메뉴 건너뛰기




Volumn 18, Issue 4, 2000, Pages 151-160

Single-cell MALDI: A new tool for direct peptide profiling

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PROTEIN;

EID: 0034176654     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-7799(00)01427-X     Document Type: Short Survey
Times cited : (222)

References (69)
  • 1
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of proteome
    • Yates, J.R., III (1998) Mass spectrometry and the age of proteome. J. Mass Spectrom. 33, 1-19
    • (1998) J. Mass Spectrom. , vol.33 , pp. 1-19
    • Yates III, J.R.1
  • 2
    • 0032528716 scopus 로고    scopus 로고
    • Mass spectrometry
    • Burlingame, A.L. et al. (1998) Mass spectrometry. Anal. Chem. 70, 647R-716R
    • (1998) Anal. Chem. , vol.70
    • Burlingame, A.L.1
  • 3
    • 0032723731 scopus 로고    scopus 로고
    • Assaying neurotransmitters in and around single neurons with information-rich detectors
    • Dahlgren, R. et al. (1999) Assaying neurotransmitters in and around single neurons with information-rich detectors. Anal. Chim. Acta 400, 13-26
    • (1999) Anal. Chim. Acta , vol.400 , pp. 13-26
    • Dahlgren, R.1
  • 4
    • 0032063676 scopus 로고    scopus 로고
    • Separation and identification of peptides in single neurons by microcolumn liquid chromatography-matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and postsource decay analysis
    • Hsieh, S. et al. (1998) Separation and identification of peptides in single neurons by microcolumn liquid chromatography-matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and postsource decay analysis. Anal. Chem. 70, 1847-1852
    • (1998) Anal. Chem. , vol.70 , pp. 1847-1852
    • Hsieh, S.1
  • 5
    • 0024289037 scopus 로고
    • Laser desorption-ionization of proteins with molecular masses exceeding 10 000 daltons
    • Karas, M. and Hillenkamp, F. (1988) Laser desorption-ionization of proteins with molecular masses exceeding 10 000 daltons. Anal. Chem. 60, 2299-2301
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 6
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • Hillenkamp, F. et al. (1991) Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal. Chem. 63, 1193A-1203A
    • (1991) Anal. Chem. , vol.63
    • Hillenkamp, F.1
  • 7
    • 12044249497 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry
    • Karas, M. et al. (1991) Matrix-assisted laser desorption/ionization mass spectrometry Mass Spectrom. Rev. 10, 335-357
    • (1991) Mass Spectrom. Rev , vol.10 , pp. 335-357
    • Karas, M.1
  • 8
    • 0029146356 scopus 로고
    • Matrix-assisted laser desorption ionization (MALDI) mass spectrometry - A novel analytical tool in molecular biology and biotechnology
    • Kaufmann, R. (1995) Matrix-assisted laser desorption ionization (MALDI) mass spectrometry - a novel analytical tool in molecular biology and biotechnology. J. Biotechnol. 41, 155-175
    • (1995) J. Biotechnol. , vol.41 , pp. 155-175
    • Kaufmann, R.1
  • 9
    • 0028909999 scopus 로고
    • Desorption-ionization mass spectrometry
    • Busch, K.L. (1995) Desorption-ionization mass spectrometry. J. Mass Spectrom. 30, 232-240
    • (1995) J. Mass Spectrom. , vol.30 , pp. 232-240
    • Busch, K.L.1
  • 10
    • 33646320380 scopus 로고    scopus 로고
    • Ion sources and sample introduction
    • Academic Press
    • Siuzdak, G. (1996) Ion sources and sample introduction. In Mass Spectrometry for Biotechnology, pp. 4-31, Academic Press
    • (1996) Mass Spectrometry for Biotechnology , pp. 4-31
    • Siuzdak, G.1
  • 11
    • 0032471497 scopus 로고    scopus 로고
    • Characterisation of the covalent structure of proteins from biological material by MALDI mass spectrometry - Possibilities and limitations
    • Kussmann, M. and Roepstorff, P. (1998) Characterisation of the covalent structure of proteins from biological material by MALDI mass spectrometry - possibilities and limitations. Spectroscopy 14, 1-27
    • (1998) Spectroscopy , vol.14 , pp. 1-27
    • Kussmann, M.1    Roepstorff, P.2
