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Volumn 35, Issue 24, 2016, Pages 2634-2657

The diverse and expanding role of mass spectrometry in structural and molecular biology

Author keywords

CRISPR Cas; ligand binding; post translational modifications; protein complexes; RNA polymerase

Indexed keywords

DEUTERIUM; HYDROGEN; MACROMOLECULE;

EID: 84995757549     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201694818     Document Type: Review
Times cited : (189)

References (263)
  • 1
    • 84923811117 scopus 로고    scopus 로고
    • The mediator complex: a central integrator of transcription
    • Allen BL, Taatjes DJ (2015) The mediator complex: a central integrator of transcription. Nat Rev Mol Cell Biol 16: 155–166
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 155-166
    • Allen, B.L.1    Taatjes, D.J.2
  • 2
    • 0034725391 scopus 로고    scopus 로고
    • Mapping protein−protein interactions in the bacteriophage T4 DNA polymerase holoenzyme using a novel trifunctional photo-cross-linking and affinity reagent
    • Alley SC, Ishmael FT, Jones AD, Benkovic SJ (2000) Mapping protein−protein interactions in the bacteriophage T4 DNA polymerase holoenzyme using a novel trifunctional photo-cross-linking and affinity reagent. J Am Chem Soc 122: 6126–6127
    • (2000) J Am Chem Soc , vol.122 , pp. 6126-6127
    • Alley, S.C.1    Ishmael, F.T.2    Jones, A.D.3    Benkovic, S.J.4
  • 3
    • 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
  • 5
    • 0141875027 scopus 로고
    • Isotopes and atomic weights
    • Aston FW (1920) Isotopes and atomic weights. Nature 105: 617–619
    • (1920) Nature , vol.105 , pp. 617-619
    • Aston, F.W.1
  • 6
    • 24944566705 scopus 로고    scopus 로고
    • Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry
    • Aye TT, Low TY, Sze SK (2005) Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry. Anal Chem 77: 5814–5822
    • (2005) Anal Chem , vol.77 , pp. 5814-5822
    • Aye, T.T.1    Low, T.Y.2    Sze, S.K.3
  • 7
    • 84986992101 scopus 로고
    • Direct chemical ionization of relatively involatile samples. Application to underivatized oligopeptides
    • Baldwin MA, McLafferty FW (1973) Direct chemical ionization of relatively involatile samples. Application to underivatized oligopeptides. Org Mass Spectrom 7: 1353–1356
    • (1973) Org Mass Spectrom , vol.7 , pp. 1353-1356
    • Baldwin, M.A.1    McLafferty, F.W.2
  • 8
    • 47249106965 scopus 로고    scopus 로고
    • Micelles protect membrane complexes from solution to vacuum
    • Barrera NP, Di Bartolo N, Booth PJ, Robinson CV (2008) Micelles protect membrane complexes from solution to vacuum. Science 321: 243–246
    • (2008) Science , vol.321 , pp. 243-246
    • Barrera, N.P.1    Di Bartolo, N.2    Booth, P.J.3    Robinson, C.V.4
  • 11
    • 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
  • 13
    • 84989008528 scopus 로고
    • Design and performance of a mass-analyzed ion kinetic energy (MIKE) spectrometer
    • Beynon JH, Cooks RG, Amy JW, Baitinger WE, Ridley TY (1973) Design and performance of a mass-analyzed ion kinetic energy (MIKE) spectrometer. Anal Chem 45: 1023A–1031A
    • (1973) Anal Chem , vol.45 , pp. 1023A-1031A
    • Beynon, J.H.1    Cooks, R.G.2    Amy, J.W.3    Baitinger, W.E.4    Ridley, T.Y.5
  • 14
    • 0025617140 scopus 로고
    • Appendix 5. Nomenclature for peptide fragment ions (positive ions)
    • Biemann K (1990) Appendix 5. Nomenclature for peptide fragment ions (positive ions). Meth Enzymol 193: 886–887
    • (1990) Meth Enzymol , vol.193 , pp. 886-887
    • Biemann, K.1
  • 16
    • 14744304574 scopus 로고    scopus 로고
    • Proteomics by FTICR mass spectrometry: top down and bottom up
    • Bogdanov B, Smith RD (2005) Proteomics by FTICR mass spectrometry: top down and bottom up. Mass Spectrom Rev 24: 168–200
    • (2005) Mass Spectrom Rev , vol.24 , pp. 168-200
    • Bogdanov, B.1    Smith, R.D.2
  • 17
    • 0031985001 scopus 로고    scopus 로고
    • Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry
    • Bothner B, Dong XF, Bibbs L, Johnson JE, Siuzdak G (1998) Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry. J Biol Chem 273: 673–676
    • (1998) J Biol Chem , vol.273 , pp. 673-676
    • Bothner, B.1    Dong, X.F.2    Bibbs, L.3    Johnson, J.E.4    Siuzdak, G.5
  • 18
    • 84896914074 scopus 로고    scopus 로고
    • Photodissociation mass spectrometry: new tools for characterization of biological molecules
