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Volumn 11, Issue 12, 2012, Pages 1951-1964

High-definition de novo sequencing of Crustacean Hyperglycemic Hormone (CHH)-family neuropeptides

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; GLUCAGON;

EID: 84870694137     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.020537     Document Type: Article
Times cited : (32)

References (56)
  • 1
    • 51949104682 scopus 로고    scopus 로고
    • Peptides in the brain: Mass spectrometry-based measurement approaches and challenges
    • Li, L., and Sweedler, J. V. (2008) Peptides in the brain: mass spectrometry-based measurement approaches and challenges. Annu. Rev. Anal. Chem. 1, 451-483
    • (2008) Annu. Rev. Anal. Chem. , vol.1 , pp. 451-483
    • Li, L.1    Sweedler, J.V.2
  • 2
    • 33748931457 scopus 로고    scopus 로고
    • Central nervous system control of food intake and body weight
    • DOI 10.1038/nature05026, PII NATURE05026
    • Morton, G. J., Cummings, D. E., Baskin, D. G., Barsh, G. S., and Schwartz, M. W. (2006) Central nervous system control of food intake and body weight. Nature 443, 289-295 (Pubitemid 44435142)
    • (2006) Nature , vol.443 , Issue.7109 , pp. 289-295
    • Morton, G.J.1    Cummings, D.E.2    Baskin, D.G.3    Barsh, G.S.4    Schwartz, M.W.5
  • 3
    • 34548100559 scopus 로고    scopus 로고
    • Neuropeptidomics to study peptide processing in animal models of obesity
    • Fricker, L. D. (2007) Neuropeptidomics to study peptide processing in animal models of obesity. Endocrinology 148, 4185-4190
    • (2007) Endocrinology , vol.148 , pp. 4185-4190
    • Fricker, L.D.1
  • 4
    • 77951757997 scopus 로고    scopus 로고
    • Comparative neuropeptidomic analysis of food intake via a multi-faceted mass spectrometric approach
    • Chen, R., Hui, L., Cape, S. S., Wang, J., and Li, L. (2010) Comparative neuropeptidomic analysis of food intake via a multi-faceted mass spectrometric approach. ACS Chem. Neurosci. 1, 204-214
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 204-214
    • Chen, R.1    Hui, L.2    Cape, S.S.3    Wang, J.4    Li, L.5
  • 5
    • 80052469137 scopus 로고    scopus 로고
    • Discovery and characterization of the Crustacean hyperglycemic hormone precursor related peptides (CPRP) and orcokinin neuropeptides in the sinus glands of the blue crab Callinectes sapidus using multiple tandem mass spectrometry techniques
    • Hui, L., Cunningham, R., Zhang, Z., Cao, W., Jia, C., and Li, L. (2011) Discovery and characterization of the Crustacean hyperglycemic hormone precursor related peptides (CPRP) and orcokinin neuropeptides in the sinus glands of the blue crab Callinectes sapidus using multiple tandem mass spectrometry techniques. J. Proteome Res. 10, 4219-4229
    • (2011) J. Proteome Res. , vol.10 , pp. 4219-4229
    • Hui, L.1    Cunningham, R.2    Zhang, Z.3    Cao, W.4    Jia, C.5    Li, L.6
  • 6
    • 84555220651 scopus 로고    scopus 로고
    • Discovery and functional study of a novel crustacean tachykinin neuropeptide
    • Hui, L., Zhang, Y., Wang, J., Cook, A., Ye, H., Nusbaum, M. P., and Li, L. (2011) Discovery and functional study of a novel crustacean tachykinin neuropeptide. ACS Chem. Neurosci 2, 711-722
    • (2011) ACS Chem. Neurosci , vol.2 , pp. 711-722
    • Hui, L.1    Zhang, Y.2    Wang, J.3    Cook, A.4    Ye, H.5    Nusbaum, M.P.6    Li, L.7
  • 7
    • 77951975795 scopus 로고    scopus 로고
    • Crustacean hyperglycemic hormone (CHH) neuropeptidesfamily: Functions, titer, and binding to target tissues
    • Chung, J. S., Zmora, N., Katayama, H., and Tsutsui, N. (2010) Crustacean hyperglycemic hormone (CHH) neuropeptidesfamily: Functions, titer, and binding to target tissues. Gen. Comp. Endocrinol. 166, 447-454
