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Volumn 50, Issue 35, 2011, Pages 7447-7461

Investigating endogenous peptides and peptidases using peptidomics

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-MICROBIAL AGENT; BIOACTIVE MOLECULES; BIOACTIVE PEPTIDES; CLASSICAL METHODS; IN-VIVO; LC-MS/MS; LIQUID CHROMATOGRAPHY-TANDEM MASS SPECTROMETRY; PEPTIDE ANALYSIS; PEPTIDE HORMONES; PEPTIDOMICS; PROTEIN DEGRADATION;

EID: 80052234401     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200417k     Document Type: Article
Times cited : (46)

References (170)
  • 5
    • 24944452076 scopus 로고    scopus 로고
    • Glucose metabolism and regulation: Beyond insulin and glucagon
    • Aronoff, S. L., Berkowitz, K., Shreiner, B., and Want, L. (2004) Glucose metabolism and regulation: Beyond insulin and glucagon Diabetes Spectrum 17, 183-190
    • (2004) Diabetes Spectrum , vol.17 , pp. 183-190
    • Aronoff, S.L.1    Berkowitz, K.2    Shreiner, B.3    Want, L.4
  • 7
    • 0032568417 scopus 로고    scopus 로고
    • Primary afferent tachykinins are required to experience moderate to intense pain
    • DOI 10.1038/32897
    • Cao, Y. Q., Mantyh, P. W., Carlson, E. J., Gillespie, A. M., Epstein, C. J., and Basbaum, A. I. (1998) Primary afferent tachykinins are required to experience moderate to intense pain Nature 392, 390-394 (Pubitemid 28168735)
    • (1998) Nature , vol.392 , Issue.6674 , pp. 390-394
    • Cao, Y.Q.1    Mantyh, P.W.2    Carlson, E.J.3    Gillespie, A.-M.4    Epstein, C.J.5    Basbaum, A.I.6
  • 8
    • 0018748052 scopus 로고
    • Multiple opiate receptors. Enkephalins and morphine bind to receptors of different specificity
    • Chang, K. J. and Cuatrecasas, P. (1979) Multiple opiate receptors. Enkephalins and morphine bind to receptors of different specificity J. Biol. Chem. 254, 2610-2618 (Pubitemid 9196094)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.8 , pp. 2610-2618
    • Chang, K.J.1    Cuatrecasas, P.2
  • 9
    • 0033013383 scopus 로고    scopus 로고
    • Opioids: First lessons from knockout mice
    • DOI 10.1016/S0165-6147(98)01279-6, PII S0165614798012796
    • Kieffer, B. L. (1999) Opioids: first lessons from knockout mice Trends Pharmacol. Sci. 20, 19-26 (Pubitemid 29304521)
    • (1999) Trends in Pharmacological Sciences , vol.20 , Issue.1 , pp. 19-26
    • Kieffer, B.L.1
  • 10
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai, Y. P. and Gallo, R. L. (2009) AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense Trends Immunol. 30, 131-141
    • (2009) Trends Immunol. , vol.30 , pp. 131-141
    • Lai, Y.P.1    Gallo, R.L.2
  • 11
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • DOI 10.1038/ni1206
    • Selsted, M. E. and Ouellette, A. J. (2005) Mammalian defensins in the antimicrobial immune response Nature Immunol. 6, 551-557 (Pubitemid 41710724)
    • (2005) Nature Immunology , vol.6 , Issue.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 13
    • 77956076972 scopus 로고    scopus 로고
    • Switching to once-daily liraglutide from twice-daily exenatide further improves glycemic control in patients with type 2 diabetes using oral agents
    • Buse, J. B., Sesti, G., Schmidt, W. E., Montanya, E., Chang, C. T., Xu, Y., Blonde, L., and Rosenstock, J. (2010) Switching to once-daily liraglutide from twice-daily exenatide further improves glycemic control in patients with type 2 diabetes using oral agents Diabetes Care 33, 1300-1303
    • (2010) Diabetes Care , vol.33 , pp. 1300-1303
    • Buse, J.B.1    Sesti, G.2    Schmidt, W.E.3    Montanya, E.4    Chang, C.T.5    Xu, Y.6    Blonde, L.7    Rosenstock, J.8
  • 15
    • 33751583983 scopus 로고    scopus 로고
    • Two toxins from Conus striatus that individually induce tetanic paralysis
    • DOI 10.1021/bi061485s
    • Kelley, W. P., Schulz, J. R., Jakubowski, J. A., Gilly, W. F., and Sweedler, J. V. (2006) Two Toxins from Conus striatus That Individually Induce Tetanic Paralysis Biochemistry 45, 14212-14222 (Pubitemid 44846210)
    • (2006) Biochemistry , vol.45 , Issue.47 , pp. 14212-14222
    • Kelley, W.P.1    Schulz, J.R.2    Jakubowski, J.A.3    Gilly, W.F.4    Sweedler, J.V.5
  • 17
    • 77954415694 scopus 로고    scopus 로고
    • Conotoxin venom peptide therapeutics
    • Lewis, R. J. (2009) Conotoxin venom peptide therapeutics Adv. Exp. Med. Biol. 655, 44-48
    • (2009) Adv. Exp. Med. Biol. , vol.655 , pp. 44-48
    • Lewis, R.J.1
  • 18
    • 62149122662 scopus 로고    scopus 로고
    • Neuroprotective and cardioprotective conopeptides: An emerging class of drug leads
    • Twede, V. D., Miljanich, G., Olivera, B. M., and Bulaj, G. (2009) Neuroprotective and cardioprotective conopeptides: an emerging class of drug leads Curr. Opin. Drug Discovery Dev. 12, 231-239
    • (2009) Curr. Opin. Drug Discovery Dev. , vol.12 , pp. 231-239
    • Twede, V.D.1    Miljanich, G.2    Olivera, B.M.3    Bulaj, G.4
  • 20
    • 0027199869 scopus 로고
    • Prohormone processing in the trans-Golgi network: Endoproteolytic cleavage of prosomatostatin and formation of nascent secretory vesicles in permeabilized cells
    • Xu, H. and Shields, D. (1993) Prohormone processing in the trans-Golgi network: endoproteolytic cleavage of prosomatostatin and formation of nascent secretory vesicles in permeabilized cells J. Cell Biol. 122, 1169-1184 (Pubitemid 23277287)
    • (1993) Journal of Cell Biology , vol.122 , Issue.6 , pp. 1169-1184
    • Xu, H.1    Shields, D.2
  • 21
    • 0025763281 scopus 로고
    • Peptide processing and targeting in the neuronal secretory pathway
    • Jung, L. J. and Scheller, R. H. (1991) Peptide processing and targeting in the neuronal secretory pathway Science 251, 1330-1335 (Pubitemid 21916912)
    • (1991) Science , vol.251 , Issue.4999 , pp. 1330-1335
    • Jung, L.J.1    Scheller, R.H.2
  • 22
    • 38849090670 scopus 로고    scopus 로고
    • Identification of the Acyltransferase that Octanoylates Ghrelin, an Appetite-Stimulating Peptide Hormone
    • DOI 10.1016/j.cell.2008.01.017, PII S0092867408001177
    • Yang, J., Brown, M. S., Liang, G., Grishin, N. V., and Goldstein, J. L. (2008) Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone Cell 132, 387-396 (Pubitemid 351192001)
    • (2008) Cell , vol.132 , Issue.3 , pp. 387-396
    • Yang, J.1    Brown, M.S.2    Liang, G.3    Grishin, N.V.4    Goldstein, J.L.5
  • 23
    • 7344250633 scopus 로고    scopus 로고
    • Met-195 of the cholecystokinin-a receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state
