메뉴 건너뛰기




Volumn , Issue , 2006, Pages 113-135

Peptidomics Technologies and Applications in Drug Research

Author keywords

Applications of differential display peptidomics; Development of peptidomics technologies; Peptides in drug research; Peptidomics technologies and applications in drug research

Indexed keywords

BIOMARKERS; DRUG INTERACTIONS; ENZYME ACTIVITY; GENE EXPRESSION; MASS SPECTROMETRY; MOLECULAR BIOLOGY; PEPTIDES; PHYSIOLOGICAL MODELS; PHYSIOLOGY; TARGETED DRUG DELIVERY;

EID: 84945282969     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/3527608230.ch6     Document Type: Chapter
Times cited : (2)

References (105)
  • 1
    • 77951382343 scopus 로고
    • The structure of bovine vasopressin
    • Acher, R., Chauvet, J. (1953). The structure of bovine vasopressin. Biochim. Biophys. Acta 12, 487-488.
    • (1953) Biochim. Biophys. Acta , vol.12 , pp. 487-488
    • Acher, R.1    Chauvet, J.2
  • 2
    • 0008327862 scopus 로고
    • Purification of oxytocin and vasopressin by way of a protein complex
    • Acher, R., Light, A., Du Vigneaud, V. (1958). Purification of oxytocin and vasopressin by way of a protein complex. J. Biol. Chem. 233, 116-120.
    • (1958) J. Biol. Chem , vol.233 , pp. 116-120
    • Acher, R.1    Light, A.2    Du Vigneaud, V.3
  • 3
    • 3442900472 scopus 로고    scopus 로고
    • PT-100, a small molecule dipeptidyl peptidase inhibitor, has potent anti-tumor effects and augments antibody-mediated cytotoxicity via a novel immune mechanism
    • Adams, S., Miller, G. T., Jesson, M. I., Watanabe, T., Jones, B., Wallner, B. P. (2004). PT-100, a small molecule dipeptidyl peptidase inhibitor, has potent anti-tumor effects and augments antibody-mediated cytotoxicity via a novel immune mechanism. Cancer Res. 64, 5471-5480.
    • (2004) Cancer Res , vol.64 , pp. 5471-5480
    • Adams, S.1    Miller, G.T.2    Jesson, M.I.3    Watanabe, T.4    Jones, B.5    Wallner, B.P.6
  • 4
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., Mann, M. (2003). Mass spectrometry-based proteomics. Nature 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 5
    • 2442482515 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase-4 reduces glycemia, sustains insulin levels, and reduces glucagon levels in type 2 diabetes
    • Ahren, B., Landin-Olsson, M., Jansson, P. A., Svensson, M., Holmes, D., Schweizer, A. (2004). Inhibition of dipeptidyl peptidase-4 reduces glycemia, sustains insulin levels, and reduces glucagon levels in type 2 diabetes. J. Clin. Endocrinol. Metab. 89, 2078-2084.
    • (2004) J. Clin. Endocrinol. Metab , vol.89 , pp. 2078-2084
    • Ahren, B.1    Landin-Olsson, M.2    Jansson, P.A.3    Svensson, M.4    Holmes, D.5    Schweizer, A.6
  • 6
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson, L., Seilhamer, J. (1997). A comparison of selected mRNA and protein abundances in human liver. Electrophoresis 18, 533-537.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 7
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: history, character, and diagnostic prospects
    • Anderson, N. L., Anderson, N. G. (2002). The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell Proteomics 1, 845-867.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 11
    • 0026425985 scopus 로고
    • Pancreatic extracts in the treatment of diabetes mellitus: preliminary report 1922
    • Banting, F. G., Best, C. H., Collip, J. B., Campbell, W. R., Fletcher, A. A. (1991). Pancreatic extracts in the treatment of diabetes mellitus: preliminary report 1922. CMAJ 145, 1281-1286.
    • (1991) CMAJ , vol.145 , pp. 1281-1286
    • Banting, F.G.1    Best, C.H.2    Collip, J.B.3    Campbell, W.R.4    Fletcher, A.A.5
  • 12
    • 0035496988 scopus 로고    scopus 로고
    • Future aspects of psychoneuroimmunology - lymphocyte peptides reflecting psychiatric disorders studied by mass spectrometry
    • Bergquist, J., Ekman, R. (2001). Future aspects of psychoneuroimmunology - lymphocyte peptides reflecting psychiatric disorders studied by mass spectrometry. Arch. Physiol. Biochem. 109, 369-371.
