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Volumn 11, Issue 5, 2012, Pages 2819-2827

High identification rates of endogenous neuropeptides from mouse brain

Author keywords

charge state directed tandem MS; identification rate; neuropeptide; neuropeptidomics

Indexed keywords

GALANIN; METENKEPHALIN; NEUROPEPTIDE; NEUROPEPTIDE Y; NEUROTENSIN; SOMATOSTATIN 28; THYMOSIN BETA4;

EID: 84860495934     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr3001699     Document Type: Article
Times cited : (36)

References (44)
  • 3
    • 79953267923 scopus 로고    scopus 로고
    • Profiling metabolites and peptides in single cells
    • Rubakhin, S. S.; Romanova, E. V.; Nemes, P.; Sweedler, J. V. Profiling metabolites and peptides in single cells Nat. Methods 2011, 8 (4 Suppl) S20-9
    • (2011) Nat. Methods , vol.8 , Issue.4 SUPPL. , pp. 20-29
    • Rubakhin, S.S.1    Romanova, E.V.2    Nemes, P.3    Sweedler, J.V.4
  • 4
    • 33644879722 scopus 로고    scopus 로고
    • Peptidomics: Identification and quantification of endogenous peptides in neuroendocrine tissues
    • Fricker, L. D.; Lim, J.; Pan, H.; Che, F. Y. Peptidomics: identification and quantification of endogenous peptides in neuroendocrine tissues Mass Spectrom. Rev. 2006, 25 (2) 327-44
    • (2006) Mass Spectrom. Rev. , vol.25 , Issue.2 , pp. 327-344
    • Fricker, L.D.1    Lim, J.2    Pan, H.3    Che, F.Y.4
  • 6
    • 61849162816 scopus 로고    scopus 로고
    • Improved identification of endogenous peptides from murine nervous tissue by multiplexed peptide extraction methods and multiplexed mass spectrometric analysis
    • Altelaar, A. F.; Mohammed, S.; Brans, M. A.; Adan, R. A.; Heck, A. J. Improved identification of endogenous peptides from murine nervous tissue by multiplexed peptide extraction methods and multiplexed mass spectrometric analysis J. Proteome Res. 2009, 8 (2) 870-6
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 870-876
    • Altelaar, A.F.1    Mohammed, S.2    Brans, M.A.3    Adan, R.A.4    Heck, A.J.5
  • 8
    • 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
    • Dowell, J. A.; Heyden, W. V.; Li, L. Rat neuropeptidomics by LC-MS/MS and MALDI-FTMS: Enhanced dissection and extraction techniques coupled with 2D RP-RP HPLC J. Proteome Res. 2006, 5 (12) 3368-75
    • (2006) J. Proteome Res. , vol.5 , Issue.12 , pp. 3368-3375
    • Dowell, J.A.1    Heyden, W.V.2    Li, L.3
  • 9
    • 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.; Kelleher, N. L. Endogenous peptide discovery of the rat circadian clock: a focused study of the suprachiasmatic nucleus by ultrahigh performance tandem mass spectrometry Mol. Cell. Proteomics 2010, 9 (2) 285-97
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.2 , 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
  • 10
    • 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.; Zhang, X. Extensive characterization of Tupaia belangeri neuropeptidome using an integrated mass spectrometric approach J. Proteome Res. 2012, 11 (3) 886-96
    • (2012) J. Proteome Res. , vol.11 , Issue.3 , 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
  • 12
    • 34648814041 scopus 로고    scopus 로고
    • Modulators in concert for cognition: Modulator interactions in the prefrontal cortex
    • Briand, L. A.; Gritton, H.; Howe, W. M.; Young, D. A.; Sarter, M. Modulators in concert for cognition: modulator interactions in the prefrontal cortex Prog. Neurobiol. 2007, 83 (2) 69-91
    • (2007) Prog. Neurobiol. , vol.83 , Issue.2 , pp. 69-91
    • Briand, L.A.1    Gritton, H.2    Howe, W.M.3    Young, D.A.4    Sarter, M.5
  • 14
    • 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.; Andren, P. E. The significance of biochemical and molecular sample integrity in brain proteomics and peptidomics: stathmin 2-20 and peptides as sample quality indicators Proteomics 2007, 7 (24) 4445-56
    • (2007) Proteomics , vol.7 , Issue.24 , pp. 4445-4456
    • Skold, K.1    Svensson, M.2    Norrman, M.3    Sjogren, B.4    Svenningsson, P.5    Andren, P.E.6
  • 15
    • 0027230760 scopus 로고
