메뉴 건너뛰기




Volumn 282, Issue 14, 2015, Pages 2612-2626

Proteomics beyond trypsin

Author keywords

bias in quantitative proteomics; cleavage specificity; digestion; mass spectrometry; middle down proteomics; proteases; protein post translational modifications; shotgun proteomics

Indexed keywords

ARGININE; ASPARTIC PROTEINASE; CHYMOTRYPSIN; CYSTEINE; CYSTEINE PROTEINASE; DNA DIRECTED RNA POLYMERASE III; EXOPEPTIDASE; GLUTAMIC ACID; LYSINE; METALLOPROTEINASE; PROTEINASE; PROTEOME; RNA POLYMERASE II; SERINE PROTEINASE; TRYPSIN; PEPTIDE HYDROLASE;

EID: 84937245669     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13287     Document Type: Review
Times cited : (261)

References (86)
  • 1
    • 84871297843 scopus 로고    scopus 로고
    • Next-generation proteomics: Towards an integrative view of proteome dynamics
    • Altelaar AFM, Munoz J, &, Heck AJR, (2013) Next-generation proteomics: towards an integrative view of proteome dynamics. Nat Rev Genet 14, 35-48.
    • (2013) Nat Rev Genet , vol.14 , pp. 35-48
    • Altelaar, A.F.M.1    Munoz, J.2    Heck, A.J.R.3
  • 2
    • 84861897793 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and network biology
    • Bensimon A, Heck AJR, &, Aebersold R, (2012) Mass spectrometry-based proteomics and network biology. Annu Rev Biochem 81, 379-405.
    • (2012) Annu Rev Biochem , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.R.2    Aebersold, R.3
  • 3
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary C, &, Mann M, (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat Rev Mol Cell Biol 11, 427-439.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 4
    • 0028788811 scopus 로고
    • From genome to proteome: Looking at a cell's proteins
    • Kahn P, (1995) From genome to proteome: looking at a cell's proteins. Science 270, 369-370.
    • (1995) Science , vol.270 , pp. 369-370
    • Kahn, P.1
  • 5
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, &, Mann M, (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 1, 2856-2860.
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 7
    • 84862660669 scopus 로고    scopus 로고
    • Recent advances in peptide separation by multidimensional liquid chromatography for proteome analysis
    • Di Palma S, Hennrich ML, Heck AJR, &, Mohammed S, (2012) Recent advances in peptide separation by multidimensional liquid chromatography for proteome analysis. J Proteomics 75, 3791-3813.
    • (2012) J Proteomics , vol.75 , pp. 3791-3813
    • Di Palma, S.1    Hennrich, M.L.2    Heck, A.J.R.3    Mohammed, S.4
  • 9
    • 84863700845 scopus 로고    scopus 로고
    • In-house construction of a UHPLC system enabling the identification of over 4000 protein groups in a single analysis
    • Cristobal A, Hennrich ML, Giansanti P, Goerdayal SS, Heck AJR, &, Mohammed S, (2012) In-house construction of a UHPLC system enabling the identification of over 4000 protein groups in a single analysis. Analyst 137, 3541-3548.
    • (2012) Analyst , vol.137 , pp. 3541-3548
    • Cristobal, A.1    Hennrich, M.L.2    Giansanti, P.3    Goerdayal, S.S.4    Heck, A.J.R.5    Mohammed, S.6
  • 10
    • 84908641937 scopus 로고    scopus 로고
    • Development and performance evaluation of an ultralow flow nanoliquid chromatography-tandem mass spectrometry set-up
    • Köcher T, Pichler P, De Pra M, Rieux L, Swart R, &, Mechtler K, (2014) Development and performance evaluation of an ultralow flow nanoliquid chromatography-tandem mass spectrometry set-up. Proteomics 14, 1999-2007.
