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Volumn 7, Issue 1, 2008, Pages 386-399

Integrated analysis of the cerebrospinal fluid peptidome and proteome

Author keywords

Cerebrospinal fluid; LC MS MS; LTQ Orbitrap; Neuropeptides; Peptidomics; Proteomics

Indexed keywords

MEMBRANE PROTEIN; NEUROPEPTIDE; PEPTIDE DERIVATIVE; PEPTIDOME; PLASMA PROTEIN; PROTEIN PRECURSOR; PROTEOME; UNCLASSIFIED DRUG;

EID: 38649136201     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr070501k     Document Type: Article
Times cited : (154)

References (88)
  • 1
    • 0004383133 scopus 로고
    • Anatomic and physiologic aspects of the cerebrospinal fluid space
    • Herndon, R. M, Brumback, R. A, Eds, Kluwer: Boston
    • Brumback, R. A. Anatomic and physiologic aspects of the cerebrospinal fluid space. In The Cerebrospinal Fluid; Herndon, R. M., Brumback, R. A., Eds.; Kluwer: Boston, 1989; pp 15-43.
    • (1989) The Cerebrospinal Fluid , pp. 15-43
    • Brumback, R.A.1
  • 2
    • 0025129636 scopus 로고
    • Laboratory investigation of cerebrospinal fluid proteins
    • Thompson, E. J.; Keir, G. Laboratory investigation of cerebrospinal fluid proteins. Ann. Clin. Biochem. 1990, 27 (Pt 5), 425-35.
    • (1990) Ann. Clin. Biochem , vol.27 , Issue.PART 5 , pp. 425-435
    • Thompson, E.J.1    Keir, G.2
  • 4
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold, R.; Goodlett, D. R. Mass spectrometry in proteomics. Chem. Rev. 2001, 101 (2), 269-95.
    • (2001) Chem. Rev , vol.101 , Issue.2 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 9
    • 3042816692 scopus 로고    scopus 로고
    • Proteomic analysis of cerebrospinal fluid from multiple sclerosis patients
    • Dumont, D.; Noben, J. P.; Raus, J.; Stinissen, P.; Robben, J. Proteomic analysis of cerebrospinal fluid from multiple sclerosis patients. Proteomics 2004, 4 (7), 2117-24.
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 2117-2124
    • Dumont, D.1    Noben, J.P.2    Raus, J.3    Stinissen, P.4    Robben, J.5
  • 10
    • 3242885511 scopus 로고    scopus 로고
    • Proteome study of human cerebrospinal fluid following traumatic brain injury indicates fibrin(ogen) degradation products as trauma-associated markers
    • Conti, A.; Sanchez-Ruiz, Y.; Bachi, A.; Beretta, L.; Grandi, E.; Beltramo, M.; Alessio, M. Proteome study of human cerebrospinal fluid following traumatic brain injury indicates fibrin(ogen) degradation products as trauma-associated markers. J. Neurotrauma 2004, 21 (7), 854-63.
    • (2004) J. Neurotrauma , vol.21 , Issue.7 , pp. 854-863
    • Conti, A.1    Sanchez-Ruiz, Y.2    Bachi, A.3    Beretta, L.4    Grandi, E.5    Beltramo, M.6    Alessio, M.7
  • 11
    • 2942560510 scopus 로고    scopus 로고
    • Proteins released from degenerating neurons are surrogate markers for acute brain damage
    • Siman, R.; McIntosh, T. K.; Soltesz, K. M.; Chen, Z.; Neumar, R. W.; Roberts, V. L. Proteins released from degenerating neurons are surrogate markers for acute brain damage. Neurobiol. Dis. 2004, 16 (2), 311-20.
    • (2004) Neurobiol. Dis , vol.16 , Issue.2 , pp. 311-320
    • Siman, R.1    McIntosh, T.K.2    Soltesz, K.M.3    Chen, Z.4    Neumar, R.W.5    Roberts, V.L.6
  • 13
    • 0036107153 scopus 로고    scopus 로고
    • Analysis of the human lumbar cerebrospinal fluid proteome
    • Yuan, X.; Russell, T.; Wood, G.; Desiderio, D. M. Analysis of the human lumbar cerebrospinal fluid proteome. Electrophoresis 2002, 23 (7-8), 1185-96.
    • (2002) Electrophoresis , vol.23 , Issue.7-8 , pp. 1185-1196
    • Yuan, X.1    Russell, T.2    Wood, G.3    Desiderio, D.M.4
  • 14
    • 13844310832 scopus 로고    scopus 로고
    • Proteomics analysis of prefractionated human lumbar cerebrospinal fluid
    • Yuan, X.; Desiderio, D. M. Proteomics analysis of prefractionated human lumbar cerebrospinal fluid. Proteomics 2005, 5 (2), 541-50.