    • (2001) Arch. Physiol. Biochem , vol.109 , pp. 369-371
    • Bergquist, J.1    Ekman, R.2
  • 13
    • 0141738373 scopus 로고    scopus 로고
    • CSF markers for incipient Alzheimer's disease
    • Blennow, K., Hampel, H. (2003). CSF markers for incipient Alzheimer's disease. Lancet Neurol. 2, 605-613.
    • (2003) Lancet Neurol , vol.2 , pp. 605-613
    • Blennow, K.1    Hampel, H.2
  • 14
    • 0036729136 scopus 로고    scopus 로고
    • Practical quantitative biomedical applications of MALDI-TOF mass spectrometry
    • Bucknall, M., Fung, K. Y., Duncan, M. W. (2002). Practical quantitative biomedical applications of MALDI-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 13, 1015-1027.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 1015-1027
    • Bucknall, M.1    Fung, K.Y.2    Duncan, M.W.3
  • 16
    • 0014961883 scopus 로고
    • Characterization of ovine hypothalamic hypophysiotropic TSH-releasing factor
    • Burgus, R., Dunn, T. F., Desiderio, D., Ward, D. N., Vale, W., Guillemin, R. (1970). Characterization of ovine hypothalamic hypophysiotropic TSH-releasing factor. Nature 226, 321-325.
    • (1970) Nature , vol.226 , pp. 321-325
    • Burgus, R.1    Dunn, T.F.2    Desiderio, D.3    Ward, D.N.4    Vale, W.5    Guillemin, R.6
  • 18
    • 0345490814 scopus 로고    scopus 로고
    • Secreted protein prediction system combining CJ-SPHMM, TMHMM, PSORT
    • Chen, Y., Yu, P., Luo, J., Jiang, Y. (2003). Secreted protein prediction system combining CJ-SPHMM, TMHMM, PSORT. Mamm. Genome 14, 859-865.
    • (2003) Mamm. Genome , vol.14 , pp. 859-865
    • Chen, Y.1    Yu, P.2    Luo, J.3    Jiang, Y.4
  • 19
    • 15044356642 scopus 로고    scopus 로고
    • Application of serum protein pattern model in diagnosis of colorectal cancer
    • Chen, Y. D., Zheng, S., Yu, J. K., Hu, X. (2004). Application of serum protein pattern model in diagnosis of colorectal cancer. Zhonghua Zhong Liu Za Zhi 26, 417-420.
    • (2004) Zhonghua Zhong Liu Za Zhi , vol.26 , pp. 417-420
    • Chen, Y.D.1    Zheng, S.2    Yu, J.K.3    Hu, X.4
  • 23
    • 0038363953 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV substrates An update on in vitro peptide hydrolysis by human DPPIV
    • de Meester, I., Lambeir, A. M., Proost, P., Scharpe, S. (2003). Dipeptidyl peptidase IV substrates An update on in vitro peptide hydrolysis by human DPPIV. Adv. Exp. Med. Biol. 524, 3-17.
    • (2003) Adv. Exp. Med. Biol , vol.524 , pp. 3-17
    • de Meester, I.1    Lambeir, A.M.2    Proost, P.3    Scharpe, S.4
  • 24
    • 0036441844 scopus 로고    scopus 로고
    • The value of improving the productivity of the drug development process: faster times and better decisions
    • DiMasi, J. A. (2002). The value of improving the productivity of the drug development process: faster times and better decisions. Pharmacoeconomics 20 (Suppl. 3), 1-10.
    • (2002) Pharmacoeconomics , vol.20 , pp. 1-10
    • DiMasi, J.A.1
  • 25
    • 0037374498 scopus 로고    scopus 로고
    • The price of innovation: new estimates of drug development costs
    • DiMasi, J. A., Hansen, R. W., Grabowski, H. G. (2003). The price of innovation: new estimates of drug development costs. J. Health Econ. 22, 151-185.
    • (2003) J. Health Econ , vol.22 , pp. 151-185
    • DiMasi, J.A.1    Hansen, R.W.2    Grabowski, H.G.3
  • 26
    • 0141446228 scopus 로고    scopus 로고
    • Enhancing incretin action for the treatment of type 2 diabetes
    • Drucker, D. J. (2003). Enhancing incretin action for the treatment of type 2 diabetes. Diabetes Care 26, 2929-2940.