    • Methionine enkephalin-like immunoreactivity, substance P-like immunoreactivity and beta-endorphin-like immunoreactivity post-mortem stability in rat pituitary
    • Zhu, X.; Desiderio, D. M. Methionine enkephalin-like immunoreactivity, substance P-like immunoreactivity and beta-endorphin-like immunoreactivity post-mortem stability in rat pituitary J. Chromatogr. 1993, 616 (2) 175-87
    • (1993) J. Chromatogr. , vol.616 , Issue.2 , pp. 175-187
    • Zhu, X.1    Desiderio, D.M.2
  • 17
    • 26844518104 scopus 로고    scopus 로고
    • Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary
    • Che, F. Y.; Lim, J.; Pan, H.; Biswas, R.; Fricker, L. D. Quantitative neuropeptidomics of microwave-irradiated mouse brain and pituitary Mol. Cell. Proteomics 2005, 4 (9) 1391-405
    • (2005) Mol. Cell. 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
  • 18
    • 61849098321 scopus 로고    scopus 로고
    • A quantitative peptidomic analysis of peptides related to the endogenous opioid and tachykinin systems in nucleus accumbens of rats following naloxone-precipitated morphine withdrawal
    • Rossbach, U.; Nilsson, A.; Falth, M.; Kultima, K.; Zhou, Q.; Hallberg, M.; Gordh, T.; Andren, P. E.; Nyberg, F. A quantitative peptidomic analysis of peptides related to the endogenous opioid and tachykinin systems in nucleus accumbens of rats following naloxone-precipitated morphine withdrawal J. Proteome Res. 2009, 8 (2) 1091-8
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 1091-1098
    • Rossbach, U.1    Nilsson, A.2    Falth, M.3    Kultima, K.4    Zhou, Q.5    Hallberg, M.6    Gordh, T.7    Andren, P.E.8    Nyberg, F.9
  • 19
    • 71049194213 scopus 로고    scopus 로고
    • Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides
    • Kultima, K.; Nilsson, A.; Scholz, B.; Rossbach, U. L.; Falth, M.; Andren, P. E. Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides Mol. Cell. Proteomics 2009, 8 (10) 2285-95
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.10 , pp. 2285-2295
    • Kultima, K.1    Nilsson, A.2    Scholz, B.3    Rossbach, U.L.4    Falth, M.5    Andren, P.E.6
  • 22
    • 22544465253 scopus 로고    scopus 로고
    • SPIDER: Software for protein identification from sequence tags with de novo sequencing error
    • Han, Y.; Ma, B.; Zhang, K. SPIDER: software for protein identification from sequence tags with de novo sequencing error J. Bioinf. Comput. Biol. 2005, 3 (3) 697-716
    • (2005) J. Bioinf. Comput. Biol. , vol.3 , Issue.3 , pp. 697-716
    • Han, Y.1    Ma, B.2    Zhang, K.3
  • 24
    • 0027174437 scopus 로고
    • Peptide amidation: Signature of bioactivity
    • 172-3; discussion 93-5
    • Cuttitta, F. Peptide amidation: signature of bioactivity Anat. Rec. 1993, 236 (1) 87-93 and 172-3; discussion 93-5.
    • (1993) Anat. Rec. , vol.236 , Issue.1 , pp. 87-93
    • Cuttitta, F.1
  • 25
    • 0026514908 scopus 로고
    • The biosynthesis of neuropeptides: Peptide alpha-amidation
    • Eipper, B. A.; Stoffers, D. A.; Mains, R. E. The biosynthesis of neuropeptides: peptide alpha-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
  • 27
    • 67449107485 scopus 로고    scopus 로고
    • Striatal alterations of secretogranin-1, somatostatin, prodynorphin, and cholecystokinin peptides in an experimental mouse model of Parkinson disease
    • Nilsson, A.; Falth, M.; Zhang, X.; Kultima, K.; Skold, K.; Svenningsson, P.; Andren, P. E. Striatal alterations of secretogranin-1, somatostatin, prodynorphin, and cholecystokinin peptides in an experimental mouse model of Parkinson disease Mol. Cell. Proteomics 2009, 8 (5) 1094-104
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.5 , pp. 1094-1104
    • Nilsson, A.1    Falth, M.2    Zhang, X.3    Kultima, K.4    Skold, K.5    Svenningsson, P.6    Andren, P.E.7
  • 30
    • 33746256408 scopus 로고    scopus 로고
    • Direct protein identification from nonspecific peptide pools by high-accuracy MS data filtering
    • An Thieu, V.; Kirsch, D.; Flad, T.; Muller, C.; Spengler, B. Direct protein identification from nonspecific peptide pools by high-accuracy MS data filtering Angew. Chem., Int. Ed. 2006, 45 (20) 3317-9
