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Volumn 3, Issue , 2014, Pages 152-170

Mass spectrometric characterization of the crustacean neuropeptidome

Author keywords

Crustacean; Mass spectrometry; Neuropeptide; NP; Peptidomics

Indexed keywords

NEUROPEPTIDE; NEUROPEPTIDOME; UNCLASSIFIED DRUG;

EID: 84902481329     PISSN: None     EISSN: 22129685     Source Type: Journal    
DOI: 10.1016/j.euprot.2014.02.015     Document Type: Article
Times cited : (10)

References (196)
  • 2
    • 84867136812 scopus 로고    scopus 로고
    • Neuropeptide transmission in brain circuits
    • van den Pol A.N. Neuropeptide transmission in brain circuits. Neuron 2012, 76:98-115.
    • (2012) Neuron , vol.76 , pp. 98-115
    • van den Pol, A.N.1
  • 4
    • 84867128022 scopus 로고    scopus 로고
    • Peptide neuromodulation in invertebrate model systems
    • Taghert P.H., Nitabach M.N. Peptide neuromodulation in invertebrate model systems. Neuron 2012, 76:82-97.
    • (2012) Neuron , vol.76 , pp. 82-97
    • Taghert, P.H.1    Nitabach, M.N.2
  • 5
    • 0034856707 scopus 로고    scopus 로고
    • Peptidomics of the pars intercerebralis-corpus cardiacum complex of the migratory locust, Locusta migratoria
    • Clynen E., Baggerman G., Veelaert D., Cerstiaens A., Van der Horst D., Harthoorn L., et al. Peptidomics of the pars intercerebralis-corpus cardiacum complex of the migratory locust, Locusta migratoria. Eur J Biochem 2001, 268:1929-1939.
    • (2001) Eur J Biochem , vol.268 , pp. 1929-1939
    • Clynen, E.1    Baggerman, G.2    Veelaert, D.3    Cerstiaens, A.4    Van der Horst, D.5    Harthoorn, L.6
  • 7
    • 0035238444 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization quadrupole Time-of-Flight Mass Spectrometry: an elegant tool for peptidomics
    • Verhaert P., Uttenweiler-Joseph S., de Vries M., Loboda A., Ens W., Standing K.G. Matrix-assisted laser desorption/ionization quadrupole Time-of-Flight Mass Spectrometry: an elegant tool for peptidomics. Proteomics 2001, 1:118-131.
    • (2001) Proteomics , vol.1 , pp. 118-131
    • Verhaert, P.1    Uttenweiler-Joseph, S.2    de Vries, M.3    Loboda, A.4    Ens, W.5    Standing, K.G.6
  • 8
    • 0026663852 scopus 로고
    • Crustacean neuropeptides: structures, functions and comparative aspects
    • Keller R. Crustacean neuropeptides: structures, functions and comparative aspects. Experientia 1992, 48:439-448.
    • (1992) Experientia , vol.48 , pp. 439-448
    • Keller, R.1
  • 9
    • 0019618004 scopus 로고
    • The use of propane/isopentane mixtures for rapid freezing of biological specimens
    • Jehl B., Bauer R., Dörge A., Rick R. The use of propane/isopentane mixtures for rapid freezing of biological specimens. J Microsc 1981, 123:307-309.
    • (1981) J Microsc , vol.123 , pp. 307-309
    • Jehl, B.1    Bauer, R.2    Dörge, A.3    Rick, R.4
  • 10
    • 0042198976 scopus 로고    scopus 로고
    • Direct tissue analysis using matrix-assisted laser desorption/ionization mass spectrometry: practical aspects of sample preparation
    • Schwartz S.A., Reyzer M.L., Caprioli R.M. Direct tissue analysis using matrix-assisted laser desorption/ionization mass spectrometry: practical aspects of sample preparation. J Mass Spectrom 2003, 38:699-708.
    • (2003) J Mass Spectrom , vol.38 , pp. 699-708
    • Schwartz, S.A.1    Reyzer, M.L.2    Caprioli, R.M.3
  • 11
    • 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, 4:1391-1405.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1391-1405
    • Che, F.-Y.1    Lim, J.2    Pan, H.3    Biswas, R.4    Fricker, L.D.5
  • 12
    • 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
    • Sköld K., Svensson M., Norrman M., Sjögren B., Svenningsson P., Andrén 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, 7:4445-4456.
    • (2007) Proteomics , vol.7 , pp. 4445-4456
    • Sköld, K.1    Svensson, M.2    Norrman, M.3    Sjögren, B.4    Svenningsson, P.5    Andrén, P.E.6
  • 13
    • 61849162815 scopus 로고    scopus 로고
    • Heat stabilization of the tissue proteome: a new technology for improved proteomics
    • Svensson M., Borén M., Skold K., Fälth M., Sjögren B., Andersson M., et al. Heat stabilization of the tissue proteome: a new technology for improved proteomics. J Proteome Res 2009, 8:974-981.
    • (2009) J Proteome Res , vol.8 , pp. 974-981
    • Svensson, M.1    Borén, M.2    Skold, K.3    Fälth, M.4    Sjögren, B.5    Andersson, M.6
  • 14
    • 34248230245 scopus 로고    scopus 로고
    • Direct analysis and MALDI imaging of formalin-fixed, paraffin-embedded tissue sections
    • Lemaire R., Desmons A., Tabet J., Day R., Salzet M., Fournier I. Direct analysis and MALDI imaging of formalin-fixed, paraffin-embedded tissue sections. J Proteome Res 2007, 6:1295-1305.
    • (2007) J Proteome Res , vol.6 , pp. 1295-1305
    • Lemaire, R.1    Desmons, A.2    Tabet, J.3    Day, R.4    Salzet, M.5    Fournier, I.6
  • 15
    • 53049107066 scopus 로고    scopus 로고
    • Imaging mass spectrometry of intact proteins from alcohol-preserved tissue specimens: bypassing formalin fixation
    • Chaurand P., Latham J.C., Lane K.B., Mobley J.A., Polosukhin V.V., Wirth P.S., et al. Imaging mass spectrometry of intact proteins from alcohol-preserved tissue specimens: bypassing formalin fixation. J Proteome Res 2008, 7:3543-3555.
    • (2008) J Proteome Res , vol.7 , pp. 3543-3555
    • Chaurand, P.1    Latham, J.C.2    Lane, K.B.3    Mobley, J.A.4    Polosukhin, V.V.5    Wirth, P.S.6
  • 16
    • 33748865022 scopus 로고    scopus 로고
    • Direct molecular analysis of whole-body animal tissue sections by imaging MALDI mass spectrometry
    • Khatib-Shahidi S., Andersson M., Herman J.L., Gillespie T.A., Caprioli R.M. Direct molecular analysis of whole-body animal tissue sections by imaging MALDI mass spectrometry. Anal Chem 2006, 78:6448-6456.
    • (2006) Anal Chem , vol.78 , pp. 6448-6456
    • Khatib-Shahidi, S.1    Andersson, M.2    Herman, J.L.3    Gillespie, T.A.4    Caprioli, R.M.5
  • 18
    • 65549086630 scopus 로고    scopus 로고
    • Three dimensional mapping of neuropeptides and lipids in crustacean brain by mass spectral imaging
    • Chen R., Hui L., Sturm R.M., Li L. Three dimensional mapping of neuropeptides and lipids in crustacean brain by mass spectral imaging. J Am Soc Mass Spectrom 2009, 20:1068-1077.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 1068-1077
    • Chen, R.1    Hui, L.2    Sturm, R.M.3    Li, L.4
  • 20
    • 79959971350 scopus 로고    scopus 로고
    • Poly[N-(2-hydroxypropyl) methacrylamide]-based tissue-embedding medium compatible with MALDI mass spectrometry imaging experiments
    • Strohalm M., Strohalm J.i., Kaftan F., Krásnyi L.s., Volnyi M., Novák P., et al. Poly[N-(2-hydroxypropyl) methacrylamide]-based tissue-embedding medium compatible with MALDI mass spectrometry imaging experiments. Anal Chem 2011, 83:5458-5462.
    • (2011) Anal Chem , vol.83 , pp. 5458-5462
    • Strohalm, M.1    Strohalm, J.2    Kaftan, F.3    Krásnyi, L.S.4    Volnyi, M.5    Novák, P.6
  • 22
    • 33751001298 scopus 로고    scopus 로고
    • New developments in profiling and imaging of proteins from tissue sections by MALDI mass spectrometry
    • Chaurand P., Norris J.L., Cornett D.S., Mobley J.A., Caprioli R.M. New developments in profiling and imaging of proteins from tissue sections by MALDI mass spectrometry. J Proteome Res 2006, 5:2889-2900.
    • (2006) J Proteome Res , vol.5 , pp. 2889-2900
    • Chaurand, P.1    Norris, J.L.2    Cornett, D.S.3    Mobley, J.A.4    Caprioli, R.M.5
  • 24
    • 33750216501 scopus 로고    scopus 로고
    • MALDI-MS direct tissue analysis of proteins: improving signal sensitivity using organic treatments
    • Lemaire R., Wisztorski M., Desmons A., Tabet J., Day R., Salzet M., et al. MALDI-MS direct tissue analysis of proteins: improving signal sensitivity using organic treatments. Anal Chem 2006, 78:7145-7153.
    • (2006) Anal Chem , vol.78 , pp. 7145-7153
    • Lemaire, R.1    Wisztorski, M.2    Desmons, A.3    Tabet, J.4    Day, R.5    Salzet, M.6
  • 25
    • 48349143151 scopus 로고    scopus 로고
    • Enhancement of protein sensitivity for MALDI imaging mass spectrometry after chemical treatment of tissue sections
    • Seeley E.H., Oppenheimer S.R., Mi D., Chaurand P., Caprioli R.M. Enhancement of protein sensitivity for MALDI imaging mass spectrometry after chemical treatment of tissue sections. J Am Soc Mass Spectrom 2008, 19:1069-1077.
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1069-1077
    • Seeley, E.H.1    Oppenheimer, S.R.2    Mi, D.3    Chaurand, P.4    Caprioli, R.M.5
  • 26
    • 70350356597 scopus 로고    scopus 로고
    • Matrix-Assisted Laser Desorption/Ionization Imaging Mass Spectrometry for the Investigation of Proteins and Peptides
    • Burnum K.E., Frappier S.L., Caprioli R.M. Matrix-Assisted Laser Desorption/Ionization Imaging Mass Spectrometry for the Investigation of Proteins and Peptides. Annu Rev Anal Chem. 2008, 1:689-705.
    • (2008) Annu Rev Anal Chem. , vol.1 , pp. 689-705
    • Burnum, K.E.1    Frappier, S.L.2    Caprioli, R.M.3
  • 27
    • 84865187320 scopus 로고    scopus 로고
    • Probing neuropeptide signaling at the organ and cellular domains via imaging mass spectrometry
    • Ye H., Greer T., Li L. Probing neuropeptide signaling at the organ and cellular domains via imaging mass spectrometry. J Proteomics 2012, 75:5014-5026.