    • (2005) Proteomics , vol.5 , Issue.2 , pp. 541-550
    • Yuan, X.1    Desiderio, D.M.2
  • 15
    • 4444358786 scopus 로고    scopus 로고
    • Towards two-dimensional electrophoresis mapping of the cerebrospinal fluid proteome from a single individual
    • Finehout, E. J.; Franck, Z.; Lee, K. H. Towards two-dimensional electrophoresis mapping of the cerebrospinal fluid proteome from a single individual. Electrophoresis 2004, 25 (15), 2564-75.
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2564-2575
    • Finehout, E.J.1    Franck, Z.2    Lee, K.H.3
  • 16
    • 0035294659 scopus 로고    scopus 로고
    • Proteome studies of human cerebrospinal fluid and brain tissue using a preparative two-dimensional electrophoresis approach prior to mass spectrometry
    • Davidsson, P.; Paulson, L.; Hesse, C.; Blennow, K.; Nilsson, C. L. Proteome studies of human cerebrospinal fluid and brain tissue using a preparative two-dimensional electrophoresis approach prior to mass spectrometry. Proteomics 2001, 1 (3), 444-52.
    • (2001) Proteomics , vol.1 , Issue.3 , pp. 444-452
    • Davidsson, P.1    Paulson, L.2    Hesse, C.3    Blennow, K.4    Nilsson, C.L.5
  • 17
    • 0035946722 scopus 로고    scopus 로고
    • Peptide repertoire of human cerebrospinal fluid: Novel proteolytic fragments of neuroendocrine proteins
    • Stark, M.; Danielsson, O.; Griffiths, W. J.; Jornvall, H.; Johansson, J. Peptide repertoire of human cerebrospinal fluid: novel proteolytic fragments of neuroendocrine proteins. J. Chromatogr. B, Biomed. Sci. Appl. 2001, 754 (2), 357-67.
    • (2001) J. Chromatogr. B, Biomed. Sci. Appl , vol.754 , Issue.2 , pp. 357-367
    • Stark, M.1    Danielsson, O.2    Griffiths, W.J.3    Jornvall, H.4    Johansson, J.5
  • 18
    • 14744274048 scopus 로고    scopus 로고
    • Human cerebrospinal fluid peptidomics
    • Yuan, X.; Desiderio, D. M. Human cerebrospinal fluid peptidomics. J. Mass Spectrom. 2005, 40 (2), 176-81.
    • (2005) J. Mass Spectrom , vol.40 , Issue.2 , pp. 176-181
    • Yuan, X.1    Desiderio, D.M.2
  • 19
    • 0035282811 scopus 로고    scopus 로고
    • Cerebrospinal fluid analysis: Disease-related data patterns and evaluation programs
    • Reiber, H.; Peter, J. B. Cerebrospinal fluid analysis: disease-related data patterns and evaluation programs. J. Neurol. Sci. 2001, 184 (2), 101-22.
    • (2001) J. Neurol. Sci , vol.184 , Issue.2 , pp. 101-122
    • Reiber, H.1    Peter, J.B.2
  • 20
    • 38649114818 scopus 로고    scopus 로고
    • Labor und Diagnose Indikation und Bewertung von Laborbefunden für die medizinische Diagnostik
    • 6th ed
    • Thomas, L. Labor und Diagnose Indikation und Bewertung von Laborbefunden für die medizinische Diagnostik, 6th ed.; TH-Books Verlagsgesellschaft:frankfurt/main, 2005.
    • (2005) TH-Books Verlagsgesellschaft:frankfurt/main
    • Thomas, L.1
  • 22
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J.; Ishihama, Y.; Mann, M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 2003, 75 (3), 663-70.
    • (2003) Anal. Chem , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 24
    • 3042818018 scopus 로고    scopus 로고
    • The International Protein Index: An integrated database for proteomics experiments
    • Kersey, P. J.; Duarte, J.; Williams, A.; Karavidopoulou, Y.; Birney, E.; Apweiler, R. The International Protein Index: an integrated database for proteomics experiments. Proteomics 2004, 4 (7), 1985-8.
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 1985-1988
    • Kersey, P.J.1    Duarte, J.2    Williams, A.3    Karavidopoulou, Y.4    Birney, E.5    Apweiler, R.6
  • 25
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20 (18), 3551-67.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 26
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen, H.; Mann, M. The ABC's (and XYZ's) of peptide sequencing. Nat. Rev. Mol. Cell Biol. 2004, 5 (9), 699-711.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , Issue.9 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 27
    • 85142151372 scopus 로고    scopus 로고
    • Maere, S.; Heymans, K.; Kuiper, M. BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 2005, 21 (16), 3448-9.
