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Volumn 12, Issue 2, 2012, Pages 173-182

A mass spectrometry-based method to screen for α-amidated peptides

Author keywords

Amidated peptide; Post translational modification; Spectral pairing; Technology

Indexed keywords

ALPHA AMIDATING ENZYME; GLYCINE;

EID: 84862944662     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100327     Document Type: Article
Times cited : (13)

References (37)
  • 2
    • 0026514908 scopus 로고
    • The biosynthesis of neuropeptides: peptide α-amidation
    • Eipper, B. A., Stoffers, D. A., Mains, R. E., The biosynthesis of neuropeptides: peptide α-amidation. Annu. Rev. Neurosci. 1992, 15, 57-85.
    • (1992) Annu. Rev. Neurosci. , vol.15 , pp. 57-85
    • Eipper, B.A.1    Stoffers, D.A.2    Mains, R.E.3
  • 3
    • 0028175481 scopus 로고
    • C-Terminal amidated peptides: Production by the in vitro enzymatic amidation of glycine-extened peptides and the importance of the amide to bioactivity
    • Merkler, D. J., C-Terminal amidated peptides: Production by the in vitro enzymatic amidation of glycine-extened peptides and the importance of the amide to bioactivity. Enzyme Microb. Technol. 1994, 16, 450-456.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 450-456
    • Merkler, D.J.1
  • 4
    • 0027174437 scopus 로고
    • Peptide amidation: Signature of bioactivity
    • Cuttitta, F., Peptide amidation: Signature of bioactivity. Anat. Rec. 1993, 236, 87-95.
    • (1993) Anat. Rec. , vol.236 , pp. 87-95
    • Cuttitta, F.1
  • 5
    • 0027364935 scopus 로고
    • Identification of α-carboxamidated and carboxy-terminal glycine forms of peptides in bovine hypothalamus, bovine pituitary and porcine heart extracts
    • Hill, J. C., Flannery, G. M., Fraser, B. A., Identification of α-carboxamidated and carboxy-terminal glycine forms of peptides in bovine hypothalamus, bovine pituitary and porcine heart extracts. Neuropeptides 1993, 25, 255-264.
    • (1993) Neuropeptides , vol.25 , pp. 255-264
    • Hill, J.C.1    Flannery, G.M.2    Fraser, B.A.3
  • 6
    • 0012664686 scopus 로고
    • Chemical determination of polypeptide hormones
    • Tatemoto, K., Mutt, V., Chemical determination of polypeptide hormones. Nature 1978, 75, 4115-4119.
    • (1978) Nature , vol.75 , pp. 4115-4119
    • Tatemoto, K.1    Mutt, V.2
  • 7
    • 0021040521 scopus 로고
    • Galanin - a novel biologically-active peptide from porcine intestine
    • Tatemoto, K., Rökaeus, Å., Jörnvall, H., McDonald, T. J., Mutt, V., Galanin - a novel biologically-active peptide from porcine intestine. FEBS Lett. 1983, 164, 124-128.
    • (1983) FEBS Lett. , vol.164 , pp. 124-128
    • Tatemoto, K.1    Rökaeus, A.2    Jörnvall, H.3    McDonald, T.J.4    Mutt, V.5
  • 8
    • 0023035470 scopus 로고
    • Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion
    • Tatemoto, K., Efendić, S., Mutt, V., Makk, G. et al., Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion. Nature 1986, 324, 476-478.
    • (1986) Nature , vol.324 , pp. 476-478
    • Tatemoto, K.1    Efendić, S.2    Mutt, V.3    Makk, G.4
  • 9
    • 0020572240 scopus 로고
    • Separation of DNS-amino acid amides by high-performance liquid chromatography
    • Simmons, W. H., Meisenberg, G., Separation of DNS-amino acid amides by high-performance liquid chromatography. J. Chromatogr. A 1983, 266, 483-489.
    • (1983) J. Chromatogr. A , vol.266 , pp. 483-489
    • Simmons, W.H.1    Meisenberg, G.2
  • 10
    • 0023641922 scopus 로고
    • Identification of the C-terminally α-amidated amino acid in peptides by high-performance liquid chromatography
    • Schmidt, W. E., Conlon, J. M., Mutt, V., Carlquist, M. et al., Identification of the C-terminally α-amidated amino acid in peptides by high-performance liquid chromatography. Eur. J. Biochem. 1987, 162, 467-472.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 467-472
    • Schmidt, W.E.1    Conlon, J.M.2    Mutt, V.3    Carlquist, M.4
  • 11
    • 0023059370 scopus 로고
    • Use of Pico-Tag methodology in the chemical analysis of peptides with carboxyl-terminal amides
    • Bennett, H. P. J., Solomon, S., Use of Pico-Tag methodology in the chemical analysis of peptides with carboxyl-terminal amides. J. Chromatogr. A 1986, 359, 221-230.
    • (1986) J. Chromatogr. A , vol.359 , pp. 221-230
    • Bennett, H.P.J.1    Solomon, S.2
  • 12
    • 0024371884 scopus 로고
    • High-performance liquid chromatography with thermospray mass spectrometric detection of α-carboxyamido amino acids