    • Brodbelt JS (2014) Photodissociation mass spectrometry: new tools for characterization of biological molecules. Chem Soc Rev 43: 2757–2783
    • (2014) Chem Soc Rev , vol.43 , pp. 2757-2783
    • Brodbelt, J.S.1
  • 19
    • 84883336409 scopus 로고    scopus 로고
    • Proteomics and the analysis of proteomic data: 2013 overview of current protein-profiling technologies
    • In, Baxevanis AD, Petsko GA, Stein LD, Stormo GD, (eds), pp, Hoboken, NJ, USA, John Wiley & Sons, Inc
    • Bruce C, Stone K, Gulcicek E, Williams K (2013) Proteomics and the analysis of proteomic data: 2013 overview of current protein-profiling technologies. In Current protocols in bioinformatics, Baxevanis AD, Petsko GA, Stein LD, Stormo GD (eds), pp 13.1.1–13.1.31. Hoboken, NJ, USA: John Wiley & Sons, Inc
    • (2013) Current protocols in bioinformatics , pp. 13.1.1-13.1.31
    • Bruce, C.1    Stone, K.2    Gulcicek, E.3    Williams, K.4
  • 22
    • 84901480283 scopus 로고    scopus 로고
    • A gas phase cleavage reaction of cross-linked peptides for protein complex topology studies by peptide fragment fingerprinting from large sequence database
    • Buncherd H, Roseboom W, de Koning LJ, de Koster CG, de Jong L (2014) A gas phase cleavage reaction of cross-linked peptides for protein complex topology studies by peptide fragment fingerprinting from large sequence database. J Proteomics 108: 65–77
    • (2014) J Proteomics , vol.108 , pp. 65-77
    • Buncherd, H.1    Roseboom, W.2    de Koning, L.J.3    de Koster, C.G.4    de Jong, L.5
  • 23
    • 84955311344 scopus 로고    scopus 로고
    • High resolution CZE-MS quantitative characterization of intact biopharmaceutical proteins: proteoforms of interferon-β1
    • Bush DR, Zang L, Belov AM, Ivanov AR, Karger BL (2016) High resolution CZE-MS quantitative characterization of intact biopharmaceutical proteins: proteoforms of interferon-β1. Anal Chem 88: 1138–1146
    • (2016) Anal Chem , vol.88 , pp. 1138-1146
    • Bush, D.R.1    Zang, L.2    Belov, A.M.3    Ivanov, A.R.4    Karger, B.L.5
  • 24
    • 0037832543 scopus 로고    scopus 로고
    • Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription
    • Bushnell DA, Kornberg RD (2003) Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription. Proc Natl Acad Sci USA 100: 6969–6973
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6969-6973
    • Bushnell, D.A.1    Kornberg, R.D.2
  • 26
    • 84867045160 scopus 로고    scopus 로고
    • Current challenges in software solutions for mass spectrometry-based quantitative proteomics
    • Cappadona S, Baker PR, Cutillas PR, Heck AJR, van Breukelen B (2012) Current challenges in software solutions for mass spectrometry-based quantitative proteomics. Amino Acids 43: 1087–1108
    • (2012) Amino Acids , vol.43 , pp. 1087-1108
    • Cappadona, S.1    Baker, P.R.2    Cutillas, P.R.3    Heck, A.J.R.4    van Breukelen, B.5
  • 27
    • 84923319299 scopus 로고    scopus 로고
    • Reconstitution of active human core Mediator complex reveals a critical role of the MED14 subunit
    • Cevher MA, Shi Y, Li D, Chait BT, Malik S, Roeder RG (2014) Reconstitution of active human core Mediator complex reveals a critical role of the MED14 subunit. Nat Struct Mol Biol 21: 1028–1034
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 1028-1034
    • Cevher, M.A.1    Shi, Y.2    Li, D.3    Chait, B.T.4    Malik, S.5    Roeder, R.G.6
  • 28
    • 84877623973 scopus 로고    scopus 로고
    • Protein interactions, post-translational modifications and topologies in human cells
    • Chavez JD, Weisbrod CR, Zheng C, Eng JK, Bruce JE (2013) Protein interactions, post-translational modifications and topologies in human cells. Mol Cell Proteomics 12: 1451–1467
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1451-1467
    • Chavez, J.D.1    Weisbrod, C.R.2    Zheng, C.3    Eng, J.K.4    Bruce, J.E.5
  • 29
    • 56449114837 scopus 로고    scopus 로고
    • Comparisons of mass spectrometry compatible surfactants for global analysis of the mammalian brain proteome
    • Chen EI, McClatchy D, Park SK, Yates JR III (2008) Comparisons of mass spectrometry compatible surfactants for global analysis of the mammalian brain proteome. Anal Chem 80: 8694–8701
    • (2008) Anal Chem , vol.80 , pp. 8694-8701
    • Chen, E.I.1    McClatchy, D.2    Park, S.K.3    Yates, J.R.4
  • 30
    • 78149244661 scopus 로고    scopus 로고
    • Temperature jump and fast photochemical oxidation probe submillisecond protein folding