    • Maere, S.; Heymans, K.; Kuiper, M. BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 2005, 21 (16), 3448-9.
  • 28
    • 84876268257 scopus 로고    scopus 로고
    • European Bioinformatics Institute Gene Ontology Annotation GOA
    • European Bioinformatics Institute Gene Ontology Annotation (GOA) Database. http://www.ebi.ac.uk/GOA/.
    • Database
  • 29
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y.; Hochberg, Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc. 1995, (B57), 289-300.
    • (1995) J. R. Stat. Soc , vol.B57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 30
    • 33745591083 scopus 로고    scopus 로고
    • Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system
    • de Godoy, L. M.; Olsen, J. V.; de Souza, G. A.; Li, G.; Mortensen, P.; Mann, M., Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system. Genome Biol. 2006, 7 (6), R50.
    • (2006) Genome Biol , vol.7 , Issue.6
    • de Godoy, L.M.1    Olsen, J.V.2    de Souza, G.A.3    Li, G.4    Mortensen, P.5    Mann, M.6
  • 31
    • 34548336772 scopus 로고    scopus 로고
    • Higher-energy C-trap dissociation for peptide modification analysis
    • Olsen, J. V.; Macek, B.; Lange, O.; Makarov, A.; Horning, S.; Mann, M. Higher-energy C-trap dissociation for peptide modification analysis. Nat Methods 2007, 4 (9), 709-12.
    • (2007) Nat Methods , vol.4 , Issue.9 , pp. 709-712
    • Olsen, J.V.1    Macek, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 32
    • 33747866382 scopus 로고    scopus 로고
    • NeuroPred: A tool to predict cleavage sites in neuropeptide precursors and provide the masses of the resulting peptides
    • Web Server issue, W267-72
    • Southey, B. R.; Amare, A.; Zimmerman, T. A.; Rodriguez-Zas, S. L.; Sweedler, J. V. NeuroPred: a tool to predict cleavage sites in neuropeptide precursors and provide the masses of the resulting peptides. Nucleic Acids Res. 2006, 34 (Web Server issue), W267-72.
    • (2006) Nucleic Acids Res , vol.34
    • Southey, B.R.1    Amare, A.2    Zimmerman, T.A.3    Rodriguez-Zas, S.L.4    Sweedler, J.V.5
  • 33
    • 0033993470 scopus 로고    scopus 로고
    • Subtilase-like pro-protein convertases: From molecular specificity to therapeutic applications
    • Bergeron, F.; Leduc, R.; Day, R. Subtilase-like pro-protein convertases: from molecular specificity to therapeutic applications. J. Mol. Endocrinol. 2000, 24 (1), 1-22.
    • (2000) J. Mol. Endocrinol , vol.24 , Issue.1 , pp. 1-22
    • Bergeron, F.1    Leduc, R.2    Day, R.3
  • 34
    • 0027418132 scopus 로고
    • Peptidylglycine alpha-amidating monooxygenase: A multifunctional protein with catalytic, processing, and routing domains
    • Eipper, B. A.; Milgram, S. L.; Husten, E. J.; Yun, H. Y.; Mains, R. E. Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains. Protein Sci. 1993, 2 (4), 489-97.
    • (1993) Protein Sci , vol.2 , Issue.4 , pp. 489-497
    • Eipper, B.A.1    Milgram, S.L.2    Husten, E.J.3    Yun, H.Y.4    Mains, R.E.5
  • 35
    • 0022558755 scopus 로고
    • Corticotropin-releasing factors receptors in the pituitary gland and central nervous system: Methods and overview
    • Desouza, E. B.; Kuhar, M. J. Corticotropin-releasing factors receptors in the pituitary gland and central nervous system: Methods and overview. Methods Enzymol. 1986, 124, 560-590.
    • (1986) Methods Enzymol , vol.124 , pp. 560-590
    • Desouza, E.B.1    Kuhar, M.J.2
  • 36
    • 30444432702 scopus 로고    scopus 로고
    • Neuropeptide-processing enzymes: Applications for drug discovery
    • Fricker, L. D. Neuropeptide-processing enzymes: applications for drug discovery. Aaps J. 2005, 7 (2), E449-55.
    • (2005) Aaps J , vol.7 , Issue.2
    • Fricker, L.D.1
  • 37
    • 0019784255 scopus 로고
    • Pyroglutamic acid: Nonmetabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal
    • Abraham, G. N.; Podell, D. N. Pyroglutamic acid: nonmetabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal. Mol. Cell. Biochem. 1981, 38, 181-190.
    • (1981) Mol. Cell. Biochem , vol.38 , pp. 181-190
    • Abraham, G.N.1    Podell, D.N.2
  • 38
    • 0015816324 scopus 로고
    • Receptors for thyrotropin-releasing hormone in prolactin producing rat pituitary cells in culture
    • Hinkle, P. M.; Tashjian, A. H., Jr. Receptors for thyrotropin-releasing hormone in prolactin producing rat pituitary cells in culture. J. Biol. Chem. 1973, 248 (17), 6180-6.