    • (2010) Gen. Comp. Endocrinol. , vol.166 , pp. 447-454
    • Chung, J.S.1    Zmora, N.2    Katayama, H.3    Tsutsui, N.4
  • 8
    • 33645010698 scopus 로고    scopus 로고
    • Biochemical and functional aspects of crustacean hyperglycemic hormone in decapod crustaceans: Review and update
    • Fanjul-Moles, M. L. (2006) Biochemical and functional aspects of crustacean hyperglycemic hormone in decapod crustaceans: review and update. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 142, 390-400
    • (2006) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.142 , pp. 390-400
    • Fanjul-Moles, M.L.1
  • 9
    • 84855224608 scopus 로고    scopus 로고
    • The CHH-superfamily of multifunctional peptide hormones controlling crustacean metabolism, osmoregulation, moulting, and reproduction
    • Webster, S. G., Keller, R., and Dircksen, H. (2012) The CHH-superfamily of multifunctional peptide hormones controlling crustacean metabolism, osmoregulation, moulting, and reproduction. Gen. Comp. Endocrinol. 175, 217-233
    • (2012) Gen. Comp. Endocrinol. , vol.175 , pp. 217-233
    • Webster, S.G.1    Keller, R.2    Dircksen, H.3
  • 10
    • 84856106395 scopus 로고    scopus 로고
    • The eyes have it: A brief history of crustacean neuroendocrinology
    • Hopkins, P. M. (2012) The eyes have it: A brief history of crustacean neuroendocrinology. Gen. Comp. Endocrinol. 175, 357-366
    • (2012) Gen. Comp. Endocrinol. , vol.175 , pp. 357-366
    • Hopkins, P.M.1
  • 12
    • 57549105030 scopus 로고    scopus 로고
    • Crustacean molt-inhibiting hormone: Structure, function, and cellular mode of action
    • Nakatsuji, T., Lee, C. Y., and Watson, R. D. (2009) Crustacean molt-inhibiting hormone: structure, function, and cellular mode of action. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 152, 139-148
    • (2009) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.152 , pp. 139-148
    • Nakatsuji, T.1    Lee, C.Y.2    Watson, R.D.3
  • 13
    • 60549109044 scopus 로고    scopus 로고
    • Conserved role of cyclic nucleotides in the regulation of ecdysteroidogenesis by the crustacean molting gland
    • Covi, J. A., Chang, E. S., and Mykles, D. L. (2009) Conserved role of cyclic nucleotides in the regulation of ecdysteroidogenesis by the crustacean molting gland. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 152, 470-477
    • (2009) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.152 , pp. 470-477
    • Covi, J.A.1    Chang, E.S.2    Mykles, D.L.3
  • 14
    • 33749175700 scopus 로고    scopus 로고
    • Members of the crustacean hyperglycemic hormone (CHH) peptide family are differentially distributed both between and within the neuroendocrine organs of Cancer crabs: Implications for differential release and pleiotropic function
    • DOI 10.1242/jeb.02372
    • Hsu, Y. W., Messinger, D. I., Chung, J. S., Webster, S. G., de la Iglesia, H. O., and Christie, A. E. (2006) Members of the crustacean hyperglycemic hormone (CHH) peptide family are differentially distributed both between and within the neuroendocrine organs of Cancer crabs: implications for differential release and pleiotropic function. J. Exp. Biol. 209, 3241-3256 (Pubitemid 44476248)
    • (2006) Journal of Experimental Biology , vol.209 , Issue.16 , pp. 3241-3256
    • Hsu, Y.-W.A.1    Messinger, D.I.2    Chung, J.S.3    Webster, S.G.4    De La, I.H.O.5    Christie, A.E.6
  • 15
    • 7244240815 scopus 로고    scopus 로고
    • Expression and release patterns of neuropeptides during embryonic development and hatching of the green shore crab, Carcinus maenas
    • Chung, J. S., and Webster, S. G. (2004) Expression and release patterns of neuropeptides during embryonic development and hatching of the green shore crab, Carcinus maenas. Development 131, 4751-4761