    • (2012) J Proteomics , vol.75 , pp. 5014-5026
    • Ye, H.1    Greer, T.2    Li, L.3
  • 28
    • 34548118192 scopus 로고    scopus 로고
    • Sublimation as a method of matrix application for mass spectrometric imaging
    • Hankin J.A., Barkley R.M., Murphy R.C. Sublimation as a method of matrix application for mass spectrometric imaging. J Am Soc Mass Spectrom 2007, 18:1646-1652.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 1646-1652
    • Hankin, J.A.1    Barkley, R.M.2    Murphy, R.C.3
  • 30
    • 79958155933 scopus 로고    scopus 로고
    • High spatial resolution imaging mass spectrometry and classical histology on a single tissue section
    • Deutskens F., Yang J., Caprioli R.M. High spatial resolution imaging mass spectrometry and classical histology on a single tissue section. J Mass Spectrom 2011, 46:568-571.
    • (2011) J Mass Spectrom , vol.46 , pp. 568-571
    • Deutskens, F.1    Yang, J.2    Caprioli, R.M.3
  • 31
    • 84881234848 scopus 로고    scopus 로고
    • A multi-scale strategy for discovery of novel endogenous neuropeptides in the crustacean nervous system
    • Jia C., Lietz C.B., Ye H., Hui L., Yu Q., Yoo S., et al. A multi-scale strategy for discovery of novel endogenous neuropeptides in the crustacean nervous system. J Proteomics 2013, 91:1-12.
    • (2013) J Proteomics , vol.91 , pp. 1-12
    • Jia, C.1    Lietz, C.B.2    Ye, H.3    Hui, L.4    Yu, Q.5    Yoo, S.6
  • 32
    • 84873862221 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the neuropeptidome of the ghost crab Ocypode ceratophthalma (Brachyura, Ocypodidae)
    • Hui L.M., D'Andrea B.T., Jia C.X., Liang Z.D., Christie A.E., Li L.J. Mass spectrometric characterization of the neuropeptidome of the ghost crab Ocypode ceratophthalma (Brachyura, Ocypodidae). Gen Comp Endocrinol 2013, 184:22-34.
    • (2013) Gen Comp Endocrinol , vol.184 , pp. 22-34
    • Hui, L.M.1    D'Andrea, B.T.2    Jia, C.X.3    Liang, Z.D.4    Christie, A.E.5    Li, L.J.6
  • 33
    • 0037066059 scopus 로고    scopus 로고
    • Orcokinin peptides in developing and adult crustacean stomatogastric nervous systems and pericardial organs
    • Li L.J., Pulver S.R., Kelley W.P., Thirumalai V., Sweedler J.V., Marder E. Orcokinin peptides in developing and adult crustacean stomatogastric nervous systems and pericardial organs. J Comp Neurol 2002, 444:227-244.
    • (2002) J Comp Neurol , vol.444 , pp. 227-244
    • Li, L.J.1    Pulver, S.R.2    Kelley, W.P.3    Thirumalai, V.4    Sweedler, J.V.5    Marder, E.6
  • 34
  • 35
    • 62149087472 scopus 로고    scopus 로고
    • Measurement of neuropeptides in crustacean hemolymph via MALDI mass spectrometry
    • Chen R.B., Ma M.M., Hui L.M., Zhang J., Li L.J. Measurement of neuropeptides in crustacean hemolymph via MALDI mass spectrometry. J Am Soc Mass Spectrom 2009, 20:708-718.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 708-718
    • Chen, R.B.1    Ma, M.M.2    Hui, L.M.3    Zhang, J.4    Li, L.J.5
  • 36
    • 42349117573 scopus 로고    scopus 로고
    • Mass spectral comparison of the neuropeptide complement of the stomatogastric ganglion and brain in the adult and embryonic lobster, Homarus americanus
    • Cape S.S., Rehm K.J., Ma M., Marder E., Li L.J. Mass spectral comparison of the neuropeptide complement of the stomatogastric ganglion and brain in the adult and embryonic lobster, Homarus americanus. J Neurochem 2008, 105:690-702.
    • (2008) J Neurochem , vol.105 , pp. 690-702
    • Cape, S.S.1    Rehm, K.J.2    Ma, M.3    Marder, E.4    Li, L.J.5
  • 37
    • 40849107736 scopus 로고    scopus 로고
    • Mass spectral characterization of peptide transmitters/hormones in the nervous system and neuroendocrine organs of the American lobster Homarus americanus
    • Ma M.M., Chen R.B., Sousa G.L., Bors E.K., Kwiatkowski M.A., Goiney C.C., et al. Mass spectral characterization of peptide transmitters/hormones in the nervous system and neuroendocrine organs of the American lobster Homarus americanus. Gen Comp Endocrinol 2008, 156:395-409.
    • (2008) Gen Comp Endocrinol , vol.156 , pp. 395-409
    • Ma, M.M.1    Chen, R.B.2    Sousa, G.L.3    Bors, E.K.4    Kwiatkowski, M.A.5    Goiney, C.C.6
  • 38
    • 3042812979 scopus 로고    scopus 로고
    • Identification of neuropeptides from the sinus gland of the crayfish Orconectes limosus using nanoscale on-line liquid chromatography tandem mass spectrometry
    • Bulau P., Meisen I., Schmitz T., Keller R., Peter-Katalinic J. Identification of neuropeptides from the sinus gland of the crayfish Orconectes limosus using nanoscale on-line liquid chromatography tandem mass spectrometry. Mol Cell Proteomics 2004, 3:558-564.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 558-564
    • Bulau, P.1    Meisen, I.2    Schmitz, T.3    Keller, R.4    Peter-Katalinic, J.5
  • 39
    • 51949117034 scopus 로고    scopus 로고
    • Combining microdialysis, nanoLC-MS, and MALDI-TOF/TOF to detect neuropeptides secreted in the crab, Cancer borealis
    • Behrens H.L., Chen R.B., Li L.J. Combining microdialysis, nanoLC-MS, and MALDI-TOF/TOF to detect neuropeptides secreted in the crab, Cancer borealis. Anal Chem 2008, 80:6949-6958.
    • (2008) Anal Chem , vol.80 , pp. 6949-6958
    • Behrens, H.L.1    Chen, R.B.2    Li, L.J.3
  • 40
    • 76149132669 scopus 로고    scopus 로고
    • Mass Spectral Analysis of Neuropeptide Expression and Distribution in the Nervous System of the Lobster Homarus americanus
    • Chen R.B., Jiang X.Y., Conaway M.C.P., Mohtashemi I., Hui L.M., Viner R., et al. Mass Spectral Analysis of Neuropeptide Expression and Distribution in the Nervous System of the Lobster Homarus americanus. J Proteome Res 2010, 9:818-832.
    • (2010) J Proteome Res , vol.9 , pp. 818-832
    • Chen, R.B.1    Jiang, X.Y.2    Conaway, M.C.P.3    Mohtashemi, I.4    Hui, L.M.5    Viner, R.6
  • 41
    • 33845654922 scopus 로고    scopus 로고
    • Mass spectrometric charting of neuropeptides in arthropod neurons
    • DeKeyser S.S., Li L.J. Mass spectrometric charting of neuropeptides in arthropod neurons. Anal Bioanal Chem 2007, 387:29-35.
    • (2007) Anal Bioanal Chem , vol.387 , pp. 29-35
    • DeKeyser, S.S.1    Li, L.J.2
  • 42
    • 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.M., Cunningham R., Zhang Z.C., Cao W.F., Jia C.X., Li L.J. 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 2011, 10:4219-4229.
    • (2011) J Proteome Res , vol.10 , pp. 4219-4229
    • Hui, L.M.1    Cunningham, R.2    Zhang, Z.C.3    Cao, W.F.4    Jia, C.X.5    Li, L.J.6
  • 43
    • 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.M., Chen R.B., Ge Y., He H., Marshall A.G., Li L.J. Combining bottom-up and top-down mass spectrometric strategies for de novo sequencing of the crustacean hyperglycemic hormone from cancer borealis. Anal Chem 2009, 81:240-247.
    • (2009) Anal Chem , vol.81 , pp. 240-247
    • Ma, M.M.1    Chen, R.B.2    Ge, Y.3    He, H.4    Marshall, A.G.5    Li, L.J.6
  • 44
    • 72749113619 scopus 로고    scopus 로고
    • Combining in silico transcriptome mining and biological mass spectrometry for neuropeptide discovery in the Pacific white shrimp Litopenaeus vannamei
    • Ma M.M., Gard A.L., Xiang F., Wang J.H., Davoodian N., Lenz P.H., et al. Combining in silico transcriptome mining and biological mass spectrometry for neuropeptide discovery in the Pacific white shrimp Litopenaeus vannamei. Peptides 2010, 31:27-43.
    • (2010) Peptides , vol.31 , pp. 27-43
    • Ma, M.M.1    Gard, A.L.2    Xiang, F.3    Wang, J.H.4    Davoodian, N.5    Lenz, P.H.6
  • 45
    • 70350131986 scopus 로고    scopus 로고
    • Immunoaffinity-based mass spectrometric characterization of the FMRFamide-related peptide family in the pericardial organ of Cancer borealis
    • Ma M.M., Sturm R.M., Kutz-Naber K.K., Fu Q., Li L.J. Immunoaffinity-based mass spectrometric characterization of the FMRFamide-related peptide family in the pericardial organ of Cancer borealis. Biochem Biophys Res Commun 2009, 390:325-330.
    • (2009) Biochem Biophys Res Commun , vol.390 , pp. 325-330
    • Ma, M.M.1    Sturm, R.M.2    Kutz-Naber, K.K.3    Fu, Q.4    Li, L.J.5
  • 46
    • 84864118478 scopus 로고    scopus 로고
    • Mass spectrometric elucidation of the neuropeptidome of a crustacean neuroendocrine organ
    • Hui L.M., Xiang F., Zhang Y.Z., Li L.J. Mass spectrometric elucidation of the neuropeptidome of a crustacean neuroendocrine organ. Peptides 2012, 36:230-239.
    • (2012) Peptides , vol.36 , pp. 230-239
    • Hui, L.M.1    Xiang, F.2    Zhang, Y.Z.3    Li, L.J.4
  • 47
    • 25144489182 scopus 로고    scopus 로고
    • Discovering neuropeptides in Caenorhabditis elegans by two dimensional liquid chromatography and mass spectrometry
    • Husson S.J., Clynen E., Baggerman G., De Loof A., Schoofs L. Discovering neuropeptides in Caenorhabditis elegans by two dimensional liquid chromatography and mass spectrometry. Biochem Biophys Res Commun 2005, 335:76-86.
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 76-86
    • Husson, S.J.1    Clynen, E.2    Baggerman, G.3    De Loof, A.4    Schoofs, L.5
  • 49
    • 77957883394 scopus 로고    scopus 로고
    • Online coupling of reverse-phase and hydrophilic interaction liquid chromatography for protein and glycoprotein characterization
    • Lam M.P.Y., Siu S.O., Lau E., Mao X.L., Sun H.Z., Chiu P.C.N., et al. Online coupling of reverse-phase and hydrophilic interaction liquid chromatography for protein and glycoprotein characterization. Anal Bioanal Chem 2010, 398:791-804.
    • (2010) Anal Bioanal Chem , vol.398 , pp. 791-804
    • Lam, M.P.Y.1    Siu, S.O.2    Lau, E.3    Mao, X.L.4    Sun, H.Z.5    Chiu, P.C.N.6
  • 50
    • 84864128566 scopus 로고    scopus 로고
    • Fully automatable two-dimensional hydrophilic interaction liquid chromatography-reversed phase liquid chromatography with online tandem mass spectrometry for shotgun proteomics
    • Zhao Y., Kong R.P.W., Li G.H., Lam M.P.Y., Law C.H., Lee S.M.Y., et al. Fully automatable two-dimensional hydrophilic interaction liquid chromatography-reversed phase liquid chromatography with online tandem mass spectrometry for shotgun proteomics. J Sep Sci 2012, 35:1755-1763.