    • (1973) J. Biol. Chem , vol.248 , Issue.17 , pp. 6180-6186
    • Hinkle, P.M.1    Tashjian Jr., A.H.2
  • 39
    • 0034839097 scopus 로고    scopus 로고
    • Screening for disulfide-rich peptides in biological sources by carboxyamidomethylation in combination with differential matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Neitz, S.; Jurgens, M.; Kellmann, M.; Schulz-Knappe, P.; Schrader, M. Screening for disulfide-rich peptides in biological sources by carboxyamidomethylation in combination with differential matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 2001, 15 (17), 1586-92.
    • (2001) Rapid Commun. Mass Spectrom , vol.15 , Issue.17 , pp. 1586-1592
    • Neitz, S.1    Jurgens, M.2    Kellmann, M.3    Schulz-Knappe, P.4    Schrader, M.5
  • 40
    • 0035010433 scopus 로고    scopus 로고
    • Evolution and classification of cystine knot-containing hormones and related extracellular signaling molecules
    • Vitt, U. A.; Hsu, S. Y.; Hsueh, A. J. Evolution and classification of cystine knot-containing hormones and related extracellular signaling molecules. Mol. Endocrinol. 2001, 15 (5), 681-94.
    • (2001) Mol. Endocrinol , vol.15 , Issue.5 , pp. 681-694
    • Vitt, U.A.1    Hsu, S.Y.2    Hsueh, A.J.3
  • 44
    • 0023779547 scopus 로고
    • Human joining peptide: A proopiomelanocortin product secreted as a homodimer
    • Bertagna, X.; Camus, F.; Lenne, F.; Girard, F.; Luton, J. P. Human joining peptide: a proopiomelanocortin product secreted as a homodimer. Mol. Endocrinol. 1988, 2 (11), 1108-14.
    • (1988) Mol. Endocrinol , vol.2 , Issue.11 , pp. 1108-1114
    • Bertagna, X.1    Camus, F.2    Lenne, F.3    Girard, F.4    Luton, J.P.5
  • 45
    • 0023755403 scopus 로고
    • Alpha-amidated peptides derived from pro-opiomelanocortin in human pituitary tumours
    • Fenger, M.; Johnsen, A. H. Alpha-amidated peptides derived from pro-opiomelanocortin in human pituitary tumours. J. Endocrinol. 1988, 118 (2), 329-38.
    • (1988) J. Endocrinol , vol.118 , Issue.2 , pp. 329-338
    • Fenger, M.1    Johnsen, A.H.2
  • 46
    • 0344382111 scopus 로고    scopus 로고
    • Neurexophilins form a conserved family of neuropeptide-like glycoproteins
    • Missler, M.; Sudhof, T. C. Neurexophilins form a conserved family of neuropeptide-like glycoproteins. J. Neurosci. 1998, 18 (10), 3630-8.
    • (1998) J. Neurosci , vol.18 , Issue.10 , pp. 3630-3638
    • Missler, M.1    Sudhof, T.C.2
  • 47
    • 0024291209 scopus 로고
    • Proline residues in the maturation and degradation of peptide hormones and neuropeptides
    • Mentlein, R. Proline residues in the maturation and degradation of peptide hormones and neuropeptides. FEBS Lett. 1988, 234 (2), 251-6.
    • (1988) FEBS Lett , vol.234 , Issue.2 , pp. 251-256
    • Mentlein, R.1
  • 48
    • 9144243918 scopus 로고    scopus 로고
    • The synaptotagmins: Calcium sensors for vesicular trafficking
    • Yoshihara, M.; Montana, E. S. The synaptotagmins: calcium sensors for vesicular trafficking. Neuroscientist 2004, 10 (6), 566-74.
    • (2004) Neuroscientist , vol.10 , Issue.6 , pp. 566-574
    • Yoshihara, M.1    Montana, E.S.2
  • 49
    • 0037458166 scopus 로고    scopus 로고
    • FXYD proteins: New tissue-specific regulators of the ubiquitous Na,K-ATPase
    • Crambert, G.; Geering, K. FXYD proteins: new tissue-specific regulators of the ubiquitous Na,K-ATPase. Sci. STKE 2003, 2003 (166), RE1.
    • (2003) Sci. STKE , vol.2003 , Issue.166
    • Crambert, G.1    Geering, K.2
  • 50
    • 0037444536 scopus 로고    scopus 로고
    • Feschenko, M. S.; Donnet, C.; Wetzel, R. K.; Asinovski, N. K.; Jones, L. R.; Sweadner, K. J. Phospholemman, a single-span membrane protein, is an accessory protein of Na,K-ATPase in cerebellum and choroid plexus. J. Neurosci. 2003, 23 (6), 2161-9.
