메뉴 건너뛰기




Volumn 172, Issue , 2007, Pages 269-293

Single-cell measurements with mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords


EID: 34547420657     PISSN: 00692883     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Review
Times cited : (5)

References (107)
  • 2
    • 0032934730 scopus 로고    scopus 로고
    • Cells on the target matrix-assisted laser-desorption/ionization time-of-flight mass-spectrometric analysis of mammalian cells grown on the target
    • Bergquist, J (1999). Cells on the target matrix-assisted laser-desorption/ionization time-of-flight mass-spectrometric analysis of mammalian cells grown on the target. Chromatographia 49:S41-S48.
    • (1999) Chromatographia , vol.49
    • Bergquist, J.1
  • 4
    • 24644492935 scopus 로고    scopus 로고
    • Biological tissue imaging with time-of-flight secondary ion mass spectrometry and cluster ion sources
    • Brunelle, A, Touboul, D, and Laprevote, O (2005). Biological tissue imaging with time-of-flight secondary ion mass spectrometry and cluster ion sources. J Mass Spectrom 40:985-999.
    • (2005) J Mass Spectrom , vol.40 , pp. 985-999
    • Brunelle, A.1    Touboul, D.2    Laprevote, O.3
  • 5
    • 17844398252 scopus 로고    scopus 로고
    • Tissue profiling by mass spectrometry: A review of methodology and applications
    • Caldwell, RL, and Caprioli, RM (2005). Tissue profiling by mass spectrometry: A review of methodology and applications. Mol Cell Proteomics 4:394-401.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 394-401
    • Caldwell, R.L.1    Caprioli, R.M.2
  • 7
    • 0033384034 scopus 로고    scopus 로고
    • Separation and detection of the alpha- and beta-chains of hemoglobin of single intact red blood cells using capillary electrophoresis/electrospray ionization time-of-flight mass spectrometry
    • Cao, P, and Moini, M (1999). Separation and detection of the alpha- and beta-chains of hemoglobin of single intact red blood cells using capillary electrophoresis/electrospray ionization time-of-flight mass spectrometry. J Am Soc Mass Spectrom 10:184-186.
    • (1999) J Am Soc Mass Spectrom , vol.10 , pp. 184-186
    • Cao, P.1    Moini, M.2
  • 8
    • 0023655560 scopus 로고
    • Microbore HPLC/mass spectrometry for the analysis of peptide mixtures using a continuous flow interface
    • Caprioli, RM, DaGue, B, Fan, T, and Moore, WT (1987). Microbore HPLC/mass spectrometry for the analysis of peptide mixtures using a continuous flow interface. Biochem Biophys Res Commun 146:291-299.
    • (1987) Biochem Biophys Res Commun , vol.146 , pp. 291-299
    • Caprioli, R.M.1    DaGue, B.2    Fan, T.3    Moore, W.T.4
  • 9
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS
    • Caprioli, RM, Farmer, TB, and Gile, J (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    Farmer, T.B.2    Gile, J.3
  • 10
    • 0001257222 scopus 로고
    • Microanalyse par emission ionique secondaire
    • Castaing, R, and Slodzian, G (1962). Microanalyse par emission ionique secondaire. Microscopie 1:395-410.
    • (1962) Microscopie , vol.1 , pp. 395-410
    • Castaing, R.1    Slodzian, G.2
  • 11
    • 0035158949 scopus 로고    scopus 로고
    • Studies of cell division (mitosis and cytokinesis) by dynamic secondary ion mass spectrometry ion microscopy: LLC-PK1 epithelial cells as a model for subcellular isotopic imaging
    • Chandra, S (2001). Studies of cell division (mitosis and cytokinesis) by dynamic secondary ion mass spectrometry ion microscopy: LLC-PK1 epithelial cells as a model for subcellular isotopic imaging. J Microsc 204:150-165.
    • (2001) J Microsc , vol.204 , pp. 150-165
    • Chandra, S.1
  • 12
    • 0037438034 scopus 로고    scopus 로고
    • SIMS ion microscopy as a novel, practical tool for subcellular chemical imaging in cancer research
    • Chandra, S (2003). SIMS ion microscopy as a novel, practical tool for subcellular chemical imaging in cancer research. Appl Surf Sci 203:679-683.
    • (2003) Appl Surf Sci , vol.203 , pp. 679-683
    • Chandra, S.1
  • 13
    • 2942592301 scopus 로고    scopus 로고
    • Subcellular SIMS imaging of isotopically labeled amino acids in cryogenically prepared cells
    • Chandra, S (2004). Subcellular SIMS imaging of isotopically labeled amino acids in cryogenically prepared cells. Appl Surf Sci 231-232:462-466.
