메뉴 건너뛰기




Volumn 372, Issue 2, 2008, Pages 156-166

Systematic characterization of high mass accuracy influence on false discovery and probability scoring in peptide mass fingerprinting

Author keywords

False positive; Fourier transform ion cyclotron resonance mass spectrometry; Mass measurement accuracy; Matrix assisted laser desorption ionization; Peptide mass fingerprinting

Indexed keywords

CYCLOTRONS; DESORPTION; ELECTRON CYCLOTRON RESONANCE; FITS AND TOLERANCES; MASS SPECTROMETRY; MEASUREMENT ERRORS; PEPTIDES; PROTEOMICS; QUERY PROCESSING; SEARCH ENGINES;

EID: 36148937543     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.10.009     Document Type: Article
Times cited : (16)

References (56)
  • 2
    • 0027608882 scopus 로고
    • Use of mass spectrometric molecular weight information to identify proteins in sequence databases
    • Mann M., Hojrup P., and Roepstorff P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol. Mass Spectrom. 22 (1993) 338-345
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 338-345
    • Mann, M.1    Hojrup, P.2    Roepstorff, P.3
  • 3
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide mass fingerprinting
    • Pappin D.J., Hojrup P., and Bleasby A.J. Rapid identification of proteins by peptide mass fingerprinting. Curr. Biol. 3 (1993) 327-332
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 4
    • 0027375364 scopus 로고
    • Peptide mass maps: A highly informative approach to protein identification
    • Yates III J.R., Speicher S., Griffin P.R., and Hunkapiller T. Peptide mass maps: A highly informative approach to protein identification. Anal. Biochem. 214 (1993) 397-408
    • (1993) Anal. Biochem. , vol.214 , pp. 397-408
    • Yates III, J.R.1    Speicher, S.2    Griffin, P.R.3    Hunkapiller, T.4
  • 5
    • 0042386240 scopus 로고    scopus 로고
    • Protein identification: The origins of peptide mass fingerprinting
    • Henzel W.J., Watanabe C., and Stults J.T. Protein identification: The origins of peptide mass fingerprinting. J. Am. Soc. Mass Spectrom. 14 (2003) 931-942
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 931-942
    • Henzel, W.J.1    Watanabe, C.2    Stults, J.T.3
  • 6
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 8
    • 0033456265 scopus 로고    scopus 로고
    • Reliable automatic protein identification from matrix-assisted laser desorption/ionization mass spectrometric peptide fingerprints
    • Berndt P., Hobohm U., and Langen H. Reliable automatic protein identification from matrix-assisted laser desorption/ionization mass spectrometric peptide fingerprints. Electrophoresis 20 (1999) 3521-3526
    • (1999) Electrophoresis , vol.20 , pp. 3521-3526
    • Berndt, P.1    Hobohm, U.2    Langen, H.3
  • 9
    • 1242307292 scopus 로고    scopus 로고
    • Probity: A protein identification algorithm with accurate assignment of the statistical significance of the results
    • Eriksson J., and Fenyo D. Probity: A protein identification algorithm with accurate assignment of the statistical significance of the results. J. Proteome Res. 3 (2004) 32-36
    • (2004) J. Proteome Res. , vol.3 , pp. 32-36
    • Eriksson, J.1    Fenyo, D.2
  • 11
    • 28544433960 scopus 로고    scopus 로고
    • MASPIC: Intensity-based tandem mass spectrometry scoring scheme that improves peptide identification at high confidence
    • Narasimhan C., Tabb D.L., Verberkmoes N.C., Thompson M.R., Hettich R.L., and Uberbacher E.C. MASPIC: Intensity-based tandem mass spectrometry scoring scheme that improves peptide identification at high confidence. Anal. Chem. 77 (2005) 7581-7593
    • (2005) Anal. Chem. , vol.77 , pp. 7581-7593
    • Narasimhan, C.1    Tabb, D.L.2    Verberkmoes, N.C.3    Thompson, M.R.4    Hettich, R.L.5    Uberbacher, E.C.6
  • 12
  • 13
    • 23944477893 scopus 로고    scopus 로고
    • Large scale analysis of MASCOT results using a mass accuracy-based threshold (MATH) effectively improves data interpretation