    • (2014) Proteomics , vol.14 , pp. 1999-2007
    • Köcher, T.1    Pichler, P.2    De Pra, M.3    Rieux, L.4    Swart, R.5    Mechtler, K.6
  • 12
    • 0033798919 scopus 로고    scopus 로고
    • Tandem mass spectrometry: Dissociation of ions by collisional activation
    • Shukla A, &, Futrell J, (2000) Tandem mass spectrometry: dissociation of ions by collisional activation. J Mass Spectrom 35, 1069-1090.
    • (2000) J Mass Spectrom , vol.35 , pp. 1069-1090
    • Shukla, A.1    Futrell, J.2
  • 13
    • 33750610654 scopus 로고    scopus 로고
    • Analysis of intact proteins on a chromatographic time scale by electron transfer dissociation tandem mass spectrometry
    • Chi A, Bai DL, Geer LY, Shabanowitz J, &, Hunt DF, (2007) Analysis of intact proteins on a chromatographic time scale by electron transfer dissociation tandem mass spectrometry. Int J Mass Spectrom 259, 197-203.
    • (2007) Int J Mass Spectrom , vol.259 , pp. 197-203
    • Chi, A.1    Bai, D.L.2    Geer, L.Y.3    Shabanowitz, J.4    Hunt, D.F.5
  • 14
  • 15
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, &, Cottrell JS, (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 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
  • 16
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, &, Yates JR, (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5, 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
  • 17
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • Craig R, &, Beavis RC, (2004) TANDEM: matching proteins with tandem mass spectra. Bioinformatics 20, 1466-1467.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 20
    • 84905397897 scopus 로고    scopus 로고
    • MS Amanda, a universal identification algorithm optimized for high accuracy tandem mass spectra
    • Dorfer V, Pichler P, Stranzl T, Stadlmann J, Taus T, Winkler S, &, Mechtler K, (2014) MS Amanda, a universal identification algorithm optimized for high accuracy tandem mass spectra. J Proteome Res 13, 3679-3684.
    • (2014) J Proteome Res , vol.13 , pp. 3679-3684
    • Dorfer, V.1    Pichler, P.2    Stranzl, T.3    Stadlmann, J.4    Taus, T.5    Winkler, S.6    Mechtler, K.7
  • 21
    • 84875521318 scopus 로고    scopus 로고
    • Byonic: Advanced peptide and protein identification software
    • Bern M, Kil YJ, &, Becker C, (2012) Byonic: advanced peptide and protein identification software. Curr Protoc Bioinformatics Chapter 13, Unit13.20.
    • (2012) Curr Protoc Bioinformatics , vol.13 , pp. Unit1320
    • Bern, M.1    Kil, Y.J.2    Becker, C.3
  • 23
    • 84879389449 scopus 로고    scopus 로고
    • High performance computational analysis of large-scale proteome data sets to assess incremental contribution to coverage of the human genome
    • Neuhauser N, Nagaraj N, McHardy P, Zanivan S, Scheltema R, Cox J, &, Mann M, (2013) High performance computational analysis of large-scale proteome data sets to assess incremental contribution to coverage of the human genome. J Proteome Res 12, 2858-2868.
    • (2013) J Proteome Res , vol.12 , pp. 2858-2868
    • Neuhauser, N.1    Nagaraj, N.2    McHardy, P.3    Zanivan, S.4    Scheltema, R.5    Cox, J.6    Mann, M.7
  • 26
    • 77949786295 scopus 로고    scopus 로고
    • Value of using multiple proteases for large-scale mass spectrometry-based proteomics
    • Swaney DL, Wenger CD, &, Coon JJ, (2010) Value of using multiple proteases for large-scale mass spectrometry-based proteomics. J Proteome Res 9, 1323-1329.
    • (2010) J Proteome Res , vol.9 , pp. 1323-1329
    • Swaney, D.L.1    Wenger, C.D.2    Coon, J.J.3
  • 27
    • 84893846021 scopus 로고    scopus 로고
    • Cleaved and missed sites for trypsin, lys-C, and lys-N can be predicted with high confidence on the basis of sequence context
    • Gershon PD, (2014) Cleaved and missed sites for trypsin, lys-C, and lys-N can be predicted with high confidence on the basis of sequence context. J Proteome Res 13, 702-709.