    • (2004) Appl Surf Sci , vol.231-232 , pp. 462-466
    • Chandra, S.1
  • 14
    • 23944491834 scopus 로고    scopus 로고
    • Quantitative imaging of subcellular calcium stores in mammalian LLC-PK1 epithelial cells undergoing mitosis by SIMS ion microscopy
    • Chandra, S (2005). Quantitative imaging of subcellular calcium stores in mammalian LLC-PK1 epithelial cells undergoing mitosis by SIMS ion microscopy. Eur J Cell Biol 84:783-797.
    • (2005) Eur J Cell Biol , vol.84 , pp. 783-797
    • Chandra, S.1
  • 15
    • 0026583518 scopus 로고
    • Sample preparation of animal tissues and cell cultures for secondary ion mass spectrometry (SIMS) microscopy
    • Chandra, S, and Morrison, GH (1992). Sample preparation of animal tissues and cell cultures for secondary ion mass spectrometry (SIMS) microscopy. Biol Cell 74:31-42.
    • (1992) Biol Cell , vol.74 , pp. 31-42
    • Chandra, S.1    Morrison, G.H.2
  • 17
    • 4644326645 scopus 로고    scopus 로고
    • Proteomics in diagnostic pathology - Profiling and imaging proteins directly in tissue sections
    • Chaurand, P, Sanders, ME, Jensen, RA, and Caprioli, RM (2004a). Proteomics in diagnostic pathology - Profiling and imaging proteins directly in tissue sections. Am J Pathol 165:1057-1068.
    • (2004) Am J Pathol , vol.165 , pp. 1057-1068
    • Chaurand, P.1    Sanders, M.E.2    Jensen, R.A.3    Caprioli, R.M.4
  • 19
    • 4143070801 scopus 로고    scopus 로고
    • Assessing protein patterns in disease using imaging mass spectrometry
    • Chaurand, P, Schwartz, SA, and Caprioli, RM (2004c). Assessing protein patterns in disease using imaging mass spectrometry. J Proteome Res 3:245-252.
    • (2004) J Proteome Res , vol.3 , pp. 245-252
    • Chaurand, P.1    Schwartz, S.A.2    Caprioli, R.M.3
  • 20
    • 20444370683 scopus 로고    scopus 로고
    • Depth profiling of peptide films with TOF-SIMS and a C60 probe
    • Cheng, J, and Winograd, N (2005). Depth profiling of peptide films with TOF-SIMS and a C60 probe. Anal Chem 77:3651-3659.
    • (2005) Anal Chem , vol.77 , pp. 3651-3659
    • Cheng, J.1    Winograd, N.2
  • 21
    • 0031251801 scopus 로고    scopus 로고
    • SIMS microscopy: Methodology, problems and perspectives in mapping drags and nuclear medicine compounds
    • Clerc, J, Fourre, C, and Fragu, P (1997). SIMS microscopy: Methodology, problems and perspectives in mapping drags and nuclear medicine compounds. Cell Biol Int 21:619-633.
    • (1997) Cell Biol Int , vol.21 , pp. 619-633
    • Clerc, J.1    Fourre, C.2    Fragu, P.3
  • 22
    • 0141457609 scopus 로고    scopus 로고
    • Probing cell chemistry with time-of-flight secondary ion mass spectrometry: Development and exploitation of instrumentation for studies of frozen-hydrated biological material
    • Cliff, B, Lockyer, N, Jungnickel, H, Stephens, G, and Vickerman, JC (2003). Probing cell chemistry with time-of-flight secondary ion mass spectrometry: Development and exploitation of instrumentation for studies of frozen-hydrated biological material. Rapid Commun Mass Spectrom 17:2163-2167.
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 2163-2167
    • Cliff, B.1    Lockyer, N.2    Jungnickel, H.3    Stephens, G.4    Vickerman, J.C.5
  • 25
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, JB, Mann, M, Meng, CK, Wong, SF, and Whitehouse, CM (1989). Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 26
    • 0035385154 scopus 로고    scopus 로고
    • Characterization of intact microorganisms by MALDI mass spectrometry
    • Fenselau, C, and Demirev, PA (2001). Characterization of intact microorganisms by MALDI mass spectrometry. Mass Spectrom Rev 20:157-171.
    • (2001) Mass Spectrom Rev , vol.20 , pp. 157-171
    • Fenselau, C.1    Demirev, P.A.2
  • 29
    • 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, RW, Moroz, LL, Moroz, TP, Shippy, SA, and Sweedler, JV (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    Moroz, L.L.2    Moroz, T.P.3    Shippy, S.A.4    Sweedler, J.V.5
  • 32
    • 0033985441 scopus 로고    scopus 로고
    • Heterogeneity within MALDI samples as revealed by mass spectrometric imaging
    • Garden, RW, and Sweedler, JV (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
  • 34
    • 34547426428 scopus 로고    scopus 로고
    • Mass analysis and associated instrumentation
    • Gross ML, and Caprioli RM eds, Elsevier Science, Oxford
    • Gross, ML, and Caprioli, RM (2004). Mass analysis and associated instrumentation. In: Gross ML, and Caprioli RM (eds.), The Encyclopedia of Mass Spectrometry. Elsevier Science, Oxford.