    • Chen J, Rempel DL, Gross ML (2010a) Temperature jump and fast photochemical oxidation probe submillisecond protein folding. J Am Chem Soc 132: 15502–15504
    • (2010) J Am Chem Soc , vol.132 , pp. 15502-15504
    • Chen, J.1    Rempel, D.L.2    Gross, M.L.3
  • 32
    • 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
  • 34
    • 10044271179 scopus 로고    scopus 로고
    • Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements
    • Clark SM, Konermann L (2004) Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements. Anal Chem 76: 7077–7083
    • (2004) Anal Chem , vol.76 , pp. 7077-7083
    • Clark, S.M.1    Konermann, L.2
  • 35
    • 0015956580 scopus 로고
    • Identification of neighbouring proteins in the ribosomes of Escherichia coli. A topographical study with the cross-linking reagent dimethyl suberimidate
    • Clegg C, Hayes D (1974) Identification of neighbouring proteins in the ribosomes of Escherichia coli. A topographical study with the cross-linking reagent dimethyl suberimidate. Eur J Biochem 42: 21–28
    • (1974) Eur J Biochem , vol.42 , pp. 21-28
    • Clegg, C.1    Hayes, D.2
  • 36
    • 0028855096 scopus 로고
    • Naked protein conformations: cytochrome c in the gas phase
    • Clemmer DE, Hudgins RR, Jarrold MF (1995) Naked protein conformations: cytochrome c in the gas phase. J Am Chem Soc 117: 10141–10142
    • (1995) J Am Chem Soc , vol.117 , pp. 10141-10142
    • Clemmer, D.E.1    Hudgins, R.R.2    Jarrold, M.F.3
  • 37
    • 0030905633 scopus 로고    scopus 로고
    • Ion mobility measurements and their applications to clusters and biomolecules
    • Clemmer DE, Jarrold MF (1997) Ion mobility measurements and their applications to clusters and biomolecules. J Mass Spectrom 32: 577–592
    • (1997) J Mass Spectrom , vol.32 , pp. 577-592
    • Clemmer, D.E.1    Jarrold, M.F.2
  • 38
    • 0029004044 scopus 로고
    • Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry
    • Cohen SL, Ferré-D'Amaré AR, Burley SK, Chait BT (1995) Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry. Protein Sci 4: 1088–1099
    • (1995) Protein Sci , vol.4 , pp. 1088-1099
    • Cohen, S.L.1    Ferré-D'Amaré, A.R.2    Burley, S.K.3    Chait, B.T.4
  • 39
    • 0002143735 scopus 로고
    • Letters to the editor The ‘Thomson’. A suggested unit for mass spectroscopists
    • Cooks RG, Rockwood AL (1991) Letters to the editor The ‘Thomson’. A suggested unit for mass spectroscopists. Rapid Commun Mass Spectrom 5: 93
    • (1991) Rapid Commun Mass Spectrom , vol.5 , pp. 93
    • Cooks, R.G.1    Rockwood, A.L.2
  • 40
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367–1372
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 41
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for data-driven systems biology
    • Cox J, Mann M (2011) Quantitative, high-resolution proteomics for data-driven systems biology. Annu Rev Biochem 80: 273–299
    • (2011) Annu Rev Biochem , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 42
    • 84883785467 scopus 로고    scopus 로고
    • Chaperone Nap1 shields histone surfaces used in a nucleosome and can put H2A-H2B in an unconventional tetrameric form
    • D'Arcy S, Martin KW, Panchenko T, Chen X, Bergeron S, Stargell LA, Black BE, Luger K (2013) Chaperone Nap1 shields histone surfaces used in a nucleosome and can put H2A-H2B in an unconventional tetrameric form. Mol Cell 51: 662–677
    • (2013) Mol Cell , vol.51 , pp. 662-677
    • D'Arcy, S.1    Martin, K.W.2    Panchenko, T.3    Chen, X.4    Bergeron, S.5    Stargell, L.A.6    Black, B.E.7    Luger, K.8
  • 44
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon B, Costello CE (1988) A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconjugate J 5: 397–409
    • (1988) Glycoconjugate J , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 46
    • 84869232519 scopus 로고    scopus 로고
    • Native tandem and ion mobility mass spectrometry highlight structural and modular similarities in clustered-regularly-interspaced shot-palindromic-repeats (CRISPR)-associated protein complexes from Escherichia coli and Pseudomonas aeruginosa
    • van Duijn E, Barbu IM, Barendregt A, Jore MM, Wiedenheft B, Lundgren M, Westra ER, Brouns SJJ, Doudna JA, van der Oost J, Heck AJR (2012) Native tandem and ion mobility mass spectrometry highlight structural and modular similarities in clustered-regularly-interspaced shot-palindromic-repeats (CRISPR)-associated protein complexes from Escherichia coli and Pseudomonas aeruginosa. Mol Cell Proteomics 11: 1430–1441
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1430-1441