    • Feschenko, M. S.; Donnet, C.; Wetzel, R. K.; Asinovski, N. K.; Jones, L. R.; Sweadner, K. J. Phospholemman, a single-span membrane protein, is an accessory protein of Na,K-ATPase in cerebellum and choroid plexus. J. Neurosci. 2003, 23 (6), 2161-9.
  • 51
    • 0026580016 scopus 로고
    • Isolation and sequence of the granulin precursor cDNA from human bone marrow reveals tandem cysteine-rich granulin domains
    • Bhandari, V.; Palfree, R. G.; Bateman, A. Isolation and sequence of the granulin precursor cDNA from human bone marrow reveals tandem cysteine-rich granulin domains. Proc. Natl. Acad. Sci. U.S.A. 1992, 89 (5), 1715-9.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , Issue.5 , pp. 1715-1719
    • Bhandari, V.1    Palfree, R.G.2    Bateman, A.3
  • 52
    • 0032541183 scopus 로고    scopus 로고
    • Post-translational processing of the insulin-like growth factor-2 precursor. Analysis of O-glycosylation and endoproteolysis
    • Duguay, S. J.; Jin, Y.; Stein, J.; Duguay, A. N.; Gardner, P.; Steiner, D. F. Post-translational processing of the insulin-like growth factor-2 precursor. Analysis of O-glycosylation and endoproteolysis. J. Biol. Chem. 1998, 273 (29), 18443-51.
    • (1998) J. Biol. Chem , vol.273 , Issue.29 , pp. 18443-18451
    • Duguay, S.J.1    Jin, Y.2    Stein, J.3    Duguay, A.N.4    Gardner, P.5    Steiner, D.F.6
  • 53
    • 0040298788 scopus 로고
    • Polypeptides with nonsuppressible insulin-like and cell-growth promoting activities in human serum: Isolation, chemical characterization, and some biological properties of forms I and II
    • Rinderknecht, E.; Humbel, R. E. Polypeptides with nonsuppressible insulin-like and cell-growth promoting activities in human serum: isolation, chemical characterization, and some biological properties of forms I and II. Proc. Natl. Acad. Sci. U.S.A. 1976, 73 (7), 2365-9.
    • (1976) Proc. Natl. Acad. Sci. U.S.A , vol.73 , Issue.7 , pp. 2365-2369
    • Rinderknecht, E.1    Humbel, R.E.2
  • 54
    • 0033305185 scopus 로고    scopus 로고
    • Recombinant E-peptides of pro-IGF-I have mitogenic activity
    • Tian, X. C.; Chen, M. J.; Pantschenko, A. G.; Yang, T. J.; Chen, T. T. Recombinant E-peptides of pro-IGF-I have mitogenic activity. Endocrinology 1999, 140 (7), 3387-90.
    • (1999) Endocrinology , vol.140 , Issue.7 , pp. 3387-3390
    • Tian, X.C.1    Chen, M.J.2    Pantschenko, A.G.3    Yang, T.J.4    Chen, T.T.5
  • 55
    • 0026673961 scopus 로고
    • Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein
    • Higashiyama, S.; Lau, K.; Besner, G. E.; Abraham, J. A.; Klagsbrun, M. Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein. J. Biol. Chem. 1992, 267 (9), 6205-12.
    • (1992) J. Biol. Chem , vol.267 , Issue.9 , pp. 6205-6212
    • Higashiyama, S.1    Lau, K.2    Besner, G.E.3    Abraham, J.A.4    Klagsbrun, M.5
  • 56
    • 33645540607 scopus 로고    scopus 로고
    • Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy
    • Miyamoto, S.; Yagi, H.; Yotsumoto, F.; Kawarabayashi, T.; Mekada, E. Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy. Cancer Sci. 2006, 97 (5), 341-7.
    • (2006) Cancer Sci , vol.97 , Issue.5 , pp. 341-347
    • Miyamoto, S.1    Yagi, H.2    Yotsumoto, F.3    Kawarabayashi, T.4    Mekada, E.5
  • 59
    • 0035006525 scopus 로고    scopus 로고
    • Hypocretin/orexin, sleep and narcolepsy
    • Hungs, M.; Mignot, E. Hypocretin/orexin, sleep and narcolepsy. Bioessays 2001, 23 (5), 397-408.
    • (2001) Bioessays , vol.23 , Issue.5 , pp. 397-408
    • Hungs, M.1    Mignot, E.2
  • 60
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins including a large proportion of membranes proteins
    • Adachi, J.; Kumar, C.; Zhang, Y.; Olsen, J. V.; Mann, M. The human urinary proteome contains more than 1500 proteins including a large proportion of membranes proteins. Genome Biol. 2006, 7 (9), R80.