    • Rudnick P.A., Wang Y.J., Evans E., Lee C.S., and Balgley B.M. Large scale analysis of MASCOT results using a mass accuracy-based threshold (MATH) effectively improves data interpretation. J. Proteome Res. 4 (2005) 1353-1360
    • (2005) J. Proteome Res. , vol.4 , pp. 1353-1360
    • Rudnick, P.A.1    Wang, Y.J.2    Evans, E.3    Lee, C.S.4    Balgley, B.M.5
  • 14
    • 21044459357 scopus 로고    scopus 로고
    • A heuristic method for assigning a false-discovery rate for protein identifications from Mascot database search results
    • Weatherly D.B., Astwood III J.A., Minning T.A., Cavola C., Tarleton R.L., and Orlando R. A heuristic method for assigning a false-discovery rate for protein identifications from Mascot database search results. Mol. Cell. Proteomics 4 (2005) 762-772
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 762-772
    • Weatherly, D.B.1    Astwood III, J.A.2    Minning, T.A.3    Cavola, C.4    Tarleton, R.L.5    Orlando, R.6
  • 15
    • 33645790020 scopus 로고    scopus 로고
    • Trade-off between high sensitivity and increased potential for false positive peptide sequence matches using a two-dimensional linear ion trap for tandem mass spectrometry-based proteomics
    • Xie H., and Griffin T.J. Trade-off between high sensitivity and increased potential for false positive peptide sequence matches using a two-dimensional linear ion trap for tandem mass spectrometry-based proteomics. J. Proteome Res. 5 (2006) 1003-1009
    • (2006) J. Proteome Res. , vol.5 , pp. 1003-1009
    • Xie, H.1    Griffin, T.J.2
  • 16
    • 33846567441 scopus 로고    scopus 로고
    • Prediction of error associated with false-positive rate determination for peptide identification in large-scale proteomics experiments using a combined reverse and forward peptide sequence database strategy
    • Huttlin E.L., Hegeman A.D., Harms A.C., and Sussman M.R. Prediction of error associated with false-positive rate determination for peptide identification in large-scale proteomics experiments using a combined reverse and forward peptide sequence database strategy. J. Proteome Res. 6 (2007) 392-398
    • (2007) J. Proteome Res. , vol.6 , pp. 392-398
    • Huttlin, E.L.1    Hegeman, A.D.2    Harms, A.C.3    Sussman, M.R.4
  • 17
    • 0035984343 scopus 로고    scopus 로고
    • Peptide mapping of proteins in human body fluids using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Bergquist J., Palmblad M., Wetterhall M., Hakansson P., and Markides K.E. Peptide mapping of proteins in human body fluids using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Mass Spectrom. Rev. 21 (2002) 2-15
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 2-15
    • Bergquist, J.1    Palmblad, M.2    Wetterhall, M.3    Hakansson, P.4    Markides, K.E.5
  • 18
    • 14744304574 scopus 로고    scopus 로고
    • Proteomics by FTICR mass spectrometry: Top down and bottom up
    • Bogdanov B., and Smith R.D. Proteomics by FTICR mass spectrometry: Top down and bottom up. Mass Spectrom. Rev. 24 (2005) 168-200
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 168-200
    • Bogdanov, B.1    Smith, R.D.2
  • 19
    • 33646264529 scopus 로고    scopus 로고
    • Advances in proteomics data analysis and display using an accurate mass and time tag approach
    • Zimmer J.S., Monroe M.E., Qian W.J., and Smith R.D. Advances in proteomics data analysis and display using an accurate mass and time tag approach. Mass Spectrom. Rev. 25 (2006) 450-482
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 450-482
    • Zimmer, J.S.1    Monroe, M.E.2    Qian, W.J.3    Smith, R.D.4
  • 20
    • 1242284991 scopus 로고    scopus 로고
    • Theoretical and experimental prospects for protein identification based solely on accurate mass measurement
    • He F., Emmett M.R., Hakansson K., Hendrickson C.L., and Marshall A.G. Theoretical and experimental prospects for protein identification based solely on accurate mass measurement. J. Proteome Res. 3 (2004) 61-67