    • (2004) The Encyclopedia of Mass Spectrometry
    • Gross, M.L.1    Caprioli, R.M.2
  • 35
    • 0033218504 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
    • Harvey, DJ (1999). Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates. Mass Spectrom Rev 18:349-450.
    • (1999) Mass Spectrom Rev , vol.18 , pp. 349-450
    • Harvey, D.J.1
  • 36
    • 15444376185 scopus 로고    scopus 로고
    • Monitoring activity-dependent peptide release from the CNS using single-bead solid-phase extraction and MALDI TOF MS detection
    • Hatcher, NG, Richmond, TA, Rubakhin, SS, and Sweedler, JV (2005). Monitoring activity-dependent peptide release from the CNS using single-bead solid-phase extraction and MALDI TOF MS detection. Anal Chem 77:1580-1587.
    • (2005) Anal Chem , vol.77 , pp. 1580-1587
    • Hatcher, N.G.1    Richmond, T.A.2    Rubakhin, S.S.3    Sweedler, J.V.4
  • 37
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption ionization mass-spectrometry of biopolymers
    • Hillenkamp, F, Karas, M, Beavis, RC, and Chait, BT (1991). Matrix-assisted laser desorption ionization mass-spectrometry of biopolymers. Anal Chem 63:A1193-A1202.
    • (1991) Anal Chem , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 38
    • 0029644541 scopus 로고
    • Capillary electrophoresis-electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry for direct analysis of cellular proteins
    • Hofstadler, SA, Swanek, FD, Gale, DC, Ewing, AG, and Smith, RD (1995). Capillary electrophoresis-electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry for direct analysis of cellular proteins. Anal Chem 67:1477-1480.
    • (1995) Anal Chem , vol.67 , pp. 1477-1480
    • Hofstadler, S.A.1    Swanek, F.D.2    Gale, D.C.3    Ewing, A.G.4    Smith, R.D.5
  • 39
    • 0029685835 scopus 로고    scopus 로고
    • Analysis of single cells with capillary electrophoresis electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Hofstadler, SA, Severs, JC, Smith, RD, Swanek, FD, and Ewing, AG (1996). Analysis of single cells with capillary electrophoresis electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Rapid Commun Mass Spectrom 10:919-922.
    • (1996) Rapid Commun Mass Spectrom , vol.10 , pp. 919-922
    • Hofstadler, S.A.1    Severs, J.C.2    Smith, R.D.3    Swanek, F.D.4    Ewing, A.G.5
  • 40
    • 20444435602 scopus 로고
    • The development of secondary ion mass spectrometry (SIMS). A retrospective
    • Honig, RE (1985). The development of secondary ion mass spectrometry (SIMS). A retrospective. Int J Mass Spectrom Ion Process 66:31-54.
    • (1985) Int J Mass Spectrom Ion Process , vol.66 , pp. 31-54
    • Honig, R.E.1
  • 41
    • 0242468940 scopus 로고    scopus 로고
    • Benchtop mass spectrometry in clinical biochemistry
    • Honour, JW (2003). Benchtop mass spectrometry in clinical biochemistry. Ann Clin Biochem 40:628-638.
    • (2003) Ann Clin Biochem , vol.40 , pp. 628-638
    • Honour, J.W.1
  • 42
    • 33644843132 scopus 로고    scopus 로고
    • Discovering new invertebrate neuropeptides using mass spectrometry
    • Hummon, AB, Amare, A, and Sweedler, JV (2005). Discovering new invertebrate neuropeptides using mass spectrometry. Mass Spectrom Rev 25:77-89.
    • (2005) Mass Spectrom Rev , vol.25 , pp. 77-89
    • Hummon, A.B.1    Amare, A.2    Sweedler, J.V.3
  • 43
    • 0037409639 scopus 로고    scopus 로고
    • Detection of fatty acids from intact microorganisms by molecular beam static secondary ion mass spectrometry
    • Ingram, JC, Bauer, WF, Lehman, RM, O'Connell, SP, and Shaw, AD (2003). Detection of fatty acids from intact microorganisms by molecular beam static secondary ion mass spectrometry. J Microbiol Methods 53:295-307.
    • (2003) J Microbiol Methods , vol.53 , pp. 295-307
    • Ingram, J.C.1    Bauer, W.F.2    Lehman, R.M.3    O'Connell, S.P.4    Shaw, A.D.5
  • 44
    • 0028009002 scopus 로고
    • Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption ionization mass spectrometry of single neurons
    • Jimenez, CR, van Veelan, PA, Li, KW, Wildering, WC, Gerearts, WP, Tjaden, UR, and van der Greef, J (1994). Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption ionization mass spectrometry of single neurons. J Neurochem 62:404-407.