    • (2003) Diabetes Care , vol.26 , pp. 2929-2940
    • Drucker, D.J.1
  • 27
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., Whitehouse, C. M. (1989). Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 28
    • 85017627784 scopus 로고    scopus 로고
    • Process for determining the status of an organism by peptide measurement
    • [WO 98/07036] 13-8-1996. Published 19-2-1998
    • Forssmann, W. G., Schulz-Knappe, P., Schrader, M., Opitz, H. G. (1996). Process for determining the status of an organism by peptide measurement [WO 98/07036] 13-8-1996. Published 19-2-1998.
    • (1996)
    • Forssmann, W.G.1    Schulz-Knappe, P.2    Schrader, M.3    Opitz, H.G.4
  • 29
    • 0038004636 scopus 로고    scopus 로고
    • Clinical biomarkers in drug discovery and development
    • Frank, R., Hargreaves, R. (2003). Clinical biomarkers in drug discovery and development. Nat. Rev. Drug Discov. 2, 566-580.
    • (2003) Nat. Rev. Drug Discov , vol.2 , pp. 566-580
    • Frank, R.1    Hargreaves, R.2
  • 30
    • 0029825451 scopus 로고    scopus 로고
    • Carboxypeptidase E activity is deficient in mice with the fat mutation Effect on peptide processing
    • Fricker, L. D., Berman, Y. L., Leiter, E. H., Devi, L. A. (1996). Carboxypeptidase E activity is deficient in mice with the fat mutation Effect on peptide processing. J. Biol. Chem. 271, 30619-30624.
    • (1996) J. Biol. Chem , vol.271 , pp. 30619-30624
    • Fricker, L.D.1    Berman, Y.L.2    Leiter, E.H.3    Devi, L.A.4
  • 32
    • 0035895526 scopus 로고    scopus 로고
    • Sequence interpretation. Making sense of the sequence
    • Galas, D. J. (2001). Sequence interpretation. Making sense of the sequence. Science 291, 1257-1260.
    • (2001) Science , vol.291 , pp. 1257-1260
    • Galas, D.J.1
  • 33
    • 3242778563 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of vertebrates
    • Ganz, T. (2004). Defensins: antimicrobial peptides of vertebrates. C. R. Biol. 327, 539-549.
    • (2004) C. R. Biol , vol.327 , pp. 539-549
    • Ganz, T.1
  • 34
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S. P., Rochon, Y., Franza, B. R., Aebersold, R. (1999). Correlation between protein and mRNA abundance in yeast. Mol. Cell Biol. 19, 1720-1730.
    • (1999) Mol. Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 35
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: a new source of antibiotics
    • Hancock, R. E., Lehrer, R. (1998). Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16, 82-88.
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 36
    • 0024829755 scopus 로고
    • Processing of pro-hormone precursor proteins
    • Harris, R. B. (1989). Processing of pro-hormone precursor proteins. Arch. Biochem. Biophys. 275, 315-333.
    • (1989) Arch. Biochem. Biophys , vol.275 , pp. 315-333
    • Harris, R.B.1
  • 37
    • 0037738906 scopus 로고    scopus 로고
    • Using BNP to diagnose, manage, treat heart failure
    • Hobbs, R. E. (2003). Using BNP to diagnose, manage, treat heart failure. Cleve Clin. J. Med. 70, 333-336.
    • (2003) Cleve Clin. J. Med , vol.70 , pp. 333-336
    • Hobbs, R.E.1
  • 38
    • 14044264798 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 and inhibitors of dipeptidyl peptidase IV in the treatment of type 2 diabetes mellitus
    • Holst, J. J., Deacon, C. F. (2004). Glucagon-like peptide 1 and inhibitors of dipeptidyl peptidase IV in the treatment of type 2 diabetes mellitus. Curr. Opin. Pharmacol. 4, 589-596.
    • (2004) Curr. Opin. Pharmacol , vol.4 , pp. 589-596
    • Holst, J.J.1    Deacon, C.F.2
  • 39
    • 3342964033 scopus 로고    scopus 로고
    • Biomarker discovery and validation: technologies and integrative approaches
    • Ilyin, S. E., Belkowski, S. M., Plata-Salaman, C. R. (2004). Biomarker discovery and validation: technologies and integrative approaches. Trends Biotechnol. 22, 411-416.