  • 12
    • 0026954721 scopus 로고
    • Time-of-flight mass spectrometry for the structural analysis of biological molecules
    • Cotter, R.J. (1992) Time-of-flight mass spectrometry for the structural analysis of biological molecules. Anal. Chem. 64, 1027A-1039A
    • (1992) Anal. Chem. , vol.64
    • Cotter, R.J.1
  • 13
    • 0030658110 scopus 로고    scopus 로고
    • Post-source decay analysis in matrix-assisted laser desorption/ionization mass spectrometry of biomolecules
    • Spengler, B. (1997) Post-source decay analysis in matrix-assisted laser desorption/ionization mass spectrometry of biomolecules. J. Mass Spectrom. 32, 1019-1036
    • (1997) J. Mass Spectrom. , vol.32 , pp. 1019-1036
    • Spengler, B.1
  • 14
    • 0029397704 scopus 로고
    • Sequence-specific fragmentation of matrix-assisted laser-desorbed protein/peptide ions
    • Brown, R.S. and Lennon, J.J. (1995) Sequence-specific fragmentation of matrix-assisted laser-desorbed protein/peptide ions. Anal. Chem. 67, 3990-3999
    • (1995) Anal. Chem. , vol.67 , pp. 3990-3999
    • Brown, R.S.1    Lennon, J.J.2
  • 15
    • 0033231065 scopus 로고    scopus 로고
    • Egg-laying hormone peptides in the Aplysiidae family
    • Li, L. et al. (1999) Egg-laying hormone peptides in the Aplysiidae family. J. Exp. Biol. 202, 2961-2973
    • (1999) J. Exp. Biol. , vol.202 , pp. 2961-2973
    • Li, L.1
  • 16
    • 0032584145 scopus 로고    scopus 로고
    • Assaying for peptides in individual Aplysia neurons with mass spectrometry
    • Chiu, D.T. and Zare, R.N. (1998) Assaying for peptides in individual Aplysia neurons with mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 95, 3338-3340
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3338-3340
    • Chiu, D.T.1    Zare, R.N.2
  • 17
    • 15144343751 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry sample preparation techniques designed for various peptide and protein analytes
    • Kussmann, M. et al. (1997) Matrix-assisted laser desorption/ionization mass spectrometry sample preparation techniques designed for various peptide and protein analytes. J. Mass Spectrom. 32, 593-601
    • (1997) J. Mass Spectrom , vol.32 , pp. 593-601
    • Kussmann, M.1
  • 18
    • 0032880096 scopus 로고    scopus 로고
    • Identification of Enterobacteriaceae bacteria by direct matrix-assisted laser desorption/ionization mass spectrometric analysis of whole cells
    • Lynn, E.G. et al. (1999) Identification of Enterobacteriaceae bacteria by direct matrix-assisted laser desorption/ionization mass spectrometric analysis of whole cells. Rapid Commun. Mass Spectrom. 13, 2022-2027
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2022-2027
    • Lynn, E.G.1
  • 19
    • 0029777367 scopus 로고    scopus 로고
    • Rapid identification of intact whole bacteria based on spectral patterns using matrix-assisted laser desorption/ionization with time-of-flight mass spectrometry
    • Holland, R.D. et al. (1996) Rapid identification of intact whole bacteria based on spectral patterns using matrix-assisted laser desorption/ionization with time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 10, 1227-1232
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1227-1232
    • Holland, R.D.1
  • 20
    • 0030467690 scopus 로고    scopus 로고
    • Rapid identification of bacteria by direct matrix-assisted laser desorption/ionization mass spectrometric analysis of whole cells
    • Krishnamurthy, T. and Ross, P.L. (1996) Rapid identification of bacteria by direct matrix-assisted laser desorption/ionization mass spectrometric analysis of whole cells. Rapid Commun. Mass Spectrom. 10, 1992-1996
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1992-1996
    • Krishnamurthy, T.1    Ross, P.L.2
  • 21
    • 0031896562 scopus 로고    scopus 로고
    • Fingerprint matching of E. coli strains with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of whole cells using a modified correlation approach