    • (2014) J Proteome Res , vol.13 , pp. 702-709
    • Gershon, P.D.1
  • 28
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina H, Horn DM, Tang N, Mathivanan S, &, Pandey A, (2007) Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci USA 104, 2199-2204.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 29
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • Swaney DL, McAlister GC, &, Coon JJ, (2008) Decision tree-driven tandem mass spectrometry for shotgun proteomics. Nat Methods 5, 959-964.
    • (2008) Nat Methods , vol.5 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 31
    • 84868327851 scopus 로고    scopus 로고
    • Large-scale quantitative assessment of different in-solution protein digestion protocols reveals superior cleavage efficiency of tandem Lys-C/trypsin proteolysis over trypsin digestion
    • Glatter T, Ludwig C, Ahrné E, Aebersold R, Heck AJR, &, Schmidt A, (2012) Large-scale quantitative assessment of different in-solution protein digestion protocols reveals superior cleavage efficiency of tandem Lys-C/trypsin proteolysis over trypsin digestion. J Proteome Res 11, 5145-5156.
    • (2012) J Proteome Res , vol.11 , pp. 5145-5156
    • Glatter, T.1    Ludwig, C.2    Ahrné, E.3    Aebersold, R.4    Heck, A.J.R.5    Schmidt, A.6
  • 33
    • 33644856320 scopus 로고    scopus 로고
    • Effects of modified digestion schemes on the identification of proteins from complex mixtures
    • Klammer AA, &, MacCoss MJ, (2006) Effects of modified digestion schemes on the identification of proteins from complex mixtures. J Proteome Res 5, 695-700.
    • (2006) J Proteome Res , vol.5 , pp. 695-700
    • Klammer, A.A.1    MacCoss, M.J.2
  • 34
    • 42949113985 scopus 로고    scopus 로고
    • Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase
    • Taouatas N, Drugan MM, Heck AJR, &, Mohammed S, (2008) Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. Nat Methods 5, 405-407.
    • (2008) Nat Methods , vol.5 , pp. 405-407
    • Taouatas, N.1    Drugan, M.M.2    Heck, A.J.R.3    Mohammed, S.4
  • 35
    • 78549293591 scopus 로고    scopus 로고
    • Cleavage specificities of the brother and sister proteases Lys-C and Lys-N
    • Raijmakers R, Neerincx P, Mohammed S, &, Heck AJR, (2010) Cleavage specificities of the brother and sister proteases Lys-C and Lys-N. Chem Commun (Camb) 46, 8827-8829.
    • (2010) Chem Commun (Camb) , vol.46 , pp. 8827-8829
    • Raijmakers, R.1    Neerincx, P.2    Mohammed, S.3    Heck, A.J.R.4
  • 36
    • 33745837768 scopus 로고    scopus 로고
    • Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases
    • Tallant C, García-Castellanos R, Seco J, Baumann U, &, Gomis-Rüth FX, (2006) Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases. J Biol Chem 281, 17920-17928.
    • (2006) J Biol Chem , vol.281 , pp. 17920-17928
    • Tallant, C.1    García-Castellanos, R.2    Seco, J.3    Baumann, U.4    Gomis-Rüth, F.X.5
  • 37
    • 77955442476 scopus 로고    scopus 로고
    • Evaluation of metalloendopeptidase Lys-N protease performance under different sample handling conditions
    • Taouatas N, Heck AJR, &, Mohammed S, (2010) Evaluation of metalloendopeptidase Lys-N protease performance under different sample handling conditions. J Proteome Res 9, 4282-4288.
    • (2010) J Proteome Res , vol.9 , pp. 4282-4288
    • Taouatas, N.1    Heck, A.J.R.2    Mohammed, S.3
  • 38
    • 43949146287 scopus 로고    scopus 로고
    • Multiplexed proteomics mapping of yeast RNA polymerase II and III allows near-complete sequence coverage and reveals several novel phosphorylation sites
    • Mohammed S, Lorenzen K, Kerkhoven R, van Breukelen B, Vannini A, Cramer P, &, Heck AJR, (2008) Multiplexed proteomics mapping of yeast RNA polymerase II and III allows near-complete sequence coverage and reveals several novel phosphorylation sites. Anal Chem 80, 3584-3592.