    • (2004) Development , vol.131 , pp. 4751-4761
    • Chung, J.S.1    Webster, S.G.2
  • 16
    • 38549095067 scopus 로고    scopus 로고
    • Functional studies of crustacean hyperglycemic hormones (CHHs) of the blue crab, Callinectes sapidus - The expression and release of CHH in eyestalk and pericardial organ in response to environmental stress
    • DOI 10.1111/j.1742-4658.2007.06231.x
    • Chung, J. S., and Zmora, N. (2008) Functional studies of crustacean hyperglycemic hormones (CHHs) of the blue crab, Callinectes sapidus - the expression and release of CHH in eyestalk and pericardial organ in response to environmental stress. FEBS J. 275, 693-704 (Pubitemid 351160962)
    • (2008) FEBS Journal , vol.275 , Issue.4 , pp. 693-704
    • Chung, J.S.1    Zmora, N.2
  • 17
    • 77957237990 scopus 로고    scopus 로고
    • Molecular cloning of a putative crustacean hyperglycemic hormone (CHH) isoform from extra-eyestalk tissue of the blue crab (Callinectes sapidus), and determination of temporal and spatial patterns of CHH gene expression
    • Zheng, J., Chen, H. Y., Choi, C. Y., Roer, R. D., and Watson, R. D. (2010) Molecular cloning of a putative crustacean hyperglycemic hormone (CHH) isoform from extra-eyestalk tissue of the blue crab (Callinectes sapidus), and determination of temporal and spatial patterns of CHH gene expression. Gen. Comp. Endocrinol. 169, 174-181
    • (2010) Gen. Comp. Endocrinol. , vol.169 , pp. 174-181
    • Zheng, J.1    Chen, H.Y.2    Choi, C.Y.3    Roer, R.D.4    Watson, R.D.5
  • 18
    • 33644879722 scopus 로고    scopus 로고
    • Peptidomics: Identification and quantification of endogenous peptides in neuroendocrine tissues
    • Fricker, L. D., Lim, J., Pan, H., and Che, F. Y. (2006) Peptidomics: identification and quantification of endogenous peptides in neuroendocrine tissues. Mass Spectrom. Rev. 25, 327-344
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 327-344
    • Fricker, L.D.1    Lim, J.2    Pan, H.3    Che, F.Y.4
  • 20
    • 79953032976 scopus 로고    scopus 로고
    • Neuropeptide profiling of the bovine hypothalamus: Thermal stabilization is an effective tool in inhibiting post-mortem degradation
    • Colgrave, M. L., Xi, L., Lehnert, S. A., Flatscher-Bader, T., Wadensten, H., Nilsson, A., Andren, P. E., and Wijffels, G. (2011) Neuropeptide profiling of the bovine hypothalamus: thermal stabilization is an effective tool in inhibiting post-mortem degradation. Proteomics 11, 1264-1276
    • (2011) Proteomics , vol.11 , pp. 1264-1276
    • Colgrave, M.L.1    Xi, L.2    Lehnert, S.A.3    Flatscher-Bader, T.4    Wadensten, H.5    Nilsson, A.6    Andren, P.E.7    Wijffels, G.8
  • 21
    • 84863012019 scopus 로고    scopus 로고
    • Extensive characterization of Tupaia belangeri neuropeptidome using an integrated mass spectrometric approach
    • Petruzziello, F., Fouillen, L., Wadensten, H., Kretz, R., Andren, P. E., Rainer, G., and Zhang, X. (2012) Extensive characterization of Tupaia belangeri neuropeptidome using an integrated mass spectrometric approach. J. Proteome Res. 11, 886-896
    • (2012) J. Proteome Res. , vol.11 , pp. 886-896
    • Petruzziello, F.1    Fouillen, L.2    Wadensten, H.3    Kretz, R.4    Andren, P.E.5    Rainer, G.6    Zhang, X.7
  • 22
    • 0347360139 scopus 로고    scopus 로고
    • Peptidomics of the locust corpora allata: Identification of novel pyrokinins (-FXPRLamides)
    • DOI 10.1016/j.peptides.2003.10.006
    • Clynen, E., Baggerman, G., Huybrechts, J., Vanden Bosch, L., De Loof, A., and Schoofs, L. (2003) Peptidomics of the locust corpora allata: identification of novel pyrokinins (-FXPRLamides). Peptides 24, 1493-1500 (Pubitemid 38045561)
