G.E., O'Brien S., Moore I.T., Wingfield J.C., et al. Gonadotropin-inhibitory hormone in Gambel's white-crowned sparrow (Zonotrichia leucophrys gambelii): cDNA identification, transcript localization and functional effects in laboratory and field experiments. J Endocrinol 182 (2004) 33-42
    • (2004) J Endocrinol , vol.182 , pp. 33-42
    • Osugi, T.1    Ukena, K.2    Bentley, G.E.3    O'Brien, S.4    Moore, I.T.5    Wingfield, J.C.6
  • 28
    • 0028088923 scopus 로고
    • Proteolytic processing of the aplysia A peptide precursor in AtT-20 cells
    • Paganetti P., and Scheller R.H. Proteolytic processing of the aplysia A peptide precursor in AtT-20 cells. Brain Res 633 (1994) 53-62
    • (1994) Brain Res , vol.633 , pp. 53-62
    • Paganetti, P.1    Scheller, R.H.2
  • 29
    • 0030789876 scopus 로고    scopus 로고
    • A human gene encoding morphine modulating peptides related to NPFF and FMRFamide
    • Perry S.J., Yi-Kung Huang E., Cronk D., Bagust J., Sharma R., Walker R.J., et al. A human gene encoding morphine modulating peptides related to NPFF and FMRFamide. FEBS Lett 409 (1997) 426-430
    • (1997) FEBS Lett , vol.409 , pp. 426-430
    • Perry, S.J.1    Yi-Kung Huang, E.2    Cronk, D.3    Bagust, J.4    Sharma, R.5    Walker, R.J.6
  • 30
    • 4644351089 scopus 로고    scopus 로고
    • Unique accumulation of neuropeptides in an insect: FMRFamide-related peptides in the cockroach, Periplanta Americana
    • Predel R., Neupert S., Wicher D., Gundel M., Roth S., and Derst C. Unique accumulation of neuropeptides in an insect: FMRFamide-related peptides in the cockroach, Periplanta Americana. Eur J Neurosci 20 (2004) 1499-1513
    • (2004) Eur J Neurosci , vol.20 , pp. 1499-1513
    • Predel, R.1    Neupert, S.2    Wicher, D.3    Gundel, M.4    Roth, S.5    Derst, C.6
  • 31
    • 77956662772 scopus 로고    scopus 로고
    • Yeast Kex2 protease
    • Dalby R.E., and Sigman D.S. (Eds), Academic Press, San Diego
    • Rockwell N.C., and Fuller R.S. Yeast Kex2 protease. In: Dalby R.E., and Sigman D.S. (Eds). The enzymes vol. XXII (2001), Academic Press, San Diego 259-289
    • (2001) The enzymes , vol.XXII , pp. 259-289
    • Rockwell, N.C.1    Fuller, R.S.2
  • 32
    • 0442292293 scopus 로고    scopus 로고
    • The kindest cuts of all: crystal structures of Kex2 and furin reveal secrets of precursor processing
    • Rockwell N.C., and Thorner J.W. The kindest cuts of all: crystal structures of Kex2 and furin reveal secrets of precursor processing. Trends Biochem Sci 29 (2004) 80-87
    • (2004) Trends Biochem Sci , vol.29 , pp. 80-87
    • Rockwell, N.C.1    Thorner, J.W.2
  • 34
    • 0027403544 scopus 로고
    • The flp-1 propeptide is processed into multiple, highly similar FMRFamide-like peptides in Caenorhabditis elegans
    • Rosoff M.L., Doble K.E., Price D.A., and Li C. The flp-1 propeptide is processed into multiple, highly similar FMRFamide-like peptides in Caenorhabditis elegans. Peptides 14 (1993) 331-338
    • (1993) Peptides , vol.14 , pp. 331-338
    • Rosoff, M.L.1    Doble, K.E.2    Price, D.A.3    Li, C.4
  • 35
    • 0033038048 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding a precursor of Carassius RFamide, structurally related to a mammalian prolactin-releasing peptide
    • Satake H., Minakata H., Wang X., and Fujimoto M. Characterization of a cDNA encoding a precursor of Carassius RFamide, structurally related to a mammalian prolactin-releasing peptide. FEBS Lett 446 (1999) 247-250
    • (1999) FEBS Lett , vol.446 , pp. 247-250
    • Satake, H.1    Minakata, H.2    Wang, X.3    Fujimoto, M.4
  • 36
    • 0035281823 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding a novel avian hypothalamic neuropeptide exerting an inhibitory effect on gonadotroin release
    • Satake H., Hisada M., Kawada T., Minakata H., Ukena K., and Tsutsui K. Characterization of a cDNA encoding a novel avian hypothalamic neuropeptide exerting an inhibitory effect on gonadotroin release. Biochem J 354 (2001) 379-385
    • (2001) Biochem J , vol.354 , pp. 379-385
    • Satake, H.1    Hisada, M.2    Kawada, T.3    Minakata, H.4    Ukena, K.5    Tsutsui, K.6
  • 37
    • 0036737720 scopus 로고    scopus 로고