    • (2012) J Sep Sci , vol.35 , pp. 1755-1763
    • Zhao, Y.1    Kong, R.P.W.2    Li, G.H.3    Lam, M.P.Y.4    Law, C.H.5    Lee, S.M.Y.6
  • 51
    • 84864827587 scopus 로고    scopus 로고
    • Quantitative Proteomics Targeting Classes of Motif-containing Peptides Using Immunoaffinity-based Mass Spectrometry
    • Olsson N., James P., Borrebaeck C.A.K., Wingren C. Quantitative Proteomics Targeting Classes of Motif-containing Peptides Using Immunoaffinity-based Mass Spectrometry. Mol Cell Proteomics 2012, 11:342-354.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 342-354
    • Olsson, N.1    James, P.2    Borrebaeck, C.A.K.3    Wingren, C.4
  • 52
    • 84870694137 scopus 로고    scopus 로고
    • High-definition de novo sequencing of crustacean hyperglycemic hormone (CHH)-family neuropeptides
    • Jia C.X., Hui L.M., Cao W.F., Lietz C.B., Jiang X.Y., Chen R.B., et al. High-definition de novo sequencing of crustacean hyperglycemic hormone (CHH)-family neuropeptides. Mol Cell Proteomics 2012, 11:1951-1964.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1951-1964
    • Jia, C.X.1    Hui, L.M.2    Cao, W.F.3    Lietz, C.B.4    Jiang, X.Y.5    Chen, R.B.6
  • 53
    • 33644879722 scopus 로고    scopus 로고
    • Peptidomics: identification and quantification of endogenous peptides in neuroendocrine tissues
    • Fricker L.D., Lim J.Y., Pan H., Che F.Y. Peptidomics: identification and quantification of endogenous peptides in neuroendocrine tissues. Mass Spectrom Rev 2006, 25:327-344.
    • (2006) Mass Spectrom Rev , vol.25 , pp. 327-344
    • Fricker, L.D.1    Lim, J.Y.2    Pan, H.3    Che, F.Y.4
  • 54
    • 0034772463 scopus 로고    scopus 로고
    • Analysis of cellular release using capillary electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry
    • Rubakhin S.S., Page J.S., Monroe B.R., Sweedler J.V. Analysis of cellular release using capillary electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 2001, 22:3752-3758.
    • (2001) Electrophoresis , vol.22 , pp. 3752-3758
    • Rubakhin, S.S.1    Page, J.S.2    Monroe, B.R.3    Sweedler, J.V.4
  • 55
    • 0142179225 scopus 로고    scopus 로고
    • Mass spectrometric investigation of the neuropeptide complement and release in the pericardial organs of the crab, Cancer borealis
    • Li L., Kelley W.P., Billimoria C.P., Christie A.E., Pulver S.R., Sweedler J.V., et al. Mass spectrometric investigation of the neuropeptide complement and release in the pericardial organs of the crab, Cancer borealis. J Neurochem 2003, 87:642-656.
    • (2003) J Neurochem , vol.87 , pp. 642-656
    • Li, L.1    Kelley, W.P.2    Billimoria, C.P.3    Christie, A.E.4    Pulver, S.R.5    Sweedler, J.V.6
  • 56
    • 25644446865 scopus 로고    scopus 로고
    • Profiling of neuropeptides released at the stomatogastric ganglion of the crab, Cancer borealis with mass spectrometry
    • Billimoria C.P., Li L., Marder E. Profiling of neuropeptides released at the stomatogastric ganglion of the crab, Cancer borealis with mass spectrometry. J Neurochem 2005, 95:191-199.
    • (2005) J Neurochem , vol.95 , pp. 191-199
    • Billimoria, C.P.1    Li, L.2    Marder, E.3
  • 57
    • 84862211299 scopus 로고    scopus 로고
    • Label-free quantitation of peptide release from neurons in a microfluidic device with mass spectrometry imaging
    • Zhong M., Lee C.Y., Croushore C.A., Sweedler J.V. Label-free quantitation of peptide release from neurons in a microfluidic device with mass spectrometry imaging. Lab Chip 2012, 12:2037-2045.
    • (2012) Lab Chip , vol.12 , pp. 2037-2045
    • Zhong, M.1    Lee, C.Y.2    Croushore, C.A.3    Sweedler, J.V.4
  • 58
    • 25844469965 scopus 로고    scopus 로고
    • Identification and characterization of a tachykinin-containing neuroendocrine organ in the commissural ganglion of the crab Cancer productus
    • Messinger D.I., Kutz K.K., Le T., Verley D.R., Hsu Y.W., Ngo C.T., et al. Identification and characterization of a tachykinin-containing neuroendocrine organ in the commissural ganglion of the crab Cancer productus. J Exp Biol 2005, 208:3303-3319.
    • (2005) J Exp Biol , vol.208 , pp. 3303-3319
    • Messinger, D.I.1    Kutz, K.K.2    Le, T.3    Verley, D.R.4    Hsu, Y.W.5    Ngo, C.T.6
  • 59
    • 33947423386 scopus 로고    scopus 로고
    • Midgut epithelial endocrine cells are a rich source of the neuropeptides APSGFLGMRamide (Cancer borealis tachykinin-related peptide Ia) and GYRKPPFNGSIFamide (Gly1-SIFamide) in the crabs Cancer borealis, Cancer magister and Cancer productus
    • Christie A.E., Kutz-Naber K.K., Stemmler E.A., Klein A., Messinger D.I., Goiney C.C., et al. Midgut epithelial endocrine cells are a rich source of the neuropeptides APSGFLGMRamide (Cancer borealis tachykinin-related peptide Ia) and GYRKPPFNGSIFamide (Gly1-SIFamide) in the crabs Cancer borealis, Cancer magister and Cancer productus. J Exp Biol 2007, 210:699-714.
    • (2007) J Exp Biol , vol.210 , pp. 699-714
    • Christie, A.E.1    Kutz-Naber, K.K.2    Stemmler, E.A.3    Klein, A.4    Messinger, D.I.5    Goiney, C.C.6
  • 60
    • 33846287934 scopus 로고    scopus 로고
    • A simple purification protocol for the detection of peptide hormones in the hemolymph of individual insects by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Fastner S., Predel R., Kahnt J., Schachtner J., Wegener C. A simple purification protocol for the detection of peptide hormones in the hemolymph of individual insects by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 2007, 21:23-28.
    • (2007) Rapid Commun Mass Spectrom , vol.21 , pp. 23-28
    • Fastner, S.1    Predel, R.2    Kahnt, J.3    Schachtner, J.4    Wegener, C.5
  • 61
    • 33644670265 scopus 로고    scopus 로고
    • Hemolymph clotting in crustaceans: implications for neuropeptide extraction from invertebrate hemolymph
    • Kwok R., Tobe S.S. Hemolymph clotting in crustaceans: implications for neuropeptide extraction from invertebrate hemolymph. Peptides 2006, 27:590-596.
    • (2006) Peptides , vol.27 , pp. 590-596
    • Kwok, R.1    Tobe, S.S.2
  • 62
    • 84885003170 scopus 로고    scopus 로고
    • Identification and expression of two oxytocin/vasopressin-related peptides in the cuttlefish Sepia officinalis
    • Henry J., Cornet V., Bernay B., Zatylny-Gaudin C. Identification and expression of two oxytocin/vasopressin-related peptides in the cuttlefish Sepia officinalis. Peptides 2013, 46:159-166.
    • (2013) Peptides , vol.46 , pp. 159-166
    • Henry, J.1    Cornet, V.2    Bernay, B.3    Zatylny-Gaudin, C.4
  • 64
    • 0026574199 scopus 로고
    • Development of a sensitive and inexpensive micropush-pull technique for the continuous analysis of brain neurotransmitters and metabolites in vivo
    • Zhang X., Wulfert E., Hanin I. Development of a sensitive and inexpensive micropush-pull technique for the continuous analysis of brain neurotransmitters and metabolites in vivo. J Neurosci Methods 1992, 42:139-147.
    • (1992) J Neurosci Methods , vol.42 , pp. 139-147
    • Zhang, X.1    Wulfert, E.2    Hanin, I.3
  • 65
    • 0035169117 scopus 로고    scopus 로고
    • A novel transverse push-pull microprobe: in vitro characterization and in vivo demonstration of the enzymatic production of adenosine in the spinal cord dorsal horn
    • Patterson S.L., Sluka K.A., Arnold M.A. A novel transverse push-pull microprobe: in vitro characterization and in vivo demonstration of the enzymatic production of adenosine in the spinal cord dorsal horn. J Neurochem 2001, 76:234-246.
    • (2001) J Neurochem , vol.76 , pp. 234-246
    • Patterson, S.L.1    Sluka, K.A.2    Arnold, M.A.3
  • 66
  • 67
    • 1842424647 scopus 로고    scopus 로고
    • The chemistry of thought: neurotransmitters in the brain
    • 121A-8A
    • Stuart J.N., Hummon A.B., Sweedler J.V. The chemistry of thought: neurotransmitters in the brain. Anal Chem 2004, 76. 121A-8A.
    • (2004) Anal Chem , vol.76
    • Stuart, J.N.1    Hummon, A.B.2    Sweedler, J.V.3
  • 68
    • 36849006523 scopus 로고    scopus 로고
    • In vivo monitoring of multiple trace metals in the brain extracellular fluid of anesthetized rats by microdialysis-membrane desalter-ICPMS
    • Chung Y.T., Ling Y.C., Yang C.S., Sun Y.C., Lee P.L., Lin C.Y., et al. In vivo monitoring of multiple trace metals in the brain extracellular fluid of anesthetized rats by microdialysis-membrane desalter-ICPMS. Anal Chem 2007, 79:8900-8910.
    • (2007) Anal Chem , vol.79 , pp. 8900-8910
    • Chung, Y.T.1    Ling, Y.C.2    Yang, C.S.3    Sun, Y.C.4    Lee, P.L.5    Lin, C.Y.6
  • 69
    • 0030955224 scopus 로고    scopus 로고
    • Brain microdialysis of GABA and glutamate: what does it signify
    • Timmerman W., Westerink B.H. Brain microdialysis of GABA and glutamate: what does it signify. Synapse 1997, 27:242-261.
    • (1997) Synapse , vol.27 , pp. 242-261
    • Timmerman, W.1    Westerink, B.H.2
  • 70
    • 84872541128 scopus 로고    scopus 로고
    • Mass spectrometric detection of neuropeptides using affinity-enhanced microdialysis with antibody-coated magnetic nanoparticles
    • Schmerberg C.M., Li L. Mass spectrometric detection of neuropeptides using affinity-enhanced microdialysis with antibody-coated magnetic nanoparticles. Anal Chem 2013, 85:915-922.
    • (2013) Anal Chem , vol.85 , pp. 915-922
    • Schmerberg, C.M.1    Li, L.2
  • 71
    • 0013974050 scopus 로고
    • The concentrations of free amino acids and other electrolytes in cerebrospinal fluid, in vivo dialysate of brain, and blood plasma of the dog
    • Bito L., Davson H., Levin E., Murray M., Snider N. The concentrations of free amino acids and other electrolytes in cerebrospinal fluid, in vivo dialysate of brain, and blood plasma of the dog. J Neurochem 1966, 13:1057-1067.