    • Arnold, R.J. and Reilley, J.P. (1998) Fingerprint matching of E. coli strains with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of whole cells using a modified correlation approach. Rapid Commun. Mass Spectrom. 12, 630-636
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 630-636
    • Arnold, R.J.1    Reilley, J.P.2
  • 22
    • 0029718059 scopus 로고    scopus 로고
    • Detection of pathogenic and nonpathogenic bacteria by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Krishnamurthy, T. et al. (1996) Detection of pathogenic and nonpathogenic bacteria by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 10, 883-888
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 883-888
    • Krishnamurthy, T.1
  • 23
    • 0031855170 scopus 로고    scopus 로고
    • Rapid identification and speciation of Haemophilus bacteria by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Haag, A.M. et al. (1998) Rapid identification and speciation of Haemophilus bacteria by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 33, 750-756
    • (1998) J. Mass Spectrom. , vol.33 , pp. 750-756
    • Haag, A.M.1
  • 24
    • 0032851171 scopus 로고    scopus 로고
    • Rapid screening of protein profiles of human breast cancer cell lines using non-porous reversed-phase high performance liquid chromatography separation with matrix-assisted laser desorption/ionization time-of-flight mass spectral analysis
    • Chong, B.E. et al. (1999) Rapid screening of protein profiles of human breast cancer cell lines using non-porous reversed-phase high performance liquid chromatography separation with matrix-assisted laser desorption/ionization time-of-flight mass spectral analysis. Rapid Commun. Mass Spectrom. 13, 1808-1812
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 1808-1812
    • Chong, B.E.1
  • 25
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS
    • Caprioli, R.M. et al. (1997) Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal. Chem. 69, 4751-4760
    • (1997) Anal. Chem. , vol.69 , pp. 4751-4760
    • Caprioli, R.M.1
  • 26
    • 0033485653 scopus 로고    scopus 로고
    • Direct profiling of proteins in biological tissue sections by MALDI mass spectrometry
    • Chaurand, P. et al. (1999) Direct profiling of proteins in biological tissue sections by MALDI mass spectrometry. Anal. Chem. 71, 5263-5270
    • (1999) Anal. Chem. , vol.71 , pp. 5263-5270
    • Chaurand, P.1
  • 27
    • 0028009002 scopus 로고
    • Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption-ionization mass spectrometry of single neurons
    • Jiménez, C.R. et al. (1994) Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption-ionization mass spectrometry of single neurons. J. Neurochem. 62, 404-409
    • (1994) J. Neurochem. , vol.62 , pp. 404-409
    • Jiménez, C.R.1
  • 28
    • 0029851666 scopus 로고    scopus 로고
    • Excess salt removal with matrix rinsing: Direct peptide profiling of neurons from marine invertebrates using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Garden, R.W. et al. (1996) Excess salt removal with matrix rinsing: direct peptide profiling of neurons from marine invertebrates using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 31, 1126-1130
    • (1996) J. Mass Spectrom. , vol.31 , pp. 1126-1130
    • Garden, R.W.1
  • 29
    • 0031569338 scopus 로고    scopus 로고
    • Analysis of fructans from higher plants by matrix-assisted laser desorption/ionization mass spectrometry
    • Stahl, B. et al. (1997) Analysis of fructans from higher plants by matrix-assisted laser desorption/ionization mass spectrometry. Anal. Biochem. 246, 195-204
    • (1997) Anal. Biochem. , vol.246 , pp. 195-204
    • Stahl, B.1
  • 30
    • 0028348774 scopus 로고
    • Processing and targeting of a molluscan egg-laying peptide prohormone as revealed by mass spectrometric peptide fingerprinting and peptide sequencing
    • Li, K.W. et al. (1994) Processing and targeting of a molluscan egg-laying peptide prohormone as revealed by mass spectrometric peptide fingerprinting and peptide sequencing. Endocrinology 134, 1812-1819