    • (1994) J Neurochem , vol.62 , pp. 404-407
    • Jimenez, C.R.1    van Veelan, P.A.2    Li, K.W.3    Wildering, W.C.4    Gerearts, W.P.5    Tjaden, U.R.6    van der Greef, J.7
  • 45
    • 15444366805 scopus 로고    scopus 로고
    • Application of TOF-SIMS with chemometrics to discriminate between four different yeast strains from the species Candida glabrata and Saccharomyces cerevisiae
    • Jungnickel, H, Jones, EA, Lockyer, NP, Oliver, SG, Stephens, GM, and Vickerman, JC (2005). Application of TOF-SIMS with chemometrics to discriminate between four different yeast strains from the species Candida glabrata and Saccharomyces cerevisiae. Anal Chem 77:1740-1745.
    • (2005) Anal Chem , vol.77 , pp. 1740-1745
    • Jungnickel, H.1    Jones, E.A.2    Lockyer, N.P.3    Oliver, S.G.4    Stephens, G.M.5    Vickerman, J.C.6
  • 47
    • 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
  • 48
    • 0038149542 scopus 로고    scopus 로고
    • Spatial profiling invertebrate ganglia using MALDI MS
    • Kruse, R, and Sweedler, JV (2003). Spatial profiling invertebrate ganglia using MALDI MS. J Am Soc Mass Spectrom 14:752-759.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 752-759
    • Kruse, R.1    Sweedler, J.V.2
  • 49
    • 0033572758 scopus 로고    scopus 로고
    • In situ sequencing of peptides from biological tissues and single cells using MALDI-PSD/CID analysis
    • Li, L, Garden, RW, Romanova, EV, and Sweedler, JV (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    Garden, R.W.2    Romanova, E.V.3    Sweedler, J.V.4
  • 50
    • 0029860907 scopus 로고    scopus 로고
    • Analysis of single mammalian cell lysates by mass spectrometry
    • Li, L, Golding, RE, and Whittal, RM (1996). Analysis of single mammalian cell lysates by mass spectrometry. J Am Chem Soc 118:11662-11663.
    • (1996) J Am Chem Soc , vol.118 , pp. 11662-11663
    • Li, L.1    Golding, R.E.2    Whittal, R.M.3
  • 51
    • 0031758717 scopus 로고    scopus 로고
    • Li, L, Moroz, TP, Garden, RW, Floyd, PD, Weiss, KR, and Sweedler, JV (1998). Mass spectrometric survey of interganglionically transported peptides in Aplysia Peptides 19:1425-1433.
    • Li, L, Moroz, TP, Garden, RW, Floyd, PD, Weiss, KR, and Sweedler, JV (1998). Mass spectrometric survey of interganglionically transported peptides in Aplysia Peptides 19:1425-1433.
  • 53
    • 0034090219 scopus 로고    scopus 로고
    • Characterizing the Hez-PBAN gene products in neuronal clusters with immunocytochemistry and MALDI MS
    • Ma, PWK, Garden, RW, Niermann, JT, O'Connor, M, Sweedler, JV, and Roelofs, WL (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    Garden, R.W.2    Niermann, J.T.3    O'Connor, M.4    Sweedler, J.V.5    Roelofs, W.L.6
  • 54
    • 0142227011 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in clinical chemistry
    • Marvin, LF, Roberts, MA, and Fay, LB (2003). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in clinical chemistry. Clin Chim Acta 337:11-21.
    • (2003) Clin Chim Acta , vol.337 , pp. 11-21
    • Marvin, L.F.1    Roberts, M.A.2    Fay, L.B.3
  • 57
    • 0036205154 scopus 로고    scopus 로고
    • A general method for precalculation of parameters for sustained off resonance irradiation/collision-induced dissociation
    • Mirgorodskaya, E, O'Connor, PB, and Costello, CE (2002). A general method for precalculation of parameters for sustained off resonance irradiation/collision-induced dissociation. J Am Soc Mass Spectrom 13:318-324.
    • (2002) J Am Soc Mass Spectrom , vol.13 , pp. 318-324
    • Mirgorodskaya, E.1    O'Connor, P.B.2    Costello, C.E.3
  • 58
    • 10944225183 scopus 로고    scopus 로고
    • Recent developments in detection for microfluidic systems
    • Mogensen, KB, Klank, H, and Kutter, JP (2004). Recent developments in detection for microfluidic systems. Electrophoresis 25:3498-3512.
    • (2004) Electrophoresis , vol.25 , pp. 3498-3512
    • Mogensen, K.B.1    Klank, H.2    Kutter, J.P.3
  • 59
    • 24644484701 scopus 로고    scopus 로고
    • Vitamin E imaging and localization in the neuronal membrane
    • Monroe, EB, Jurchen, JC, Rubakhin, SS, and Sweedler, JV (2005). Vitamin E imaging and localization in the neuronal membrane. J Am Chem Soc 127:12152-12153.