    • van Duijn, E.1    Barbu, I.M.2    Barendregt, A.3    Jore, M.M.4    Wiedenheft, B.5    Lundgren, M.6    Westra, E.R.7    Brouns, S.J.J.8    Doudna, J.A.9    van der Oost, J.10    Heck, A.J.R.11
  • 48
  • 49
    • 84934889079 scopus 로고    scopus 로고
    • Tandem native mass-spectrometry on antibody-drug conjugates and submillion da antibody-antigen protein assemblies on an orbitrap EMR equipped with a high-mass quadrupole mass selector
    • Dyachenko A, Wang G, Belov M, Makarov A, de Jong RN, van den Bremer ETJ, Parren PWHI, Heck AJR (2015) Tandem native mass-spectrometry on antibody-drug conjugates and submillion da antibody-antigen protein assemblies on an orbitrap EMR equipped with a high-mass quadrupole mass selector. Anal Chem 87: 6095–6102
    • (2015) Anal Chem , vol.87 , pp. 6095-6102
    • Dyachenko, A.1    Wang, G.2    Belov, M.3    Makarov, A.4    de Jong, R.N.5    van den Bremer, E.T.J.6    Parren, P.W.H.I.7    Heck, A.J.R.8
  • 50
    • 84860487856 scopus 로고    scopus 로고
    • Quantifying ligand binding to large protein complexes using electrospray ionization mass spectrometry
    • El-Hawiet A, Kitova EN, Arutyunov D, Simpson DJ, Szymanski CM, Klassen JS (2012a) Quantifying ligand binding to large protein complexes using electrospray ionization mass spectrometry. Anal Chem 84: 3867–3870
    • (2012) Anal Chem , vol.84 , pp. 3867-3870
    • El-Hawiet, A.1    Kitova, E.N.2    Arutyunov, D.3    Simpson, D.J.4    Szymanski, C.M.5    Klassen, J.S.6
  • 51
    • 84855379601 scopus 로고    scopus 로고
    • Applications of a catch and release electrospray ionization mass spectrometry assay for carbohydrate library screening
    • El-Hawiet A, Shoemaker GK, Daneshfar R, Kitova EN, Klassen JS (2012b) Applications of a catch and release electrospray ionization mass spectrometry assay for carbohydrate library screening. Anal Chem 84: 50–58
    • (2012) Anal Chem , vol.84 , pp. 50-58
    • El-Hawiet, A.1    Shoemaker, G.K.2    Daneshfar, R.3    Kitova, E.N.4    Klassen, J.S.5
  • 54
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: a historical perspective
    • Englander SW (2006) Hydrogen exchange and mass spectrometry: a historical perspective. J Am Soc Mass Spectrom 17: 1481–1489
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 55
    • 30144441624 scopus 로고    scopus 로고
    • Hybrid quadrupole/time-of-flight mass spectrometers for analysis of biomolecules
    • Ens W, Standing KG (2005) Hybrid quadrupole/time-of-flight mass spectrometers for analysis of biomolecules. Meth Enzymol 402: 49–78
    • (2005) Meth Enzymol , vol.402 , pp. 49-78
    • Ens, W.1    Standing, K.G.2
  • 57
    • 84938674767 scopus 로고    scopus 로고
    • In cell footprinting coupled with mass spectrometry for the structural analysis of proteins in live cells
    • Espino JA, Mali VS, Jones LM (2015) In cell footprinting coupled with mass spectrometry for the structural analysis of proteins in live cells. Anal Chem 87: 7971–7978
    • (2015) Anal Chem , vol.87 , pp. 7971-7978
    • Espino, J.A.1    Mali, V.S.2    Jones, L.M.3
  • 60
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, 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
  • 62
    • 84891758507 scopus 로고    scopus 로고
    • Quantitative cross-linking/mass spectrometry using isotope-labelled cross-linkers
    • Fischer L, Chen ZA, Rappsilber J (2013) Quantitative cross-linking/mass spectrometry using isotope-labelled cross-linkers. J Proteomics 88: 120–128
    • (2013) J Proteomics , vol.88 , pp. 120-128
    • Fischer, L.1    Chen, Z.A.2    Rappsilber, J.3
  • 63
    • 0029959433 scopus 로고    scopus 로고
    • Probing the oligomeric structure of an enzyme by electrospray ionization time-of-flight mass spectrometry
    • Fitzgerald MC, Chernushevich I, Standing KG, Whitman CP, Kent SB (1996) Probing the oligomeric structure of an enzyme by electrospray ionization time-of-flight mass spectrometry. Proc Natl Acad Sci USA 93: 6851–6856
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6851-6856
    • Fitzgerald, M.C.1    Chernushevich, I.2    Standing, K.G.3    Whitman, C.P.4    Kent, S.B.5
  • 64
    • 0031866589 scopus 로고    scopus 로고
    • Comprehensive nomenclature for the fragment ions produced from collisional activation of peptide nucleic acids
    • Flora JW, Muddiman DC (1998) Comprehensive nomenclature for the fragment ions produced from collisional activation of peptide nucleic acids. Rapid Commun Mass Spectrom 12: 759–762