    • (1966) J Neurochem , vol.13 , pp. 1057-1067
    • Bito, L.1    Davson, H.2    Levin, E.3    Murray, M.4    Snider, N.5
  • 72
    • 44649087659 scopus 로고    scopus 로고
    • Application of long-term microdialysis in circadian rhythm research
    • Borjigin J., Liu T. Application of long-term microdialysis in circadian rhythm research. Pharmacol Biochem Behav 2008, 90:148-155.
    • (2008) Pharmacol Biochem Behav , vol.90 , pp. 148-155
    • Borjigin, J.1    Liu, T.2
  • 73
    • 0026577307 scopus 로고
    • Intravenous microdialysis sampling in awake, freely-moving rats
    • Telting-Diaz M., Scott D.O., Lunte C.E. Intravenous microdialysis sampling in awake, freely-moving rats. Anal Chem 1992, 64:806-810.
    • (1992) Anal Chem , vol.64 , pp. 806-810
    • Telting-Diaz, M.1    Scott, D.O.2    Lunte, C.E.3
  • 74
    • 83255194078 scopus 로고    scopus 로고
    • Increased in vivo release of neuropeptide S in the amygdala of freely moving rats after local depolarisation and emotional stress
    • Ebner K., Rjabokon A., Pape H.C., Singewald N. Increased in vivo release of neuropeptide S in the amygdala of freely moving rats after local depolarisation and emotional stress. Amino Acids 2011, 41:991-996.
    • (2011) Amino Acids , vol.41 , pp. 991-996
    • Ebner, K.1    Rjabokon, A.2    Pape, H.C.3    Singewald, N.4
  • 75
    • 0035497747 scopus 로고    scopus 로고
    • Capillary LC-MS2 at the attomole level for monitoring and discovering endogenous peptides in microdialysis samples collected in vivo
    • Haskins W.E., Wang Z., Watson C.J., Rostand R.R., Witowski S.R., Powell D.H., et al. Capillary LC-MS2 at the attomole level for monitoring and discovering endogenous peptides in microdialysis samples collected in vivo. Anal Chem 2001, 73:5005-5014.
    • (2001) Anal Chem , vol.73 , pp. 5005-5014
    • Haskins, W.E.1    Wang, Z.2    Watson, C.J.3    Rostand, R.R.4    Witowski, S.R.5    Powell, D.H.6
  • 76
    • 0030222513 scopus 로고    scopus 로고
    • Quantitative in vivo monitoring of primary amines in rat caudate nucleus using microdialysis coupled by a flow-gated interface to capillary electrophoresis with laser-induced fluorescence detection
    • Lada M.W., Kennedy R.T. Quantitative in vivo monitoring of primary amines in rat caudate nucleus using microdialysis coupled by a flow-gated interface to capillary electrophoresis with laser-induced fluorescence detection. Anal Chem 1996, 68:2790-2797.
    • (1996) Anal Chem , vol.68 , pp. 2790-2797
    • Lada, M.W.1    Kennedy, R.T.2
  • 77
    • 60749121149 scopus 로고    scopus 로고
    • Quantitative microdialysis using modified ultraslow microdialysis: direct rapid and reliable determination of free brain concentrations with the MetaQuant technique
    • Cremers T.I., de Vries M.G., Huinink K.D., van Loon J.P., v d Hart M., Ebert B., et al. Quantitative microdialysis using modified ultraslow microdialysis: direct rapid and reliable determination of free brain concentrations with the MetaQuant technique. J Neurosci Methods 2009, 178:249-254.
    • (2009) J Neurosci Methods , vol.178 , pp. 249-254
    • Cremers, T.I.1    de Vries, M.G.2    Huinink, K.D.3    van Loon, J.P.4    van dan Hart, M.5    Ebert, B.6
  • 78
    • 77049128212 scopus 로고    scopus 로고
    • A high recovery microsampling device based on a microdialysis probe for peptide sampling
    • Roy M.C., Ikimura K., Nishino H., Naito T. A high recovery microsampling device based on a microdialysis probe for peptide sampling. Anal Biochem 2010, 399:305-307.
    • (2010) Anal Biochem , vol.399 , pp. 305-307
    • Roy, M.C.1    Ikimura, K.2    Nishino, H.3    Naito, T.4
  • 79
    • 44649157689 scopus 로고    scopus 로고
    • Microdialysis and the neurochemistry of addiction
    • Torregrossa M.M., Kalivas P.W. Microdialysis and the neurochemistry of addiction. Pharmacol Biochem Behav 2008, 90:261-272.
    • (2008) Pharmacol Biochem Behav , vol.90 , pp. 261-272
    • Torregrossa, M.M.1    Kalivas, P.W.2
  • 80
    • 33644945519 scopus 로고    scopus 로고
    • Microdialysis sampling of cytokines
    • Ao X., Stenken J.A. Microdialysis sampling of cytokines. Methods 2006, 38:331-341.
    • (2006) Methods , vol.38 , pp. 331-341
    • Ao, X.1    Stenken, J.A.2
  • 81
    • 33748207171 scopus 로고    scopus 로고
    • Natural and synthetic affinity agents as microdialysis sampling mass transport enhancers: current progress and future perspectives
    • Duo J., Fletcher H., Stenken J.A. Natural and synthetic affinity agents as microdialysis sampling mass transport enhancers: current progress and future perspectives. Biosens Bioelectron 2006, 22:449-457.
    • (2006) Biosens Bioelectron , vol.22 , pp. 449-457
    • Duo, J.1    Fletcher, H.2    Stenken, J.A.3
  • 82
    • 0025150819 scopus 로고
    • Microdialysis measurement of in vivo neuropeptide release
    • Kendrick K.M. Microdialysis measurement of in vivo neuropeptide release. J Neurosci Methods 1990, 34:35-46.
    • (1990) J Neurosci Methods , vol.34 , pp. 35-46
    • Kendrick, K.M.1
  • 83
    • 44649093249 scopus 로고    scopus 로고
    • Listening to neuropeptides by microdialysis: echoes and new sounds
    • Wotjak C.T., Landgraf R., Engelmann M. Listening to neuropeptides by microdialysis: echoes and new sounds. Pharmacol Biochem Behav 2008, 90:125-134.
    • (2008) Pharmacol Biochem Behav , vol.90 , pp. 125-134
    • Wotjak, C.T.1    Landgraf, R.2    Engelmann, M.3
  • 84
    • 81055157123 scopus 로고    scopus 로고
    • Antibody-enhanced microdialysis collection of CCL2 from rat brain
    • Herbaugh A.W., Stenken J.A. Antibody-enhanced microdialysis collection of CCL2 from rat brain. J Neurosci Methods 2011, 202:124-127.
    • (2011) J Neurosci Methods , vol.202 , pp. 124-127
    • Herbaugh, A.W.1    Stenken, J.A.2
  • 86
  • 87
    • 80955179989 scopus 로고    scopus 로고
    • Microdialysis and mass spectrometric monitoring of dopamine and enkephalins in the globus pallidus reveal reciprocal interactions that regulate movement
    • Mabrouk O.S., Li Q., Song P., Kennedy R.T. Microdialysis and mass spectrometric monitoring of dopamine and enkephalins in the globus pallidus reveal reciprocal interactions that regulate movement. J Neurochem 2011, 118:24-33.
    • (2011) J Neurochem , vol.118 , pp. 24-33
    • Mabrouk, O.S.1    Li, Q.2    Song, P.3    Kennedy, R.T.4
  • 88
    • 77953728878 scopus 로고    scopus 로고
    • Collection of nanoliter microdialysate fractions in plugs for off-line in vivo chemical monitoring with up to 2s temporal resolution
    • Wang M., Slaney T., Mabrouk O., Kennedy R.T. Collection of nanoliter microdialysate fractions in plugs for off-line in vivo chemical monitoring with up to 2s temporal resolution. J Neurosci Methods 2010, 190:39-48.
    • (2010) J Neurosci Methods , vol.190 , pp. 39-48
    • Wang, M.1    Slaney, T.2    Mabrouk, O.3    Kennedy, R.T.4
  • 89
    • 84862839009 scopus 로고    scopus 로고
    • Mass spectral charting of neuropeptidomic expression in the stomatogastric ganglion at multiple developmental stages of the lobster Homarus americanus
    • Jiang X.Y., Chen R.B., Wang J.H., Metzler A., Tlusty M., Li L.J. Mass spectral charting of neuropeptidomic expression in the stomatogastric ganglion at multiple developmental stages of the lobster Homarus americanus. ACS Chem Neurosci 2012, 3:439-450.
    • (2012) ACS Chem Neurosci , vol.3 , pp. 439-450
    • Jiang, X.Y.1    Chen, R.B.2    Wang, J.H.3    Metzler, A.4    Tlusty, M.5    Li, L.J.6
  • 90
    • 77951757997 scopus 로고    scopus 로고
    • Comparative Neuropeptidomic Analysis of Food Intake via a Multifaceted Mass Spectrometric Approach
    • Chen R.B., Hui L.M., Cape S.S., Wang J.H., Li L.J. Comparative Neuropeptidomic Analysis of Food Intake via a Multifaceted Mass Spectrometric Approach. ACS Chem Neurosci 2010, 1:204-214.
    • (2010) ACS Chem Neurosci , vol.1 , pp. 204-214
    • Chen, R.B.1    Hui, L.M.2    Cape, S.S.3    Wang, J.H.4    Li, L.J.5
  • 91
    • 79960502698 scopus 로고    scopus 로고
    • Distribution and physiological effects of B-type allatostatins (Myoinhibitory Peptides, MIPs) in the stomatogastric nervous system of the crab Cancer borealis
    • Szabo T.M., Chen R.B., Goeritz M.L., Maloney R.T., Tang L.S., Li L.J., et al. Distribution and physiological effects of B-type allatostatins (Myoinhibitory Peptides, MIPs) in the stomatogastric nervous system of the crab Cancer borealis. J Comp Neurol 2011, 519:2658-2676.
    • (2011) J Comp Neurol , vol.519 , pp. 2658-2676
    • Szabo, T.M.1    Chen, R.B.2    Goeritz, M.L.3    Maloney, R.T.4    Tang, L.S.5    Li, L.J.6
  • 92
    • 79959458959 scopus 로고    scopus 로고
    • The application of MALDI TOF MS in biopharmaceutical research
    • Kafka A.P., Kleffmann T., Rades T., McDowell A. The application of MALDI TOF MS in biopharmaceutical research. Int J Pharmaceut 2011, 417:70-82.
    • (2011) Int J Pharmaceut , vol.417 , pp. 70-82
    • Kafka, A.P.1    Kleffmann, T.2    Rades, T.3    McDowell, A.4
  • 94
    • 84867456874 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: a technique to access the information beyond the molecular weight of the analyte
    • Banerjee S., Mazumdar S. Electrospray ionization mass spectrometry: a technique to access the information beyond the molecular weight of the analyte. Int J Anal Chem 2012, 2012:282574.
    • (2012) Int J Anal Chem , vol.2012 , pp. 282574
    • Banerjee, S.1    Mazumdar, S.2
  • 95
    • 40449115854 scopus 로고    scopus 로고
    • The integrated approach of MS, hyphenated techniques and bioinformatics for neuropeptide analysis
    • Boonen K., Landuyt B., Baggerman G., Husson S.J., Huybrechts J., Schoofs L., et al. The integrated approach of MS, hyphenated techniques and bioinformatics for neuropeptide analysis. J Sep Sci 2008, 31:427-445.