    • (1994) Endocrinology , vol.134 , pp. 1812-1819
    • Li, K.W.1
  • 31
    • 84989092293 scopus 로고
    • Direct peptide profiling of single neurons by matrix-assisted laser desorption-ionization mass spectrometry
    • van Veelen, P.A. et al. (1993) Direct peptide profiling of single neurons by matrix-assisted laser desorption-ionization mass spectrometry. Org. Mass Spectrom. 28, 1542-1546
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1542-1546
    • Van Veelen, P.A.1
  • 32
    • 0038588683 scopus 로고    scopus 로고
    • Direct mass spectrometric peptide profiling and sequencing of single neurons reveals differential peptide patterns in a small neuronal network
    • Jiménez, C.R. et al. (1998) Direct mass spectrometric peptide profiling and sequencing of single neurons reveals differential peptide patterns in a small neuronal network. Biochemistry 37, 2070-2076
    • (1998) Biochemistry , vol.37 , pp. 2070-2076
    • Jiménez, C.R.1
  • 33
    • 0029776037 scopus 로고    scopus 로고
    • Myomodulin gene of Lymnaea: Structure, expression, and analysis of neuropeptides
    • Kellett, E. et al. (1996) Myomodulin gene of Lymnaea: structure, expression, and analysis of neuropeptides. J. Neurosci. 16, 4949-4957
    • (1996) J. Neurosci. , vol.16 , pp. 4949-4957
    • Kellett, E.1
  • 34
    • 0001181081 scopus 로고    scopus 로고
    • Structural elucidation of a peptide from a single neuron by matrix-assisted laser desorption/ionization employing a tandem double-focusing magnetic-orthogonal acceleration time-of-flight mass spectrometer
    • Li, K.W. et al. (1997) Structural elucidation of a peptide from a single neuron by matrix-assisted laser desorption/ionization employing a tandem double-focusing magnetic-orthogonal acceleration time-of-flight mass spectrometer. Anal. Chem. 69, 563-565
    • (1997) Anal. Chem. , vol.69 , pp. 563-565
    • Li, K.W.1
  • 35
    • 0030822139 scopus 로고    scopus 로고
    • Intracellular degradation of C-peptides in molluscan neurons producing insulin-related hormones
    • de With, N.D. et al. (1997) Intracellular degradation of C-peptides in molluscan neurons producing insulin-related hormones. Peptides 18, 765-770
    • (1997) Peptides , vol.18 , pp. 765-770
    • De With, N.D.1
  • 36
    • 0032466068 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time of flight mass spectrometric analysis of the pattern of peptide expression in single neurons resulting from alternative mRNA splicing of FMR Famide gene
    • Worster, B.M. et al. (1998) Matrix-assisted laser desorption/ionization time of flight mass spectrometric analysis of the pattern of peptide expression in single neurons resulting from alternative mRNA splicing of FMR Famide gene. Eur. J. Neurosci. 10, 3489-3507
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 3489-3507
    • Worster, B.M.1
  • 37
    • 0033010299 scopus 로고    scopus 로고
    • Small cardioactive peptide gene: Structure, expression and mass spectrometric analysis reveals a complex pattern of co-transmitters in a snail feeding neuron
    • Perry, S.J. et al. (1999) Small cardioactive peptide gene: structure, expression and mass spectrometric analysis reveals a complex pattern of co-transmitters in a snail feeding neuron. Eur. J. Neurosci. 11, 655-662
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 655-662
    • Perry, S.J.1
  • 38
    • 0031470980 scopus 로고    scopus 로고
    • Characterization of myomodulin-related peptides from the pulmonate snail Helix aspersa
    • Greenberg, M.J. et al. (1997) Characterization of myomodulin-related peptides from the pulmonate snail Helix aspersa. Peptides 18, 1099-1106
    • (1997) Peptides , vol.18 , pp. 1099-1106
    • Greenberg, M.J.1
  • 39
    • 0032584248 scopus 로고    scopus 로고
    • Proteolytic processing of the Aplysia egg-laying hormone prohormone
    • Garden, R.W. et al. (1998) Proteolytic processing of the Aplysia egg-laying hormone prohormone. Proc. Natl. Acad. Sci. U. S. A. 95, 3972-3977
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3972-3977