    • (1998) Rapid Commun Mass Spectrom , vol.12 , pp. 759-762
    • Flora, J.W.1    Muddiman, D.C.2
  • 65
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana A, Fassina G, Vita C, Dalzoppo D, Zamai M, Zambonin M (1986) Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry 25: 1847–1851
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 67
    • 0003015919 scopus 로고
    • Reaction of formaldehyde with proteins. II. Participation of the guanidyl groups and evidence of crosslinking
    • Fraenkel-Conrat H, Olcott HS (1946) Reaction of formaldehyde with proteins. II. Participation of the guanidyl groups and evidence of crosslinking. J Am Chem Soc 68: 34–37
    • (1946) J Am Chem Soc , vol.68 , pp. 34-37
    • Fraenkel-Conrat, H.1    Olcott, H.S.2
  • 68
    • 84869393114 scopus 로고    scopus 로고
    • Toward full peptide sequence coverage by dual fragmentation combining electron-transfer and higher-energy collision dissociation tandem mass spectrometry
    • Frese CK, Altelaar AFM, van den Toorn H, Nolting D, Griep-Raming J, Heck AJR, Mohammed S (2012) Toward full peptide sequence coverage by dual fragmentation combining electron-transfer and higher-energy collision dissociation tandem mass spectrometry. Anal Chem 84: 9668–9673
    • (2012) Anal Chem , vol.84 , pp. 9668-9673
    • Frese, C.K.1    Altelaar, A.F.M.2    van den Toorn, H.3    Nolting, D.4    Griep-Raming, J.5    Heck, A.J.R.6    Mohammed, S.7
  • 70
    • 0001413545 scopus 로고
    • Detection of noncovalent receptor-ligand complexes by mass spectrometry
    • Ganem B, Li YT, Henion JD (1991) Detection of noncovalent receptor-ligand complexes by mass spectrometry. J Am Chem Soc 113: 6294–6296
    • (1991) J Am Chem Soc , vol.113 , pp. 6294-6296
    • Ganem, B.1    Li, Y.T.2    Henion, J.D.3
  • 73
  • 74
    • 0032544207 scopus 로고    scopus 로고
    • Identification of the binding surface on β-lactamase for GroEL by limited proteolysis and MALDI-mass spectrometry †
    • Gervasoni P, Staudenmann W, James P, Plückthun A (1998) Identification of the binding surface on β-lactamase for GroEL by limited proteolysis and MALDI-mass spectrometry †. Biochemistry 37: 11660–11669
    • (1998) Biochemistry , vol.37 , pp. 11660-11669
    • Gervasoni, P.1    Staudenmann, W.2    James, P.3    Plückthun, A.4
  • 77
    • 33644670152 scopus 로고    scopus 로고
    • An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network
    • Guerrero C, Tagwerker C, Kaiser P, Huang L (2006) An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol Cell Proteomics 5: 366–378
    • (2006) Mol Cell Proteomics , vol.5 , pp. 366-378
    • Guerrero, C.1    Tagwerker, C.2    Kaiser, P.3    Huang, L.4
  • 78
    • 0000396852 scopus 로고
    • Metastable ion characteristics. VII. Collision-induced metastables
    • Haddon WF, McLafferty FW (1968) Metastable ion characteristics. VII. Collision-induced metastables. J Am Chem Soc 90: 4745–4746
    • (1968) J Am Chem Soc , vol.90 , pp. 4745-4746
    • Haddon, W.F.1    McLafferty, F.W.2
  • 79
    • 27844593258 scopus 로고    scopus 로고
    • Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale
    • Hambly DM, Gross ML (2005) Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale. J Am Soc Mass Spectrom 16: 2057–2063
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 2057-2063
    • Hambly, D.M.1    Gross, M.L.2
  • 81
    • 84922511434 scopus 로고    scopus 로고
    • Sheathless capillary electrophoresis-tandem mass spectrometry for top-down characterization of pyrococcus furiosus proteins on a proteome scale
    • Han X, Wang Y, Aslanian A, Bern M, Lavallée-Adam M, Yates JR III (2014b) Sheathless capillary electrophoresis-tandem mass spectrometry for top-down characterization of pyrococcus furiosus proteins on a proteome scale. Anal Chem 86: 11006–11012
    • (2014) Anal Chem , vol.86 , pp. 11006-11012
    • Han, X.1    Wang, Y.2    Aslanian, A.3    Bern, M.4    Lavallée-Adam, M.5    Yates, J.R.6
  • 82
    • 84922249668 scopus 로고    scopus 로고
    • Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex
    • Han Y, Luo J, Ranish J, Hahn S (2014c) Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex. EMBO J 33: 2534–2546
    • (2014) EMBO J , vol.33 , pp. 2534-2546
    • Han, Y.1    Luo, J.2    Ranish, J.3    Hahn, S.4
  • 84
    • 84872405841 scopus 로고    scopus 로고
    • Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
    • Heidemann M, Hintermair C, Voß K, Eick D (2013) Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription. Biochim Biophys Acta 1829: 55–62