    • (2004) J. Proteome Res. , vol.3 , pp. 61-67
    • He, F.1    Emmett, M.R.2    Hakansson, K.3    Hendrickson, C.L.4    Marshall, A.G.5
  • 21
    • 33745686436 scopus 로고    scopus 로고
    • Probabilistic enrichment of phosphopeptides by their mass defect
    • Bruce C., Shifman M.A., Miller P., and Gulcicek E.E. Probabilistic enrichment of phosphopeptides by their mass defect. Anal. Chem. 78 (2006) 4374-4382
    • (2006) Anal. Chem. , vol.78 , pp. 4374-4382
    • Bruce, C.1    Shifman, M.A.2    Miller, P.3    Gulcicek, E.E.4
  • 22
    • 33646751578 scopus 로고    scopus 로고
    • Mass defect labeling of cysteine for improving peptide assignment in shotgun proteomic analyses
    • Hernandez H., Niehauser S., Boltz S.A., Gawandi V., Phillips R.S., and Amster I.J. Mass defect labeling of cysteine for improving peptide assignment in shotgun proteomic analyses. Anal. Chem. 78 (2006) 3417-3423
    • (2006) Anal. Chem. , vol.78 , pp. 3417-3423
    • Hernandez, H.1    Niehauser, S.2    Boltz, S.A.3    Gawandi, V.4    Phillips, R.S.5    Amster, I.J.6
  • 23
    • 33645111699 scopus 로고    scopus 로고
    • Determination of unique amino acid substitutions in protein variants by peptide mass mapping with FT-ICR MS
    • Tanaka K., Takenaka S., Tsuyama S., and Wada Y. Determination of unique amino acid substitutions in protein variants by peptide mass mapping with FT-ICR MS. J. Am. Soc. Mass Spectrom. 17 (2006) 508-513
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 508-513
    • Tanaka, K.1    Takenaka, S.2    Tsuyama, S.3    Wada, Y.4
  • 24
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., Mccormack A.L., and Yates J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5 (1994) 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    Mccormack, A.L.2    Yates, J.R.3
  • 25
    • 33645235084 scopus 로고    scopus 로고
    • Cross-correlation algorithm for calculation of peptide molecular weight from tandem mass spectra
    • Venable J.D., Xu T., Cociorva D., and Yates III J.R. Cross-correlation algorithm for calculation of peptide molecular weight from tandem mass spectra. Anal. Chem. 78 (2006) 1921-1929
    • (2006) Anal. Chem. , vol.78 , pp. 1921-1929
    • Venable, J.D.1    Xu, T.2    Cociorva, D.3    Yates III, J.R.4
  • 26
    • 30744476222 scopus 로고    scopus 로고
    • Performance of a linear ion trap-Orbitrap hybrid for peptide analysis
    • Yates J.R., Cociorva D., Liao L., and Zabrouskov V. Performance of a linear ion trap-Orbitrap hybrid for peptide analysis. Anal. Chem. 78 (2006) 493-500
    • (2006) Anal. Chem. , vol.78 , pp. 493-500
    • Yates, J.R.1    Cociorva, D.2    Liao, L.3    Zabrouskov, V.4
  • 27
    • 0242670001 scopus 로고    scopus 로고
    • An automated matrix-assisted laser desorption/ionization quadrupole Fourier transform ion cyclotron resonance mass spectrometer for "bottom-up" proteomics
    • Brock A., Horn D.M., Peters E.C., Shaw C.M., Ericson C., Phung Q.T., and Salomon A.R. An automated matrix-assisted laser desorption/ionization quadrupole Fourier transform ion cyclotron resonance mass spectrometer for "bottom-up" proteomics. Anal. Chem. 75 (2003) 3419-3428
    • (2003) Anal. Chem. , vol.75 , pp. 3419-3428
    • Brock, A.1    Horn, D.M.2    Peters, E.C.3    Shaw, C.M.4    Ericson, C.5    Phung, Q.T.6    Salomon, A.R.7
  • 28
    • 2342593352 scopus 로고    scopus 로고
    • De novo sequencing, peptide composition analysis, and composition-based sequencing: A new strategy employing accurate mass determination by Fourier transform ion cyclotron resonance mass spectrometry
    • Spengler B. De novo sequencing, peptide composition analysis, and composition-based sequencing: A new strategy employing accurate mass determination by Fourier transform ion cyclotron resonance mass spectrometry. J. Am. Soc. Mass Spectrom. 15 (2004) 703-714
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 703-714
    • Spengler, B.1
  • 29
    • 21044441542 scopus 로고    scopus 로고