    • DOI 10.1074/jbc.273.23.14380
    • Gigoux, V., Escrieut, C., Silvente-Poirot, S., Maigret, B., Gouilleux, L., Fehrentz, J. A., Gully, D., Moroder, L., Vaysse, N., and Fourmy, D. (1998) Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state J. Biol. Chem. 273, 14380-14386 (Pubitemid 28319156)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.23 , pp. 14380-14386
    • Gigoux, V.1    Escrieut, C.2    Silvente-Poirot, S.3    Maigret, B.4    Gouilleux, L.5    Fehrentz, J.-A.6    Gully, D.7    Moroder, L.8    Vaysse, N.9    Fourmy, D.10
  • 24
    • 0034006587 scopus 로고    scopus 로고
    • + channel-dependent and -independent glucose-stimulated insulin secretion
    • Hohmeier, H. E., Mulder, H., Chen, G., Henkel-Rieger, R., Prentki, M., and Newgard, C. B. (2000) Isolation of INS-1-derived cell lines with robust ATP-sensitive K+ channel-dependent and -independent glucose-stimulated insulin secretion Diabetes 49, 424-430 (Pubitemid 30131788)
    • (2000) Diabetes , vol.49 , Issue.3 , pp. 424-430
    • Hohmeier, H.E.1    Mulder, H.2    Chen, G.3    Henkel-Rieger, R.4    Prentki, M.5    Newgard, C.B.6
  • 27
    • 20244385394 scopus 로고    scopus 로고
    • Double Incretin Receptor Knockout (DIRKO) Mice Reveal an Essential Role for the Enteroinsular Axis in Transducing the Glucoregulatory Actions of DPP-IV Inhibitors
    • DOI 10.2337/diabetes.53.5.1326
    • Hansotia, T., Baggio, L. L., Delmeire, D., Hinke, S. A., Yamada, Y., Tsukiyama, K., Seino, Y., Holst, J. J., Schuit, F., and Drucker, D. J. (2004) Double incretin receptor knockout (DIRKO) mice reveal an essential role for the enteroinsular axis in transducing the glucoregulatory actions of DPP-IV inhibitors Diabetes 53, 1326-1335 (Pubitemid 38569020)
    • (2004) Diabetes , vol.53 , Issue.5 , pp. 1326-1335
    • Hansotia, T.1    Baggio, L.L.2    Delmeire, D.3    Hinke, S.A.4    Yamada, Y.5    Tsukiyama, K.6    Seino, Y.7    Holst, J.J.8    Schuit, F.9    Drucker, D.J.10
  • 28
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance
    • Hotamisligil, G. S., Peraldi, P., Budavari, A., Ellis, R., White, M. F., and Spiegelman, B. M. (1996) IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance Science 271, 665-668 (Pubitemid 26052915)
    • (1996) Science , vol.271 , Issue.5249 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 29
    • 0018045663 scopus 로고
    • Peptide hormones and their analogues: Distribution, clearance from the circulation, and inactivation in vivo
    • Bennett, H. P. and McMartin, C. (1978) Peptide hormones and their analogues: distribution, clearance from the circulation, and inactivation in vivo Pharmacol. Rev. 30, 247-292 (Pubitemid 10198931)
    • (1978) Pharmacological Reviews , vol.30 , Issue.3 , pp. 247-292
    • Bennett, H.P.J.1    McMartin, C.2
  • 30
    • 33947690115 scopus 로고    scopus 로고
    • Discovery of JANUVIA™ (sitagliptin), a selective dipeptidyl peptidase IV inhibitor for the treatment of type2 diabetes
    • DOI 10.2174/156802607780091028
    • Thornberry, N. A. and Weber, A. E. (2007) Discovery of JANUVIA (Sitagliptin), a selective dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes Curr. Top. Med. Chem. 7, 557-568 (Pubitemid 46488280)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.6 , pp. 557-568
    • Thornberry, N.A.1    Weber, A.E.2
  • 31
    • 77955953677 scopus 로고    scopus 로고
    • Deorphanization of Novel Peptides and Their Receptors
    • Ozawa, A., Lindberg, I., Roth, B., and Kroeze, W. K. (2010) Deorphanization of Novel Peptides and Their Receptors AAPS J. 12, 378-384
    • (2010) AAPS J. , vol.12 , pp. 378-384
    • Ozawa, A.1    Lindberg, I.2    Roth, B.3    Kroeze, W.K.4
  • 32
    • 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
  • 33
    • 0001693313 scopus 로고
    • Aqueous Extracts of Pancreas
    • Kimball, C. P. and Murlin, J. R. (1923) Aqueous Extracts of Pancreas J. Biol. Chem. 58, 337-346
    • (1923) J. Biol. Chem. , vol.58 , pp. 337-346
    • Kimball, C.P.1    Murlin, J.R.2
  • 34
    • 0039824615 scopus 로고
    • Purification and crystallization of glucagon
    • Staub, A., Sinn, L., and Behrens, O. K. (1955) Purification and crystallization of glucagon J. Biol. Chem. 214, 619-632
    • (1955) J. Biol. Chem. , vol.214 , pp. 619-632
    • Staub, A.1    Sinn, L.2    Behrens, O.K.3
  • 35
    • 0016706732 scopus 로고
    • Isolation of an endogenous compound from brain with pharmacological properties similar to morphine
    • Hughes, J. (1975) Isolation of an endogenous compound from brain with pharmacological properties similar to morphine Brain Res. 88, 295-308
    • (1975) Brain Res. , vol.88 , pp. 295-308
    • Hughes, J.1
  • 36
    • 0016701344 scopus 로고
    • Identification of 2 related pentapeptides from brain with potenet opiate agonist activity
    • Hughes, J., Smith, T. W., Kosterlitz, H. W., Fothergill, L. A., Morgan, B. A., and Morris, H. R. (1975) Identification of 2 related pentapeptides from brain with potenet opiate agonist activity Nature 258, 577-579
    • (1975) Nature , vol.258 , pp. 577-579
    • Hughes, J.1    Smith, T.W.2    Kosterlitz, H.W.3    Fothergill, L.A.4    Morgan, B.A.5    Morris, H.R.6
  • 38
    • 13244253657 scopus 로고    scopus 로고
    • Reverse pharmacology and the de-orphanization of 7TM receptors
    • DOI 10.1016/j.ddtec.2004.07.003, PII S1740674904000095
    • Kotarsky, K. and Niclas, E. N. (2004) Reverse pharmacology and the de-orphanization of 7TM receptors Drug Discovery Today: Technol. 1, 99-104 (Pubitemid 40186323)
    • (2004) Drug Discovery Today: Technologies , vol.1 , Issue.2 , pp. 99-104
    • Kotarsky, K.1    Nilsson, N.E.2
  • 39
    • 11144246968 scopus 로고    scopus 로고
    • GPCR deorphanizations: The novel, the known and the unexpected transmitters
    • DOI 10.1016/j.tips.2004.11.005, PII S0165614704003116
    • Civelli, O. (2005) GPCR deorphanizations: the novel, the known and the unexpected transmitters Trends Pharmacol. Sci. 26, 15-19 (Pubitemid 40052705)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.1 , pp. 15-19
    • Civelli, O.1
  • 40
    • 33846909764 scopus 로고    scopus 로고
    • "Phenotypic" pharmacology: The influence of cellular environment on G protein-coupled receptor antagonist and inverse agonist pharmacology
    • DOI 10.1016/j.bcp.2006.09.005, PII S0006295206005752