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 55-62
    • Heidemann, M.1    Hintermair, C.2    Voß, K.3    Eick, D.4
  • 86
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C (1993) Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci USA 90: 5011–5015
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 89
    • 4644327652 scopus 로고    scopus 로고
    • Native protein mass spectrometry: from intact oligomers to functional machineries
    • van den Heuvel RHH, Heck AJR (2004) Native protein mass spectrometry: from intact oligomers to functional machineries. Curr Opin Chem Biol 8: 519–526
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 519-526
    • van den Heuvel, R.H.H.1    Heck, A.J.R.2
  • 92
    • 33745652264 scopus 로고    scopus 로고
    • Applications of ESI-MS in drug discovery: interrogation of noncovalent complexes
    • Hofstadler SA, Sannes-Lowery KA (2006) Applications of ESI-MS in drug discovery: interrogation of noncovalent complexes. Nat Rev Drug Discov 5: 585–595
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 585-595
    • Hofstadler, S.A.1    Sannes-Lowery, K.A.2
  • 94
    • 0034667929 scopus 로고    scopus 로고
    • Activated ion electron capture dissociation for mass spectral sequencing of larger (42 kDa) proteins
    • Horn DM, Ge Y, McLafferty FW (2000) Activated ion electron capture dissociation for mass spectral sequencing of larger (42 kDa) proteins. Anal Chem 72: 4778–4784
    • (2000) Anal Chem , vol.72 , pp. 4778-4784
    • Horn, D.M.1    Ge, Y.2    McLafferty, F.W.3
  • 95
    • 84920797201 scopus 로고    scopus 로고
    • Structural analyses of the CRISPR protein Csc2 reveal the RNA-binding interface of the type I-D Cas7 family
    • Hrle A, Maier LK, Sharma K, Ebert J, Basquin C, Urlaub H, Marchfelder A, Conti E (2014) Structural analyses of the CRISPR protein Csc2 reveal the RNA-binding interface of the type I-D Cas7 family. RNA Biol 11: 1072–1082
    • (2014) RNA Biol , vol.11 , pp. 1072-1082
    • Hrle, A.1    Maier, L.K.2    Sharma, K.3    Ebert, J.4    Basquin, C.5    Urlaub, H.6    Marchfelder, A.7    Conti, E.8
  • 96
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited proteolysis of native proteins
    • Hubbard SJ (1998) The structural aspects of limited proteolysis of native proteins. BBA Protein Struct Mol Enzymol 1382: 191–206
    • (1998) BBA Protein Struct Mol Enzymol , vol.1382 , pp. 191-206
    • Hubbard, S.J.1
  • 97
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling
    • Hunter T (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80: 225–236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 99
    • 84863194842 scopus 로고    scopus 로고
    • Crosslinking-MS analysis reveals RNA polymerase I domain architecture and basis of rRNA cleavage
    • Jennebach S, Herzog F, Aebersold R, Cramer P (2012) Crosslinking-MS analysis reveals RNA polymerase I domain architecture and basis of rRNA cleavage. Nucleic Acids Res 40: 5591–5601
    • (2012) Nucleic Acids Res , vol.40 , pp. 5591-5601
    • Jennebach, S.1    Herzog, F.2    Aebersold, R.3    Cramer, P.4
  • 100
    • 0001341506 scopus 로고
    • Collision-induced decompositions of aromatic molecular ions
    • Jennings KR (1968) Collision-induced decompositions of aromatic molecular ions. Int J Mass Spectrom Ion Phys 1: 227–235
    • (1968) Int J Mass Spectrom Ion Phys , vol.1 , pp. 227-235
    • Jennings, K.R.1
  • 101
    • 70349330577 scopus 로고    scopus 로고
    • The regulation of protein phosphorylation
    • Johnson LN (2009) The regulation of protein phosphorylation. Biochem Soc Trans 37: 627–641
    • (2009) Biochem Soc Trans , vol.37 , pp. 627-641
    • Johnson, L.N.1
  • 104
    • 84857385799 scopus 로고    scopus 로고
    • Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling
    • Kalisman N, Adams CM, Levitt M (2012) Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling. Proc Natl Acad Sci USA 109: 2884–2889
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 2884-2889
    • Kalisman, N.1    Adams, C.M.2    Levitt, M.3
  • 106
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, 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
  • 107
    • 0001401150 scopus 로고
    • Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry
    • Katta V, Chait BT (1991) Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry. J Am Chem Soc 113: 8534–8535
    • (1991) J Am Chem Soc , vol.113 , pp. 8534-8535
    • Katta, V.1    Chait, B.T.2
  • 108
    • 0007501806 scopus 로고