    • (2003) Peptides , vol.24 , Issue.10 , pp. 1493-1500
    • Clynen, E.1    Baggerman, G.2    Huybrechts, J.3    Vanden, B.L.4    De Loof, A.5    Schoofs, L.6
  • 23
    • 76649132991 scopus 로고    scopus 로고
    • Endogenous peptide discovery of the rat circadian clock: A focused study of the suprachiasmatic nucleus by ultrahigh performance tandem mass spectrometry
    • Lee, J. E., Atkins, N., Jr., Hatcher, N. G., Zamdborg, L., Gillette, M. U., Sweedler, J. V., and Kelleher, N. L. (2010) Endogenous peptide discovery of the rat circadian clock: a focused study of the suprachiasmatic nucleus by ultrahigh performance tandem mass spectrometry. Mol. Cell. Proteomics 9, 285-297
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 285-297
    • Lee, J.E.1    Atkins Jr., N.2    Hatcher, N.G.3    Zamdborg, L.4    Gillette, M.U.5    Sweedler, J.V.6    Kelleher, N.L.7
  • 25
    • 66749086310 scopus 로고    scopus 로고
    • Expanding the Crustacean neuropeptidome using a multifaceted mass spectrometric approach
    • Ma, M., Wang, J., Chen, R., and Li, L. (2009) Expanding the Crustacean neuropeptidome using a multifaceted mass spectrometric approach. J. Proteome Res. 8, 2426-2437
    • (2009) J. Proteome Res. , vol.8 , pp. 2426-2437
    • Ma, M.1    Wang, J.2    Chen, R.3    Li, L.4
  • 27
    • 26844542155 scopus 로고    scopus 로고
    • Identification of neuropeptides from the decapod crustacean sinus glands using nanoscale liquid chromatography tandem mass spectrometry
    • DOI 10.1016/j.bbrc.2005.09.111, PII S0006291X05021406
    • Fu, Q., Goy, M. F., and Li, L. (2005) Identification of neuropeptides from the decapod crustacean sinus glands using nanoscale liquid chromatography tandem mass spectrometry. Biochem. Biophys. Res. Commun. 337, 765-778 (Pubitemid 41446981)
    • (2005) Biochemical and Biophysical Research Communications , vol.337 , Issue.3 , pp. 765-778
    • Fu, Q.1    Goy, M.F.2    Li, L.3
  • 28
    • 28544431940 scopus 로고    scopus 로고
    • De novo sequencing of neuropeptides using reductive isotopic methylation and investigation of ESI QTOF MS/MS fragmentation pattern of neuropeptides with N-terminal dimethylation
    • DOI 10.1021/ac051324e
    • Fu, Q., and Li, L. (2005) De novo sequencing of neuropeptides using reductive isotopic methylation and investigation of ESI QTOF MS/MS fragmentation pattern of neuropeptides with N-terminal dimethylation. Anal. Chem. 77, 7783-7795 (Pubitemid 41746247)
    • (2005) Analytical Chemistry , vol.77 , Issue.23 , pp. 7783-7795
    • Fu, Q.1    Li, L.2
  • 29
    • 76149132669 scopus 로고    scopus 로고
    • Mass spectral analysis of neuropeptide expression and distribution in the nervous system of the lobster Homarus americanus
    • Chen, R., Jiang, X., Conaway, M. C., Mohtashemi, I., Hui, L., Viner, R., and Li, L. (2010) Mass spectral analysis of neuropeptide expression and distribution in the nervous system of the lobster Homarus americanus. J. Proteome Res. 9, 818-832
    • (2010) J. Proteome Res. , vol.9 , pp. 818-832
    • Chen, R.1    Jiang, X.2    Conaway, M.C.3    Mohtashemi, I.4    Hui, L.5    Viner, R.6    Li, L.7
  • 30
    • 70350131986 scopus 로고    scopus 로고
    • Immuno-affinity-based mass spectrometric characterization of the FMRFamiderelated peptide family in the pericardial organ of Cancer borealis
    • Ma, M., Sturm, R. M., Kutz-Naber, K. K., Fu, Q., and Li, L. (2009) Immuno-affinity-based mass spectrometric characterization of the FMRFamiderelated peptide family in the pericardial organ of Cancer borealis. Biochem. Biophys. Res. Commun. 390, 325-330
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 325-330