    • Nelson, C. P. and Challiss, R. A. J. (2007) "Phenotypic" pharmacology: The influence of cellular environment on G protein-coupled receptor antagonist and inverse agonist pharmacology Biochem. Pharmacol. 73, 737-751 (Pubitemid 46237612)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.6 , pp. 737-751
    • Nelson, C.P.1    Challiss, R.A.J.2
  • 44
    • 0019310264 scopus 로고
    • Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides
    • DOI 10.1038/285417a0
    • Tatemoto, K. and Mutt, V. (1980) Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides Nature 285, 417-418 (Pubitemid 10047227)
    • (1980) Nature , vol.285 , Issue.5764 , pp. 417-418
    • Tatemoto, K.1    Mutt, V.2
  • 45
    • 0012659760 scopus 로고
    • Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon-secretin family
    • Tatemoto, K. and Mutt, V. (1981) Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon - secretin family Proc. Natl. Acad. Sci. U. S. A. 78, 6603-6607 (Pubitemid 12214865)
    • (1981) Proceedings of the National Academy of Sciences of the United States of America , vol.78 , Issue.11 , pp. 6603-6607
    • Tatemoto, K.1    Mutt, V.2
  • 46
    • 0019944850 scopus 로고
    • Neuropeptide Y - a novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide
    • DOI 10.1038/296659a0
    • Tatemoto, K., Carlquist, M., and Mutt, V. (1982) Neuropeptide Y - a novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide Nature 296, 659-660 (Pubitemid 12089070)
    • (1982) Nature , vol.296 , Issue.5858 , pp. 659-660
    • Tatemoto, K.1    Carlquist, M.2    Mutt, V.3
  • 47
    • 0020626777 scopus 로고
    • Identification and characterization of variant forms of the gastrin-releasing peptide (GRP)
    • DOI 10.1016/0014-5793(83)80527-4
    • McDonald, T. J., Jornvall, H., Tatemoto, K., and Mutt, V. (1983) Identification and characterization of variant forms of the gastrin-releasing peptide (GRP) FEBS Lett. 156, 349-356 (Pubitemid 13038676)
    • (1983) FEBS Letters , vol.156 , Issue.2 , pp. 349-356
    • McDonald, T.J.1    Jornvall, H.2    Tatemoto, K.3    Mutt, V.4
  • 48
    • 0021040521 scopus 로고
    • Galanin - a novel biologically active peptide from porcine intestine
    • DOI 10.1016/0014-5793(83)80033-7
    • Tatemoto, K., Rokaeus, A., Jornvall, H., McDonald, T. J., and Mutt, V. (1983) Galanin-a novel biologically active peptide from porcine intestine FEBS Lett. 164, 124-128 (Pubitemid 14201839)
    • (1983) FEBS Letters , vol.164 , Issue.1 , pp. 124-128
    • Tatemoto, K.1    Rokaeus, A.2    Jornvall, H.3
  • 50
    • 33845924482 scopus 로고    scopus 로고
    • The catalytic role of the copper ligand H172 of peptidylglycine α-hydroxylating monooxygenase: A kinetic study of the H172A mutant
    • DOI 10.1021/bi061734c
    • Evans, J. P., Blackburn, N. J., and Klinman, J. P. (2006) The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase: a kinetic study of the H172A mutant Biochemistry 45, 15419-15429 (Pubitemid 46032466)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15419-15429
    • Evans, J.P.1    Blackburn, N.J.2    Klinman, J.P.3
  • 51
    • 67649964485 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of the lyase domain of the amidating enzyme
    • Chufan, E. E., De, M., Eipper, B. A., Mains, R. E., and Amzel, L. M. (2009) Amidation of bioactive peptides: the structure of the lyase domain of the amidating enzyme Structure 17, 965-973
    • (2009) Structure , vol.17 , pp. 965-973
    • Chufan, E.E.1    De, M.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 52
    • 0028175481 scopus 로고
    • C-terminal amidated peptides: Production by the in vitro enzymatic amidation of glycine-extended peptides and the importance of the amide to bioactivity
    • Merkler, D. J. (1994) C-terminal amidated peptides: production by the in vitro enzymatic amidation of glycine-extended peptides and the importance of the amide to bioactivity Enzyme Microbial Technol. 16, 450-456
    • (1994) Enzyme Microbial Technol. , vol.16 , pp. 450-456
    • Merkler, D.J.1
  • 53
    • 0019948176 scopus 로고
    • Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products
    • DOI 10.1038/298240a0
    • Amara, S. G., Jonas, V., Rosenfeld, M. G., Ong, E. S., and Evans, R. M. (1982) Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products Nature 298, 240-244 (Pubitemid 12089405)
    • (1982) Nature , vol.298 , Issue.5871 , pp. 240-244
    • Amara, S.G.1    Jonas, V.2    Rosenfeld, M.G.3
  • 54
    • 0020507455 scopus 로고
    • Stimulation of noradrenergic sympathetic outflow by calcitonin gene-related peptide
    • DOI 10.1038/305534a0
    • Fisher, L. A., Kikkawa, D. O., Rivier, J. E., Amara, S. G., Evans, R. M., Rosenfeld, M. G., Vale, W. W., and Brown, M. R. (1983) Stimulation of noradrenergic sympathetic outflow by calcitonin gene-related peptide Nature 305, 534-536 (Pubitemid 13009094)
    • (1983) Nature , vol.305 , Issue.5934 , pp. 534-536
    • Fisher, L.A.1    Kikkawa, D.O.2    Rivier, J.E.3
  • 55
    • 0020607936 scopus 로고
    • Production of a novel neuropeptide encoded by the calcitonin gene via tissue-specific RNA processing
    • Rosenfeld, M. G., Mermod, J. J., Amara, S. G., Swanson, L. W., Sawchenko, P. E., Rivier, J., Vale, W. W., and Evans, R. M. (1983) Production of a novel neuropeptide encoded by the calcitonin gene via tissue-specific RNA processing Nature 304, 129-135 (Pubitemid 13079138)
    • (1983) Nature , vol.304 , Issue.5922 , pp. 129-135
    • Rosenfeld, M.G.1    Mermod, J.J.2    Amara, S.G.3
  • 56
    • 0021711526 scopus 로고
    • Calcitonin gene-related peptide immunoreactivity in the spinal cord of man and of eight other species
    • Gibson, S. J., Polak, J. M., Bloom, S. R., Sabate, I. M., Mulderry, P. M., Ghatei, M. A., McGregor, G. P., Morrison, J. F., Kelly, J. S., and Evans, R. M. 1984, Calcitonin gene-related peptide immunoreactivity in the spinal cord of man and of eight other species J. Neurosci. 4, 3101-3111 (Pubitemid 15191179)
    • (1984) Journal of Neuroscience , vol.4 , Issue.12 , pp. 3101-3111
    • Gibson, S.J.1    Polak, J.M.2    Bloom, S.R.3
  • 57
    • 0021997471 scopus 로고
    • Calcitonin gene-related peptide is a potent vasodilator
    • DOI 10.1038/313054a0
    • Brain, S. D., Williams, T. J., Tippins, J. R., Morris, H. R., and MacIntyre, I. (1985) Calcitonin gene-related peptide is a potent vasodilator Nature 313, 54-56 (Pubitemid 15192304)
    • (1985) Nature , vol.313 , Issue.5997 , pp. 54-56
    • Brain, S.D.1    Williams, T.J.2    Tippins, J.R.3
  • 58
    • 1542286029 scopus 로고    scopus 로고
    • CGRP-Receptor Antagonists - A Fresh Approach to Migraine Therapy?