    • Treston, A. M., Vicchio, D., Mulshine, J. L., Yergey, A. L., High-performance liquid chromatography with thermospray mass spectrometric detection of α-carboxyamido amino acids. J. Chromatogr. A 1989, 474, 187-195.
    • (1989) J. Chromatogr. A , vol.474 , pp. 187-195
    • Treston, A.M.1    Vicchio, D.2    Mulshine, J.L.3    Yergey, A.L.4
  • 13
    • 0033008070 scopus 로고    scopus 로고
    • Selective fluorescence derivatization and capillary electrophoretic separation of amidated amino acids
    • Feng, L., Mitchell, M. E., Selective fluorescence derivatization and capillary electrophoretic separation of amidated amino acids. J. Chromatogr. A 1999, 832, 211-224.
    • (1999) J. Chromatogr. A , vol.832 , pp. 211-224
    • Feng, L.1    Mitchell, M.E.2
  • 15
    • 69449095268 scopus 로고    scopus 로고
    • A new approach for detecting C-terminal amidation of proteins and peptides by mass spectrometry in conjunction with chemical derivatization
    • Kuyama, H., Nakajima, C., Nakazawa, T., Nishimura, O., Tsunasawa, S., A new approach for detecting C-terminal amidation of proteins and peptides by mass spectrometry in conjunction with chemical derivatization. Proteomics 2009, 9, 4063-4070.
    • (2009) Proteomics , vol.9 , pp. 4063-4070
    • Kuyama, H.1    Nakajima, C.2    Nakazawa, T.3    Nishimura, O.4    Tsunasawa, S.5
  • 17
    • 33745860090 scopus 로고    scopus 로고
    • Efficient high-throughput discovery of large peptidic hormones and biomarkers
    • Taylor, S. W., Andon, N. L., Bilakovics, J. M., Lowe, C. et al., Efficient high-throughput discovery of large peptidic hormones and biomarkers. J. Proteome Res. 2006, 5, 1776-1884.
    • (2006) J. Proteome Res. , vol.5 , pp. 1776-1884
    • Taylor, S.W.1    Andon, N.L.2    Bilakovics, J.M.3    Lowe, C.4
  • 18
    • 34548857069 scopus 로고    scopus 로고
    • Peptidomic identification and biological validation of neuroendocrine regulatory peptide-1 and -2
    • Yamaguchi, H., Sasaki, K., Satomi, Y., Shimbara, T. et al., Peptidomic identification and biological validation of neuroendocrine regulatory peptide-1 and -2. J. Biol. Chem. 2007, 282, 26354-26360.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26354-26360
    • Yamaguchi, H.1    Sasaki, K.2    Satomi, Y.3    Shimbara, T.4
  • 19
    • 77954191980 scopus 로고    scopus 로고
    • Open MS/MS spectral library search to identify unanticipated post-translational modifications and increase spectral rate
    • Ye, D., Fu, Y., Sun, R.-X., Wang, H.-P. et al., Open MS/MS spectral library search to identify unanticipated post-translational modifications and increase spectral rate. Bioinformatics 2010, 26, i399-i406.
    • (2010) Bioinformatics , vol.26
    • Ye, D.1    Fu, Y.2    Sun, R.-X.3    Wang, H.-P.4
  • 20
    • 33646903914 scopus 로고    scopus 로고
    • ModifiComb, a new proteomic tool for mapping substoichiometric post-translational modifications, finding novel types of modifications, and fingerprinting complex protein mixtures
    • Savitski, M. M., Nielsen, M. L., Zubarev, R. A., ModifiComb, a new proteomic tool for mapping substoichiometric post-translational modifications, finding novel types of modifications, and fingerprinting complex protein mixtures. Mol. Cell. Proteomics 2006, 5, 935-948.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 935-948
    • Savitski, M.M.1    Nielsen, M.L.2    Zubarev, R.A.3
  • 21
    • 34250702089 scopus 로고    scopus 로고
    • The Mass Distance Fingerprint: a statistical framework for de novo detection of predominant modifications using high-accuracy mass spectrometry
    • Potthast, F., Gerrits, B., Häkkinen, J., Rutishauser, D. et al., The Mass Distance Fingerprint: a statistical framework for de novo detection of predominant modifications using high-accuracy mass spectrometry. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2007, 854, 173-182.
    • (2007) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.854 , pp. 173-182
    • Potthast, F.1    Gerrits, B.2    Häkkinen, J.3    Rutishauser, D.4
  • 23
    • 60849104087 scopus 로고    scopus 로고
    • Efficient discovery of abundant post-translational modifications and spectral pairs using peptide mass and retention time differences
    • Fu, Y., Jia, W., Lu, Z., Wang, H. P. et al., Efficient discovery of abundant post-translational modifications and spectral pairs using peptide mass and retention time differences. BMC Bioinformatics 2009, 10, S50.
    • (2009) BMC Bioinformatics , vol.10
    • Fu, Y.1    Jia, W.2    Lu, Z.3    Wang, H.P.4
  • 25
    • 0028050404 scopus 로고
    • Growth-promoting effects of glycine-extended gastrin