    • (2004) Trends Biotechnol , vol.22 , pp. 411-416
    • Ilyin, S.E.1    Belkowski, S.M.2    Plata-Salaman, C.R.3
  • 44
    • 0029832475 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization MS: a progress report
    • Karas, M. (1996). Matrix-assisted laser desorption ionization MS: a progress report. Biochem. Soc. Trans. 24, 897-900.
    • (1996) Biochem. Soc. Trans , vol.24 , pp. 897-900
    • Karas, M.1
  • 46
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher, N. L. (2004). Top-down proteomics. Anal. Chem. 76, 197A-203A.
    • (2004) Anal. Chem , vol.76 , pp. 197A-203A
    • Kelleher, N.L.1
  • 48
    • 0345392692 scopus 로고    scopus 로고
    • Protein & Peptide Drug Delivery - Third International Conference. Minimally invasive delivery methods 22-23 September 2003, Philadelphia, PA, USA
    • Kochendoerfer, G. (2003). Protein & Peptide Drug Delivery - Third International Conference. Minimally invasive delivery methods 22-23 September 2003, Philadelphia, PA, USA. IDrugs 6, 1043-1045.
    • (2003) IDrugs , vol.6 , pp. 1043-1045
    • Kochendoerfer, G.1
  • 50
    • 0030722252 scopus 로고    scopus 로고
    • Carboxypeptidase E and obesity in the mouse
    • Leiter, E. H. (1997). Carboxypeptidase E and obesity in the mouse. J. Endocrinol. 155, 211-214.
    • (1997) J. Endocrinol , vol.155 , pp. 211-214
    • Leiter, E.H.1
  • 51
    • 0035037328 scopus 로고    scopus 로고
    • Use of biomarkers and surrogate endpoints in drug development and regulatory decision making: criteria, validation, strategies
    • Lesko, L. J., Atkinson, A. J. (2001). Use of biomarkers and surrogate endpoints in drug development and regulatory decision making: criteria, validation, strategies. Annu. Rev. Pharmacol. Toxicol. 41, 347-366.
    • (2001) Annu. Rev. Pharmacol. Toxicol , vol.41 , pp. 347-366
    • Lesko, L.J.1    Atkinson, A.J.2
  • 52
    • 0034176654 scopus 로고    scopus 로고
    • Single-cell MALDI: a new tool for direct peptide profiling
    • Li, L., Garden, R. W., Sweedler, J. V. (2000). Single-cell MALDI: a new tool for direct peptide profiling. Trends Biotechnol. 18, 151-160.
    • (2000) Trends Biotechnol , vol.18 , pp. 151-160
    • Li, L.1    Garden, R.W.2    Sweedler, J.V.3
  • 54
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyzes gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein, R., Gallwitz, B., Schmidt, W. E. (1993). Dipeptidyl-peptidase IV hydrolyzes gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. 214, 829-835.
    • (1993) Eur. J. Biochem , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 55
    • 0035261653 scopus 로고    scopus 로고
    • Protein functions and biological contexts
    • Miklos, G. L., Maleszka, R. (2001). Protein functions and biological contexts. Proteomics 1, 169-178.
    • (2001) Proteomics , vol.1 , pp. 169-178
    • Miklos, G.L.1    Maleszka, R.2
  • 56
    • 14744276328 scopus 로고    scopus 로고
    • Top-down identification of endogenous peptides up to 9 kDa in cerebrospinal fluid and brain tissue by nanoelectrospray quadrupole time-of-flight tandem mass spectrometry
    • Möhring, T., Kellmann, M., Jürgens, M., Schrader, M. (2005). Top-down identification of endogenous peptides up to 9 kDa in cerebrospinal fluid and brain tissue by nanoelectrospray quadrupole time-of-flight tandem mass spectrometry. J. Mass Spectrom. 40, 214-226.
    • (2005) J. Mass Spectrom , vol.40 , pp. 214-226
    • Möhring, T.1    Kellmann, M.2    Jürgens, M.3    Schrader, M.4
  • 57
    • 7344242379 scopus 로고
    • On the necessity of isolating peptides
    • Schneider, C. H., Eberle, A. N. (Eds.), ESCOM, Leiden
    • Mutt, V. (1992). On the necessity of isolating peptides. In Schneider, C. H., Eberle, A. N. (Eds.), Peptides. ESCOM, Leiden, pp. 3-20.