    • DOI 10.1056/NEJMp048016
    • Durham, P. L. (2004) CGRP-receptor antagonists - a fresh approach to migraine therapy? N. Engl. J. Med. 350, 1073-1075 (Pubitemid 38298985)
    • (2004) New England Journal of Medicine , vol.350 , Issue.11 , pp. 1073-1075
    • Durham, P.L.1
  • 59
    • 0034192812 scopus 로고    scopus 로고
    • Evidence for increased plasma levels of calcitonin gene-related peptide in migraine outside of attacks
    • DOI 10.1016/S0304-3959(00)00232-3, PII S0304395900002323
    • Ashina, M., Bendtsen, L., Jensen, R., Schifter, S., and Olesen, J. (2000) Evidence for increased plasma levels of calcitonin gene-related peptide in migraine outside of attacks Pain 86, 133-138 (Pubitemid 30211712)
    • (2000) Pain , vol.86 , Issue.1-2 , pp. 133-138
    • Ashina, M.1    Bendtsen, L.2    Jensen, R.3    Schifter, S.4    Olesen, J.5
  • 61
    • 42249087655 scopus 로고    scopus 로고
    • Randomized controlled trial of an oral CGRP receptor antagonist, MK-0974, in acute treatment of migraine
    • DOI 10.1212/01.WNL.0000286940.29755.61
    • Ho, T. W., Mannix, L. K., Fan, X., Assaid, C., Furtek, C., Jones, C. J., Lines, C. R., and Rapoport, A. M. (2008) Randomized controlled trial of an oral CGRP receptor antagonist, MK-0974, in acute treatment of migraine Neurology 70, 1304-1312 (Pubitemid 351550355)
    • (2008) Neurology , vol.70 , Issue.16 , pp. 1304-1312
    • Ho, T.W.1    Mannix, L.K.2    Fan, X.3    Assaid, C.4    Furtek, C.5    Jones, C.J.6    Lines, C.R.7    Rapoport, A.M.8
  • 62
    • 0035814935 scopus 로고    scopus 로고
    • Biological activities of glucagon-like peptide-1 analogues in vitro and in vivo
    • DOI 10.1021/bi0014498
    • Xiao, Q., Giguere, J., Parisien, M., Jeng, W., St-Pierre, S. A., Brubaker, P. L., and Wheeler, M. B. (2001) Biological activities of glucagon-like peptide-1 analogues in vitro and in vivo Biochemistry 40, 2860-2869 (Pubitemid 32198288)
    • (2001) Biochemistry , vol.40 , Issue.9 , pp. 2860-2869
    • Xiao, Q.1    Giguere, J.2    Parisien, M.3    Jeng, W.4    St. Pierre, S.A.5    Brubaker, P.L.6    Wheeler, M.B.7
  • 63
    • 0030726198 scopus 로고    scopus 로고
    • Bioavailability and transport of peptides and peptide drugs into the brain
    • DOI 10.1016/S0196-9781(97)00242-8, PII S0196978197002428
    • Egleton, R. D. and Davis, T. P. (1997) Bioavailability and transport of peptides and peptide drugs into the brain Peptides 18, 1431-1439 (Pubitemid 27519756)
    • (1997) Peptides , vol.18 , Issue.9 , pp. 1431-1439
    • Egleton, R.D.1    Davis, T.P.2
  • 67
    • 58849153281 scopus 로고    scopus 로고
    • Regulation and signaling of human bombesin receptors and their biological effects
    • Weber, H. C. (2009) Regulation and signaling of human bombesin receptors and their biological effects Curr. Opin. Endocrinol., Diabetes Obes. 16, 66-71
    • (2009) Curr. Opin. Endocrinol., Diabetes Obes. , vol.16 , pp. 66-71
    • Weber, H.C.1
  • 70
    • 0022971804 scopus 로고
    • Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas
    • Orskov, C., Holst, J. J., Knuhtsen, S., Baldissera, F. G., Poulsen, S. S., and Nielsen, O. V. (1986) Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas Endocrinology 119, 1467-1475 (Pubitemid 17170509)
    • (1986) Endocrinology , vol.119 , Issue.4 , pp. 1467-1475
    • Orskov, C.1    Holst, J.J.2    Knuhtsen, S.3
  • 71
    • 0033304603 scopus 로고    scopus 로고
    • The glucagon-like peptides
    • Kieffer, T. J. and Habener, J. F. (1999) The glucagon-like peptides Endocr. Rev. 20, 876-913 (Pubitemid 30647076)
    • (1999) Endocrine Reviews , vol.20 , Issue.6 , pp. 876-913
    • Kieffer, T.J.1    Habener, J.F.2
  • 72
    • 34547726181 scopus 로고    scopus 로고
    • A gastrin-releasing peptide receptor mediates the itch sensation in the spinal cord
    • Sun, Y. G. and Chen, Z. F. (2007) A gastrin-releasing peptide receptor mediates the itch sensation in the spinal cord Nature 448, 700-703
    • (2007) Nature , vol.448 , pp. 700-703
    • Sun, Y.G.1    Chen, Z.F.2
  • 73
    • 33747615019 scopus 로고    scopus 로고
    • Ablation of the glucagon receptor gene increases fetal lethality and produces alterations in islet development and maturation
    • DOI 10.1210/en.2005-1410
    • Vuguin, P. M., Kedees, M. H., Cui, L., Guz, Y., Gelling, R. W., Nejathaim, M., Charron, M. J., and Teitelman, G. (2006) Ablation of the glucagon receptor gene increases fetal lethality and produces alterations in islet development and maturation Endocrinology 147, 3995-4006 (Pubitemid 44268351)
    • (2006) Endocrinology , vol.147 , Issue.9 , pp. 3995-4006
    • Vuguin, P.M.1    Kedees, M.H.2    Cui, L.3    Guz, Y.4    Gelling, R.W.5    Nejathaim, M.6    Charron, M.J.7    Teitelman, G.8
  • 75
    • 0019274399 scopus 로고
    • A new class of angiotensin converting enzyme inhibitors
    • DOI 10.1038/288280a0
    • Patchett, A. A., Harris, E., Tristram, E. W., Wyvratt, M. J., Wu, M. T., Taub, D., Peterson, E. R., Ikeler, T. J., ten Broeke, J., Payne, L. G., Ondeyka, D. L., Thorsett, E. D., Greenlee, W. J., Lohr, N. S., Hoffsommer, R. D., Joshua, H., Ruyle, W. V., Rothrock, J. W., Aster, S. D., Maycock, A. L., Robinson, F. M., Hirschmann, R., Sweet, C. S., Ulm, E. H., Gross, D. M., Vassil, T. C., and Stone, C. A. (1980) A new class of angiotensin-converting enzyme inhibitors Nature 288, 280-283 (Pubitemid 11165879)
    • (1980) Nature , vol.288 , Issue.5788 , pp. 280-283
    • Patchett, A.A.1    Harris, E.2    Tristram, E.W.3
  • 76
    • 0037312821 scopus 로고    scopus 로고
    • The influence of GLP-1 on glucose-stimulated insulin secretion: Effects on β-cell sensitivity in type 2 and nondiabetic subjects
    • DOI 10.2337/diabetes.52.2.380
    • Kjems, L. L., Holst, J. J., Volund, A., and Madsbad, S. (2003) The influence of GLP-1 on glucose-stimulated insulin secretion: effects on beta-cell sensitivity in type 2 and nondiabetic subjects Diabetes 52, 380-386 (Pubitemid 36173193)
    • (2003) Diabetes , vol.52 , Issue.2 , pp. 380-386
    • Kjems, L.L.1    Holst, J.J.2    Volund, A.3    Madsbad, S.4
  • 78
    • 0043073112 scopus 로고    scopus 로고
    • Prolyl peptidases: A serine protease subfamily with high potential for drug discovery
    • DOI 10.1016/S1367-5931(03)00084-X
    • Rosenblum, J. S. and Kozarich, J. W. (2003) Prolyl peptidases: a serine protease subfamily with high potential for drug discovery Curr. Opin. Chem. Biol. 7, 496-504 (Pubitemid 36980841)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.4 , pp. 496-504
    • Rosenblum, J.S.1    Kozarich, J.W.2
  • 80
    • 69849101787 scopus 로고    scopus 로고
    • Immunoassays for the incretin hormones GIP and GLP-1, Best practice & research
    • Deacon, C. F. and Holst, J. J. (2009) Immunoassays for the incretin hormones GIP and GLP-1, Best practice & research Clin. Endocrinol. Metab. 23, 425-432
    • (2009) Clin. Endocrinol. Metab. , vol.23 , pp. 425-432
    • Deacon, C.F.1    Holst, J.J.2
  • 81
    • 74649083366 scopus 로고    scopus 로고
    • Measurement of human growth hormone by immunoassays: Current status, unsolved problems and clinical consequences
    • Bidlingmaier, M. and Freda, P. U. (2010) Measurement of human growth hormone by immunoassays: current status, unsolved problems and clinical consequences Growth Horm. IGF Res. 20, 19-25
    • (2010) Growth Horm. IGF Res. , vol.20 , pp. 19-25