    • Garden, R.W.1
  • 40
    • 0033568850 scopus 로고    scopus 로고
    • Aplysia californica insulin: Prohormone processing, distribution, and relation to metabolism
    • Floyd, P.D. et al. (1999) Aplysia californica insulin: prohormone processing, distribution, and relation to metabolism. J. Neurosci. 19, 7732-7741
    • (1999) J. Neurosci. , vol.19 , pp. 7732-7741
    • Floyd, P.D.1
  • 41
    • 0031758717 scopus 로고    scopus 로고
    • Mass spectrometric survey of interganglionically transported peptides in Aplysia
    • Li, L. et al. (1998) Mass spectrometric survey of interganglionically transported peptides in Aplysia. Peptides 19, 1425-1433
    • (1998) Peptides , vol.19 , pp. 1425-1433
    • Li, L.1
  • 42
    • 0032924612 scopus 로고    scopus 로고
    • Formation of N-pyroglutamyl peptides from N-Glu and N-Gln precursors in Aplysia neurons
    • Garden, R.W. et al. (1999) Formation of N-pyroglutamyl peptides from N-Glu and N-Gln precursors in Aplysia neurons. J. Neurochem. 72, 676-681
    • (1999) J. Neurochem. , vol.72 , pp. 676-681
    • Garden, R.W.1
  • 43
    • 0033024521 scopus 로고    scopus 로고
    • Characterization of the Aplysia californica cerebral ganglion F cluster
    • Rubakhin, S.S. et al. (1999) Characterization of the Aplysia californica cerebral ganglion F cluster. J. Neurophysiol. 81, 1251-1260
    • (1999) J. Neurophysiol. , vol.81 , pp. 1251-1260
    • Rubakhin, S.S.1
  • 44
    • 0033232719 scopus 로고    scopus 로고
    • The Aplysia Mytilus inhibitory peptide-related peptides: Identification, cloning, processing, distribution, and action
    • Fujisawa, Y. et al. (1999) The Aplysia Mytilus inhibitory peptide-related peptides: identification, cloning, processing, distribution, and action. J. Neurosci. 19, 9618-9634
    • (1999) J. Neurosci. , vol.19 , pp. 9618-9634
    • Fujisawa, Y.1
  • 45
    • 0033572758 scopus 로고    scopus 로고
    • In situ sequencing of peptides from biological tissues and single cells using MALDI-PSD/CID analysis
    • Li, L. et al. (1999) In situ sequencing of peptides from biological tissues and single cells using MALDI-PSD/CID analysis. Anal. Chem. 71, 5451-5458
    • (1999) Anal. Chem. , vol.71 , pp. 5451-5458
    • Li, L.1
  • 46
    • 0033985441 scopus 로고    scopus 로고
    • Heterogeneity within MALDI samples as revealed by mass spectrometric imaging
    • Garden, R.W. and Sweedler, J.V. (2000) Heterogeneity within MALDI samples as revealed by mass spectrometric imaging. Anal. Chem. 72, 30-36
    • (2000) Anal. Chem. , vol.72 , pp. 30-36
    • Garden, R.W.1    Sweedler, J.V.2
  • 47
    • 0033967547 scopus 로고    scopus 로고
    • Measuring the peptides in individual organelles with mass spectrometry
    • Rubakhin, S.S. et al. (2000) Measuring the peptides in individual organelles with mass spectrometry. Nat. Biotechnol. 18, 172-175
    • (2000) Nat. Biotechnol. , vol.18 , pp. 172-175
    • Rubakhin, S.S.1
  • 48
    • 0032067863 scopus 로고    scopus 로고
    • Combination of peptide profiling by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and immunodetection on single glands or cells
    • Redeker, V. et al. (1998) Combination of peptide profiling by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and immunodetection on single glands or cells. Anal. Chem. 70, 1805-1811
    • (1998) Anal. Chem. , vol.70 , pp. 1805-1811
    • Redeker, V.1
  • 49
    • 0032524866 scopus 로고    scopus 로고
    • MALDI-TOF-MS for direct neuropeptide profiling of the insect corpus cardiacum
    • Verhaert, P. and de Loof, A. (1998) MALDI-TOF-MS for direct neuropeptide profiling of the insect corpus cardiacum. Ann. New York Acad. Sci. 839, 343-345
    • (1998) Ann. New York Acad. Sci. , vol.839 , pp. 343-345
    • Verhaert, P.1    De Loof, A.2
  • 50
    • 0034090219 scopus 로고    scopus 로고
    • Characterizing the Hez-PBAN gene products in neuronal clusters with immunocytochemistry and MALDI-MS
    • Ma, P.W.K. et al. (2000) Characterizing the Hez-PBAN gene products in neuronal clusters with immunocytochemistry and MALDI-MS. J. Insect Physiol. 46, 221-230