    • Identification of a cDNA encoding a novel amphibian growth hormone-releasing peptide and localization of its transcript
    • Sawada K., Ukena K., Kikuyama S., and Tsutsui K. Identification of a cDNA encoding a novel amphibian growth hormone-releasing peptide and localization of its transcript. J Endocrinol 174 (2002) 395-402
    • (2002) J Endocrinol , vol.174 , pp. 395-402
    • Sawada, K.1    Ukena, K.2    Kikuyama, S.3    Tsutsui, K.4
  • 39
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27 (1967) 157-162
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 40
    • 77956663111 scopus 로고    scopus 로고
    • Cellular limited proteolysis of precursor proteins and peptides
    • Dalby R.E., and Sigman D.S. (Eds), Academic Press, San Diego
    • Seidah N.G. Cellular limited proteolysis of precursor proteins and peptides. In: Dalby R.E., and Sigman D.S. (Eds). The enzymes vol. XXII (2001), Academic Press, San Diego 237-258
    • (2001) The enzymes , vol.XXII , pp. 237-258
    • Seidah, N.G.1
  • 41
    • 0026742108 scopus 로고
    • Proprotein and prohormone convertases of the subtilisin family: recent developments and future perspectives
    • Seidah N.G., and Chretien M. Proprotein and prohormone convertases of the subtilisin family: recent developments and future perspectives. Trends Endocrinol Metab 3 (1992) 133-140
    • (1992) Trends Endocrinol Metab , vol.3 , pp. 133-140
    • Seidah, N.G.1    Chretien, M.2
  • 42
    • 77956664692 scopus 로고    scopus 로고
    • The prohormone convertases and precursor processing in protein biosynthesis
    • Dalby R.E., and Sigman D.S. (Eds), Academic Press, San Diego
    • Steiner D.F. The prohormone convertases and precursor processing in protein biosynthesis. In: Dalby R.E., and Sigman D.S. (Eds). The enzymes vol. XXII (2001), Academic Press, San Diego 163-198
    • (2001) The enzymes , vol.XXII , pp. 163-198
    • Steiner, D.F.1
  • 45
    • 0037070155 scopus 로고    scopus 로고
    • A novel rat hypothalamic RFamide-related peptide identified by immunoaffinity chromatography and mass spectrometry
    • Ukena K., Iwakoshi E., Minakata H., and Tsutui K. A novel rat hypothalamic RFamide-related peptide identified by immunoaffinity chromatography and mass spectrometry. FEBS Lett 512 (2002) 255-258
    • (2002) FEBS Lett , vol.512 , pp. 255-258
    • Ukena, K.1    Iwakoshi, E.2    Minakata, H.3    Tsutui, K.4
  • 46
    • 0034132245 scopus 로고    scopus 로고
    • Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors
    • Veenstra J.A. Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors. Arch Insect Biochem Phys 43 (2000) 49-63
    • (2000) Arch Insect Biochem Phys , vol.43 , pp. 49-63
    • Veenstra, J.A.1
  • 48
    • 4544257878 scopus 로고    scopus 로고
    • Biosynthesis of peptide hormones derived from precursor sequences
    • von Eggelkraut R., and Beck-Sickinger A.G. Biosynthesis of peptide hormones derived from precursor sequences. Curr Med Chem 11 (2004) 2651-2665
    • (2004) Curr Med Chem , vol.11 , pp. 2651-2665
    • von Eggelkraut, R.1    Beck-Sickinger, A.G.2
  • 49
    • 0037441867 scopus 로고    scopus 로고
    • Molecular properties of endogenous RFamide-related peptide-3 and its interaction with receptors
    • Yoshida H., Habata Y., Hosoya M., Kawamata Y., Kitada C., and Hinuma S. Molecular properties of endogenous RFamide-related peptide-3 and its interaction with receptors. Biochim Biophys Acta 1593 (2003) 151-157
    • (2003) Biochim Biophys Acta , vol.1593 , pp. 151-157
    • Yoshida, H.1    Habata, Y.2    Hosoya, M.3    Kawamata, Y.4    Kitada, C.5    Hinuma, S.6
  • 50
    • 0011981114 scopus 로고
    • Isolation, sequencing, synthesis, and pharmacological characterization of two brain neuropeptides that modulate the action of morphine
    • Yang H.Y., Fratta W., Majane E.A., and Costa E. Isolation, sequencing, synthesis, and pharmacological characterization of two brain neuropeptides that modulate the action of morphine. Proc Natl Acad Sci USA 82 (1985) 7757-7761
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7757-7761
    • Yang, H.Y.1    Fratta, W.2    Majane, E.A.3    Costa, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.