    • (2005) J Am Chem Soc , vol.127 , pp. 12152-12153
    • Monroe, E.B.1    Jurchen, J.C.2    Rubakhin, S.S.3    Sweedler, J.V.4
  • 63
    • 11844301656 scopus 로고    scopus 로고
    • Mass spectrometric analysis of single identified neurons of an insect
    • Neupert, S, and Predel, R (2005). Mass spectrometric analysis of single identified neurons of an insect. Biochem Biophys Res Commun 327:640-645.
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 640-645
    • Neupert, S.1    Predel, R.2
  • 65
    • 13444282002 scopus 로고    scopus 로고
    • Bioimaging TOF-SIMS of tissues by gold ion bombardment of a silver-coated thin section
    • Nygren, H, Johansson, BR, and Malmberg, P (2004a). Bioimaging TOF-SIMS of tissues by gold ion bombardment of a silver-coated thin section. Microsc Res Tech 65:282-286.
    • (2004) Microsc Res Tech , vol.65 , pp. 282-286
    • Nygren, H.1    Johansson, B.R.2    Malmberg, P.3
  • 66
    • 2442595112 scopus 로고    scopus 로고
    • Bioimaging TOF-SIMS: Localization of cholesterol in rat kidney sections
    • Nygren, H, Malmberg, P, Kriegeskotte, C, and Arlinghaus, HF (2004b). Bioimaging TOF-SIMS: Localization of cholesterol in rat kidney sections. FEBS Lett 566:291-293.
    • (2004) FEBS Lett , vol.566 , pp. 291-293
    • Nygren, H.1    Malmberg, P.2    Kriegeskotte, C.3    Arlinghaus, H.F.4
  • 67
    • 3042706949 scopus 로고    scopus 로고
    • Mass spectrometric imaging of highly curved membranes during tetrahymena mating
    • Ostrowski, SG, Van Bell, CT, Winograd, N, and Ewing, AG (2004). Mass spectrometric imaging of highly curved membranes during tetrahymena mating. Science 305:71-73.
    • (2004) Science , vol.305 , pp. 71-73
    • Ostrowski, S.G.1    Van Bell, C.T.2    Winograd, N.3    Ewing, A.G.4
  • 68
    • 0742286847 scopus 로고    scopus 로고
    • Analysis of boron-10 in soft tissue by dynamic secondary ion mass spectrometry
    • Oyedepo, AC, Brooke, SL, Heard, PJ, Day, JC, Allen, GC, and Patel, H (2004). Analysis of boron-10 in soft tissue by dynamic secondary ion mass spectrometry. J Microsc 213:39-45.
    • (2004) J Microsc , vol.213 , pp. 39-45
    • Oyedepo, A.C.1    Brooke, S.L.2    Heard, P.J.3    Day, J.C.4    Allen, G.C.5    Patel, H.6
  • 69
    • 0000530593 scopus 로고    scopus 로고
    • Direct acquisition of matrix-assisted laser desorption/ionization time-of-flight mass spectra from laser capture microdissected tissues
    • Palmer-Toy, DE, Sarracino, DA, Sgroi, D, LeVangie, R, and Leopold, PE (2000). Direct acquisition of matrix-assisted laser desorption/ionization time-of-flight mass spectra from laser capture microdissected tissues. Clin Chem 46:1513-1516.
    • (2000) Clin Chem , vol.46 , pp. 1513-1516
    • Palmer-Toy, D.E.1    Sarracino, D.A.2    Sgroi, D.3    LeVangie, R.4    Leopold, P.E.5
  • 70
    • 3342996780 scopus 로고    scopus 로고
    • Molecular profiling of experimental Parkinson's disease: Direct analysis of peptides and proteins on brain tissue sections by MALDI mass spectrometry
    • Pierson, J, Norris, JL, Aerni, HR, Svenningsson, P, Caprioli, RM, and Andren, PE (2004). Molecular profiling of experimental Parkinson's disease: Direct analysis of peptides and proteins on brain tissue sections by MALDI mass spectrometry. J Proteome Res 3:289-295.
    • (2004) J Proteome Res , vol.3 , pp. 289-295
    • Pierson, J.1    Norris, J.L.2    Aerni, H.R.3    Svenningsson, P.4    Caprioli, R.M.5    Andren, P.E.6
  • 71
    • 2942534275 scopus 로고    scopus 로고
    • Molecule-specific imaging analysis of carcinogens in breast cancer cells using time-of-flight secondary ion mass spectrometry
    • Quong, JN, Knize, MG, Kulp, KS, and Wu, KJ (2004). Molecule-specific imaging analysis of carcinogens in breast cancer cells using time-of-flight secondary ion mass spectrometry. Appl Surf Sci 231-232:424-427.