    • (2000) J. Insect Physiol. , vol.46 , pp. 221-230
    • Ma, P.W.K.1
  • 51
    • 0030033363 scopus 로고    scopus 로고
    • Identification of POMC processing products in single melanotrope cells by matrix-assisted laser desorption/ionization mass spectrometry
    • van Strien, F.J.C. et al. (1996) Identification of POMC processing products in single melanotrope cells by matrix-assisted laser desorption/ionization mass spectrometry. FEBS Lett. 379, 165-170
    • (1996) FEBS Lett , vol.379 , pp. 165-170
    • Van Strien, F.J.C.1
  • 52
    • 0033083315 scopus 로고    scopus 로고
    • Direct sequencing of neuropeptides in biological tissue by MALDI-PSD mass spectrometry
    • Jespersen, S. et al. (1999) Direct sequencing of neuropeptides in biological tissue by MALDI-PSD mass spectrometry. Anal. Chem. 71, 660-666
    • (1999) Anal. Chem. , vol.71 , pp. 660-666
    • Jespersen, S.1
  • 53
    • 0033525216 scopus 로고    scopus 로고
    • Analysis by mass spectrometry of POMC-derived peptides in amphibian melanotrope subpopulations
    • Vazquez-Martinez, R.M. et al. (1999) Analysis by mass spectrometry of POMC-derived peptides in amphibian melanotrope subpopulations. Life Sci. 64, 923-930
    • (1999) Life Sci , vol.64 , pp. 923-930
    • Vazquez-Martinez, R.M.1
  • 54
    • 12644256625 scopus 로고    scopus 로고
    • Pattern changes of pituitary peptides in rat after salt-loading as detected by means of direct, semiquantitative mass spectrometric profiling
    • Jiménez, C.R. et al. (1997) Pattern changes of pituitary peptides in rat after salt-loading as detected by means of direct, semiquantitative mass spectrometric profiling. Proc. Natl. Acad. Sci. U. S. A. 94, 9481-9486
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9481-9486
    • Jiménez, C.R.1
  • 55
    • 0031708544 scopus 로고    scopus 로고
    • Ultramicroanalysis of peptide profiles in biological samples using MALDI mass spectrometry
    • Jiménez, C.R. and Burlingame, A.L. (1998) Ultramicroanalysis of peptide profiles in biological samples using MALDI mass spectrometry. Exp. Nephrol. 6, 421-428
    • (1998) Exp. Nephrol. , vol.6 , pp. 421-428
    • Jiménez, C.R.1    Burlingame, A.L.2
  • 56
    • 0343852690 scopus 로고    scopus 로고
    • C-terminal truncation of thymosin beta10 by an intracellular protease and its influence on the interaction with G-actin studied by ultraflltration
    • Huff, T. et al. (1997) C-terminal truncation of thymosin beta10 by an intracellular protease and its influence on the interaction with G-actin studied by ultraflltration. FEBS Lett. 414, 39-44
    • (1997) FEBS Lett , vol.414 , pp. 39-44
    • Huff, T.1
  • 57
    • 0032549803 scopus 로고    scopus 로고
    • Substance P and related peptides in porcine cortex: Whole tissue and nuclear localization
    • Nilsson, C.L. et al (1998) Substance P and related peptides in porcine cortex: whole tissue and nuclear localization. J. Chromatogr. A 800, 21-27
    • (1998) J. Chromatogr. A , vol.800 , pp. 21-27
    • Nilsson, C.L.1
  • 59
    • 0001328391 scopus 로고
    • The peptidergic neuroendocrine control of egg-laying behavior in Aplysia and Lymnaea
    • Laufer, H. and Downer, R.G.H., eds, Alan R. Liss
    • Geraerts, W.P.M. et al. (1988) The peptidergic neuroendocrine control of egg-laying behavior in Aplysia and Lymnaea. In Endocrinology of Selected Invertebrate Types (Laufer, H. and Downer, R.G.H., eds), pp.141-231, Alan R. Liss
    • (1988) Endocrinology of Selected Invertebrate Types , pp. 141-231
    • Geraerts, W.P.M.1
  • 60
    • 0032535474 scopus 로고    scopus 로고
    • Nanoliter chemistry combined with mass spectrometry for peptide mapping of proteins from single mammalian cell lysates
    • Whittal, R.M. et al. (1998) Nanoliter chemistry combined with mass spectrometry for peptide mapping of proteins from single mammalian cell lysates. Anal. Chem. 70, 5344-5347
    • (1998) Anal. Chem. , vol.70 , pp. 5344-5347
    • Whittal, R.M.1