    • (1992) Peptides , pp. 3-20
    • Mutt, V.1
  • 59
    • 0028874417 scopus 로고
    • Aerosolization of lactide/glycolide copolymer (PLGA) nanospheres for pulmonary delivery of peptide-drugs
    • Niwa, T., Takeuchi, H., Hino, T., Kawashima, Y. (1995). Aerosolization of lactide/glycolide copolymer (PLGA) nanospheres for pulmonary delivery of peptide-drugs. Yakugaku Zasshi 115, 732-741.
    • (1995) Yakugaku Zasshi , vol.115 , pp. 732-741
    • Niwa, T.1    Takeuchi, H.2    Hino, T.3    Kawashima, Y.4
  • 60
    • 3242777139 scopus 로고    scopus 로고
    • Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors
    • Overall, C. M., Tam, E. M., Kappelhoff, R., Connor, A., Ewart, T., Morrison, C. J., Puente, X., Lopez-Otin, C., Seth, A. (2004). Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors. Biol. Chem. 385, 493-504.
    • (2004) Biol. Chem , vol.385 , pp. 493-504
    • Overall, C.M.1    Tam, E.M.2    Kappelhoff, R.3    Connor, A.4    Ewart, T.5    Morrison, C.J.6    Puente, X.7    Lopez-Otin, C.8    Seth, A.9
  • 61
    • 0036633358 scopus 로고    scopus 로고
    • New horizons - alternative routes for insulin therapy
    • Owens, D. R. (2002). New horizons - alternative routes for insulin therapy. Nat. Rev. Drug Discov. 1, 529-540.
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 529-540
    • Owens, D.R.1
  • 62
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey, A., Mann, M. (2000). Proteomics to study genes and genomes. Nature 405, 837-846.
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 63
    • 0020447594 scopus 로고
    • The importance of silica type for reverse-phase protein separations
    • Pearson, J. D., Lin, N. T., Regnier, F. E. (1982). The importance of silica type for reverse-phase protein separations. Anal. Biochem. 124, 217-230.
    • (1982) Anal. Biochem , vol.124 , pp. 217-230
    • Pearson, J.D.1    Lin, N.T.2    Regnier, F.E.3
  • 64
    • 1242328742 scopus 로고    scopus 로고
    • SELDI-TOF-based serum proteomic pattern diagnostics for early detection of cancer
    • Petricoin, E. F., Liotta, L. A. (2004). SELDI-TOF-based serum proteomic pattern diagnostics for early detection of cancer. Curr. Opin. Biotechnol. 15, 24-30.
    • (2004) Curr. Opin. Biotechnol , vol.15 , pp. 24-30
    • Petricoin, E.F.1    Liotta, L.A.2
  • 65
    • 18844465935 scopus 로고    scopus 로고
    • Fasting intact proinsulin is a highly specific predictor of insulin resistance in type 2 diabetes
    • Pfützner, A., Kunt, T., Hohberg, C., Mondok, A., Pahler, S., Konrad, T., Lubben, G., Forst, T. (2004). Fasting intact proinsulin is a highly specific predictor of insulin resistance in type 2 diabetes. Diabetes Care 27, 682-687.
    • (2004) Diabetes Care , vol.27 , pp. 682-687
    • Pfützner, A.1    Kunt, T.2    Hohberg, C.3    Mondok, A.4    Pahler, S.5    Konrad, T.6    Lubben, G.7    Forst, T.8
  • 68
    • 0033399737 scopus 로고    scopus 로고
    • Liquid chromatography and electrospray mass spectrometric mapping of peptides from human plasma filtrate
    • Raida, M., Schulz-Knappe, P., Heine, G., Forssmann, W. G. (1999). Liquid chromatography and electrospray mass spectrometric mapping of peptides from human plasma filtrate. J. Am. Soc. Mass Spectrom. 10, 45-54.
    • (1999) J. Am. Soc. Mass Spectrom , vol.10 , pp. 45-54
    • Raida, M.1    Schulz-Knappe, P.2    Heine, G.3    Forssmann, W.G.4
  • 69
    • 2542460134 scopus 로고    scopus 로고
    • Miniaturized proteomics and peptidomics using capillary liquid separation and high resolution mass spectrometry
    • Ramstrom, M., Bergquist, J. (2004). Miniaturized proteomics and peptidomics using capillary liquid separation and high resolution mass spectrometry, FEBS Lett. 567, 92-95.