    • Improving protein identification using complementary fragmentation techniques in Fourier transform mass spectrometry
    • Nielsen M.L., Savitski M.M., and Zubarev R.A. Improving protein identification using complementary fragmentation techniques in Fourier transform mass spectrometry. Mol. Cell. Proteomics 4 (2005) 835-845
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 835-845
    • Nielsen, M.L.1    Savitski, M.M.2    Zubarev, R.A.3
  • 32
    • 24044508863 scopus 로고    scopus 로고
    • New database-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse scores, recovers below threshold data, singles out modified peptides, and assesses the quality of MS/MS techniques
    • Savitski M.M., Nielsen M.L., and Zubarev R.A. New database-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse scores, recovers below threshold data, singles out modified peptides, and assesses the quality of MS/MS techniques. Mol. Cell. Proteomics 4 (2005) 1180-1188
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1180-1188
    • Savitski, M.M.1    Nielsen, M.L.2    Zubarev, R.A.3
  • 33
    • 23944490667 scopus 로고    scopus 로고
    • Increased protein identification capabilities through novel tandem MS calibration strategies
    • Wu S., Kaiser N.K., Meng D., Anderson G.A., Zhang K., and Bruce J.E. Increased protein identification capabilities through novel tandem MS calibration strategies. J. Proteome Res. 4 (2005) 1434-1441
    • (2005) J. Proteome Res. , vol.4 , pp. 1434-1441
    • Wu, S.1    Kaiser, N.K.2    Meng, D.3    Anderson, G.A.4    Zhang, K.5    Bruce, J.E.6
  • 34
    • 33644841619 scopus 로고    scopus 로고
    • PhosTShunter: A fast and reliable tool to detect phosphorylated peptides in liquid chromatography Fourier transform tandem mass spectrometry data sets
    • Kocher T., Savitski M.M., Nielsen M.L., and Zubarev R.A. PhosTShunter: A fast and reliable tool to detect phosphorylated peptides in liquid chromatography Fourier transform tandem mass spectrometry data sets. J. Proteome Res. 5 (2006) 659-668
    • (2006) J. Proteome Res. , vol.5 , pp. 659-668
    • Kocher, T.1    Savitski, M.M.2    Nielsen, M.L.3    Zubarev, R.A.4
  • 35
    • 31844448971 scopus 로고    scopus 로고
    • Combining low and high mass ion accumulation for enhancing shotgun proteome analysis by accurate mass measurement
    • Wong R.L., and Amster I.J. Combining low and high mass ion accumulation for enhancing shotgun proteome analysis by accurate mass measurement. J. Am. Soc. Mass Spectrom. 17 (2006) 205-212
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 205-212
    • Wong, R.L.1    Amster, I.J.2
  • 37
    • 33845926390 scopus 로고    scopus 로고
    • Sub parts-per-million mass measurement accuracy of intact proteins and product ions achieved using a dual electrospray ionization quadrupole Fourier transform ion cyclotron resonance mass spectrometer
    • Williams D.K., Hawkridge A.M., and Muddiman D.C. Sub parts-per-million mass measurement accuracy of intact proteins and product ions achieved using a dual electrospray ionization quadrupole Fourier transform ion cyclotron resonance mass spectrometer. J. Am. Soc. Mass Spectrom. 18 (2007) 1-7
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1-7
    • Williams, D.K.1    Hawkridge, A.M.2    Muddiman, D.C.3
  • 38
    • 0031298696 scopus 로고    scopus 로고
    • Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching
    • Jensen O.N., Podtelejnikov A.V., and Mann M. Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. Anal. Chem. 69 (1997) 4741-4750
    • (1997) Anal. Chem. , vol.69 , pp. 4741-4750
    • Jensen, O.N.1    Podtelejnikov, A.V.2    Mann, M.3
  • 39
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement ((10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser K.R., Baker P., and Burlingame A.L. Role of accurate mass measurement ((10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal. Chem. 71 (1999) 2871-2882