    • (2006) Genome Biol , vol.7 , Issue.9
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4    Mann, M.5
  • 61
    • 33745104040 scopus 로고    scopus 로고
    • Large-scale and high-confidence proteomic analysis of human seminal plasma
    • Pilch, B.; Mann, M., Large-scale and high-confidence proteomic analysis of human seminal plasma. Genome Biol. 2006, 7 (5), R40.
    • (2006) Genome Biol , vol.7 , Issue.5
    • Pilch, B.1    Mann, M.2
  • 62
    • 33748754288 scopus 로고    scopus 로고
    • Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors
    • de Souza, G. A.; Godoy, L. M.; Mann, M. Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors. Genome Biol. 2006, 7 (8), R72.
    • (2006) Genome Biol , vol.7 , Issue.8
    • de Souza, G.A.1    Godoy, L.M.2    Mann, M.3
  • 63
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • Olsen, J. V.; Mann, M. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (37), 13417-22.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.37 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 64
    • 0038175144 scopus 로고    scopus 로고
    • Zeeberg, B. R.; Feng, W.; Wang, G.; Wang, M. D.; Fojo, A. T.; Sunshine, M.; Narasimhan, S.; Kane, D. W.; Reinhold, W. C.; Lababidi, S.; Bussey, K. J.; Riss, J.; Barrett, J. C.; Weinstein, J. N. GoMiner: a resource for biological interpretation of genomic and proteomic data. Genome Biol. 2003, 4 (4). R28.
    • Zeeberg, B. R.; Feng, W.; Wang, G.; Wang, M. D.; Fojo, A. T.; Sunshine, M.; Narasimhan, S.; Kane, D. W.; Reinhold, W. C.; Lababidi, S.; Bussey, K. J.; Riss, J.; Barrett, J. C.; Weinstein, J. N. GoMiner: a resource for biological interpretation of genomic and proteomic data. Genome Biol. 2003, 4 (4). R28.
  • 65
    • 0346801873 scopus 로고    scopus 로고
    • Harris, M. A, Clark, J, Ireland, A, Lomax, J, Ashburner, M, Foulger, R, Eilbeck, K, Lewis, S, Marshall, B, Mungall, C, Richter, J, Rubin, G. M, Blake, J. A, Bult, C, Dolan, M, Drabkin, H, Eppig, J. T, Hill, D. P, Ni, L, Ringwald, M, Balakrishnan, R, Cherry, J. M, Christie, K. R, Costanzo, M. C, Dwight, S. S, Engel, S, Fisk, D. G, Hirschman, J. E, Hong, E. L, Nash, R. S, Sethuraman, A, Theesfeld, C. L, Botstein, D, Dolinski, K, Feierbach, B, Berardini, T, Mundodi, S, Rhee, S. Y, Apweiler, R, Barrell, D, Camon, E, Dimmer, E, Lee, V, Chisholm, R, Gaudet, P, Kibbe, W, Kishore, R, Schwarz, E. M, Sternberg, P, Gwinn, M, Hannick, L, Wortman, J, Berriman, M, Wood, V, de la Cruz, N, Tonellato, P, Jaiswal, P, Seigfried, T, White, R. The Gene Ontology (GO) database and informatics resource. Nucleic Acids Res. 2004, 32 Database issue, D258-61
    • Harris, M. A.; Clark, J.; Ireland, A.; Lomax, J.; Ashburner, M.; Foulger, R.; Eilbeck, K.; Lewis, S.; Marshall, B.; Mungall, C.; Richter, J.; Rubin, G. M.; Blake, J. A.; Bult, C.; Dolan, M.; Drabkin, H.; Eppig, J. T.; Hill, D. P.; Ni, L.; Ringwald, M.; Balakrishnan, R.; Cherry, J. M.; Christie, K. R.; Costanzo, M. C.; Dwight, S. S.; Engel, S.; Fisk, D. G.; Hirschman, J. E.; Hong, E. L.; Nash, R. S.; Sethuraman, A.; Theesfeld, C. L.; Botstein, D.; Dolinski, K.; Feierbach, B.; Berardini, T.; Mundodi, S.; Rhee, S. Y.; Apweiler, R.; Barrell, D.; Camon, E.; Dimmer, E.; Lee, V.; Chisholm, R.; Gaudet, P.; Kibbe, W.; Kishore, R.; Schwarz, E. M.; Sternberg, P.; Gwinn, M.; Hannick, L.; Wortman, J.; Berriman, M.; Wood, V.; de la Cruz, N.; Tonellato, P.; Jaiswal, P.; Seigfried, T.; White, R. The Gene Ontology (GO) database and informatics resource. Nucleic Acids Res. 2004, 32 (Database issue), D258-61.