    • Bidlingmaier, M.1    Freda, P.U.2
  • 83
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo
    • Deacon, C. F., Johnsen, A. H., and Holst, J. J. (1995) Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo J. Clin. Endocrinol. Metab. 80, 952-957
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3
  • 86
    • 33645813378 scopus 로고    scopus 로고
    • Review - Mass spectrometry and protein analysis
    • Domon, B. and Aebersold, R. (2006) Review-Mass spectrometry and protein analysis Science 312, 212-217
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 87
    • 38049025746 scopus 로고    scopus 로고
    • The significance of biochemical and molecular sample integrity in brain proteomics and peptidomics: Stathmin 2-20 and peptides as sample quality indicators
    • Skold, K., Svensson, M., Norrman, M., Sjogren, B., Svenningsson, P., and Andren, P. E. (2007) The significance of biochemical and molecular sample integrity in brain proteomics and peptidomics: stathmin 2-20 and peptides as sample quality indicators Proteomics 7, 4445-4456
    • (2007) Proteomics , vol.7 , pp. 4445-4456
    • Skold, K.1    Svensson, M.2    Norrman, M.3    Sjogren, B.4    Svenningsson, P.5    Andren, P.E.6
  • 88
    • 26444573301 scopus 로고    scopus 로고
    • Sample-dependent effects on the neuropeptidome detected in rat brain tissue preparations by capillary liquid chromatography with tandem mass spectrometry
    • DOI 10.1021/ac050712d
    • Parkin, M. C., Wei, H., OCallaghan, J. P., and Kennedy, R. T. (2005) Sample-dependent effects on the neuropeptidome detected in rat brain tissue preparations by capillary liquid chromatography with tandem mass spectrometry Anal. Chem. 77, 6331-6338 (Pubitemid 41436970)
    • (2005) Analytical Chemistry , vol.77 , Issue.19 , pp. 6331-6338
    • Parkin, M.C.1    Wei, H.2    O'Callaghan, J.P.3    Kennedy, R.T.4
  • 89
    • 26844518104 scopus 로고    scopus 로고
    • Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary
    • DOI 10.1074/mcp.T500010-MCP200
    • Che, F. Y., Lim, J., Pan, H., Biswas, R., and Fricker, L. D. (2005) Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary Mol. Cell. Proteomics 4, 1391-1405 (Pubitemid 41448725)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1391-1405
    • Che, F.-Y.1    Lim, J.2    Pan, H.3    Biswas, R.4    Fricker, L.D.5
  • 90
    • 72449148123 scopus 로고    scopus 로고
    • Peptidomics of prolyl endopeptidase in the central nervous system
    • Nolte, W. M., Tagore, D. M., Lane, W. S., and Saghatelian, A. (2009) Peptidomics of prolyl endopeptidase in the central nervous system Biochemistry 48, 11971-11981
    • (2009) Biochemistry , vol.48 , pp. 11971-11981
    • Nolte, W.M.1    Tagore, D.M.2    Lane, W.S.3    Saghatelian, A.4
  • 92
    • 77949821699 scopus 로고    scopus 로고
    • Expanding the dipeptidyl peptidase 4-regulated peptidome via an optimized peptidomics platform
    • Tinoco, A. D., Tagore, D. M., and Saghatelian, A. (2010) Expanding the dipeptidyl peptidase 4-regulated peptidome via an optimized peptidomics platform J. Am. Chem. Soc. 132, 3819-3830
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3819-3830
    • Tinoco, A.D.1    Tagore, D.M.2    Saghatelian, A.3
  • 93
    • 18744398125 scopus 로고    scopus 로고
    • Large-scale database searching using tandem mass spectra: Looking up the answer in the back of the book
    • Sadygov, R. G., Cociorva, D., and Yates, J. R., III (2004) Large-scale database searching using tandem mass spectra: looking up the answer in the back of the book Nature Methods 1, 195-202
    • (2004) Nature Methods , vol.1 , pp. 195-202
    • Sadygov, R.G.1    Cociorva, D.2    Yates III, J.R.3
  • 94
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • DOI 10.1038/nmeth785
    • Elias, J. E., Haas, W., Faherty, B. K., and Gygi, S. P. (2005) Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations Nature Methods 2, 667-675 (Pubitemid 41223093)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 97
    • 0028889112 scopus 로고
    • Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane
    • Nielsen, S., Chou, C. L., Marples, D., Christensen, E. I., Kishore, B. K., and Knepper, M. A. (1995) Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane Proc. Natl. Acad. Sci. U. S. A. 92, 1013-1017
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 1013-1017
    • Nielsen, S.1    Chou, C.L.2    Marples, D.3    Christensen, E.I.4    Kishore, B.K.5    Knepper, M.A.6
  • 99
    • 77950222543 scopus 로고    scopus 로고
    • The challenge of translation in social neuroscience: A review of oxytocin, vasopressin, and affiliative behavior
    • Insel, T. R. (2010) The challenge of translation in social neuroscience: a review of oxytocin, vasopressin, and affiliative behavior Neuron 65, 768-779
    • (2010) Neuron , vol.65 , pp. 768-779
    • Insel, T.R.1
  • 100
    • 77955906640 scopus 로고    scopus 로고
    • Vasopressin receptor antagonists for the treatment of hyponatremia: Systematic review and meta-analysis
    • Rozen-Zvi, B., Yahav, D., Gheorghiade, M., Korzets, A., Leibovici, L., and Gafter, U. (2010) Vasopressin receptor antagonists for the treatment of hyponatremia: systematic review and meta-analysis Am. J. Kidney Dis. 56, 325-337
    • (2010) Am. J. Kidney Dis. , vol.56 , pp. 325-337
    • Rozen-Zvi, B.1    Yahav, D.2    Gheorghiade, M.3    Korzets, A.4    Leibovici, L.5    Gafter, U.6
  • 101
    • 55849119537 scopus 로고    scopus 로고
    • Oxytocin, vasopressin, and the neurogenetics of sociality
    • Donaldson, Z. R. and Young, L. J. (2008) Oxytocin, vasopressin, and the neurogenetics of sociality Science 322, 900-904
    • (2008) Science , vol.322 , pp. 900-904
    • Donaldson, Z.R.1    Young, L.J.2
  • 102
    • 77957348112 scopus 로고    scopus 로고
    • A peptidomics strategy for discovering endogenous bioactive peptides
    • Sasaki, K., Takahashi, N., Satoh, M., Yamasaki, M., and Minamino, N. (2010) A peptidomics strategy for discovering endogenous bioactive peptides J. Proteome Res. 9, 5047-5052
    • (2010) J. Proteome Res. , vol.9 , pp. 5047-5052
    • Sasaki, K.1    Takahashi, N.2    Satoh, M.3    Yamasaki, M.4    Minamino, N.5
  • 103
    • 79953718792 scopus 로고    scopus 로고
    • Peptidomics-Based Discovery of an Antimicrobial Peptide Derived from Insulin-Like Growth Factor-Binding Protein 5
    • Osaki, T., Sasaki, K., and Minamino, N. (2011) Peptidomics-Based Discovery of an Antimicrobial Peptide Derived from Insulin-Like Growth Factor-Binding Protein 5 J. Proteome Res. 10, 1870-1880
    • (2011) J. Proteome Res. , vol.10 , pp. 1870-1880
    • Osaki, T.1    Sasaki, K.2    Minamino, N.3
  • 104
    • 0027160032 scopus 로고
    • Extracellular matrix contains insulin-like growth factor binding protein-5: Potentiation of the effects of IGF-I
    • Jones, J. I., Gockerman, A., Busby, W. H., Jr., Camacho-Hubner, C., and Clemmons, D. R. (1993) Extracellular matrix contains insulin-like growth factor binding protein-5: potentiation of the effects of IGF-I J. Cell Biol. 121, 679-687
    • (1993) J. Cell Biol. , vol.121 , pp. 679-687
    • Jones, J.I.1    Gockerman, A.2    Busby Jr., W.H.3    Camacho-Hubner, C.4    Clemmons, D.R.5
  • 105
    • 38049021087 scopus 로고    scopus 로고
    • Insulin-like growth factor (IGF) binding protein-5 blocks skeletal muscle differentiation by inhibiting IGF actions