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 40
    • 0033230052 scopus 로고    scopus 로고
    • Mass accuracy and sequence requirements for protein database searching
    • Green M.K., Johnston M.V., and Larsen B.S. Mass accuracy and sequence requirements for protein database searching. Anal. Biochem. 275 (1999) 39-46
    • (1999) Anal. Biochem. , vol.275 , pp. 39-46
    • Green, M.K.1    Johnston, M.V.2    Larsen, B.S.3
  • 41
    • 0038149492 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry with NanoLC/microelectrospray ionization and matrix-assisted laser desorption/ionization: Analytical performance in peptide mass fingerprint analysis
    • Witt M., Fuchser J., and Baykut G. Fourier transform ion cyclotron resonance mass spectrometry with NanoLC/microelectrospray ionization and matrix-assisted laser desorption/ionization: Analytical performance in peptide mass fingerprint analysis. J. Am. Soc. Mass Spectrom. 14 (2003) 553-561
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 553-561
    • Witt, M.1    Fuchser, J.2    Baykut, G.3
  • 42
    • 8444229270 scopus 로고    scopus 로고
    • Improved protein identification using automated high mass measurement accuracy MALDI FT-ICR MS peptide mass fingerprinting
    • Horn D.M., Peters E.C., Klock H., Meyers A., and Brock A. Improved protein identification using automated high mass measurement accuracy MALDI FT-ICR MS peptide mass fingerprinting. Intl. J. Mass Spectrom. 238 (2004) 189-196
    • (2004) Intl. J. Mass Spectrom. , vol.238 , pp. 189-196
    • Horn, D.M.1    Peters, E.C.2    Klock, H.3    Meyers, A.4    Brock, A.5
  • 43
    • 34147173417 scopus 로고    scopus 로고
    • On the proper use of mass accuracy in proteomics
    • Zubarev R., and Mann M. On the proper use of mass accuracy in proteomics. Mol. Cell. Proteomics 6 (2007) 377-381
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 377-381
    • Zubarev, R.1    Mann, M.2
  • 44
    • 0034671977 scopus 로고    scopus 로고
    • Broad-band ion accumulation with an internal source MALDI-FTICR-MS
    • Mize T.H., and Amster I.J. Broad-band ion accumulation with an internal source MALDI-FTICR-MS. Anal. Chem. 72 (2000) 5886-5891
    • (2000) Anal. Chem. , vol.72 , pp. 5886-5891
    • Mize, T.H.1    Amster, I.J.2
  • 45
    • 0034671965 scopus 로고    scopus 로고
    • Internal calibration on adjacent samples (InCAS) with Fourier transform mass spectrometry
    • O'Connor P.B., and Costello C.E. Internal calibration on adjacent samples (InCAS) with Fourier transform mass spectrometry. Anal. Chem. 72 (2000) 5881-5885
    • (2000) Anal. Chem. , vol.72 , pp. 5881-5885
    • O'Connor, P.B.1    Costello, C.E.2
  • 46
    • 21844457685 scopus 로고    scopus 로고
    • Fragmentation pathways of protonated peptides
    • Paizs B., and Suhai S. Fragmentation pathways of protonated peptides. Mass Spectrom. Rev. 24 (2005) 508-548
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 508-548
    • Paizs, B.1    Suhai, S.2
  • 47
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: A primer
    • Marshall A.G., Hendrickson C.L., and Jackson G.S. Fourier transform ion cyclotron resonance mass spectrometry: A primer. Mass Spectrom. Rev. 17 (1998) 1-35
    • (1998) Mass Spectrom. Rev. , vol.17 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 48
    • 14744267430 scopus 로고    scopus 로고
    • Accurate mass measurements by Fourier transform mass spectrometry
    • Zhang L.K., Rempel D., Pramanik B.N., and Gross M.L. Accurate mass measurements by Fourier transform mass spectrometry. Mass Spectrom. Rev. 24 (2005) 286-309
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 286-309
    • Zhang, L.K.1    Rempel, D.2    Pramanik, B.N.3    Gross, M.L.4
  • 49
    • 36148938843 scopus 로고    scopus 로고
    • M. Mann, Useful tables of possible and probable peptide masses, 43rd Annual Conference on Mass Spectrometry and Allied Topics, Atlanta, GA, 1995. (American Society for Mass Spectrometry).