  • 66
    • 33847151166 scopus 로고    scopus 로고
    • A combined dataset of human cerebrospinal fluid proteins identified by multidimensional chromatography and tandem mass spectrometry
    • Pan, S.; Zhu, D.; Quinn, J. F.; Peskind, E. R.; Montine, T. J.; Lin, B.; Goodlett, D. R.; Taylor, G.; Eng, J.; Zhang, J. A combined dataset of human cerebrospinal fluid proteins identified by multidimensional chromatography and tandem mass spectrometry. Proteomics 2007, 7 (3), 469-73.
    • (2007) Proteomics , vol.7 , Issue.3 , pp. 469-473
    • Pan, S.1    Zhu, D.2    Quinn, J.F.3    Peskind, E.R.4    Montine, T.J.5    Lin, B.6    Goodlett, D.R.7    Taylor, G.8    Eng, J.9    Zhang, J.10
  • 67
    • 29244469691 scopus 로고    scopus 로고
    • Protein analysis in human cerebrospinal fluid: Physiological aspects, current progress and future challenges
    • Huhmer, A. F.; Biringer, R. G.; Amato, H.; Fonteh, A. N.; Harrington, M. G. Protein analysis in human cerebrospinal fluid: Physiological aspects, current progress and future challenges. Dis. Markers 2006, 22 (1-2), 3-26.
    • (2006) Dis. Markers , vol.22 , Issue.1-2 , pp. 3-26
    • Huhmer, A.F.1    Biringer, R.G.2    Amato, H.3    Fonteh, A.N.4    Harrington, M.G.5
  • 68
    • 33644864034 scopus 로고    scopus 로고
    • Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study
    • States, D. J.; Omenn, G. S.; Blackwell, T. W.; Fermin, D.; Eng, J.; Speicher, D. W.; Hanash, S. M. Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study. Nat. Biotechnol. 2006, 24 (3), 333-8.
    • (2006) Nat. Biotechnol , vol.24 , Issue.3 , pp. 333-338
    • States, D.J.1    Omenn, G.S.2    Blackwell, T.W.3    Fermin, D.4    Eng, J.5    Speicher, D.W.6    Hanash, S.M.7
  • 69
    • 0033817591 scopus 로고    scopus 로고
    • Remarkable roles of proteolysis on and beyond the cell surface
    • Blobel, C. P. Remarkable roles of proteolysis on and beyond the cell surface. Curr. Opin. Cell Biol. 2000, 12 (5), 606-12.
    • (2000) Curr. Opin. Cell Biol , vol.12 , Issue.5 , pp. 606-612
    • Blobel, C.P.1
  • 70
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun, T.; Shen, R. F.; Knepper, M. A. Identification and proteomic profiling of exosomes in human urine. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (36), 13368-73.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.36 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 71
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 2001, 81 (2), 741-66.
    • (2001) Physiol. Rev , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 72
    • 0033615580 scopus 로고    scopus 로고
    • The presenilins in Alzheimer's disease - proteolysis holds the key
    • Haass, C.; De Strooper, B. The presenilins in Alzheimer's disease - proteolysis holds the key. Science 1999, 286 (5441), 916-9.
    • (1999) Science , vol.286 , Issue.5441 , pp. 916-919
    • Haass, C.1    De Strooper, B.2
  • 73
    • 33646349010 scopus 로고    scopus 로고
    • Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor protein
    • Neumann, S.; Schobel, S.; Jager, S.; Trautwein, A.; Haass, C.; Pietrzik, C. U.; Lichtenthaler, S. F. Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor protein. J. Biol. Chem. 2006, 281 (11), 7583-94.
    • (2006) J. Biol. Chem , vol.281 , Issue.11 , pp. 7583-7594
    • Neumann, S.1    Schobel, S.2    Jager, S.3    Trautwein, A.4    Haass, C.5    Pietrzik, C.U.6    Lichtenthaler, S.F.7
  • 74
    • 33747075228 scopus 로고    scopus 로고
    • Interaction of the amyloid precursor like protein 1 with the alpha(2A)-adrenergic receptor increases agonist-mediated inhibition of adenylate cyclase
    • Weber, B.; Schaper, C.; Scholz, J.; Bein, B.; Rodde, C.; Tonner, P. Interaction of the amyloid precursor like protein 1 with the alpha(2A)-adrenergic receptor increases agonist-mediated inhibition of adenylate cyclase. Cell Signal 2006, 18 (10), 1748-1757.