    • (2008) Anal Chem , vol.80 , pp. 3584-3592
    • Mohammed, S.1    Lorenzen, K.2    Kerkhoven, R.3    Van Breukelen, B.4    Vannini, A.5    Cramer, P.6    Heck, A.J.R.7
  • 39
    • 66349106471 scopus 로고    scopus 로고
    • Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach
    • Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJR, &, Mohammed S, (2009) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem 81, 4493-4501.
    • (2009) Anal Chem , vol.81 , pp. 4493-4501
    • Gauci, S.1    Helbig, A.O.2    Slijper, M.3    Krijgsveld, J.4    Heck, A.J.R.5    Mohammed, S.6
  • 41
    • 84901945789 scopus 로고    scopus 로고
    • Confetti: A multiprotease map of the HeLa proteome for comprehensive proteomics
    • Guo X, Trudgian DC, Lemoff A, Yadavalli S, &, Mirzaei H, (2014) Confetti: a multiprotease map of the HeLa proteome for comprehensive proteomics. Mol Cell Proteomics 13, 1573-1584.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1573-1584
    • Guo, X.1    Trudgian, D.C.2    Lemoff, A.3    Yadavalli, S.4    Mirzaei, H.5
  • 42
    • 84857966803 scopus 로고    scopus 로고
    • Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography
    • Leitner A, Reischl R, Walzthoeni T, Herzog F, Bohn S, Förster F, &, Aebersold R, (2012) Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography. Mol Cell Proteomics 11, M111.014126.
    • (2012) Mol Cell Proteomics , vol.11 , pp. M111014126
    • Leitner, A.1    Reischl, R.2    Walzthoeni, T.3    Herzog, F.4    Bohn, S.5    Förster, F.6    Aebersold, R.7
  • 45
    • 84899010486 scopus 로고    scopus 로고
    • Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics
    • Benevento M, Di Palma S, Snijder J, Moyer CL, Reddy VS, Nemerow GR, &, Heck AJR, (2014) Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics. J Biol Chem 289, 11421-11430.
    • (2014) J Biol Chem , vol.289 , pp. 11421-11430
    • Benevento, M.1    Di Palma, S.2    Snijder, J.3    Moyer, C.L.4    Reddy, V.S.5    Nemerow, G.R.6    Heck, A.J.R.7
  • 47
    • 57649155302 scopus 로고    scopus 로고
    • Proteases: Multifunctional enzymes in life and disease
    • Lõpez-Otín C, &, Bond JS, (2008) Proteases: multifunctional enzymes in life and disease. J Biol Chem 283, 30433-30437.
    • (2008) J Biol Chem , vol.283 , pp. 30433-30437
    • Lõpez-Otín, C.1    Bond, J.S.2
  • 48
    • 33644545381 scopus 로고    scopus 로고
    • Tumour microenvironment - Opinion: Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • Overall CM, &, Kleifeld O, (2006) Tumour microenvironment-opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat Rev Cancer 6, 227-239.
    • (2006) Nat Rev Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 49
    • 55049133250 scopus 로고    scopus 로고
    • Metadegradomics: Toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome
    • Doucet A, Butler GS, Rodríguez D, Prudova A, &, Overall CM, (2008) Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome. Mol Cell Proteomics 7, 1925-1951.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1925-1951
    • Doucet, A.1    Butler, G.S.2    Rodríguez, D.3    Prudova, A.4    Overall, C.M.5
  • 50
    • 84864237480 scopus 로고    scopus 로고
    • Functional interplay between caspase cleavage and phosphorylation sculpts the apoptotic proteome
    • Dix MM, Simon GM, Wang C, Okerberg E, Patricelli MP, &, Cravatt BF, (2012) Functional interplay between caspase cleavage and phosphorylation sculpts the apoptotic proteome. Cell 150, 426-440.