    • Hydrogen/deuterium exchange electrospray ionization mass spectrometry: a method for probing protein conformational changes in solution
    • Katta V, Chait BT (1993) Hydrogen/deuterium exchange electrospray ionization mass spectrometry: a method for probing protein conformational changes in solution. J Am Chem Soc 115: 6317–6321
    • (1993) J Am Chem Soc , vol.115 , pp. 6317-6321
    • Katta, V.1    Chait, B.T.2
  • 112
    • 0001200868 scopus 로고
    • [46] Acylation with dicarboxylic acid anhydrides
    • In, Part B., London, UK, Elsevier
    • Klapper MH, Klotz IM (1972) [46] Acylation with dicarboxylic acid anhydrides. In Enzyme structure, Part B. London, UK: Elsevier
    • (1972) Enzyme structure
    • Klapper, M.H.1    Klotz, I.M.2
  • 113
    • 84921981257 scopus 로고    scopus 로고
    • Architecture of the Saccharomyces cerevisiae RNA polymerase I core factor complex
    • Knutson BA, Luo J, Ranish J, Hahn S (2014) Architecture of the Saccharomyces cerevisiae RNA polymerase I core factor complex. Nat Struct Mol Biol 21: 810–816
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 810-816
    • Knutson, B.A.1    Luo, J.2    Ranish, J.3    Hahn, S.4
  • 114
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann L, Pan J, Liu Y (2011) Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem Soc Rev 40: 1224–1234
    • (2011) Chem Soc Rev , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.3
  • 116
    • 84923290002 scopus 로고    scopus 로고
    • Xlink analyzer: software for analysis and visualization of cross-linking data in the context of three-dimensional structures
    • Kosinski J, von Appen A, Ori A, Karius K, Müller CW, Beck M (2015) Xlink analyzer: software for analysis and visualization of cross-linking data in the context of three-dimensional structures. J Struct Biol 189: 177–183
    • (2015) J Struct Biol , vol.189 , pp. 177-183
    • Kosinski, J.1    von Appen, A.2    Ori, A.3    Karius, K.4    Müller, C.W.5    Beck, M.6
  • 121
    • 84896933849 scopus 로고    scopus 로고
    • The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics
    • Lanucara F, Holman SW, Gray CJ, Eyers CE (2014) The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics. Nat Chem 6: 281–294
    • (2014) Nat Chem , vol.6 , pp. 281-294
    • Lanucara, F.1    Holman, S.W.2    Gray, C.J.3    Eyers, C.E.4
  • 123
    • 84924663951 scopus 로고    scopus 로고
    • Computational phosphoproteomics: from identification to localization
    • Lee DCH, Jones AR, Hubbard SJ (2015) Computational phosphoproteomics: from identification to localization. Proteomics 15: 950–963
    • (2015) Proteomics , vol.15 , pp. 950-963
    • Lee, D.C.H.1    Jones, A.R.2    Hubbard, S.J.3
  • 125
    • 84980134608 scopus 로고
    • Collisional activation mass spectrometry?: a new probe for determining the structure of ions in the gas phase
    • Levsen K, Schwarz H (1976) Collisional activation mass spectrometry?: a new probe for determining the structure of ions in the gas phase. Angew Chem Int Ed Engl 15: 509–519
    • (1976) Angew Chem Int Ed Engl , vol.15 , pp. 509-519
    • Levsen, K.1    Schwarz, H.2
  • 126
    • 84921273143 scopus 로고    scopus 로고
    • From pathways to networks: connecting dots by establishing protein-protein interaction networks in signaling pathways using affinity purification and mass spectrometry
    • Li X, Wang W, Chen J (2015) From pathways to networks: connecting dots by establishing protein-protein interaction networks in signaling pathways using affinity purification and mass spectrometry. Proteomics 15: 188–202
    • (2015) Proteomics , vol.15 , pp. 188-202
    • Li, X.1    Wang, W.2    Chen, J.3
  • 127
    • 0000391706 scopus 로고
    • Observation of the multimeric forms of concanavalin A by electrospray ionization mass spectrometry
    • Light-Wahl KJ, Winger BE, Smith RD (1993) Observation of the multimeric forms of concanavalin A by electrospray ionization mass spectrometry. J Am Chem Soc 115: 5869–5870
    • (1993) J Am Chem Soc , vol.115 , pp. 5869-5870
    • Light-Wahl, K.J.1    Winger, B.E.2    Smith, R.D.3
  • 128
    • 84892629413 scopus 로고    scopus 로고
    • Measuring positive cooperativity using the direct ESI-MS assay. Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide
    • Lin HY, Kitova EN, Klassen JS (2014) Measuring positive cooperativity using the direct ESI-MS assay. Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide. J Am Soc Mass Spectrom 25: 104–110