    • (2008) J Sep Sci , vol.31 , pp. 427-445
    • Boonen, K.1    Landuyt, B.2    Baggerman, G.3    Husson, S.J.4    Huybrechts, J.5    Schoofs, L.6
  • 96
    • 1442324456 scopus 로고    scopus 로고
    • Influence of basic residue content on fragment ion peak intensities in low-energy - collision-induced dissociation spectra of peptides
    • Tabb D.L., Huang Y.Y., Wysocki V.H., Yates J.R. Influence of basic residue content on fragment ion peak intensities in low-energy - collision-induced dissociation spectra of peptides. Anal Chem 2004, 76:1243-1248.
    • (2004) Anal Chem , vol.76 , pp. 1243-1248
    • Tabb, D.L.1    Huang, Y.Y.2    Wysocki, V.H.3    Yates, J.R.4
  • 98
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka J.E.P., Coon J.J., Schroeder M.J., Shabanowitz J., Hunt D.F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci USA 2004, 101:9528-9533.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9528-9533
    • Syka, J.E.P.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 99
    • 79955831978 scopus 로고    scopus 로고
    • Improved Peptide Identification by Targeted Fragmentation Using CID, HCD and ETD on an LTQ-Orbitrap Velos
    • Frese C.K., Altelaar A.F.M., Hennrich M.L., Nolting D., Zeller M., Griep-Raming J., et al. Improved Peptide Identification by Targeted Fragmentation Using CID, HCD and ETD on an LTQ-Orbitrap Velos. J Proteome Res 2011, 10:2377-2388.
    • (2011) J Proteome Res , vol.10 , pp. 2377-2388
    • Frese, C.K.1    Altelaar, A.F.M.2    Hennrich, M.L.3    Nolting, D.4    Zeller, M.5    Griep-Raming, J.6
  • 100
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner J., Premsler T., Sickmann A. Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications. Proteomics 2008, 8:4466-4483.
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 101
    • 70649108890 scopus 로고    scopus 로고
    • De novo peptide sequencing by tandem MS using complementary CID and electron transfer dissociation
    • Bertsch A., Leinenbach A., Pervukhin A., Lubeck M., Hartmer R., Baessmann C., et al. De novo peptide sequencing by tandem MS using complementary CID and electron transfer dissociation. Electrophoresis 2009, 30:3736-3747.
    • (2009) Electrophoresis , vol.30 , pp. 3736-3747
    • Bertsch, A.1    Leinenbach, A.2    Pervukhin, A.3    Lubeck, M.4    Hartmer, R.5    Baessmann, C.6
  • 102
    • 69749124866 scopus 로고    scopus 로고
    • Comparison of CID versus ETD based MS/MS fragmentation for the analysis of protein ubiquitination
    • Sobott F., Watt S.J., Smith J., Edelmann M.J., Kramer H.B., Kessler B.M. Comparison of CID versus ETD based MS/MS fragmentation for the analysis of protein ubiquitination. J Am Soc Mass Spectrom 2009, 20:1652-1659.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 1652-1659
    • Sobott, F.1    Watt, S.J.2    Smith, J.3    Edelmann, M.J.4    Kramer, H.B.5    Kessler, B.M.6
  • 103
    • 84872716508 scopus 로고    scopus 로고
    • Cell fate conversion: direct induction of hepatocyte-like cells from fibroblasts
    • Ji S., Zhang L., Hui L. Cell fate conversion: direct induction of hepatocyte-like cells from fibroblasts. J Cell Biochem 2013, 114:256-265.
    • (2013) J Cell Biochem , vol.114 , pp. 256-265
    • Ji, S.1    Zhang, L.2    Hui, L.3
  • 104
    • 66749086310 scopus 로고    scopus 로고
    • Expanding the crustacean neuropeptidome using a multifaceted mass spectrometric approach
    • Ma M.M., Wang J.H., Chen R.B., Li L.J. Expanding the crustacean neuropeptidome using a multifaceted mass spectrometric approach. J Proteome Res 2009, 8:2426-2437.
    • (2009) J Proteome Res , vol.8 , pp. 2426-2437
    • Ma, M.M.1    Wang, J.H.2    Chen, R.B.3    Li, L.J.4
  • 105
    • 67849128540 scopus 로고    scopus 로고
    • Mass spectrometric characterization and physiological actions of novel crustacean C-type allatostatins
    • Ma M.M., Szabo T.M., Jia C.X., Marder E., Li L.J. Mass spectrometric characterization and physiological actions of novel crustacean C-type allatostatins. Peptides 2009, 30:1660-1668.
    • (2009) Peptides , vol.30 , pp. 1660-1668
    • Ma, M.M.1    Szabo, T.M.2    Jia, C.X.3    Marder, E.4    Li, L.J.5
  • 106
    • 84865737357 scopus 로고    scopus 로고
    • Peptide identification by tandem mass spectrometry with alternate fragmentation modes
    • Guthals A., Bandeira N. Peptide identification by tandem mass spectrometry with alternate fragmentation modes. Mol Cell Proteomics 2012, 11:550-557.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 550-557
    • Guthals, A.1    Bandeira, N.2
  • 107
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • Swaney D.L., McAlister G.C., Coon J.J. Decision tree-driven tandem mass spectrometry for shotgun proteomics. Nat Methods 2008, 5:959-964.
    • (2008) Nat Methods , vol.5 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 108
    • 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
    • Hsu Y.W.A., Messinger D.I., Chung J.S., Webster S.G., de la Iglesia H.O., Christie A.E. 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 2006, 209:3241-3256.
    • (2006) J Exp Biol , vol.209 , pp. 3241-3256
    • Hsu, Y.W.A.1    Messinger, D.I.2    Chung, J.S.3    Webster, S.G.4    de la Iglesia, H.O.5    Christie, A.E.6
  • 109
    • 84855224608 scopus 로고    scopus 로고
    • The CHH-superfamily of multifunctional peptide hormones controlling crustacean metabolism, osmoregulation, moulting, and reproduction
    • Webster S.G., Keller R., Dircksen H. The CHH-superfamily of multifunctional peptide hormones controlling crustacean metabolism, osmoregulation, moulting, and reproduction. Gen Comp Endocrinol 2012, 175:217-233.
    • (2012) Gen Comp Endocrinol , vol.175 , pp. 217-233
    • Webster, S.G.1    Keller, R.2    Dircksen, H.3
  • 110
    • 0033168282 scopus 로고    scopus 로고
    • Purification and characterization of an isoform of crustacean hyperglycemic hormone from the eyestalk of Macrobrachium rosenbergii
    • Sithigorngul W., Jaideechoey S., Saraithongkum W., Longyant S., Sithigorngul P. Purification and characterization of an isoform of crustacean hyperglycemic hormone from the eyestalk of Macrobrachium rosenbergii. J Exp Zool 1999, 284:217-224.
    • (1999) J Exp Zool , vol.284 , pp. 217-224
    • Sithigorngul, W.1    Jaideechoey, S.2    Saraithongkum, W.3    Longyant, S.4    Sithigorngul, P.5
  • 111
    • 0036161198 scopus 로고    scopus 로고
    • Structure and phylogeny of the crustacean hyperglycemic hormone and its precursor from a hydrothermal vent crustacean: the crab Bythograea thermydron
    • Toullec J.Y., Vinh J., Le Caer J.P., Shillito B., Soyez D. Structure and phylogeny of the crustacean hyperglycemic hormone and its precursor from a hydrothermal vent crustacean: the crab Bythograea thermydron. Peptides 2002, 23:31-42.
    • (2002) Peptides , vol.23 , pp. 31-42
    • Toullec, J.Y.1    Vinh, J.2    Le Caer, J.P.3    Shillito, B.4    Soyez, D.5
  • 112
    • 25844519417 scopus 로고    scopus 로고
    • Mass spectrometric characterization of crustacean hyperglycemic hormone precursor-related peptides (CPRPs) from the sinus gland of the crab, Cancer productus
    • Fu Q., Christie A.E., Li L.J. Mass spectrometric characterization of crustacean hyperglycemic hormone precursor-related peptides (CPRPs) from the sinus gland of the crab, Cancer productus. Peptides 2005, 26:2137-2150.
    • (2005) Peptides , vol.26 , pp. 2137-2150
    • Fu, Q.1    Christie, A.E.2    Li, L.J.3
  • 113
    • 26844542155 scopus 로고    scopus 로고
    • Identification of neuropeptides from the decapod crustacean sinus glands using nanoscale liquid chromatography tandem mass spectrometry
    • Fu Q., Goy M.F., Li L.J. Identification of neuropeptides from the decapod crustacean sinus glands using nanoscale liquid chromatography tandem mass spectrometry. Biochem Biophys Res Commun 2005, 337:765-778.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 765-778
    • Fu, Q.1    Goy, M.F.2    Li, L.J.3
  • 114
    • 14844331822 scopus 로고    scopus 로고
    • Beyond quantitative proteomics: signal enhancement of the a(1) ion as a mass tag for peptide sequencing using dimethyl labeling
    • Hsu J.L., Huang S.Y., Shiea J.T., Huang W.Y., Chen S.H. Beyond quantitative proteomics: signal enhancement of the a(1) ion as a mass tag for peptide sequencing using dimethyl labeling. J Proteome Res 2005, 4:101-108.
    • (2005) J Proteome Res , vol.4 , pp. 101-108
    • Hsu, J.L.1    Huang, S.Y.2    Shiea, J.T.3    Huang, W.Y.4    Chen, S.H.5
  • 115
    • 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
    • Fu Q., Li L.J. 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 2005, 77:7783-7795.
    • (2005) Anal Chem , vol.77 , pp. 7783-7795
    • Fu, Q.1    Li, L.J.2
  • 116
    • 63449100532 scopus 로고    scopus 로고
    • Characterization of the Carcinus maenas neuropeptidome by mass spectrometry and functional genomics
    • Ma M.M., Bors E.K., Dickinson E.S., Kwiatkowski M.A., Sousa G.L., Henry R.P., et al. Characterization of the Carcinus maenas neuropeptidome by mass spectrometry and functional genomics. Gen Comp Endocrinol 2009, 161:320-334.
    • (2009) Gen Comp Endocrinol , vol.161 , pp. 320-334
    • Ma, M.M.1    Bors, E.K.2    Dickinson, E.S.3    Kwiatkowski, M.A.4    Sousa, G.L.5    Henry, R.P.6
  • 117
    • 77950398579 scopus 로고    scopus 로고
    • N,N-Dimethyl leucines as novel isobaric tandem mass tags for quantitative proteomics and peptidomics
    • Xiang F., Ye H., Chen R.B., Fu Q., Li L.J. N,N-Dimethyl leucines as novel isobaric tandem mass tags for quantitative proteomics and peptidomics. Anal Chem 2010, 82:2817-2825.
    • (2010) Anal Chem , vol.82 , pp. 2817-2825
    • Xiang, F.1    Ye, H.2    Chen, R.B.3    Fu, Q.4    Li, L.J.5
  • 118
    • 77953540114 scopus 로고    scopus 로고
    • Combining capillary electrophoresis matrix-assisted laser desorption/ionization mass spectrometry and stable isotopic labeling techniques for comparative crustacean peptidomics
    • Wang J.H., Zhang Y.Z., Xiang F., Zhang Z.C., Li L.J. Combining capillary electrophoresis matrix-assisted laser desorption/ionization mass spectrometry and stable isotopic labeling techniques for comparative crustacean peptidomics. J Chromatogr A 2010, 1217:4463-4470.