    • (2012) Cell , vol.150 , pp. 426-440
    • Dix, M.M.1    Simon, G.M.2    Wang, C.3    Okerberg, E.4    Patricelli, M.P.5    Cravatt, B.F.6
  • 51
    • 84891804220 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings ND, Waller M, Barrett AJ, &, Bateman A, (2014) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 42, D503-D509.
    • (2014) Nucleic Acids Res , vol.42 , pp. D503-D509
    • Rawlings, N.D.1    Waller, M.2    Barrett, A.J.3    Bateman, A.4
  • 53
    • 78651069641 scopus 로고    scopus 로고
    • Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry
    • Schilling O, Huesgen PF, Barré O, Auf dem Keller U, &, Overall CM, (2011) Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry. Nat Protoc 6, 111-120.
    • (2011) Nat Protoc , vol.6 , pp. 111-120
    • Schilling, O.1    Huesgen, P.F.2    Barré, O.3    Auf Dem Keller, U.4    Overall, C.M.5
  • 54
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu CC, &, Yates JR, (2003) The application of mass spectrometry to membrane proteomics. Nat Biotechnol 21, 262-267.
    • (2003) Nat Biotechnol , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates, J.R.2
  • 57
    • 84871911898 scopus 로고    scopus 로고
    • On the size of the active site in proteases. I. Papain. 1967
    • Schechter I, &, Berger A, (2012) On the size of the active site in proteases. I. Papain. 1967. Biochem Biophys Res Commun 425, 497-502.
    • (2012) Biochem Biophys Res Commun , vol.425 , pp. 497-502
    • Schechter, I.1    Berger, A.2
  • 58
    • 0015523789 scopus 로고
    • Purification and properties of an extracellular protease of Staphylococcus aureus
    • Drapeau GR, Boily Y, &, Houmard J, (1972) Purification and properties of an extracellular protease of Staphylococcus aureus. J Biol Chem 247, 6720-6726.
    • (1972) J Biol Chem , vol.247 , pp. 6720-6726
    • Drapeau, G.R.1    Boily, Y.2    Houmard, J.3
  • 60
    • 84875787565 scopus 로고    scopus 로고
    • Data-dependent middle-down nano-liquid chromatography-electron capture dissociation-tandem mass spectrometry: An application for the analysis of unfractionated histones
    • Kalli A, Sweredoski MJ, &, Hess S, (2013) Data-dependent middle-down nano-liquid chromatography-electron capture dissociation-tandem mass spectrometry: an application for the analysis of unfractionated histones. Anal Chem 85, 3501-3507.
    • (2013) Anal Chem , vol.85 , pp. 3501-3507
    • Kalli, A.1    Sweredoski, M.J.2    Hess, S.3
  • 61
    • 84908056869 scopus 로고    scopus 로고
    • Middle-down hybrid chromatography/tandem mass spectrometry workflow for characterization of combinatorial post-translational modifications in histones
    • Sidoli S, Schwämmle V, Ruminowicz C, Hansen TA, Wu X, Helin K, &, Jensen ON, (2014) Middle-down hybrid chromatography/tandem mass spectrometry workflow for characterization of combinatorial post-translational modifications in histones. Proteomics 14, 2200-2211.
    • (2014) Proteomics , vol.14 , pp. 2200-2211
    • Sidoli, S.1    Schwämmle, V.2    Ruminowicz, C.3    Hansen, T.A.4    Wu, X.5    Helin, K.6    Jensen, O.N.7
  • 62
    • 0024342419 scopus 로고
    • Specificity of endoproteinase Asp-N (Pseudomonas fragi): Cleavage at glutamyl residues in two proteins
    • Ingrosso D, Fowler AV, Bleibaum J, &, Clarke S, (1989) Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins. Biochem Biophys Res Commun 162, 1528-1534.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 1528-1534
    • Ingrosso, D.1    Fowler, A.V.2    Bleibaum, J.3    Clarke, S.4
  • 63
    • 84910123221 scopus 로고    scopus 로고
    • Peptide scrambling during collision-induced dissociation is influenced by N-terminal residue basicity
    • Chawner R, Holman SW, Gaskell SJ, &, Eyers CE, (2014) Peptide scrambling during collision-induced dissociation is influenced by N-terminal residue basicity. J Am Soc Mass Spectrom 25, 1927-1938.