    • Ma, M.1    Sturm, R.M.2    Kutz-Naber, K.K.3    Fu, Q.4    Li, L.5
  • 31
    • 67849128540 scopus 로고    scopus 로고
    • Mass spectrometric characterization and physiological actions of novel crustacean C-type allatostatins
    • Ma, M., Szabo, T. M., Jia, C., Marder, E., and Li, L. (2009) Mass spectrometric characterization and physiological actions of novel crustacean C-type allatostatins. Peptides 30, 1660-1668
    • (2009) Peptides , vol.30 , pp. 1660-1668
    • Ma, M.1    Szabo, T.M.2    Jia, C.3    Marder, E.4    Li, L.5
  • 32
    • 33845388969 scopus 로고    scopus 로고
    • Rat neuropeptidomics by LC-MS/MS and MALDI-FTMS: Enhanced dissection and extraction techniques coupled with 2D RP-RP HPLC
    • DOI 10.1021/pr0603452
    • Dowell, J. A., Heyden, W. V., and Li, L. (2006) Rat neuropeptidomics by LC-MS/MS and MALDI-FTMS: Enhanced dissection and extraction techniques coupled with 2D RP-RP HPLC. J. Proteome Res. 5, 3368-3375 (Pubitemid 44904328)
    • (2006) Journal of Proteome Research , vol.5 , Issue.12 , pp. 3368-3375
    • Dowell, J.A.1    Vander, H.W.2    Li, L.3
  • 34
    • 58149473112 scopus 로고    scopus 로고
    • Combining bottom-up and top-down mass spectrometric strategies for de novo sequencing of the crustacean hyperglycemic hormone from Cancer borealis
    • Ma, M., Chen, R., Ge, Y., He, H., Marshall, A. G., and Li, L. (2009) Combining bottom-up and top-down mass spectrometric strategies for de novo sequencing of the crustacean hyperglycemic hormone from Cancer borealis. Anal. Chem. 81, 240-247
    • (2009) Anal. Chem. , vol.81 , pp. 240-247
    • Ma, M.1    Chen, R.2    Ge, Y.3    He, H.4    Marshall, A.G.5    Li, L.6
  • 35
    • 77951064458 scopus 로고    scopus 로고
    • Top-down de novo protein sequencing of a 13.6 kDa camelid single heavy chain antibody by matrix-assisted laser desorption ionization-time-of-flight/ time-of-flight mass spectrometry
    • Resemann, A., Wunderlich, D., Rothbauer, U., Warscheid, B., Leonhardt, H., Fuchser, J., Kuhlmann, K., and Suckau, D. (2010) Top-down de novo protein sequencing of a 13.6 kDa camelid single heavy chain antibody by matrix-assisted laser desorption ionization-time-of-flight/time-of-flight mass spectrometry. Anal. Chem. 82, 3283-3292
    • (2010) Anal. Chem. , vol.82 , pp. 3283-3292
    • Resemann, A.1    Wunderlich, D.2    Rothbauer, U.3    Warscheid, B.4    Leonhardt, H.5    Fuchser, J.6    Kuhlmann, K.7    Suckau, D.8
  • 37
    • 84862971333 scopus 로고    scopus 로고
    • Deep amino acid sequencing of native brain GABAA receptors using high-resolution mass spectrometry
    • doi: 10.1074/mcp.M111.011445
    • Chen, Z. W., Fuchs, K., Sieghart, W., Townsend, R. R., and Evers, A. S. (2012) Deep amino acid sequencing of native brain GABAA receptors using high-resolution mass spectrometry. Mol Cell Proteomics 11, doi: 10.1074/mcp.M111.011445
    • (2012) Mol Cell Proteomics , vol.11
    • Chen, Z.W.1    Fuchs, K.2    Sieghart, W.3    Townsend, R.R.4    Evers, A.S.5
  • 38
    • 84861112803 scopus 로고    scopus 로고
    • Mapping the protein interaction network of the human COP9 signalosome (CSN) complex using a label-free QTAX strategy
    • Fang, L., Kaake, R. M., Patel, V. R., Yang, Y., Baldi, P., and Huang, L. (2012) Mapping the protein interaction network of the human COP9 signalosome (CSN) complex using a label-free QTAX strategy. Mol. Cell. Proteomics 11, 138-147
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 138-147
    • Fang, L.1    Kaake, R.M.2    Patel, V.R.3    Yang, Y.4    Baldi, P.5    Huang, L.6
  • 40
    • 79958016332 scopus 로고    scopus 로고
    • A comparative review of short and long neuropeptide F signaling in invertebrates: Any similarities to vertebrate neuropeptide Y signaling?