    • (2010) J Chromatogr A , vol.1217 , pp. 4463-4470
    • Wang, J.H.1    Zhang, Y.Z.2    Xiang, F.3    Zhang, Z.C.4    Li, L.J.5
  • 119
    • 4644314911 scopus 로고
    • Preferential fragmentation of protonated gas-phase peptide ions adjacent to acidic amino-acid-residues
    • Qin J., Chait B.T. Preferential fragmentation of protonated gas-phase peptide ions adjacent to acidic amino-acid-residues. J Am Chem Soc 1995, 117:5411-5412.
    • (1995) J Am Chem Soc , vol.117 , pp. 5411-5412
    • Qin, J.1    Chait, B.T.2
  • 120
    • 0036636707 scopus 로고    scopus 로고
    • Sequence dependent fragmentation of peptides generated by MALDI quadrupole time-of-flight (MALDI Q-TOF) mass spectrometry and its implications for protein identification
    • Wattenberg A., Organ A.J., Schneider K., Tyldesley R., Bordoli R., Bateman R.H. Sequence dependent fragmentation of peptides generated by MALDI quadrupole time-of-flight (MALDI Q-TOF) mass spectrometry and its implications for protein identification. J Am Soc Mass Spectrom 2002, 13:772-783.
    • (2002) J Am Soc Mass Spectrom , vol.13 , pp. 772-783
    • Wattenberg, A.1    Organ, A.J.2    Schneider, K.3    Tyldesley, R.4    Bordoli, R.5    Bateman, R.H.6
  • 121
    • 33846206036 scopus 로고    scopus 로고
    • Methyl esterification assisted MALDI FTMS characterization of the orcokinin neuropeptide family
    • Ma M.M., Kutz-Naber K.K., Li L.J. Methyl esterification assisted MALDI FTMS characterization of the orcokinin neuropeptide family. Anal Chem 2007, 79:673-681.
    • (2007) Anal Chem , vol.79 , pp. 673-681
    • Ma, M.M.1    Kutz-Naber, K.K.2    Li, L.J.3
  • 122
    • 79954429035 scopus 로고    scopus 로고
    • Improving peptide fragmentation by N-terminal derivatization with high proton affinity
    • Miyashita M., Hanai Y., Awane H., Yoshikawa T., Miyagawa H. Improving peptide fragmentation by N-terminal derivatization with high proton affinity. Rapid Commun Mass Spectrom 2011, 25:1130-1140.
    • (2011) Rapid Commun Mass Spectrom , vol.25 , pp. 1130-1140
    • Miyashita, M.1    Hanai, Y.2    Awane, H.3    Yoshikawa, T.4    Miyagawa, H.5
  • 123
    • 70349102102 scopus 로고    scopus 로고
    • Effect of chemical modifications on peptide fragmentation behavior upon electron transfer induced dissociation
    • Hennrich M.L., Boersema P.J., van den Toorn H., Mischerikow N., Heck A.J.R., Mohammed S. Effect of chemical modifications on peptide fragmentation behavior upon electron transfer induced dissociation. Anal Chem 2009, 81:7814-7822.
    • (2009) Anal Chem , vol.81 , pp. 7814-7822
    • Hennrich, M.L.1    Boersema, P.J.2    van den Toorn, H.3    Mischerikow, N.4    Heck, A.J.R.5    Mohammed, S.6
  • 124
    • 84885634003 scopus 로고    scopus 로고
    • Chemical derivatization of peptide carboxyl groups for highly efficient electron transfer dissociation
    • Frey B.L., Ladror D.T., Sondalle S.B., Krusemark C.J., Jue A.L., Coon J.J., et al. Chemical derivatization of peptide carboxyl groups for highly efficient electron transfer dissociation. J Am Soc Mass Spectrom 2013, 24:1710-1721.
    • (2013) J Am Soc Mass Spectrom , vol.24 , pp. 1710-1721
    • Frey, B.L.1    Ladror, D.T.2    Sondalle, S.B.3    Krusemark, C.J.4    Jue, A.L.5    Coon, J.J.6
  • 125
    • 80054063140 scopus 로고    scopus 로고
    • C-terminal de novo sequencing of peptides using oxazolone-based derivatization with bromine signature
    • Kim J.S., Shin M., Song J.S., An S., Kim H.J. C-terminal de novo sequencing of peptides using oxazolone-based derivatization with bromine signature. Anal Biochem 2011, 419:211-216.
    • (2011) Anal Biochem , vol.419 , pp. 211-216
    • Kim, J.S.1    Shin, M.2    Song, J.S.3    An, S.4    Kim, H.J.5
  • 126
    • 0036828610 scopus 로고    scopus 로고
    • Searching sequence databases via de novo peptide sequencing by tandem mass spectrometry
    • Johnson R.S., Taylor J.A. Searching sequence databases via de novo peptide sequencing by tandem mass spectrometry. Mol Biotechnol 2002, 22:301-315.
    • (2002) Mol Biotechnol , vol.22 , pp. 301-315
    • Johnson, R.S.1    Taylor, J.A.2
  • 127
    • 13844319908 scopus 로고    scopus 로고
    • PepNovo: de novo peptide sequencing via probabilistic network modeling
    • Frank A., Pevzner P. PepNovo: de novo peptide sequencing via probabilistic network modeling. Anal Chem 2005, 77:964-973.
    • (2005) Anal Chem , vol.77 , pp. 964-973
    • Frank, A.1    Pevzner, P.2
  • 128
    • 77952048255 scopus 로고    scopus 로고
    • PNovo: de novo peptide sequencing and identification using HCD spectra
    • Chi H., Sun R.X., Yang B., Song C.Q., Wang L.H., Liu C., et al. pNovo: de novo peptide sequencing and identification using HCD spectra. J Proteome Res 2010, 9:2713-2724.
    • (2010) J Proteome Res , vol.9 , pp. 2713-2724
    • Chi, H.1    Sun, R.X.2    Yang, B.3    Song, C.Q.4    Wang, L.H.5    Liu, C.6
  • 130
    • 77950521889 scopus 로고    scopus 로고
    • A high-throughput de novo sequencing approach for shotgun proteomics using high-resolution tandem mass spectrometry
    • Pan C., Park B.H., McDonald W.H., Carey P.A., Banfield J.F., VerBerkmoes N.C., et al. A high-throughput de novo sequencing approach for shotgun proteomics using high-resolution tandem mass spectrometry. BMC Bioinform 2010, 2010.
    • (2010) BMC Bioinform , pp. 2010
    • Pan, C.1    Park, B.H.2    McDonald, W.H.3    Carey, P.A.4    Banfield, J.F.5    VerBerkmoes, N.C.6
  • 131
    • 34447323085 scopus 로고    scopus 로고
    • MSNovo A dynamic programming algorithm for de novo peptide sequencing via tandem mass spectrometry
    • Mo L.J., Dutta D., Wan Y.H., Chen T. MSNovo A dynamic programming algorithm for de novo peptide sequencing via tandem mass spectrometry. Anal Chem 2007, 79:4870-4878.
    • (2007) Anal Chem , vol.79 , pp. 4870-4878
    • Mo, L.J.1    Dutta, D.2    Wan, Y.H.3    Chen, T.4
  • 132
    • 1942423061 scopus 로고    scopus 로고
    • High-throughput identification of proteins and unanticipated sequence modifications using a mass-based alignment algorithm for MS/MS de novo sequencing results
    • Searle B.C., Dasari S., Turner M., Reddy A.P., Choi D.S., Wilmarth P.A., et al. High-throughput identification of proteins and unanticipated sequence modifications using a mass-based alignment algorithm for MS/MS de novo sequencing results. Anal Chem 2004, 76:2220-2230.
    • (2004) Anal Chem , vol.76 , pp. 2220-2230
    • Searle, B.C.1    Dasari, S.2    Turner, M.3    Reddy, A.P.4    Choi, D.S.5    Wilmarth, P.A.6
  • 133
    • 84856692718 scopus 로고    scopus 로고
    • De novo sequencing and homology searching
    • Ma B., Johnson R. De novo sequencing and homology searching. Mol Cell Proteomics 2012, 11.
    • (2012) Mol Cell Proteomics , vol.11
    • Ma, B.1    Johnson, R.2
  • 134
    • 51949104682 scopus 로고    scopus 로고
    • Peptides in the brain: mass spectrometry-based measurement approaches and challenges
    • Li L.J., Sweedler J.V. Peptides in the brain: mass spectrometry-based measurement approaches and challenges. Annu Rev Anal Chem 2008, 1:451-483.
    • (2008) Annu Rev Anal Chem , vol.1 , pp. 451-483
    • Li, L.J.1    Sweedler, J.V.2
  • 135
    • 58249122605 scopus 로고    scopus 로고
    • Molecular, mass spectral, and physiological analyses of orcokinins and orcokinin precursor-related peptides in the lobster Homarus americanus and the crayfish Procambarus clarkii
    • Dickinson P.S., Stemmler E.A., Barton E.E., Cashman C.R., Gardner N.P., Rus S., et al. Molecular, mass spectral, and physiological analyses of orcokinins and orcokinin precursor-related peptides in the lobster Homarus americanus and the crayfish Procambarus clarkii. Peptides 2009, 30:297-317.
    • (2009) Peptides , vol.30 , pp. 297-317
    • Dickinson, P.S.1    Stemmler, E.A.2    Barton, E.E.3    Cashman, C.R.4    Gardner, N.P.5    Rus, S.6
  • 136
    • 17844398252 scopus 로고    scopus 로고
    • Tissue profiling by mass spectrometry - a review of methodology and applications
    • Caldwell R.L., Caprioli R.M. Tissue profiling by mass spectrometry - a review of methodology and applications. Mol Cell Proteomics 2005, 4:394-401.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 394-401
    • Caldwell, R.L.1    Caprioli, R.M.2
  • 137
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS
    • Caprioli R.M., Farmer T.B., Gile J. Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal Chem 1997, 69:4751-4760.
    • (1997) Anal Chem , vol.69 , pp. 4751-4760
    • Caprioli, R.M.1    Farmer, T.B.2    Gile, J.3
  • 138
    • 0028500184 scopus 로고
    • Allatostatin peptides in the crab stomatogastric nervous system: inhibition of the pyloric motor pattern and distribution of allatostatin-like immunoreactivity
    • Skiebe P., Schneider H. Allatostatin peptides in the crab stomatogastric nervous system: inhibition of the pyloric motor pattern and distribution of allatostatin-like immunoreactivity. J Exp Biol 1994, 194:195-208.
    • (1994) J Exp Biol , vol.194 , pp. 195-208
    • Skiebe, P.1    Schneider, H.2
  • 139
    • 34247611483 scopus 로고    scopus 로고
    • Mass spectrometric characterization and physiological actions of VPNDWAHFRGSWamide, a novel B type allatostatin in the crab, Cancer borealis
    • Fu Q., Tang L.S., Marder E., Li L. Mass spectrometric characterization and physiological actions of VPNDWAHFRGSWamide, a novel B type allatostatin in the crab, Cancer borealis. J Neurochem 2007, 101:1099-1107.
    • (2007) J Neurochem , vol.101 , pp. 1099-1107
    • Fu, Q.1    Tang, L.S.2    Marder, E.3    Li, L.4
  • 140
    • 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., Prieto Conaway M.C., Mohtashemi I., Hui L., Viner R., et al. Mass spectral analysis of neuropeptide expression and distribution in the nervous system of the lobster Homarus americanus. J Proteome Res 2010, 9:818-832.