    • (2014) J Am Soc Mass Spectrom , vol.25 , pp. 1927-1938
    • Chawner, R.1    Holman, S.W.2    Gaskell, S.J.3    Eyers, C.E.4
  • 64
    • 0036882287 scopus 로고    scopus 로고
    • Protein disulfide bond determination by mass spectrometry
    • Gorman JJ, Wallis TP, &, Pitt JJ, (2002) Protein disulfide bond determination by mass spectrometry. Mass Spectrom Rev 21, 183-216.
    • (2002) Mass Spectrom Rev , vol.21 , pp. 183-216
    • Gorman, J.J.1    Wallis, T.P.2    Pitt, J.J.3
  • 65
    • 84907958801 scopus 로고    scopus 로고
    • Facilitating protein disulfide mapping by a combination of pepsin digestion, electron transfer higher energy dissociation (EThcD), and a dedicated search algorithm SlinkS
    • Liu F, van Breukelen B, &, Heck AJR, (2014) Facilitating protein disulfide mapping by a combination of pepsin digestion, electron transfer higher energy dissociation (EThcD), and a dedicated search algorithm SlinkS. Mol Cell Proteomics 13, 2776-2786.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 2776-2786
    • Liu, F.1    Van Breukelen, B.2    Heck, A.J.R.3
  • 66
    • 84891371604 scopus 로고    scopus 로고
    • Microscale immobilized enzyme reactors in proteomics: Latest developments
    • Safdar M, Spross J, &, Jänis J, (2014) Microscale immobilized enzyme reactors in proteomics: latest developments. J Chromatogr A 1324, 1-10.
    • (2014) J Chromatogr A , vol.1324 , pp. 1-10
    • Safdar, M.1    Spross, J.2    Jänis, J.3
  • 67
    • 84908565764 scopus 로고    scopus 로고
    • Hybridizing ultraviolet photodissociation with electron transfer dissociation for intact protein characterization
    • Cannon JR, Holden DD, &, Brodbelt JS, (2014) Hybridizing ultraviolet photodissociation with electron transfer dissociation for intact protein characterization. Anal Chem 86, 10970-10977.
    • (2014) Anal Chem , vol.86 , pp. 10970-10977
    • Cannon, J.R.1    Holden, D.D.2    Brodbelt, J.S.3
  • 68
    • 33749606981 scopus 로고    scopus 로고
    • Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons
    • Han X, Jin M, Breuker K, &, McLafferty FW, (2006) Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons. Science 314, 109-112.
    • (2006) Science , vol.314 , pp. 109-112
    • Han, X.1    Jin, M.2    Breuker, K.3    McLafferty, F.W.4
  • 72
    • 58149119846 scopus 로고    scopus 로고
    • Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis
    • Wang B, Malik R, Nigg EA, &, Körner R, (2008) Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem 80, 9526-9533.
    • (2008) Anal Chem , vol.80 , pp. 9526-9533
    • Wang, B.1    Malik, R.2    Nigg, E.A.3    Körner, R.4
  • 73
    • 84896784289 scopus 로고    scopus 로고
    • The top-down, middle-down, and bottom-up mass spectrometry approaches for characterization of histone variants and their post-translational modifications
    • Moradian A, Kalli A, Sweredoski MJ, &, Hess S, (2014) The top-down, middle-down, and bottom-up mass spectrometry approaches for characterization of histone variants and their post-translational modifications. Proteomics 14, 489-497.
    • (2014) Proteomics , vol.14 , pp. 489-497
    • Moradian, A.1    Kalli, A.2    Sweredoski, M.J.3    Hess, S.4
  • 74
    • 42049105662 scopus 로고    scopus 로고
    • Characterization of polyubiquitin chain structure by middle-down mass spectrometry
    • Xu P, &, Peng J, (2008) Characterization of polyubiquitin chain structure by middle-down mass spectrometry. Anal Chem 80, 3438-3444.