    • (2006) Angew. Chem., Int. Ed. , vol.45 , Issue.20 , pp. 3317-3319
    • An Thieu, V.1    Kirsch, D.2    Flad, T.3    Muller, C.4    Spengler, B.5
  • 32
    • 70549084975 scopus 로고    scopus 로고
    • Directed mass spectrometry: Towards hypothesis-driven proteomics
    • Schmidt, A.; Claassen, M.; Aebersold, R. Directed mass spectrometry: towards hypothesis-driven proteomics Curr. Opin. Chem. Biol. 2009, 13 (5-6) 510-7
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , Issue.5-6 , pp. 510-517
    • Schmidt, A.1    Claassen, M.2    Aebersold, R.3
  • 33
    • 0035151481 scopus 로고    scopus 로고
    • Postmortem changes in the level of brain proteins
    • Fountoulakis, M.; Hardmeier, R.; Hoger, H.; Lubec, G. Postmortem changes in the level of brain proteins Exp. Neurol. 2001, 167 (1) 86-94
    • (2001) Exp. Neurol. , vol.167 , Issue.1 , pp. 86-94
    • Fountoulakis, M.1    Hardmeier, R.2    Hoger, H.3    Lubec, G.4
  • 34
    • 0142244521 scopus 로고    scopus 로고
    • Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome
    • Franzen, B.; Yang, Y.; Sunnemark, D.; Wickman, M.; Ottervald, J.; Oppermann, M.; Sandberg, K. Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome Proteomics 2003, 3 (10) 1920-9
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1920-1929
    • Franzen, B.1    Yang, Y.2    Sunnemark, D.3    Wickman, M.4    Ottervald, J.5    Oppermann, M.6    Sandberg, K.7
  • 36
    • 41549129862 scopus 로고    scopus 로고
    • Assessing quantitative post-mortem changes in the gray matter of the human frontal cortex proteome by 2-D DIGE
    • Crecelius, A.; Gotz, A.; Arzberger, T.; Frohlich, T.; Arnold, G. J.; Ferrer, I.; Kretzschmar, H. A. Assessing quantitative post-mortem changes in the gray matter of the human frontal cortex proteome by 2-D DIGE Proteomics 2008, 8 (6) 1276-91
    • (2008) Proteomics , vol.8 , Issue.6 , pp. 1276-1291
    • Crecelius, A.1    Gotz, A.2    Arzberger, T.3    Frohlich, T.4    Arnold, G.J.5    Ferrer, I.6    Kretzschmar, H.A.7
  • 38
    • 71049141684 scopus 로고    scopus 로고
    • Snapshot peptidomics of the regulated secretory pathway
    • Sasaki, K.; Satomi, Y.; Takao, T.; Minamino, N. Snapshot peptidomics of the regulated secretory pathway Mol. Cell. Proteomics 2009, 8 (7) 1638-47
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.7 , pp. 1638-1647
    • Sasaki, K.1    Satomi, Y.2    Takao, T.3    Minamino, N.4
  • 40
    • 75949114410 scopus 로고    scopus 로고
    • Neuropeptidomic analysis establishes a major role for prohormone convertase-2 in neuropeptide biosynthesis
    • Zhang, X.; Pan, H.; Peng, B.; Steiner, D. F.; Pintar, J. E.; Fricker, L. D. Neuropeptidomic analysis establishes a major role for prohormone convertase-2 in neuropeptide biosynthesis J. Neurochem. 2010, 112 (5) 1168-79
    • (2010) J. Neurochem. , vol.112 , Issue.5 , pp. 1168-1179
    • Zhang, X.1    Pan, H.2    Peng, B.3    Steiner, D.F.4    Pintar, J.E.5    Fricker, L.D.6
  • 41
    • 77954573017 scopus 로고    scopus 로고
    • Analysis of mouse brain peptides using mass spectrometry-based peptidomics: Implications for novel functions ranging from non-classical neuropeptides to microproteins
    • Fricker, L. D. Analysis of mouse brain peptides using mass spectrometry-based peptidomics: implications for novel functions ranging from non-classical neuropeptides to microproteins Mol. Biosyst. 2010, 6 (8) 1355-65
    • (2010) Mol. Biosyst. , vol.6 , Issue.8 , pp. 1355-1365
    • Fricker, L.D.1
  • 44
    • 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
    • Parkin, M. C.; Wei, H.; OCallaghan, J. P.; Kennedy, R. T. Sample-dependent effects on the neuropeptidome detected in rat brain tissue preparations by capillary liquid chromatography with tandem mass spectrometry Anal. Chem. 2005, 77 (19) 6331-8
    • (2005) Anal. Chem. , vol.77 , Issue.19 , pp. 6331-6338
    • Parkin, M.C.1    Wei, H.2    Ocallaghan, J.P.3    Kennedy, R.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.