    • (2010) J Proteome Res , vol.9 , pp. 818-832
    • Chen, R.1    Jiang, X.2    Prieto Conaway, M.C.3    Mohtashemi, I.4    Hui, L.5    Viner, R.6
  • 141
    • 0347320650 scopus 로고    scopus 로고
    • Identification of GYRKPPFNGSIFamide (crustacean-SIFamide) in the crayfish Procambarus clarkii by topological mass spectrometry analysis
    • Yasuda A., Yasuda-Kamatani Y., Nozaki M., Nakajima T. Identification of GYRKPPFNGSIFamide (crustacean-SIFamide) in the crayfish Procambarus clarkii by topological mass spectrometry analysis. Gen Comp Endocrinol 2004, 135:391-400.
    • (2004) Gen Comp Endocrinol , vol.135 , pp. 391-400
    • Yasuda, A.1    Yasuda-Kamatani, Y.2    Nozaki, M.3    Nakajima, T.4
  • 142
    • 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., et al. Discovery and functional study of a novel crustacean tachykinin neuropeptide. Acs Chem Neurosci 2011, 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
  • 143
    • 79951746099 scopus 로고    scopus 로고
    • From pixel to voxel: a deeper view of biological tissue by 3D mass spectral imaging
    • Ye H., Greer T., Li L. From pixel to voxel: a deeper view of biological tissue by 3D mass spectral imaging. Bioanalysis 2011, 3:313-332.
    • (2011) Bioanalysis , vol.3 , pp. 313-332
    • Ye, H.1    Greer, T.2    Li, L.3
  • 144
    • 84877984031 scopus 로고    scopus 로고
    • Function-driven discovery of neuropeptides with mass spectrometry-based tools
    • Schmerberg C.M., Li L.J. Function-driven discovery of neuropeptides with mass spectrometry-based tools. Protein Peptide Lett 2013, 20:681-694.
    • (2013) Protein Peptide Lett , vol.20 , pp. 681-694
    • Schmerberg, C.M.1    Li, L.J.2
  • 145
    • 33646413906 scopus 로고    scopus 로고
    • Fragmentation of peptides with N-terminal dimethylation and imine/methylol adduction at the tryptophan side-chain
    • Fu Q., Li L. Fragmentation of peptides with N-terminal dimethylation and imine/methylol adduction at the tryptophan side-chain. J Am Soc Mass Spectrom 2006, 17:859-866.
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 859-866
    • Fu, Q.1    Li, L.2
  • 146
    • 84555220651 scopus 로고    scopus 로고
    • Discovery and functional study of a novel crustacean tachykinin neuropeptide
    • Hui L.M., Zhang Y.Z., Wang J.H., Cook A., Ye H., Nusbaum M.P., et al. Discovery and functional study of a novel crustacean tachykinin neuropeptide. ACS Chem Neurosci 2011, 2:711-722.
    • (2011) ACS Chem Neurosci , vol.2 , pp. 711-722
    • Hui, L.M.1    Zhang, Y.Z.2    Wang, J.H.3    Cook, A.4    Ye, H.5    Nusbaum, M.P.6
  • 147
    • 84885106989 scopus 로고    scopus 로고
    • Quantitative assessment of in-solution digestion efficiency identifies optimal protocols for unbiased protein analysis
    • Leon I.R., Schwammle V., Jensen O.N., Sprenger R.R. Quantitative assessment of in-solution digestion efficiency identifies optimal protocols for unbiased protein analysis. Mol Cell Proteomics 2013, 12:2992-3005.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 2992-3005
    • Leon, I.R.1    Schwammle, V.2    Jensen, O.N.3    Sprenger, R.R.4
  • 148
    • 84877905853 scopus 로고    scopus 로고
    • Quantitative label-free proteomics for discovery of biomarkers in cerebrospinal fluid: assessment of technical and inter-individual variation
    • Perrin R.J., Payton J.E., Malone J.P., Gilmore P., Davis A.E., Xiong C., et al. Quantitative label-free proteomics for discovery of biomarkers in cerebrospinal fluid: assessment of technical and inter-individual variation. PLoS ONE 2013, 8:e64314.
    • (2013) PLoS ONE , vol.8
    • Perrin, R.J.1    Payton, J.E.2    Malone, J.P.3    Gilmore, P.4    Davis, A.E.5    Xiong, C.6
  • 150
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters D.A., Washburn M.P., Yates J.R. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem 2001, 73:5683-5690.
    • (2001) Anal Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates, J.R.3
  • 151
    • 84873340560 scopus 로고    scopus 로고
    • Protein changes in immunodepleted cerebrospinal fluid from a transgenic mouse model of Alexander disease detected using mass spectrometry
    • Cunningham R., Jany P., Messing A., Li L. Protein changes in immunodepleted cerebrospinal fluid from a transgenic mouse model of Alexander disease detected using mass spectrometry. J Proteome Res 2013, 12:719-728.
    • (2013) J Proteome Res , vol.12 , pp. 719-728
    • Cunningham, R.1    Jany, P.2    Messing, A.3    Li, L.4
  • 152
    • 84881525417 scopus 로고    scopus 로고
    • Differential expression of proteins in naive and IL-2 stimulated primary human NK cells identified by global proteomic analysis
    • Ma D., Cao W., Kapur A., Felder M., Scarlett C.O., Patankar M.S., et al. Differential expression of proteins in naive and IL-2 stimulated primary human NK cells identified by global proteomic analysis. J Proteomics 2013, 91C:151-163.
    • (2013) J Proteomics , vol.91 , Issue.C , pp. 151-163
    • Ma, D.1    Cao, W.2    Kapur, A.3    Felder, M.4    Scarlett, C.O.5    Patankar, M.S.6
  • 153
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H., Sadygov R.G., Yates J.R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 2004, 76:4193-4201.
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 154
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 2002, 1:376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 157
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong S.E., Mann M. Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol 2005, 1:252-262.
    • (2005) Nat Chem Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 159
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S.P., Rist B., Gerber S.A., Turecek F., Gelb M.H., Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 1999, 17:994-999.
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 160
    • 0347334566 scopus 로고    scopus 로고
    • Mass spectrometric analysis of protein mixtures at low levels using cleavable 13C-isotope-coded affinity tag and multidimensional chromatography
    • Hansen K.C., Schmitt-Ulms G., Chalkley R.J., Hirsch J., Baldwin M.A., Burlingame A.L. Mass spectrometric analysis of protein mixtures at low levels using cleavable 13C-isotope-coded affinity tag and multidimensional chromatography. Mol Cell Proteomics 2003, 2:299-314.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 299-314
    • Hansen, K.C.1    Schmitt-Ulms, G.2    Chalkley, R.J.3    Hirsch, J.4    Baldwin, M.A.5    Burlingame, A.L.6
  • 161
    • 1042284932 scopus 로고    scopus 로고
    • Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: the yeast salinity stress response
    • Li J., Steen H., Gygi S.P. Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: the yeast salinity stress response. Mol Cell Proteomics 2003, 2:1198-1204.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1198-1204
    • Li, J.1    Steen, H.2    Gygi, S.P.3
  • 162
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross P.L., Huang Y.N., Marchese J.N., Williamson B., Parker K., Hattan S., et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 2004, 3:1154-1169.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4    Parker, K.5    Hattan, S.6
  • 163
    • 41949139372 scopus 로고    scopus 로고
    • Quantitative shotgun proteomics of enriched heterocysts from Nostoc sp. PCC 7120 using 8-plex isobaric peptide tags
    • Ow S.Y., Cardona T., Taton A., Magnuson A., Lindblad P., Stensjo K., et al. Quantitative shotgun proteomics of enriched heterocysts from Nostoc sp. PCC 7120 using 8-plex isobaric peptide tags. J Proteome Res 2008, 7:1615-1628.
    • (2008) J Proteome Res , vol.7 , pp. 1615-1628
    • Ow, S.Y.1    Cardona, T.2    Taton, A.3    Magnuson, A.4    Lindblad, P.5    Stensjo, K.6
  • 164
    • 43849113605 scopus 로고    scopus 로고
    • Eight-channel iTRAQ enables comparison of the activity of six leukemogenic tyrosine kinases
    • Pierce A., Unwin R.D., Evans C.A., Griffiths S., Carney L., Zhang L., et al. Eight-channel iTRAQ enables comparison of the activity of six leukemogenic tyrosine kinases. Mol Cell Proteomics 2008, 7:853-863.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 853-863
    • Pierce, A.1    Unwin, R.D.2    Evans, C.A.3    Griffiths, S.4    Carney, L.5    Zhang, L.6
  • 165
    • 84883813280 scopus 로고    scopus 로고
    • Hyperplex-MRM: a hybrid multiple reaction monitoring method using mTRAQ/iTRAQ labeling for multiplex absolute quantification of human colorectal cancer biomarker
    • Yin H.R., Zhang L., Xie L.Q., Huang L.Y., Xu Y., Cai S.J., et al. Hyperplex-MRM: a hybrid multiple reaction monitoring method using mTRAQ/iTRAQ labeling for multiplex absolute quantification of human colorectal cancer biomarker. J Proteome Res 2013, 12:3912-3919.
    • (2013) J Proteome Res , vol.12 , pp. 3912-3919
    • Yin, H.R.1    Zhang, L.2    Xie, L.Q.3    Huang, L.Y.4    Xu, Y.5    Cai, S.J.6
  • 166
    • 53049096977 scopus 로고    scopus 로고
    • Multiple reaction monitoring of mTRAQ-labeled peptides enables absolute quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissues
    • DeSouza L.V., Taylor A.M., Li W., Minkoff M.S., Romaschin A.D., Colgan T.J., et al. Multiple reaction monitoring of mTRAQ-labeled peptides enables absolute quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissues. J Proteome Res 2008, 7:3525-3534.
    • (2008) J Proteome Res , vol.7 , pp. 3525-3534
    • DeSouza, L.V.1    Taylor, A.M.2    Li, W.3    Minkoff, M.S.4    Romaschin, A.D.5    Colgan, T.J.6
  • 167
    • 84877114083 scopus 로고    scopus 로고
    • Quantitative analysis of the human AKR family members in cancer cell lines using the mTRAQ/MRM approach
    • Zhang S., Wen B., Zhou B., Yang L., Cha C., Xu S., et al. Quantitative analysis of the human AKR family members in cancer cell lines using the mTRAQ/MRM approach. J Proteome Res 2013, 12:2022-2033.
    • (2013) J Proteome Res , vol.12 , pp. 2022-2033
    • Zhang, S.1    Wen, B.2    Zhou, B.3    Yang, L.4    Cha, C.5    Xu, S.6
  • 169
    • 77951022016 scopus 로고    scopus 로고
    • A comparison of the accuracy of iTRAQ quantification by nLC-ESI MSMS and nLC-MALDI MSMS methods
    • Shirran S.L., Botting C.H. A comparison of the accuracy of iTRAQ quantification by nLC-ESI MSMS and nLC-MALDI MSMS methods. J Proteomics 2010, 73:1391-1403.
    • (2010) J Proteomics , vol.73 , pp. 1391-1403
    • Shirran, S.L.1    Botting, C.H.2
  • 170
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures: the good, the bad and the ugly
    • Ow S.Y., Salim M., Noirel J., Evans C., Rehman I., Wright P.C. iTRAQ underestimation in simple and complex mixtures: the good, the bad and the ugly. J Proteome Res 2009, 8:5347-5355.
    • (2009) J Proteome Res , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 171
    • 80155124832 scopus 로고    scopus 로고
    • MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
    • Ting L., Rad R., Gygi S.P., Haas W. MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nat Methods 2011, 8:937-940.