    • (2008) Anal Chem , vol.80 , pp. 3438-3444
    • Xu, P.1    Peng, J.2
  • 75
    • 84905714913 scopus 로고    scopus 로고
    • Middle-down mass spectrometry enables characterization of branched ubiquitin chains
    • Valkevich EM, Sanchez NA, Ge Y, &, Strieter ER, (2014) Middle-down mass spectrometry enables characterization of branched ubiquitin chains. Biochemistry 53, 4979-4989.
    • (2014) Biochemistry , vol.53 , pp. 4979-4989
    • Valkevich, E.M.1    Sanchez, N.A.2    Ge, Y.3    Strieter, E.R.4
  • 79
    • 0035852860 scopus 로고    scopus 로고
    • Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries
    • Dekker N, Cox RC, Kramer RA, &, Egmond MR, (2001) Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries. Biochemistry 40, 1694-1701.
    • (2001) Biochemistry , vol.40 , pp. 1694-1701
    • Dekker, N.1    Cox, R.C.2    Kramer, R.A.3    Egmond, M.R.4
  • 80
    • 84890055825 scopus 로고    scopus 로고
    • Proteome digestion specificity analysis for rational design of extended bottom-up and middle-down proteomics experiments
    • Laskay ÜA, Lobas AA, Srzentic K, Gorshkov MV, &, Tsybin YO, (2013) Proteome digestion specificity analysis for rational design of extended bottom-up and middle-down proteomics experiments. J Proteome Res 12, 5558-5569.
    • (2013) J Proteome Res , vol.12 , pp. 5558-5569
    • Laskay, Ü.1    Lobas, A.A.2    Srzentic, K.3    Gorshkov, M.V.4    Tsybin, Y.O.5
  • 82
    • 84906660621 scopus 로고    scopus 로고
    • Extended bottom-up proteomics with secreted aspartic protease Sap9
    • Laskay UA, Srzentic K, Monod M, &, Tsybin YO, (2014) Extended bottom-up proteomics with secreted aspartic protease Sap9. J Proteomics 110, 20-31.
    • (2014) J Proteomics , vol.110 , pp. 20-31
    • Laskay, U.A.1    Srzentic, K.2    Monod, M.3    Tsybin, Y.O.4
  • 83
    • 77956235279 scopus 로고    scopus 로고
    • Analysis of isoaspartic Acid by selective proteolysis with Asp-N and electron transfer dissociation mass spectrometry
    • Ni W, Dai S, Karger BL, &, Zhou ZS, (2010) Analysis of isoaspartic Acid by selective proteolysis with Asp-N and electron transfer dissociation mass spectrometry. Anal Chem 82, 7485-7491.
    • (2010) Anal Chem , vol.82 , pp. 7485-7491
    • Ni, W.1    Dai, S.2    Karger, B.L.3    Zhou, Z.S.4
  • 84
    • 84927649779 scopus 로고    scopus 로고
    • Genetic screens and functional genomics with CRISPR/Cas9 technology
    • Hartenian E, &, Doench JG, (2015) Genetic screens and functional genomics with CRISPR/Cas9 technology. FEBS J doi: 10.1111/febs.13248.
    • (2015) FEBS J
    • Hartenian, E.1    Doench, J.G.2
  • 85
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk K, Rötzschke O, Stevanovic S, Jung G, &, Rammensee HG, (1991) Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351, 290-296.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rötzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.G.5
  • 86
    • 0037290828 scopus 로고    scopus 로고
    • Assembly and export of MHC class i peptide ligands
    • Antoniou AN, Powis SJ, &, Elliott T, (2003) Assembly and export of MHC class I peptide ligands. Curr Opin Immunol 15, 75-81.
    • (2003) Curr Opin Immunol , vol.15 , pp. 75-81
    • Antoniou, A.N.1    Powis, S.J.2    Elliott, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.