    • Seva, C., Dickinson, C. J., Yamada, T., Growth-promoting effects of glycine-extended gastrin. Science 1994, 265, 410-412.
    • (1994) Science , vol.265 , pp. 410-412
    • Seva, C.1    Dickinson, C.J.2    Yamada, T.3
  • 26
    • 0023028516 scopus 로고
    • Inhibition of peptide amidation by disulfiram and diethyldithiocarbamate
    • Mains, R. E., Park, L. P., Eipper, B. A., Inhibition of peptide amidation by disulfiram and diethyldithiocarbamate. J. Biol. Chem. 1986, 261, 11938-11941.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11938-11941
    • Mains, R.E.1    Park, L.P.2    Eipper, B.A.3
  • 27
    • 0023000532 scopus 로고
    • Amidation of joining peptide, a major pro-ACTH/endorphin-derived product peptide
    • Eipper, B. A., Park, L., Keutmann, H. T., Mains, R. E., Amidation of joining peptide, a major pro-ACTH/endorphin-derived product peptide. J. Biol. Chem. 1986, 261, 8686-8694.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8686-8694
    • Eipper, B.A.1    Park, L.2    Keutmann, H.T.3    Mains, R.E.4
  • 28
    • 77949756247 scopus 로고    scopus 로고
    • Molecular evolution of the crustacean hyperglycemic hormone family in ecdysozoans
    • Montagné, N., Desdevises, Y., Soyez, D., Toullec, J.-Y., Molecular evolution of the crustacean hyperglycemic hormone family in ecdysozoans. BMC Evol. Biol. 2010, 10, 62.
    • (2010) BMC Evol. Biol. , vol.10 , pp. 62
    • Montagné, N.1    Desdevises, Y.2    Soyez, D.3    Toullec, J.-Y.4
  • 29
    • 33745167385 scopus 로고    scopus 로고
    • Phoneutria nigriventer toxin 1: a novel, state-dependent inhibitor of neuronal sodium channels that interacts with α conotoxin binding sites
    • Martin-Moutot, N., Mansuelle, P., Alcaraz, G., Gouvêa, R. et al., Phoneutria nigriventer toxin 1: a novel, state-dependent inhibitor of neuronal sodium channels that interacts with α conotoxin binding sites. Mol. Pharmacol. 2006, 69, 1931-1937.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1931-1937
    • Martin-Moutot, N.1    Mansuelle, P.2    Alcaraz, G.3    Gouvêa, R.4
  • 31
    • 33745584056 scopus 로고    scopus 로고
    • SwePep, a database designed for endogenous peptides and mass spectrometry
    • Falth, M., Skold, K., Norrman, M., Svensson, M. et al., SwePep, a database designed for endogenous peptides and mass spectrometry. Mol. Cell. Proteomics 2006, 5, 998-1005.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 998-1005
    • Falth, M.1    Skold, K.2    Norrman, M.3    Svensson, M.4
  • 32
    • 51649096674 scopus 로고    scopus 로고
    • Validation of endogenous peptide identifications using a database of tandem mass spectra
    • Falth, M., Svensson, M., Nilsson, A., Skold, K. et al., Validation of endogenous peptide identifications using a database of tandem mass spectra. J. Proteome Res. 2008, 7, 3049-3053.
    • (2008) J. Proteome Res. , vol.7 , pp. 3049-3053
    • Falth, M.1    Svensson, M.2    Nilsson, A.3    Skold, K.4
  • 33
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., Aebersold, R., Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 2002, 74, 5383-5392.
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 34
    • 76749136727 scopus 로고    scopus 로고
    • Reducing the haystack to find the needle: improved protein identification after fast elimination of non-interpretable peptide MS/MS spectra and noise reduction
    • Mujezinovic, N., Schneider, G., Wildpaner, M., Mechtler, K., Eisenhaber, F., Reducing the haystack to find the needle: improved protein identification after fast elimination of non-interpretable peptide MS/MS spectra and noise reduction. BMC Genomics 2010, 11, S13.
    • (2010) BMC Genomics , vol.11
    • Mujezinovic, N.1    Schneider, G.2    Wildpaner, M.3    Mechtler, K.4    Eisenhaber, F.5
  • 35
    • 77954583307 scopus 로고    scopus 로고
    • Identification of tandem mass spectra of mixtures of isomeric peptides
    • Chen, X., Drogaris, P., Bern, M., Identification of tandem mass spectra of mixtures of isomeric peptides. J. Proteome Res. 2010, 9, 3270-3279.
    • (2010) J. Proteome Res. , vol.9 , pp. 3270-3279
    • Chen, X.1    Drogaris, P.2    Bern, M.3
  • 36
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt, P., Lamas, S., Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur. J. Biochem. 2000, 267, 4928-4944.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 37
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., Shelton, M. D., Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 2008, 10, 1941-1988.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.