    • Mukherjee, A., Wilson, E. M., and Rotwein, P. (2008) Insulin-like growth factor (IGF) binding protein-5 blocks skeletal muscle differentiation by inhibiting IGF actions Mol. Endocrinol. 22, 206-215
    • (2008) Mol. Endocrinol. , vol.22 , pp. 206-215
    • Mukherjee, A.1    Wilson, E.M.2    Rotwein, P.3
  • 106
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., and Borregaard, N. (2001) Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3 Blood 97, 3951-3959
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 108
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi, F., Weinberg, C. R., Meagher, D. A., Imai, B. S., and Mische, S. M. (1999) Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity Electrophoresis 20, 601-605 (Pubitemid 29183427)
    • (1999) Electrophoresis , vol.20 , Issue.3 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 110
    • 0037230511 scopus 로고    scopus 로고
    • Human kallikrein 8: Immunoassay development and identification in tissue extracts and biological fluids
    • DOI 10.1373/49.1.87
    • Kishi, T., Grass, L., Soosaipillai, A., Shimizu-Okabe, C., and Diamandis, E. P. (2003) Human kallikrein 8: immunoassay development and identification in tissue extracts and biological fluids Clin. Chem. 49, 87-96 (Pubitemid 36078557)
    • (2003) Clinical Chemistry , vol.49 , Issue.1 , pp. 87-96
    • Kishi, T.1    Grass, L.2    Soosaipillai, A.3    Shimizu-Okabe, C.4    Diamandis, E.P.5
  • 114
    • 14744275484 scopus 로고    scopus 로고
    • fat/fat mouse pituitary using stable isotopic tags and mass spectrometry
    • DOI 10.1002/jms.742
    • Che, F. Y., Biswas, R., and Fricker, L. D. (2005) Relative quantitation of peptides in wild-type and Cpe(fat/fat) mouse pituitary using stable isotopic tags and mass spectrometry J. Mass Spectrom. 40, 227-237 (Pubitemid 40327262)
    • (2005) Journal of Mass Spectrometry , vol.40 , Issue.2 , pp. 227-237
    • Che, F.-Y.1    Biswas, R.2    Flicker, L.D.3
  • 115
    • 0036645730 scopus 로고    scopus 로고
    • fat mice using differential isotopic tags and mass spectrometry
    • DOI 10.1021/ac015681a
    • Che, F. Y. and Fricker, L. D. (2002) Quantitation of neuropeptides in Cpe(fat)/Cpe(fat) mice using differential isotopic tags and mass spectrometry Anal. Chem. 74, 3190-3198 (Pubitemid 34755235)
    • (2002) Analytical Chemistry , vol.74 , Issue.13 , pp. 3190-3198
    • Che, F.-Y.1    Fricker, L.D.2
  • 116
    • 57449116568 scopus 로고    scopus 로고
    • Multiple isotopic labels for quantitative mass spectrometry
    • Morano, C., Zhang, X., and Fricker, L. D. (2008) Multiple isotopic labels for quantitative mass spectrometry Anal. Chem. 80, 9298-9309
    • (2008) Anal. Chem. , vol.80 , pp. 9298-9309
    • Morano, C.1    Zhang, X.2    Fricker, L.D.3
  • 118
    • 69749094420 scopus 로고    scopus 로고
    • A label-free nano-liquid chromatography-mass spectrometry approach for quantitative serum peptidomics in Crohns disease patients
    • Nanni, P., Levander, F., Roda, G., Caponi, A., James, P., and Roda, A. (2009) A label-free nano-liquid chromatography-mass spectrometry approach for quantitative serum peptidomics in Crohns disease patients J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. 877, 3127-3136
    • (2009) J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. , vol.877 , pp. 3127-3136
    • Nanni, P.1    Levander, F.2    Roda, G.3    Caponi, A.4    James, P.5    Roda, A.6
  • 120
    • 68049101085 scopus 로고    scopus 로고
    • Application of label-free quantitative peptidomics for the identification of urinary biomarkers of kidney chronic allograft dysfunction
    • Quintana, L. F., Campistol, J. M., Alcolea, M. P., Banon-Maneus, E., Sol-Gonzalez, A., and Cutillas, P. R. (2009) Application of label-free quantitative peptidomics for the identification of urinary biomarkers of kidney chronic allograft dysfunction Mol. Cell. Proteomics 8, 1658-1673
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1658-1673
    • Quintana, L.F.1    Campistol, J.M.2    Alcolea, M.P.3    Banon-Maneus, E.4    Sol-Gonzalez, A.5    Cutillas, P.R.6
  • 122
    • 0029876522 scopus 로고    scopus 로고
    • Learning and memory in honeybees: From behavior to neural substrates
    • Menzel, R. and Muller, U. (1996) Learning and memory in honeybees: from behavior to neural substrates Annu. Rev. Neurosci. 19, 379-404 (Pubitemid 26080833)
    • (1996) Annual Review of Neuroscience , vol.19 , pp. 379-404
    • Menzel, R.1    Muller, U.2
  • 123
    • 0141958956 scopus 로고    scopus 로고
    • Gene expression profiles in the brain predict behavior in individual honey bees
    • DOI 10.1126/science.1086807
    • Whitfield, C. W., Cziko, A. M., and Robinson, G. E. (2003) Gene expression profiles in the brain predict behavior in individual honey bees Science 302, 296-299 (Pubitemid 37248762)
    • (2003) Science , vol.302 , Issue.5643 , pp. 296-299
    • Whitfield, C.W.1    Cziko, A.-M.2    Robinson, G.E.3
  • 124
    • 6044238246 scopus 로고    scopus 로고
    • Pleiotropy, epistasis and new QTL: The genetic architecture of honey bee foraging behavior
    • DOI 10.1093/jhered/esh072
    • Ruppell, O., Pankiw, T., and Page, R. E., Jr. (2004) Pleiotropy, epistasis and new QTL: the genetic architecture of honey bee foraging behavior J. Hered. 95, 481-491 (Pubitemid 39383156)
    • (2004) Journal of Heredity , vol.95 , Issue.6 , pp. 481-491
    • Ruppell, O.1    Pankiw, T.2    Page Jr., R.E.3
  • 126
    • 8544253237 scopus 로고    scopus 로고
    • Assignment of endogenous substrates to enzymes by global metabolite profiling
    • DOI 10.1021/bi0480335
    • Saghatelian, A., Trauger, S. A., Want, E. J., Hawkins, E. G., Siuzdak, G., and Cravatt, B. F. (2004) Assignment of endogenous substrates to enzymes by global metabolite profiling Biochemistry 43, 14332-14339 (Pubitemid 39491967)
    • (2004) Biochemistry , vol.43 , Issue.45 , pp. 14332-14339
    • Saghatelian, A.1    Trauger, S.A.2    Want, E.J.3    Hawkins, E.G.4    Siuzdak, G.5    Cravatt, B.F.6
  • 127
    • 0033951198 scopus 로고    scopus 로고
    • Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin
    • DOI 10.1038/72642
    • Backes, B. J., Harris, J. L., Leonetti, F., Craik, C. S., and Ellman, J. A. (2000) Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin Nature Biotechnol. 18, 187-193 (Pubitemid 30091180)
    • (2000) Nature Biotechnology , vol.18 , Issue.2 , pp. 187-193
    • Backes, B.J.1    Harris, J.L.2    Leonetti, F.3    Craik, C.S.4    Ellman, J.A.5
  • 129
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyses 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., and Schmidt, W. E. (1993) Dipeptidyl-peptidase IV hydrolyses 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 (Pubitemid 23188160)
    • (1993) European Journal of Biochemistry , vol.214 , Issue.3 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 130
    • 84984752764 scopus 로고    scopus 로고
    • Assignment of protein function in the postgenomic era
    • Saghatelian, A. and Cravatt, B. F. (2005) Assignment of protein function in the postgenomic era Nat. Chem. Biol. 1, 130-142
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 130-142
    • Saghatelian, A.1    Cravatt, B.F.2
  • 131
    • 79952940093 scopus 로고    scopus 로고