    • (2004) Appl Surf Sci , vol.231-232 , pp. 424-427
    • Quong, J.N.1    Knize, M.G.2    Kulp, K.S.3    Wu, K.J.4
  • 72
    • 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, Toullec, JY, Vinh, J, Rossier, J, and Soyez, D (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    Toullec, J.Y.2    Vinh, J.3    Rossier, J.4    Soyez, D.5
  • 73
    • 0242606377 scopus 로고    scopus 로고
    • Direct analysis of drag candidates in tissue by matrix-assisted laser desorption/ionization mass spectrometry
    • Reyzer, ML, Hsieh, Y, Ng, K, Korfmacher, WA, and Caprioli, RM (2003). Direct analysis of drag candidates in tissue by matrix-assisted laser desorption/ionization mass spectrometry. J Mass Spectrom 38:1081-1092.
    • (2003) J Mass Spectrom , vol.38 , pp. 1081-1092
    • Reyzer, M.L.1    Hsieh, Y.2    Ng, K.3    Korfmacher, W.A.4    Caprioli, R.M.5
  • 74
    • 0037102266 scopus 로고    scopus 로고
    • Imaging of freeze-fractured cells with in situ fluorescence and time-of-flight secondary ion mass spectrometry
    • Roddy, TP, Cannon, DM, Meserole, CA, Winograd, N, and Ewing, AG (2002). Imaging of freeze-fractured cells with in situ fluorescence and time-of-flight secondary ion mass spectrometry. Anal Chem 74:4011-4019.
    • (2002) Anal Chem , vol.74 , pp. 4011-4019
    • Roddy, T.P.1    Cannon, D.M.2    Meserole, C.A.3    Winograd, N.4    Ewing, A.G.5
  • 75
    • 0033967547 scopus 로고    scopus 로고
    • Measuring the peptides in individual organelles with mass spectrometry
    • Rubakhin, SS, Garden, RW, Fuller, RR, and Sweedler, JV (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    Garden, R.W.2    Fuller, R.R.3    Sweedler, J.V.4
  • 76
    • 0142104131 scopus 로고    scopus 로고
    • Spatial profiling with MALDI MS: Distribution of neuropeptides within single neurons
    • Rubakhin, SS, Greenough, WT, and Sweedler, JV (2003). Spatial profiling with MALDI MS: Distribution of neuropeptides within single neurons. Anal Chem 75:5374-5380.
    • (2003) Anal Chem , vol.75 , pp. 5374-5380
    • Rubakhin, S.S.1    Greenough, W.T.2    Sweedler, J.V.3
  • 77
  • 78
    • 33750205820 scopus 로고    scopus 로고
    • Profiling signaling peptides in single mammalian cells using mass spectrometry
    • Rubakhin, SS, Churchill, JD, Greenough, WT, Sweedler, JV (2006) Profiling signaling peptides in single mammalian cells using mass spectrometry. Anal Chem 78:7267-7272.
    • (2006) Anal Chem , vol.78 , pp. 7267-7272
    • Rubakhin, S.S.1    Churchill, J.D.2    Greenough, W.T.3    Sweedler, J.V.4
  • 80
    • 1042290316 scopus 로고    scopus 로고
    • Protein profiling in brain tumors using mass spectrometry: Feasibility of a new technique for the analysis of protein expression
    • Schwartz, SA, Weil, RJ, Johnson, MD, Toms, SA, and Caprioli, RM (2004). Protein profiling in brain tumors using mass spectrometry: Feasibility of a new technique for the analysis of protein expression. Clin Cancer Res 10:981-987.
    • (2004) Clin Cancer Res , vol.10 , pp. 981-987
    • Schwartz, S.A.1    Weil, R.J.2    Johnson, M.D.3    Toms, S.A.4    Caprioli, R.M.5
  • 81
    • 84984076334 scopus 로고
    • Application of the laser microprobe mass analyzer (LAMMA) to qualitative and quantitative single cell analysis
    • Seydel, U, and Linder, B (1981). Application of the laser microprobe mass analyzer (LAMMA) to qualitative and quantitative single cell analysis. Int J Quant Chem 20:505-512.
    • (1981) Int J Quant Chem , vol.20 , pp. 505-512
    • Seydel, U.1    Linder, B.2
  • 82
    • 0023808195 scopus 로고
    • Monitoring of bacterial drug response by mass spectrometry of single cells
    • Seydel, U, and Lindner, B (1988). Monitoring of bacterial drug response by mass spectrometry of single cells. Biomed Environ Mass Spectrom 16:457-459.