    • (2011) Nat Methods , vol.8 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.P.3    Haas, W.4
  • 172
    • 80155205237 scopus 로고    scopus 로고
    • Gas-phase purification enables accurate, multiplexed proteome quantification with isobaric tagging
    • Wenger C.D., Lee M.V., Hebert A.S., McAlister G.C., Phanstiel D.H., Westphall M.S., et al. Gas-phase purification enables accurate, multiplexed proteome quantification with isobaric tagging. Nat Methods 2011, 8:933-935.
    • (2011) Nat Methods , vol.8 , pp. 933-935
    • Wenger, C.D.1    Lee, M.V.2    Hebert, A.S.3    McAlister, G.C.4    Phanstiel, D.H.5    Westphall, M.S.6
  • 173
    • 84868542018 scopus 로고    scopus 로고
    • Accurate multiplexed proteomics at the MS2 level using the complement reporter ion cluster
    • Wuhr M., Haas W., McAlister G.C., Peshkin L., Rad R., Kirschner M.W., et al. Accurate multiplexed proteomics at the MS2 level using the complement reporter ion cluster. Anal Chem 2012, 84:9214-9221.
    • (2012) Anal Chem , vol.84 , pp. 9214-9221
    • Wuhr, M.1    Haas, W.2    McAlister, G.C.3    Peshkin, L.4    Rad, R.5    Kirschner, M.W.6
  • 176
    • 0023628165 scopus 로고
    • Determination of serum cortisol by thermospray liquid chromatography/mass spectrometry: comparison with gas chromatography/mass spectrometry
    • Gaskell S.J., Rollins K., Smith R.W., Parker C.E. Determination of serum cortisol by thermospray liquid chromatography/mass spectrometry: comparison with gas chromatography/mass spectrometry. Biomed Environ Mass Spectrom 1987, 14:717-722.
    • (1987) Biomed Environ Mass Spectrom , vol.14 , pp. 717-722
    • Gaskell, S.J.1    Rollins, K.2    Smith, R.W.3    Parker, C.E.4
  • 177
    • 0023443155 scopus 로고
    • Metabolic kinetics and quantitative analysis by isotope dilution thermospray LC/MS
    • Yergey A.L., Esteban N.V., Liberato D.J. Metabolic kinetics and quantitative analysis by isotope dilution thermospray LC/MS. Biomed Environ Mass Spectrom 1987, 14:623-625.
    • (1987) Biomed Environ Mass Spectrom , vol.14 , pp. 623-625
    • Yergey, A.L.1    Esteban, N.V.2    Liberato, D.J.3
  • 178
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber S.A., Rush J., Stemman O., Kirschner M.W., Gygi S.P. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 2003, 100:6940-6945.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 179
    • 84865725559 scopus 로고    scopus 로고
    • Absolute quantification of prion protein (90-231) using stable isotope-labeled chymotryptic peptide standards in a LC-MRM AQUA workflow
    • Sturm R., Sheynkman G., Booth C., Smith L.M., Pedersen J.A., Li L. Absolute quantification of prion protein (90-231) using stable isotope-labeled chymotryptic peptide standards in a LC-MRM AQUA workflow. J Am Soc Mass Spectrom 2012, 23:1522-1533.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 1522-1533
    • Sturm, R.1    Sheynkman, G.2    Booth, C.3    Smith, L.M.4    Pedersen, J.A.5    Li, L.6
  • 180
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick D.S., Gerber S.A., Gygi S.P. The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 2005, 35:265-273.
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 181
    • 84869233177 scopus 로고    scopus 로고
    • Parallel reaction monitoring for high resolution and high mass accuracy quantitative, targeted proteomics
    • Peterson A.C., Russell J.D., Bailey D.J., Westphall M.S., Coon J.J. Parallel reaction monitoring for high resolution and high mass accuracy quantitative, targeted proteomics. Mol Cell Proteomics 2012, 11:1475-1488.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1475-1488
    • Peterson, A.C.1    Russell, J.D.2    Bailey, D.J.3    Westphall, M.S.4    Coon, J.J.5
  • 184
    • 46749145331 scopus 로고    scopus 로고
    • Performance characteristics of an FT MS-based workflow for label-free differential MS analysis of human plasma: standards, reproducibility, targeted feature investigation, and application to a model of controlled myocardial infarction
    • Sutton J., Richmond T., Shi X., Athanas M., Ptak C., Gerszten R., et al. Performance characteristics of an FT MS-based workflow for label-free differential MS analysis of human plasma: standards, reproducibility, targeted feature investigation, and application to a model of controlled myocardial infarction. Proteomics Clin Appl 2008, 2:862-881.
    • (2008) Proteomics Clin Appl , vol.2 , pp. 862-881
    • Sutton, J.1    Richmond, T.2    Shi, X.3    Athanas, M.4    Ptak, C.5    Gerszten, R.6
  • 185
    • 34547746723 scopus 로고    scopus 로고
    • Reproducibility assessment of relative quantitation strategies for LC-MS based proteomics
    • Kim Y.J., Zhan P., Feild B., Ruben S.M., He T. Reproducibility assessment of relative quantitation strategies for LC-MS based proteomics. Anal Chem 2007, 79:5651-5658.
    • (2007) Anal Chem , vol.79 , pp. 5651-5658
    • Kim, Y.J.1    Zhan, P.2    Feild, B.3    Ruben, S.M.4    He, T.5
  • 186
    • 72449185502 scopus 로고    scopus 로고
    • Range charts for agreement in measurement comparison studies, with application to replicate mass spectrometry experiments
    • Koziol J.A., Feng A.C., Yu J., Griffin N.M., Schnitzer J.E. Range charts for agreement in measurement comparison studies, with application to replicate mass spectrometry experiments. J Proteomics Bioinform 2008, 1:287-292.
    • (2008) J Proteomics Bioinform , vol.1 , pp. 287-292
    • Koziol, J.A.1    Feng, A.C.2    Yu, J.3    Griffin, N.M.4    Schnitzer, J.E.5
  • 188
    • 34447513049 scopus 로고    scopus 로고
    • Identification and cardiotropic actions of sulfakinin peptides in the American lobster Homarus americanus
    • Dickinson P.S., Stevens J.S., Rus S., Brennan H.R., Goiney C.C., Smith C.M., et al. Identification and cardiotropic actions of sulfakinin peptides in the American lobster Homarus americanus. J Exp Biol 2007, 210:2278-2289.
    • (2007) J Exp Biol , vol.210 , pp. 2278-2289
    • Dickinson, P.S.1    Stevens, J.S.2    Rus, S.3    Brennan, H.R.4    Goiney, C.C.5    Smith, C.M.6
  • 189
    • 80053919693 scopus 로고    scopus 로고
    • Genomics, transcriptomics, and peptidomics of Daphnia pulex neuropeptides and protein hormones
    • Dircksen H., Neupert S., Predel R., Verleyen P., Huybrechts J., Strauss J., et al. Genomics, transcriptomics, and peptidomics of Daphnia pulex neuropeptides and protein hormones. J Proteome Res 2011, 10:4478-4504.
    • (2011) J Proteome Res , vol.10 , pp. 4478-4504
    • Dircksen, H.1    Neupert, S.2    Predel, R.3    Verleyen, P.4    Huybrechts, J.5    Strauss, J.6
  • 190
    • 0034050353 scopus 로고    scopus 로고
    • Identification of orcokinin gene-related peptides in the brain of the crayfish Procambarus clarkii by the combination of MALDI-TOF and on-line capillary HPLC/Q-Tof mass spectrometries and molecular cloning
    • Yasuda-Kamatani Y., Yasuda A. Identification of orcokinin gene-related peptides in the brain of the crayfish Procambarus clarkii by the combination of MALDI-TOF and on-line capillary HPLC/Q-Tof mass spectrometries and molecular cloning. Gen Comp Endocrinol 2000, 118:161-172.
    • (2000) Gen Comp Endocrinol , vol.118 , pp. 161-172
    • Yasuda-Kamatani, Y.1    Yasuda, A.2
  • 191
    • 84858342301 scopus 로고    scopus 로고
    • Visualization of neuropeptides in paraffin-embedded tissue sections of the central nervous system in the decapod crustacean, Penaeus monodon, by imaging mass spectrometry
    • Chansela P., Goto-Inoue N., Zaima N., Sroyraya M., Sobhon P., Setou M. Visualization of neuropeptides in paraffin-embedded tissue sections of the central nervous system in the decapod crustacean, Penaeus monodon, by imaging mass spectrometry. Peptides 2012, 34:10-18.
    • (2012) Peptides , vol.34 , pp. 10-18
    • Chansela, P.1    Goto-Inoue, N.2    Zaima, N.3    Sroyraya, M.4    Sobhon, P.5    Setou, M.6
  • 192
    • 0033982729 scopus 로고    scopus 로고
    • Sulfakinin neuropeptides in a crustacean - isolation, identification and tissue localization in the tiger prawn Penaeus monodon
    • Johnsen A.H., Duve H., Davey M., Hall M., Thorpe A. Sulfakinin neuropeptides in a crustacean - isolation, identification and tissue localization in the tiger prawn Penaeus monodon. Eur J Biochem 2000, 267:1153-1160.
    • (2000) Eur J Biochem , vol.267 , pp. 1153-1160
    • Johnsen, A.H.1    Duve, H.2    Davey, M.3    Hall, M.4    Thorpe, A.5
  • 193
    • 0036849337 scopus 로고    scopus 로고
    • Four novel PYFs: members of NPY/PP peptide superfamily from the eyestalk of the giant tiger prawn Penaeus monodon
    • Sithigorngul P., Pupuem H., Krungkolsem C., Longyant S., Panchan N., Chaivisuthangkura P., et al. Four novel PYFs: members of NPY/PP peptide superfamily from the eyestalk of the giant tiger prawn Penaeus monodon. Peptides 2002, 23:1895-1906.
    • (2002) Peptides , vol.23 , pp. 1895-1906
    • Sithigorngul, P.1    Pupuem, H.2    Krungkolsem, C.3    Longyant, S.4    Panchan, N.5    Chaivisuthangkura, P.6
  • 195
    • 0037066056 scopus 로고    scopus 로고
    • Identification of orcokinins in single neurons in the stomatogastric nervous system of the crayfish, Cherax destructor
    • Skiebe P., Dreger M., Meseke M., Evers J.F., Hucho F. Identification of orcokinins in single neurons in the stomatogastric nervous system of the crayfish, Cherax destructor. J Comp Neurol 2002, 444:245-259.
    • (2002) J Comp Neurol , vol.444 , pp. 245-259
    • Skiebe, P.1    Dreger, M.2    Meseke, M.3    Evers, J.F.4    Hucho, F.5
  • 196
    • 25844435020 scopus 로고    scopus 로고
    • Hormone complement of the Cancer productus sinus gland and pericardial organ: an anatomical and mass spectrometric investigation
    • Fu Q., Kutz K.K., Schmidt J.J., Hsu Y.W.A., Messinger D.I., Cain S.D., et al. Hormone complement of the Cancer productus sinus gland and pericardial organ: an anatomical and mass spectrometric investigation. J Comp Neurol 2005, 493:607-626.
    • (2005) J Comp Neurol , vol.493 , pp. 607-626
    • Fu, Q.1    Kutz, K.K.2    Schmidt, J.J.3    Hsu, Y.W.A.4    Messinger, D.I.5    Cain, S.D.6


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