    • A Peptidomics Strategy to Elucidate the Proteolytic Pathways That Inactivate Peptide Hormones
    • Tinoco, A. D., Kim, Y. G., Tagore, D. M., Wiwczar, J., Lane, W. S., Danial, N. N., and Saghatelian, A. (2011) A Peptidomics Strategy To Elucidate the Proteolytic Pathways That Inactivate Peptide Hormones Biochemistry 50, 2213-2222
    • (2011) Biochemistry , vol.50 , pp. 2213-2222
    • Tinoco, A.D.1    Kim, Y.G.2    Tagore, D.M.3    Wiwczar, J.4    Lane, W.S.5    Danial, N.N.6    Saghatelian, A.7
  • 133
    • 67650991807 scopus 로고    scopus 로고
    • Combination of snap freezing, differential pH two-dimensional reverse-phase high-performance liquid chromatography, and iTRAQ technology for the peptidomic analysis of the effect of prolyl oligopeptidase inhibition in the rat brain
    • Tenorio-Laranga, J., Valero, M. L., Mannisto, P. T., Sanchez del Pino, M., and Garcia-Horsman, J. A. (2009) Combination of snap freezing, differential pH two-dimensional reverse-phase high-performance liquid chromatography, and iTRAQ technology for the peptidomic analysis of the effect of prolyl oligopeptidase inhibition in the rat brain Anal. Biochem. 393, 80-87
    • (2009) Anal. Biochem. , vol.393 , pp. 80-87
    • Tenorio-Laranga, J.1    Valero, M.L.2    Mannisto, P.T.3    Sanchez Del Pino, M.4    Garcia-Horsman, J.A.5
  • 134
    • 33748051433 scopus 로고    scopus 로고
    • The role of prohormone convertase-2 in hypothalamic neuropeptide processing: A quantitative neuropeptidomic study
    • DOI 10.1111/j.1471-4159.2006.04067.x
    • Pan, H., Che, F. Y., Peng, B., Steiner, D. F., Pintar, J. E., and Fricker, L. D. (2006) The role of prohormone convertase-2 in hypothalamic neuropeptide processing: a quantitative neuropeptidomic study J. Neurochem. 98, 1763-1777 (Pubitemid 44298243)
    • (2006) Journal of Neurochemistry , vol.98 , Issue.6 , pp. 1763-1777
    • Pan, H.1    Che, F.-Y.2    Peng, B.3    Steiner, D.F.4    Pintar, J.E.5    Fricker, L.D.6
  • 136
    • 0035882519 scopus 로고    scopus 로고
    • Altered processing of pro-orphanin FQ/nociceptin and pro- opiomelanocortin-derived peptides in the brains of mice expressing defective prohormone convertase 2
    • Allen, R. G., Peng, B., Pellegrino, M. J., Miller, E. D., Grandy, D. K., Lundblad, J. R., Washburn, C. L., and Pintar, J. E. (2001) Altered processing of pro-orphanin FQ/nociceptin and pro-opiomelanocortin-derived peptides in the brains of mice expressing defective prohormone convertase 2 J. Neurosci. 21, 5864-5870 (Pubitemid 32737719)
    • (2001) Journal of Neuroscience , vol.21 , Issue.16 , pp. 5864-5870
    • Allen, R.G.1    Peng, B.2    Pellegrino, M.J.3    Miller, E.D.4    Grandy, D.K.5    Lundblad, J.R.6    Washburn, C.L.7    Pintar, J.E.8
  • 138
    • 0015242348 scopus 로고
    • Leucylglycinamide released from oxytocin by human uterine enzyme
    • Walter, R., Shlank, H., Glass, J. D., Schwartz, I. L., and Kerenyi, T. D. (1971) Leucylglycinamide released from oxytocin by human uterine enzyme Science 173, 827-829
    • (1971) Science , vol.173 , pp. 827-829
    • Walter, R.1    Shlank, H.2    Glass, J.D.3    Schwartz, I.L.4    Kerenyi, T.D.5
  • 139
    • 0029027926 scopus 로고
    • JTP-4819: A novel prolyl endopeptidase inhibitor with potential as a cognitive enhancer
    • Toide, K., Iwamoto, Y., Fujiwara, T., and Abe, H. (1995) JTP-4819: a novel prolyl endopeptidase inhibitor with potential as a cognitive enhancer J. Pharmacol. Exp. Ther. 274, 1370-1378
    • (1995) J. Pharmacol. Exp. Ther. , vol.274 , pp. 1370-1378
    • Toide, K.1    Iwamoto, Y.2    Fujiwara, T.3    Abe, H.4
  • 140
    • 0029061068 scopus 로고
    • Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on prolyl endopeptidase activity and substance P- and arginine-vasopressin-like immunoreactivity in the brains of aged rats
    • Toide, K., Okamiya, K., Iwamoto, Y., and Kato, T. (1995) Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on prolyl endopeptidase activity and substance P- and arginine-vasopressin-like immunoreactivity in the brains of aged rats J. Neurochem. 65, 234-240
    • (1995) J. Neurochem. , vol.65 , pp. 234-240
    • Toide, K.1    Okamiya, K.2    Iwamoto, Y.3    Kato, T.4
  • 141
    • 2342466215 scopus 로고    scopus 로고
    • Prolyl Oligopeptidase Is Involved in Release of the Antifibrotic Peptide Ac-SDKP
    • DOI 10.1161/01.HYP.0000126172.01673.84
    • Cavasin, M. A., Rhaleb, N. E., Yang, X. P., and Carretero, O. A. (2004) Prolyl oligopeptidase is involved in release of the antifibrotic peptide Ac-SDKP Hypertension 43, 1140-1145 (Pubitemid 38579927)
    • (2004) Hypertension , vol.43 , Issue.5 , pp. 1140-1145
    • Cavasin, M.A.1    Rhaleb, N.-E.2    Yang, X.-P.3    Carretero, O.A.4
  • 143
    • 0036146663 scopus 로고    scopus 로고
    • Effects of the prolyl endopeptidase inhibitor S 17092 on cognitive deficits in Chronic low dose MPTP-treated monkeys
    • DOI 10.1016/S0893-133X(01)00307-4, PII S0893133X01003074
    • Schneider, J. S., Giardiniere, M., and Morain, P. (2002) Effects of the prolyl endopeptidase inhibitor S 17092 on cognitive deficits in chronic low dose MPTP-treated monkeys Neuropsychopharmacology 26, 176-182 (Pubitemid 34093080)
    • (2002) Neuropsychopharmacology , vol.26 , Issue.2 , pp. 176-182
    • Schneider, J.S.1    Giardiniere, M.2    Morain, P.3
  • 144
    • 0036077069 scopus 로고    scopus 로고
    • S 17092: A prolyl endopeptidase inhibitor as a potential therapeutic drug for memory impairment. Preclinical and clinical studies
    • Morain, P., Lestage, P., De Nanteuil, G., Jochemsen, R., Robin, J. L., Guez, D., and Boyer, P. A. (2002) S 17092: a prolyl endopeptidase inhibitor as a potential therapeutic drug for memory impairment. Preclinical and clinical studies CNS Drug Rev. 8, 31-52 (Pubitemid 34651314)
    • (2002) CNS Drug Reviews , vol.8 , Issue.1 , pp. 31-52
    • Morain, P.1    Lestage, P.2    De Nanteuil, G.3    Jochemsen, R.4    Robin, J.-L.5    Guez, D.6    Boyer, P.-A.7
  • 145
    • 19044379994 scopus 로고    scopus 로고
    • Effect of prolyl endopeptidase inhibition on arginine-vasopressin and thyrotrophin-releasing hormone catabolism in the rat brain
    • DOI 10.1111/j.1365-2826.2005.01308.x
    • Bellemere, G., Vaudry, H., Morain, P., and Jegou, S. (2005) Effect of prolyl endopeptidase inhibition on arginine-vasopressin and thyrotrophin-
    • (2005) Journal of Neuroendocrinology , vol.17 , Issue.5 , pp. 306-313
    • Bellemere, G.1    Vaudry, H.2    Morain, P.3    Jegou, S.4
  • 146
    • 33847174067 scopus 로고    scopus 로고
    • Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
    • DOI 10.1002/pmic.200600422
    • Wiese, S., Reidegeld, K. A., Meyer, H. E., and Warscheid, B. (2007) Protein labeling by iTRAQ: a new tool for quantitative mass spectrometry in proteome research Proteomics 7, 340-350 (Pubitemid 46293976)
    • (2007) Proteomics , vol.7 , Issue.3 , pp. 340-350
    • Wiese, S.1    Reidegeld, K.A.2    Meyer, H.E.3    Warscheid, B.4
  • 147
    • 0012659760 scopus 로고
    • Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon-secretin family
    • Tatemoto, K. and Mutt, V. (1981) Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon - secretin family Proc. Natl. Acad. Sci. U. S. A. 78, 6603-6607 (Pubitemid 12214865)
    • (1981) Proceedings of the National Academy of Sciences of the United States of America , vol.78 , Issue.11 , pp. 6603-6607