    • (1988) Biomed Environ Mass Spectrom , vol.16 , pp. 457-459
    • Seydel, U.1    Lindner, B.2
  • 83
    • 0037262711 scopus 로고    scopus 로고
    • Development of the single-cell MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight) mass-spectroscopic assay
    • Shimizu, M, Ojima, N, Ohnishi, H, Shingaki, T, Hirakawa, Y, and Masujima, T (2003). Development of the single-cell MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight) mass-spectroscopic assay. Anal Sci 19:49-53.
    • (2003) Anal Sci , vol.19 , pp. 49-53
    • Shimizu, M.1    Ojima, N.2    Ohnishi, H.3    Shingaki, T.4    Hirakawa, Y.5    Masujima, T.6
  • 84
    • 0141497108 scopus 로고    scopus 로고
    • Mass spectrometry - A key technology in proteome research
    • Sickmann, A, Mreyen, M, and Meyer, HE (2003). Mass spectrometry - A key technology in proteome research. Adv Biochem Eng Biotechnol 83:141-176.
    • (2003) Adv Biochem Eng Biotechnol , vol.83 , pp. 141-176
    • Sickmann, A.1    Mreyen, M.2    Meyer, H.E.3
  • 85
    • 0031942731 scopus 로고    scopus 로고
    • Probing viruses with mass spectrometry
    • Siuzdak, G (1998). Probing viruses with mass spectrometry. J Mass Spectrom 33:203-211.
    • (1998) J Mass Spectrom , vol.33 , pp. 203-211
    • Siuzdak, G.1
  • 86
    • 0242501563 scopus 로고    scopus 로고
    • Imaging of membrane lipids in single cells by imprint-imaging time-of-flight secondary ion mass spectrometry
    • Sjovall, P, Lausmaa, J, Nygren, H, Carlsson, L, and Malmberg, P (2003). Imaging of membrane lipids in single cells by imprint-imaging time-of-flight secondary ion mass spectrometry. Anal Chem 75:3429-3434.
    • (2003) Anal Chem , vol.75 , pp. 3429-3434
    • Sjovall, P.1    Lausmaa, J.2    Nygren, H.3    Carlsson, L.4    Malmberg, P.5
  • 88
    • 6944233454 scopus 로고    scopus 로고
    • Ion activation methods for tandem mass spectrometry
    • Sleno, L, and Volmer, DA (2004). Ion activation methods for tandem mass spectrometry. J Mass Spectrom 39:1091-1112.
    • (2004) J Mass Spectrom , vol.39 , pp. 1091-1112
    • Sleno, L.1    Volmer, D.A.2
  • 89
    • 0033238005 scopus 로고    scopus 로고
    • Automated mass spectrometry imaging with a matrix-assisted laser desorption ionization time-of-flight instrument
    • Stoeckli, M, Farmer, TB, and Caprioli, RM (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    Farmer, T.B.2    Caprioli, R.M.3
  • 90
    • 0035048372 scopus 로고    scopus 로고
    • Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues
    • Stoeckli, M, Chaurand, P, Hallahan, DE, and Caprioli, RM (2001). Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues. Nat Med 7:493-496.
    • (2001) Nat Med , vol.7 , pp. 493-496
    • Stoeckli, M.1    Chaurand, P.2    Hallahan, D.E.3    Caprioli, R.M.4
  • 91
    • 0036903299 scopus 로고    scopus 로고
    • Molecular imaging of amyloid beta peptides in mouse brain sections using mass spectrometry
    • Stoeckli, M, Staab, D, Staufenbiel, M, Wiederhold, KH, and Signor, L (2002). Molecular imaging of amyloid beta peptides in mouse brain sections using mass spectrometry. Anal Biochem 311:33-39.
    • (2002) Anal Biochem , vol.311 , pp. 33-39
    • Stoeckli, M.1    Staab, D.2    Staufenbiel, M.3    Wiederhold, K.H.4    Signor, L.5
  • 92
    • 18844383150 scopus 로고    scopus 로고
    • Chip-based microfluidic devices coupled with electrospray ionization-mass spectrometry
    • Sung, WC, Makamba, H, and Chen, SH (2005). Chip-based microfluidic devices coupled with electrospray ionization-mass spectrometry. Electrophoresis 26:1783-1791.
    • (2005) Electrophoresis , vol.26 , pp. 1783-1791
    • Sung, W.C.1    Makamba, H.2    Chen, S.H.3
  • 93
    • 84984042980 scopus 로고
    • Protein and polymer analysis up to m/z 100.000 by laser ionisation time-of-flight mass spectrometry
    • Tanaka, K, Waki, H, Ido, Y, Akita, S, Yoshida, Y, and Yoshida, T (1988). Protein and polymer analysis up to m/z 100.000 by laser ionisation time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 2:151-153.