    • (2004) FEBS Lett , vol.567 , pp. 92-95
    • Ramstrom, M.1    Bergquist, J.2
  • 70
    • 0345864015 scopus 로고    scopus 로고
    • MEROPS: the peptidase database
    • Database issue
    • Rawlings, N. D., Tolle, D. P., Barrett, A. J. (2004). MEROPS: the peptidase database. Nucleic Acids Res. 32, Database issue, D160-D164.
    • (2004) Nucleic Acids Res , vol.32 , pp. D160-D164
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 71
    • 0031722813 scopus 로고    scopus 로고
    • The new biology of gastrointestinal hormones
    • Rehfeld, J. F. (1998). The new biology of gastrointestinal hormones. Physiol. Rev. 78, 1087-1108.
    • (1998) Physiol. Rev , vol.78 , pp. 1087-1108
    • Rehfeld, J.F.1
  • 72
    • 0037304027 scopus 로고    scopus 로고
    • The post-translational phase of gene expression: new possibilities in molecular diagnosis
    • Rehfeld, J. F., Goetze, J. P. (2003). The post-translational phase of gene expression: new possibilities in molecular diagnosis. Curr. Mol. Med. 3, 25-38.
    • (2003) Curr. Mol. Med , vol.3 , pp. 25-38
    • Rehfeld, J.F.1    Goetze, J.P.2
  • 73
    • 0036107064 scopus 로고    scopus 로고
    • Long-term inhibition of dipeptidyl peptidase IV improves glucose tolerance and preserves islet function in mice
    • Reimer, M. K., Holst, J. J., Ahren, B. (2002). Long-term inhibition of dipeptidyl peptidase IV improves glucose tolerance and preserves islet function in mice. Eur J. Endocrinol. 146, 717-727.
    • (2002) Eur J. Endocrinol , vol.146 , pp. 717-727
    • Reimer, M.K.1    Holst, J.J.2    Ahren, B.3
  • 74
    • 0036430140 scopus 로고    scopus 로고
    • The determination and use of optimized protease substrates in drug discovery and development
    • Richardson, P. L. (2002). The determination and use of optimized protease substrates in drug discovery and development. Curr. Pharm. Des. 8, 2559-2581.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 2559-2581
    • Richardson, P.L.1
  • 76
    • 0031013294 scopus 로고    scopus 로고
    • Mass spectrometry in protein studies from genome to function
    • Roepstorff, P. (1997). Mass spectrometry in protein studies from genome to function. Curr. Opin. Biotechnol. 8, 6-13.
    • (1997) Curr. Opin. Biotechnol , vol.8 , pp. 6-13
    • Roepstorff, P.1
  • 78
    • 0036885616 scopus 로고    scopus 로고
    • Insulin: discovery and controversy
    • Rosenfeld, L. (2002). Insulin: discovery and controversy. Clin. Chem. 48, 2270-2288.
    • (2002) Clin. Chem , vol.48 , pp. 2270-2288
    • Rosenfeld, L.1
  • 79
    • 37049241552 scopus 로고
    • Chemistry of insulin; determination of the structure of insulin opens the way to greater understanding of life processes
    • Sanger, F. (1959). Chemistry of insulin; determination of the structure of insulin opens the way to greater understanding of life processes. Science 129, 1340-1344.
    • (1959) Science , vol.129 , pp. 1340-1344
    • Sanger, F.1
  • 80
    • 0036733748 scopus 로고    scopus 로고
    • Peptidomics-based approach reveals the secretion of the 29-residue COOH-terminal fragment of the putative tumor suppressor protein DMBT1 from pancreatic adenocarcinoma cell lines
    • Sasaki, K., Sato, K., Akiyama, Y., Yanagihara, K., Oka, M., Yamaguchi, K. (2002). Peptidomics-based approach reveals the secretion of the 29-residue COOH-terminal fragment of the putative tumor suppressor protein DMBT1 from pancreatic adenocarcinoma cell lines. Cancer Res. 62, 4894-4898.
    • (2002) Cancer Res , vol.62 , pp. 4894-4898
    • Sasaki, K.1    Sato, K.2    Akiyama, Y.3    Yanagihara, K.4    Oka, M.5    Yamaguchi, K.6
  • 81
    • 0037169869 scopus 로고    scopus 로고
    • Peptide differential display of serum-free conditioned medium from cancer cell lines
    • Sato, K., Sasaki, K., Tsao, M. S., Yamaguchi, K. (2002). Peptide differential display of serum-free conditioned medium from cancer cell lines. Cancer Lett. 176, 199-203.