  • 61
    • 0029822412 scopus 로고    scopus 로고
    • Phosphopeptide analysis by matrix-assisted laser desorption time-of-flight mass spectrometry
    • Annan, R.S. and Carr, S.A. (1996) Phosphopeptide analysis by matrix-assisted laser desorption time-of-flight mass spectrometry. Anal. Chem. 68, 3413-3421
    • (1996) Anal. Chem. , vol.68 , pp. 3413-3421
    • Annan, R.S.1    Carr, S.A.2
  • 62
    • 0000833068 scopus 로고    scopus 로고
    • Enhancement of charge remote fragmentation in protonated peptides by high-energy CID MALDI-TOF MS using cold matrices
    • Stimson, E. et al. (1997) Enhancement of charge remote fragmentation in protonated peptides by high-energy CID MALDI-TOF MS using cold matrices. Int. J. Mass Spectrom. Ion Processes 169/170, 231-240
    • (1997) Int. J. Mass Spectrom. Ion Processes , vol.169-170 , pp. 231-240
    • Stimson, E.1
  • 63
    • 0031444782 scopus 로고    scopus 로고
    • Improving mass spectrometric sequencing of arginine-containing peptides by derivatization with acetylacetone
    • Dickler, S. et al. (1997) Improving mass spectrometric sequencing of arginine-containing peptides by derivatization with acetylacetone. J. Mass Spectrom. 32, 1337-1349
    • (1997) J. Mass Spectrom. , vol.32 , pp. 1337-1349
    • Dickler, S.1
  • 64
    • 0345040858 scopus 로고    scopus 로고
    • A strategy for rapid and efficient sequencing of Lys-C peptides by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry post-source decay
    • Pfeifer, T. et al. (1999) A strategy for rapid and efficient sequencing of Lys-C peptides by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry post-source decay. Rapid Commun. Mass Spectrom. 13, 362-369
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 362-369
    • Pfeifer, T.1
  • 65
    • 0033594994 scopus 로고    scopus 로고
    • A method for high-sensitivity peptide sequencing using postsource decay matrix-assisted laser desorption ionization mass spectrometry
    • Keough, T. et al. (1999) A method for high-sensitivity peptide sequencing using postsource decay matrix-assisted laser desorption ionization mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 96, 7131-7136
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7131-7136
    • Keough, T.1
  • 66
    • 0027656441 scopus 로고
    • Reproducibility and quantitation of matrix-assisted laser desorption ionization mass spectrometry: Effects of nitrocellulose on peptide ion yields
    • Preston, L.M. et al. (1993) Reproducibility and quantitation of matrix-assisted laser desorption ionization mass spectrometry: effects of nitrocellulose on peptide ion yields. Biol. Mass Spectrom. 22, 544-550
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 544-550
    • Preston, L.M.1
  • 67
    • 0028868280 scopus 로고
    • Application of the fast-evaporation sample preparation method for improving quantification of angiotensin II by matrix-assisted laser desorption/ionization
    • Nicola, A.J. et al. (1995) Application of the fast-evaporation sample preparation method for improving quantification of angiotensin II by matrix-assisted laser desorption/ionization. Rapid Commun. Mass Spectrom. 9, 1164-1171
    • (1995) Rapid Commun. Mass Spectrom. , vol.9 , pp. 1164-1171
    • Nicola, A.J.1
  • 68
    • 0033238005 scopus 로고    scopus 로고
    • Automated mass spectrometry imaging with a matrix-assisted laser desorption ionization time-of-flight instrument
    • Stoeckli, M. et al. (1999) Automated mass spectrometry imaging with a matrix-assisted laser desorption ionization time-of-flight instrument. J. Am. Soc. Mass Spectrom. 10, 67-71
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 67-71
    • Stoeckli, M.1
  • 69
    • 0345188660 scopus 로고    scopus 로고
    • Desorption-ionization mass spectrometry on porous silicon
    • Wei, J. et al. (1999) Desorption-ionization mass spectrometry on porous silicon. Nature 399, 243-246
    • (1999) Nature , vol.399 , pp. 243-246
    • Wei, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.