    • Tatemoto, K.1    Mutt, V.2
  • 148
    • 0021089879 scopus 로고
    • Effect of the peptide PHI-27 on prolactin release in vitro
    • Werner, S., Hulting, A. L., Hokfelt, T., Eneroth, P., Tatemoto, K., Mutt, V., Maroder, L., and Wunsch, E. (1983) Effect of the peptide PHI-27 on prolactin release in vitro Neuroendocrinology 37, 476-478 (Pubitemid 14230667)
    • (1983) Neuroendocrinology , vol.37 , Issue.6 , pp. 476-478
    • Werner, S.1    Hulting, A.L.2    Hokfelt, T.3
  • 149
    • 0019222498 scopus 로고
    • Interaction of a newly isolated intestinal polypeptide (PHI) with glucose and arginine to effect the secretion of insulin and glucagon
    • DOI 10.1016/0024-3205(80)90162-9
    • Szecowka, J., Tatemoto, K., Mutt, V., and Efendic, S. (1980) Interaction of a newly isolated intestinal polypeptide (PHI) with glucose and arginine to effect the secretion of insulin and glucagon Life Sci. 26, 435-438 (Pubitemid 10116567)
    • (1980) Life Sciences , vol.26 , Issue.6 , pp. 435-438
    • Szecowka, J.1    Tatemoto, K.2    Mutt, V.3    Efendic, S.4
  • 153
    • 0038485614 scopus 로고    scopus 로고
    • Humanin peptide suppresses apoptosis by interfering with Bax activation
    • DOI 10.1038/nature01627
    • Guo, B., Zhai, D., Cabezas, E., Welsh, K., Nouraini, S., Satterthwait, A. C., and Reed, J. C. (2003) Humanin peptide suppresses apoptosis by interfering with Bax activation Nature 423, 456-461 (Pubitemid 36626999)
    • (2003) Nature , vol.423 , Issue.6938 , pp. 456-461
    • Guo, B.1    Zhai, D.2    Cabezas, E.3    Welsh, K.4    Nouraini, S.5    Satterthwait, A.C.6    Reed, J.C.7
  • 154
    • 44249122651 scopus 로고    scopus 로고
    • Lilliputians get into the limelight: Novel class of small peptide genes in morphogenesis
    • Hashimoto, Y., Kondo, T., and Kageyama, Y. (2008) Lilliputians get into the limelight: novel class of small peptide genes in morphogenesis Dev. Growth Differ. 50 (Suppl. 1) S269-276
    • (2008) Dev. Growth Differ. , vol.50 , Issue.SUPPL. 1 , pp. 269-276
    • Hashimoto, Y.1    Kondo, T.2    Kageyama, Y.3
  • 155
    • 38049115217 scopus 로고    scopus 로고
    • A dual function for a bacterial small RNA: SgrS performs base pairing-dependent regulation and encodes a functional polypeptide
    • Wadler, C. S. and Vanderpool, C. K. (2007) A dual function for a bacterial small RNA: SgrS performs base pairing-dependent regulation and encodes a functional polypeptide Proc. Natl. Acad. Sci. U. S. A. 104, 20454-20459
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 20454-20459
    • Wadler, C.S.1    Vanderpool, C.K.2
  • 156
    • 44249122651 scopus 로고    scopus 로고
    • Lilliputians get into the limelight: Novel class of small peptide genes in morphogenesis
    • Hashimoto, Y., Kondo, T., and Kageyama, Y. (2008) Lilliputians get into the limelight: Novel class of small peptide genes in morphogenesis Dev., Growth Differ. 50, S269-S276
    • (2008) Dev., Growth Differ. , vol.50
    • Hashimoto, Y.1    Kondo, T.2    Kageyama, Y.3
  • 157
    • 0037166058 scopus 로고    scopus 로고
    • Evidence for in vivo production of Humanin peptide, a neuroprotective factor against Alzheimer's disease-related insults
    • DOI 10.1016/S0304-3940(02)00199-4, PII S0304394002001994
    • Tajima, H., Niikura, T., Hashimoto, Y., Ito, Y., Kita, Y., Terashita, K., Yamazaki, K., Koto, A., Aiso, S., and Nishimoto, I. (2002) Evidence for in vivo production of Humanin peptide, a neuroprotective factor against Alzheimers disease-related insults Neurosci. Lett. 324, 227-231 (Pubitemid 34493875)
    • (2002) Neuroscience Letters , vol.324 , Issue.3 , pp. 227-231
    • Tajima, H.1    Niikura, T.2    Hashimoto, Y.3    Ito, Y.4    Kita, Y.5    Terashita, K.6    Yamazaki, K.7    Koto, A.8    Aiso, S.9    Nishimoto, I.10
  • 162
    • 14944383798 scopus 로고    scopus 로고
    • The evolving role of natural products in drug discovery
    • DOI 10.1038/nrd1657
    • Koehn, F. E. and Carter, G. T. (2005) The evolving role of natural products in drug discovery Nat. Rev. Drug Discovery 4, 206-220 (Pubitemid 40372555)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.3 , pp. 206-220
    • Koehn, F.E.1    Carter, G.T.2
  • 163
    • 0036257686 scopus 로고    scopus 로고
    • Converting a peptide into a drug: Strategies to improve stability and bioavailability
    • Adessi, C. and Soto, C. (2002) Converting a peptide into a drug: strategies to improve stability and bioavailability Curr. Med. Chem. 9, 963-978 (Pubitemid 34498572)
    • (2002) Current Medicinal Chemistry , vol.9 , Issue.9 , pp. 963-978
    • Adessi, C.1    Soto, C.2
  • 164
    • 33846079219 scopus 로고    scopus 로고
    • The comparative efficacy and safety of biologics for the treatment of rheumatoid arthritis: A systematic review and metaanalysis
    • Gartlehner, G., Hansen, R. A., Jonas, B. L., Thieda, P., and Lohr, K. N. (2006) The comparative efficacy and safety of biologics for the treatment of rheumatoid arthritis: a systematic review and metaanalysis J. Rheumatol. 33, 2398-2408 (Pubitemid 46067817)
    • (2006) Journal of Rheumatology , vol.33 , Issue.12 , pp. 2398-2408
    • Gartlehner, G.1    Hansen, R.A.2    Jonas, B.L.3    Thieda, P.4    Lohr, K.N.5
  • 166
    • 16444363534 scopus 로고    scopus 로고
    • Cellular and molecular signal transduction pathways modulated by rituximab (rituxan, anti-CD20 mAb) in non-Hodgkin's lymphoma: Implications in chemosensitization and therapeutic intervention
    • DOI 10.1038/sj.onc.1208349
    • Jazirehi, A. R. and Bonavida, B. (2005) Cellular and molecular signal transduction pathways modulated by rituximab (rituxan, anti-CD20 mAb) in non-Hodgkins lymphoma: implications in chemosensitization and therapeutic intervention Oncogene 24, 2121-2143 (Pubitemid 40516580)
    • (2005) Oncogene , vol.24 , Issue.13 , pp. 2121-2143
    • Jazirehi, A.R.1    Bonavida, B.2
  • 167
    • 0042167233 scopus 로고    scopus 로고
    • Pramlintide as an adjunct to insulin therapy improves long-term glycemic and weight control in patients with type 2 diabetes: A 1-year randomized controlled trial
    • DOI 10.2337/diacare.26.3.784
    • Hollander, P. A., Levy, P., Fineman, M. S., Maggs, D. G., Shen, L. Z., Strobel, S. A., Weyer, C., and Kolterman, O. G. (2003) Pramlintide as an adjunct to insulin therapy improves long-term glycemic and weight control in patients with type 2 diabetes: a 1-year randomized controlled trial Diabetes Care 26, 784-790 (Pubitemid 36929344)
    • (2003) Diabetes Care , vol.26 , Issue.3 , pp. 784-790
    • Hollander, P.A.1    Levy, P.2    Fineman, M.S.3    Maggs, D.G.4    Shen, L.Z.5    Strobel, S.A.6    Weyer, C.7    Kolterman, O.G.8
  • 170
    • 77955881153 scopus 로고    scopus 로고
    • Potent delivery of functional proteins into Mammalian cells in vitro and in vivo using a supercharged protein
    • Cronican, J. J., Thompson, D. B., Beier, K. T., McNaughton, B. R., Cepko, C. L., and Liu, D. R. (2010) Potent delivery of functional proteins into Mammalian cells in vitro and in vivo using a supercharged protein ACS Chem. Biol. 5, 747-752
    • (2010) ACS Chem. Biol. , vol.5 , pp. 747-752
    • Cronican, J.J.1    Thompson, D.B.2    Beier, K.T.3    McNaughton, B.R.4    Cepko, C.L.5    Liu, D.R.6


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