    • (2002) Cancer Lett , vol.176 , pp. 199-203
    • Sato, K.1    Sasaki, K.2    Tsao, M.S.3    Yamaguchi, K.4
  • 82
    • 0343924648 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionisation mass spectrometry guided purification of human guanylin from blood ultra-filtrate
    • Schrader, M., Jürgens, M., Hess, R., Schulz-Knappe, P., Raida, M., Forssmann, W. G. (1997). Matrix-assisted laser desorption/ionisation mass spectrometry guided purification of human guanylin from blood ultra-filtrate. J. Chromatogr. A 776, 139-145.
    • (1997) J. Chromatogr. A , vol.776 , pp. 139-145
    • Schrader, M.1    Jürgens, M.2    Hess, R.3    Schulz-Knappe, P.4    Raida, M.5    Forssmann, W.G.6
  • 83
    • 0002652573 scopus 로고    scopus 로고
    • Peptidomics technologies for human body fluids
    • Schrader, M., Schulz-Knappe, P. (2001). Peptidomics technologies for human body fluids. Trends Biotechnol. 19, S55-S60.
    • (2001) Trends Biotechnol , vol.19 , pp. S55-S60
    • Schrader, M.1    Schulz-Knappe, P.2
  • 87
    • 0037304325 scopus 로고    scopus 로고
    • Quantitative proteomics using mass spectrometry
    • Sechi, S., Oda, Y. (2003). Quantitative proteomics using mass spectrometry. Curr. Opin. Chem. Biol. 7, 70-77.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 70-77
    • Sechi, S.1    Oda, Y.2
  • 88
    • 0033452452 scopus 로고    scopus 로고
    • Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides
    • Seidah, N. G., Chretien, M. (1999). Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res. 848, 45-62.
    • (1999) Brain Res , vol.848 , pp. 45-62
    • Seidah, N.G.1    Chretien, M.2
  • 90
    • 0027397306 scopus 로고
    • Chemical assay for cyst(e)ine-rich peptides detects a novel intestinal peptide ZF-1, homologous to a single zinc-finger motif
    • Sillard, R., Jornvall, H., Carlquist, M., Mutt, V. (1993). Chemical assay for cyst(e)ine-rich peptides detects a novel intestinal peptide ZF-1, homologous to a single zinc-finger motif. Eur. J. Biochem. 211, 377-380.
    • (1993) Eur. J. Biochem , vol.211 , pp. 377-380
    • Sillard, R.1    Jornvall, H.2    Carlquist, M.3    Mutt, V.4
  • 91
    • 2942617034 scopus 로고    scopus 로고
    • Has the yo-yo stopped? An assessment of human protein-coding gene number
    • Southan, C. (2004). Has the yo-yo stopped? An assessment of human protein-coding gene number. Proteomics 4, 1712-1726.
    • (2004) Proteomics , vol.4 , pp. 1712-1726
    • Southan, C.1
  • 92
    • 77956664692 scopus 로고    scopus 로고
    • The prohormone convertases and precursor processing in protein biosynthesis
    • Dalbey, R. E., Sigman, D. S. (Eds.), Academic, San Diego
    • Steiner, D. F. (2002). The prohormone convertases and precursor processing in protein biosynthesis. In Dalbey, R. E., Sigman, D. S. (Eds.), The enzymes: coand post-translational proteolysis of proteins, Vol. XXII. Academic, San Diego.
    • (2002) The enzymes: coand post-translational proteolysis of proteins , vol.22
    • Steiner, D.F.1
  • 93
    • 0035048372 scopus 로고    scopus 로고
    • Imaging mass spectrometry: a new technology for the analysis of protein expression in mammalian tissues
    • Stoeckli, M., Chaurand, P., Hallahan, D. E., Caprioli, R. M. (2001). Imaging mass spectrometry: a new technology for the analysis of protein expression in mammalian tissues. Nat. Med. 7, 493-496.
    • (2001) Nat. Med , vol.7 , pp. 493-496
    • Stoeckli, M.1    Chaurand, P.2    Hallahan, D.E.3    Caprioli, R.M.4
  • 95
    • 23944470664 scopus 로고    scopus 로고
    • Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display
    • Tammen, H., Schulte, I., Hess, R., Mencel, C., Kellmann, M., Mohring, T., Schulz-Knappe, P. (2005). Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics 5, 414-422.