    • (2006) Cell Signal , vol.18 , Issue.10 , pp. 1748-1757
    • Weber, B.1    Schaper, C.2    Scholz, J.3    Bein, B.4    Rodde, C.5    Tonner, P.6
  • 75
    • 0000216230 scopus 로고
    • Structure and metabolism of connective tissue proteoglycans
    • Lennarz, W, Ed, Plenum Press: NY
    • Roden, L. Structure and metabolism of connective tissue proteoglycans. In The Biochemistry of Glycoproteins and Proteoglycans, Lennarz, W., Ed.; Plenum Press: NY, 1980; pp 269-314.
    • (1980) The Biochemistry of Glycoproteins and Proteoglycans , pp. 269-314
    • Roden, L.1
  • 76
    • 0001186480 scopus 로고
    • Simultaneous secretion of xylosyltransferase and chondroitin sulphate proteoglycane in chondrocyte cultures
    • Kähnert, H.; Paddenberg, R.; Kleesiek, K. Simultaneous secretion of xylosyltransferase and chondroitin sulphate proteoglycane in chondrocyte cultures. Eur. J. Clin. Chem. Clin. Biochem. 1991, 29, 624-625.
    • (1991) Eur. J. Clin. Chem. Clin. Biochem , vol.29 , pp. 624-625
    • Kähnert, H.1    Paddenberg, R.2    Kleesiek, K.3
  • 77
    • 84941402393 scopus 로고
    • UDP-D-xylose: Proteoglycan core protein beta-D-xylosyltransferase: a new marker of cartilage destruction in chronic joint diseases
    • Kleesiek, K.; Reinards, R.; Okusi, J.; Wolf, B.; Greiling, H. UDP-D-xylose: proteoglycan core protein beta-D-xylosyltransferase: a new marker of cartilage destruction in chronic joint diseases. J. Clin. Chem. Clin. Biochem. 1987, 25 (8), 473-81.
    • (1987) J. Clin. Chem. Clin. Biochem , vol.25 , Issue.8 , pp. 473-481
    • Kleesiek, K.1    Reinards, R.2    Okusi, J.3    Wolf, B.4    Greiling, H.5
  • 80
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • Vidal, R.; Frangione, B.; Rostagno, A.; Mead, S.; Revesz, T.; Plant, G.; Ghiso, J. A stop-codon mutation in the BRI gene associated with familial British dementia, Nature 1999, 399 (6738), 776-81.
    • (1999) Nature , vol.399 , Issue.6738 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Revesz, T.5    Plant, G.6    Ghiso, J.7
  • 83
    • 0344825108 scopus 로고    scopus 로고
    • Receptor and nonreceptor protein tyrosine phosphatases in the nervous system
    • Paul, S.; Lombroso, P. J. Receptor and nonreceptor protein tyrosine phosphatases in the nervous system. Cell. Mol. Life Sci. 2003, 60 (11), 2465-82.
    • (2003) Cell. Mol. Life Sci , vol.60 , Issue.11 , pp. 2465-2482
    • Paul, S.1    Lombroso, P.J.2
  • 84
    • 0036842987 scopus 로고    scopus 로고
    • A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions
    • Harroch, S.; Furtado, G. C.; Brueck, W.; Rosenbluth, J.; Lafaille, J.; Chao, M.; Buxbaum, J. D.; Schlessinger, J. A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions. Nat. Genet. 2002, 32 (3), 411-4.
    • (2002) Nat. Genet , vol.32 , Issue.3 , pp. 411-414
    • Harroch, S.1    Furtado, G.C.2    Brueck, W.3    Rosenbluth, J.4    Lafaille, J.5    Chao, M.6    Buxbaum, J.D.7    Schlessinger, J.8
  • 86
    • 0029940504 scopus 로고    scopus 로고
    • ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules
    • Solimena, M.; Dirkx, R., Jr.; Hermel, J. M.; Pleasic-Williams, S.; Shapiro, J. A.; Caron, L.; Rabin, D. U. ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules. EMBO J. 1996, 15 (9), 2102-14.
    • (1996) EMBO J , vol.15 , Issue.9 , pp. 2102-2114
    • Solimena, M.1    Dirkx Jr., R.2    Hermel, J.M.3    Pleasic-Williams, S.4    Shapiro, J.A.5    Caron, L.6    Rabin, D.U.7
  • 87
    • 0034534086 scopus 로고    scopus 로고
    • Growth cone steering by receptor tyrosine phosphatase delta defines a distinct class of guidance cue
    • Sun, Q. L.; Wang, J.; Bookman, R. J.; Bixby, J. L. Growth cone steering by receptor tyrosine phosphatase delta defines a distinct class of guidance cue. Mol. Cell Neurosci. 2000, 16 (5), 686-95.
    • (2000) Mol. Cell Neurosci , vol.16 , Issue.5 , pp. 686-695
    • Sun, Q.L.1    Wang, J.2    Bookman, R.J.3    Bixby, J.L.4


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