    • Nässel, D. R., and Wegener, C. (2011) A comparative review of short and long neuropeptide F signaling in invertebrates: Any similarities to vertebrate neuropeptide Y signaling? Peptides 32, 1335-1355
    • (2011) Peptides , vol.32 , pp. 1335-1355
    • Nässel, D.R.1    Wegener, C.2
  • 41
    • 77949786295 scopus 로고    scopus 로고
    • Value of using multiple proteases for large-scale mass spectrometry-based proteomics
    • Swaney, D. L., Wenger, C. D., and Coon, J. J. (2010) Value of using multiple proteases for large-scale mass spectrometry-based proteomics. J Proteome Res 9, 1323-1329
    • (2010) J Proteome Res , vol.9 , pp. 1323-1329
    • Swaney, D.L.1    Wenger, C.D.2    Coon, J.J.3
  • 42
    • 69149100342 scopus 로고    scopus 로고
    • Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state
    • Ge, Y., Rybakova, I. N., Xu, Q., and Moss, R. L. (2009) Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state. Proc. Natl. Acad. Sci. U.S.A. 106, 12658-12663
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 12658-12663
    • Ge, Y.1    Rybakova, I.N.2    Xu, Q.3    Moss, R.L.4
  • 43
    • 0029933661 scopus 로고    scopus 로고
    • Structure and significance of mandibular organ-inhibiting hormone in the crab, Cancer pagurus. Involvement in multihormonal regulation of growth and reproduction
    • Wainwright, G., Webster, S. G., Wilkinson, M. C., Chung, J. S., and Rees, H. H. (1996) Structure and significance of mandibular organ-inhibiting hormone in the crab, Cancer pagurus. Involvement in multihormonal regulation of growth and reproduction. J. Biol. Chem. 271, 12749-12754
    • (1996) J. Biol. Chem. , vol.271 , pp. 12749-12754
    • Wainwright, G.1    Webster, S.G.2    Wilkinson, M.C.3    Chung, J.S.4    Rees, H.H.5
  • 44
    • 0033569703 scopus 로고    scopus 로고
    • Molecular characterization and expression of mandibular organ-inhibiting hormone, a recently discovered neuropeptide involved in the regulation of growth and reproduction in the crab Cancer pagurus
    • DOI 10.1042/0264-6021:3430355
    • Tang, C., Lu, W., Wainwright, G., Webster, S. G., Rees, H. H., and Turner, P. C. (1999) Molecular characterization and expression of mandibular organ-inhibiting hormone, a recently discovered neuropeptide involved in the regulation of growth and reproduction in the crab Cancer pagurus. Biochem. J. 343, 355-360 (Pubitemid 29511768)
    • (1999) Biochemical Journal , vol.343 , Issue.2 , pp. 355-360
    • Tang, C.1    Lu, W.2    Wainwright, G.3    Webster, S.G.4    Rees, H.H.5    Turner, P.C.6
  • 45
    • 68849108925 scopus 로고    scopus 로고
    • Molecular and cellular specificity of post-translational aminoacyl isomerization in the crustacean hyperglycaemic hormone family
    • Ollivaux, C., Gallois, D., Amiche, M., Boscaméric, M., and Soyez, D. (2009) Molecular and cellular specificity of post-translational aminoacyl isomerization in the crustacean hyperglycaemic hormone family. FEBS J 276, 4790-4802
    • (2009) FEBS J , vol.276 , pp. 4790-4802
    • Ollivaux, C.1    Gallois, D.2    Amiche, M.3    Boscaméric, M.4    Soyez, D.5
  • 47
    • 78449267576 scopus 로고    scopus 로고
    • Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology
    • Bush, M. F., Hall, Z., Giles, K., Hoyes, J., Robinson, C. V., and Ruotolo, B. T. (2010) Collision cross sections of proteins and their complexes: a calibration framework and database for gas-phase structural biology. Anal. Chem. 82, 9557-9565
    • (2010) Anal. Chem. , vol.82 , pp. 9557-9565
    • Bush, M.F.1    Hall, Z.2    Giles, K.3    Hoyes, J.4    Robinson, C.V.5    Ruotolo, B.T.6
  • 48
    • 84859826519 scopus 로고    scopus 로고
    • PEAKS DB: De novo sequencing assisted database search for sensitive and accurate peptide identification
    • doi: 10.1074/mcp.M111.010587
    • Zhang, J., Xin, L., Shan, B., Chen, W., Xie, M., Yuen, D., Zhang, W., Zhang, Z., Lajoie, G. A., and Ma, B. (2012) PEAKS DB: De novo sequencing assisted database search for sensitive and accurate peptide identification. Mol. Cell. Proteomics 11, 1-8, doi: 10.1074/mcp.M111.010587