    • (2005) Proteomics , vol.5 , pp. 414-422
    • Tammen, H.1    Schulte, I.2    Hess, R.3    Mencel, C.4    Kellmann, M.5    Mohring, T.6    Schulz-Knappe, P.7
  • 96
    • 0032530593 scopus 로고    scopus 로고
    • Differential display of peptides induced during the immune response of Drosophila: A matrix-assisted laser desorption ionization time-of-flight mass spectrometry study
    • Uttenweiler-Joseph, S., Moniatte, M., Lagueux, M., Van Dorsselaer, A., Hoffmann, J. A., Bulet, P. (1998). Differential display of peptides induced during the immune response of Drosophila: A matrix-assisted laser desorption ionization time-of-flight mass spectrometry study. Proc. Natl. Acad. Sci. USA 95, 11342-11347.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11342-11347
    • Uttenweiler-Joseph, S.1    Moniatte, M.2    Lagueux, M.3    Van Dorsselaer, A.4    Hoffmann, J.A.5    Bulet, P.6
  • 97
    • 0035238444 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry: an elegant tool for peptidomics
    • Verhaert, P., Uttenweiler-Joseph, S., de Vries, M., Loboda, A., Ens, W., Standing, K. G. (2001). Matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry: an elegant tool for peptidomics. Proteomics 1, 118-131.
    • (2001) Proteomics , vol.1 , pp. 118-131
    • Verhaert, P.1    Uttenweiler-Joseph, S.2    de Vries, M.3    Loboda, A.4    Ens, W.5    Standing, K.G.6
  • 98
    • 1542617944 scopus 로고    scopus 로고
    • Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry
    • Villanueva, J., Philip, J., Entenberg, D., Chaparro, C. A., Tanwar, M. K., Holland, E. C., Tempst, P. (2004). Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry. Anal. Chem. 76, 1560-1570.
    • (2004) Anal. Chem , vol.76 , pp. 1560-1570
    • Villanueva, J.1    Philip, J.2    Entenberg, D.3    Chaparro, C.A.4    Tanwar, M.K.5    Holland, E.C.6    Tempst, P.7
  • 99
    • 1842766389 scopus 로고    scopus 로고
    • Application of proteomic technologies in the drug development process
    • Walgren, J. L., Thompson, D. C. (2004). Application of proteomic technologies in the drug development process. Toxicol. Lett. 149, 377-385.
    • (2004) Toxicol. Lett , vol.149 , pp. 377-385
    • Walgren, J.L.1    Thompson, D.C.2
  • 100
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang, W., Zhou, H., Lin, H., Roy, S., Shaler, T. A., Hill, L. R., Norton, S., Kumar, P., Anderle, M., Becker, C. H. (2003). Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal. Chem. 75, 4818-4826.
    • (2003) Anal. Chem , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3    Roy, S.4    Shaler, T.A.5    Hill, L.R.6    Norton, S.7    Kumar, P.8    Anderle, M.9    Becker, C.H.10
  • 103
    • 0029834931 scopus 로고    scopus 로고
    • Superiority of brain natriuretic peptide as a hormonal marker of ventricular systolic and diastolic dysfunction and ventricular hypertrophy
    • Yamamoto, K., Burnett, J. C. Jr., Jougasaki, M., Nishimura, R. A., Bailey, K. R., Saito, Y., Nakao, K., Redfield, M. M. (1996). Superiority of brain natriuretic peptide as a hormonal marker of ventricular systolic and diastolic dysfunction and ventricular hypertrophy. Hypertension 28, 988-994.
    • (1996) Hypertension , vol.28 , pp. 988-994
    • Yamamoto, K.1    Burnett, J.C.2    Jougasaki, M.3    Nishimura, R.A.4    Bailey, K.R.5    Saito, Y.6    Nakao, K.7    Redfield, M.M.8
  • 104
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. (1987). Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84, 5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 105
    • 2542544270 scopus 로고    scopus 로고
    • How industry is approaching the search for new diagnostic markers and biomarkers
    • Zolg, J. W., Langen, H. (2004). How industry is approaching the search for new diagnostic markers and biomarkers. Mol. Cell Proteomics 3, 345-354.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 345-354
    • Zolg, J.W.1    Langen, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.