  • 50
    • 2742576125 scopus 로고    scopus 로고
    • Accuracy requirements for peptide characterization by monoisotopic molecular mass measurements
    • Zubarev R.A., Hakansson P., and Sundqvist B. Accuracy requirements for peptide characterization by monoisotopic molecular mass measurements. Anal. Chem. 68 (1996) 4060-4063
    • (1996) Anal. Chem. , vol.68 , pp. 4060-4063
    • Zubarev, R.A.1    Hakansson, P.2    Sundqvist, B.3
  • 51
    • 1842869992 scopus 로고    scopus 로고
    • Artifacts and unassigned masses encountered in peptide mass mapping
    • Karty J.A., Ireland M.M.E., Brun Y.V., and Reilly J.P. Artifacts and unassigned masses encountered in peptide mass mapping. J. Chromatogr. B 782 (2002) 363-383
    • (2002) J. Chromatogr. B , vol.782 , pp. 363-383
    • Karty, J.A.1    Ireland, M.M.E.2    Brun, Y.V.3    Reilly, J.P.4
  • 53
    • 33646555091 scopus 로고    scopus 로고
    • Enhanced peptide mass fingerprinting through high mass accuracy: Exclusion of non-peptide signals based on residual mass
    • Dodds E.D., An H.J., Hagerman P.J., and Lebrilla C.B. Enhanced peptide mass fingerprinting through high mass accuracy: Exclusion of non-peptide signals based on residual mass. J. Proteome Res. 5 (2006) 1195-1203
    • (2006) J. Proteome Res. , vol.5 , pp. 1195-1203
    • Dodds, E.D.1    An, H.J.2    Hagerman, P.J.3    Lebrilla, C.B.4
  • 54
    • 36148973687 scopus 로고    scopus 로고
    • E. D. Dodds, B. H. Clowers, H. J. An, P. J. Hagerman, C. B. Lebrilla, Low mass error tolerance and the Mass Sieve approach to peptide mass fingerprinting with MALDI-FTICR-MS, 54th Annual Conference on Mass Spectrometry and Allied Topics, Seattle, WA, 2006. (American Society for Mass Spectrometry).
  • 55
    • 36148978289 scopus 로고    scopus 로고
    • D. J. Slotta, M. A. McFarland, A. J. Makusky, S. P. Markey, MassSieve: A new visualization tool for mass spectrometry-based proteomics, 55th Annual Conference on Mass Spectrometry and Allied Topics, Indianapolis, IN, 2007. (American Society for Mass Spectrometry).
  • 56
    • 33846632267 scopus 로고    scopus 로고
    • Prediction of missed cleavage sites in tryptic peptides aids protein identification in proteomics
    • Siepen J.A., Keevil E.J., Knight D., and Hubbard S.J. Prediction of missed cleavage sites in tryptic peptides aids protein identification in proteomics. J. Proteome Res. 6 (2007) 399-408
    • (2007) J. Proteome Res. , vol.6 , pp. 399-408
    • Siepen, J.A.1    Keevil, E.J.2    Knight, D.3    Hubbard, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.