    • (1988) Rapid Commun Mass Spectrom , vol.2 , pp. 151-153
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 94
    • 2942538075 scopus 로고    scopus 로고
    • ToF-SIMS studies as a tool to discriminate between spores and vegetative cells of bacteria
    • Thompson, CE, Jungnickel, H, Lockyer, NP, Stephens, GM, and Vickerman, JC (2004). ToF-SIMS studies as a tool to discriminate between spores and vegetative cells of bacteria. Appl Surf Sci 231-232:420-423.
    • (2004) Appl Surf Sci , vol.231-232 , pp. 420-423
    • Thompson, C.E.1    Jungnickel, H.2    Lockyer, N.P.3    Stephens, G.M.4    Vickerman, J.C.5
  • 95
    • 0035052023 scopus 로고    scopus 로고
    • Organic ion imaging of biological tissue with secondary ion mass spectrometry and matrix-assisted laser desorption/ionization
    • Todd, PJ, Schaaff, TG, Chaurand, P, and Caprioli, RM (2001). Organic ion imaging of biological tissue with secondary ion mass spectrometry and matrix-assisted laser desorption/ionization. J Mass Spectrom 36:355-369.
    • (2001) J Mass Spectrom , vol.36 , pp. 355-369
    • Todd, P.J.1    Schaaff, T.G.2    Chaurand, P.3    Caprioli, R.M.4
  • 98
    • 0029841145 scopus 로고    scopus 로고
    • Attomole protein characterization by capillary electrophoresis-mass spectrometry
    • Valaskovic, GA, Kelleher, NL, and McLafferty, FW (1996). Attomole protein characterization by capillary electrophoresis-mass spectrometry. Science 273:1199-1202.
    • (1996) Science , vol.273 , pp. 1199-1202
    • Valaskovic, G.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 99
    • 0030033363 scopus 로고    scopus 로고
    • Identification of POMC processing products in single melanotrope cells by matrix-assisted laser desorption/ ionization mass spectrometry
    • van Strien, FJ, Jespersen, S, van der Greef, J, Jenks, BG, and Roubos, EW (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.1    Jespersen, S.2    van der Greef, J.3    Jenks, B.G.4    Roubos, E.W.5
  • 101
    • 16244363702 scopus 로고    scopus 로고
    • The magic of cluster SIMS
    • Winograd, N (2005). The magic of cluster SIMS. Anal Chem 77:143A-149A.
    • (2005) Anal Chem , vol.77
    • Winograd, N.1
  • 102
    • 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 splicing of the FMRFamide gene
    • Worster, BM, Yeoman, MS, and Benjamin, PR (1998). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis of the pattern of peptide expression in single neurons resulting from alternative splicing of the FMRFamide gene. Eur J Biochem 10:3498-3507.
    • (1998) Eur J Biochem , vol.10 , pp. 3498-3507
    • Worster, B.M.1    Yeoman, M.S.2    Benjamin, P.R.3
  • 103
    • 10644272773 scopus 로고    scopus 로고
    • Molecular depth profiling of histamine in ice using a buckminsterfullerene probe
    • Wucher, A, Sun, S, Szakal, C, and Winograd, N (2004). Molecular depth profiling of histamine in ice using a buckminsterfullerene probe. Anal Chem 76:7234-7242.
    • (2004) Anal Chem , vol.76 , pp. 7234-7242
    • Wucher, A.1    Sun, S.2    Szakal, C.3    Winograd, N.4
  • 104
    • 13844275962 scopus 로고    scopus 로고
    • Mass spectrometry of peptides and proteins
    • Wysocki, VH, Resing, KA, Zhang, Q, and Cheng, G (2005). Mass spectrometry of peptides and proteins. Methods 35:211-222.
    • (2005) Methods , vol.35 , pp. 211-222
    • Wysocki, V.H.1    Resing, K.A.2    Zhang, Q.3    Cheng, G.4
  • 105
    • 0030471998 scopus 로고    scopus 로고
    • Intraneuronal aluminum potentiates iron-induced oxidative stress in cultured rat hippocampal neurons
    • Xie, CX, Mattson, MP, Lovell, MA, and Yokel, RA (1996). Intraneuronal aluminum potentiates iron-induced oxidative stress in cultured rat hippocampal neurons. Brain Res 743:271-277.
    • (1996) Brain Res , vol.743 , pp. 271-277
    • Xie, C.X.1    Mattson, M.P.2    Lovell, M.A.3    Yokel, R.A.4
  • 106
    • 0036831909 scopus 로고    scopus 로고
    • Direct analysis of laser capture microdissected cells by MALDI mass spectrometry
    • Xu, B J, Caprioli, RM, Sanders, ME, and Jensen, RA (2002). Direct analysis of laser capture microdissected cells by MALDI mass spectrometry. J Am Soc Mass Spectrom 13:1292-1297.
    • (2002) J Am Soc Mass Spectrom , vol.13 , pp. 1292-1297
    • Xu, B.J.1    Caprioli, R.M.2    Sanders, M.E.3    Jensen, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.