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1-8
    • Zhang, J.1    Xin, L.2    Shan, B.3    Chen, W.4    Xie, M.5    Yuen, D.6    Zhang, W.7    Zhang, Z.8    Lajoie, G.A.9    Ma, B.10
  • 49
    • 57449097186 scopus 로고    scopus 로고
    • Automated de novo protein sequencing of monoclonal antibodies
    • Bandeira, N., Pham, V., Pevzner, P., Arnott, D., and Lill, J. R. (2008) Automated de novo protein sequencing of monoclonal antibodies. Nat. Biotechnol. 26, 1336-1338
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1336-1338
    • Bandeira, N.1    Pham, V.2    Pevzner, P.3    Arnott, D.4    Lill, J.R.5
  • 50
    • 4644262588 scopus 로고    scopus 로고
    • A new and sensitive on-line liquid chromatography/mass spectrometric approach for top-down protein analysis: The comprehensive analysis of human growth hormone in an E. coli lysate using a hybrid linear ion trap/Fourier transform ion cyclotron resonance mass spectrometer
    • DOI 10.1002/rcm.1609
    • Wu, S. L., Jardine, I., Hancock, W. S., and Karger, B. L. (2004) A new and sensitive on-line liquid chromatography/mass spectrometric approach for top-down protein analysis: the comprehensive analysis of human growth hormone in an E. coli lysate using a hybrid linear ion trap/Fourier transform ion cyclotron resonance mass spectrometer. Rapid Commun. Mass Spectrom. 18, 2201-2207 (Pubitemid 39297354)
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , Issue.19 , pp. 2201-2207
    • Wu, S.-L.1    Jardine, I.2    Hancock, W.S.3    Karger, B.L.4
  • 51
    • 77951833317 scopus 로고    scopus 로고
    • High resolution electron transfer dissociation studies of unfractionated intact histones from murine embryonic stem cells using on-line capillary LC separation: Determination of abundant histone isoforms and post-translational modifications
    • Eliuk, S. M., Maltby, D., Panning, B., and Burlingame, A. L. (2010) High resolution electron transfer dissociation studies of unfractionated intact histones from murine embryonic stem cells using on-line capillary LC separation: determination of abundant histone isoforms and post-translational modifications. Mol. Cell. Proteomics 9, 824-837
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 824-837
    • Eliuk, S.M.1    Maltby, D.2    Panning, B.3    Burlingame, A.L.4
  • 52
    • 80052485658 scopus 로고    scopus 로고
    • Effectiveness of CID, HCD, and ETD with FT MS/MS for degradomic- peptidomic analysis: Comparison of peptide identification methods
    • Shen, Y., Tolić, N., Xie, F., Zhao, R., Purvine, S. O., Schepmoes, A. A., Moore, R. J., Anderson, G. A., and Smith, R. D. (2011) Effectiveness of CID, HCD, and ETD with FT MS/MS for degradomic-peptidomic analysis: comparison of peptide identification methods. J. Proteome Res. 10, 3929-3943
    • (2011) J. Proteome Res. , vol.10 , pp. 3929-3943
    • Shen, Y.1    Tolić, N.2    Xie, F.3    Zhao, R.4    Purvine, S.O.5    Schepmoes, A.A.6    Moore, R.J.7    Anderson, G.A.8    Smith, R.D.9
  • 54
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 56
    • 0033536938 scopus 로고    scopus 로고
    • Crustacean hyperglycemic hormone in the lobster nervous system: Localization and release from cells in the subesophageal ganglion and thoracic second roots
    • DOI 10.1002/(SICI)1096-9861(19991108)414:1<50::AID-CNE4>3.0.CO;2-Q
    • Chang, E. S., Chang, S. A., Beltz, B. S., and Kravitz, E. A. (1999) Crustacean hyperglycemic hormone in the lobster nervous system: localization and release from cells in the subesophageal ganglion and thoracic second roots. J. Comp. Neurol. 414, 50-56 (Pubitemid 29477141)
    • (1999) Journal of Comparative Neurology , vol.414 , Issue.1 , pp. 50-56
    • Chang, E.S.1    Chang, S.A.2    Beltz, B.S.3    Kravitz, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.