    • (2014) J Am Soc Mass Spectrom , vol.25 , pp. 104-110
    • Lin, H.Y.1    Kitova, E.N.2    Klassen, J.S.3
  • 130
    • 74249102477 scopus 로고    scopus 로고
    • Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism
    • Liu X, Bushnell DA, Wang D, Calero G, Kornberg RD (2010) Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism. Science 327: 206–209
    • (2010) Science , vol.327 , pp. 206-209
    • Liu, X.1    Bushnell, D.A.2    Wang, D.3    Calero, G.4    Kornberg, R.D.5
  • 132
    • 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
  • 133
    • 84949106630 scopus 로고    scopus 로고
    • Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry
    • Liu F, Rijkers DTS, Post H, Heck AJR (2015) Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry. Nat Meth 12: 1179–1184
    • (2015) Nat Meth , vol.12 , pp. 1179-1184
    • Liu, F.1    Rijkers, D.T.S.2    Post, H.3    Heck, A.J.R.4
  • 134
    • 35148816658 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture
    • Lorenzen K, Vannini A, Cramer P, Heck AJR (2007) Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture. Structure 15: 1237–1245
    • (2007) Structure , vol.15 , pp. 1237-1245
    • Lorenzen, K.1    Vannini, A.2    Cramer, P.3    Heck, A.J.R.4
  • 136
    • 85010313292 scopus 로고    scopus 로고
    • Deciphering the interplay among multisite phosphorylation, interaction dynamics, and conformational transitions in a tripartite protein system
    • Lössl P, Brunner AM, Liu F, Leney AC, Yamashita M, Scheltema RA, Heck AJR (2016) Deciphering the interplay among multisite phosphorylation, interaction dynamics, and conformational transitions in a tripartite protein system. ACS Cent Sci 2: 445–455
    • (2016) ACS Cent Sci , vol.2 , pp. 445-455
    • Lössl, P.1    Brunner, A.M.2    Liu, F.3    Leney, A.C.4    Yamashita, M.5    Scheltema, R.A.6    Heck, A.J.R.7
  • 137
    • 77955435456 scopus 로고    scopus 로고
    • Ultrafast ultraviolet photodissociation at 193 nm and its applicability to proteomic workflows
    • Madsen JA, Boutz DR, Brodbelt JS (2010) Ultrafast ultraviolet photodissociation at 193 nm and its applicability to proteomic workflows. J Proteome Res 9: 4205–4214
    • (2010) J Proteome Res , vol.9 , pp. 4205-4214
    • Madsen, J.A.1    Boutz, D.R.2    Brodbelt, J.S.3
  • 139
    • 84899097282 scopus 로고    scopus 로고
    • Advances in radical probe mass spectrometry for protein footprinting in chemical biology applications
    • Maleknia SD, Downard KM (2014) Advances in radical probe mass spectrometry for protein footprinting in chemical biology applications. Chem Soc Rev 43: 3244–3258
    • (2014) Chem Soc Rev , vol.43 , pp. 3244-3258
    • Maleknia, S.D.1    Downard, K.M.2
  • 142
    • 84883466602 scopus 로고    scopus 로고
    • Twenty years of gas phase structural biology
    • Marcoux J, Robinson CV (2013) Twenty years of gas phase structural biology. Structure 21: 1541–1550
    • (2013) Structure , vol.21 , pp. 1541-1550
    • Marcoux, J.1    Robinson, C.V.2
  • 147
    • 2442527851 scopus 로고    scopus 로고
    • Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP
    • McCammon MG, Hernández H, Sobott F, Robinson CV (2004) Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP. J Am Chem Soc 126: 5950–5951
    • (2004) J Am Chem Soc , vol.126 , pp. 5950-5951
    • McCammon, M.G.1    Hernández, H.2    Sobott, F.3    Robinson, C.V.4
  • 148
    • 0031568420 scopus 로고    scopus 로고
    • Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level
    • McCormack AL, Schieltz DM, Goode B, Yang S, Barnes G, Drubin D, Yates JR III (1997) Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level. Anal Chem 69: 767–776
    • (1997) Anal Chem , vol.69 , pp. 767-776
    • McCormack, A.L.1    Schieltz, D.M.2    Goode, B.3    Yang, S.4    Barnes, G.5    Drubin, D.6    Yates, J.R.7
  • 149
    • 0032195850 scopus 로고    scopus 로고
    • Ion/ion chemistry of high-mass multiply charged ions
    • McLuckey SA, Stephenson JL (1998) Ion/ion chemistry of high-mass multiply charged ions. Mass Spectrom Rev 17: 369–407
    • (1998) Mass Spectrom Rev , vol.17 , pp. 369-407
    • McLuckey, S.A.1    Stephenson, J.L.2
  • 150
    • 69849100869 scopus 로고    scopus 로고
    • Probing protein structure by amino acid-specific covalent labeling and mass spectrometry
    • Mendoza VL, Vachet RW (2009) Probing protein structure by amino acid-specific covalent labeling and mass spectrometry. Mass Spectrom Rev 28: 785–815
    • (2009) Mass Spectrom Rev , vol.28 , pp. 785-815
    • Mendoza, V.L.1    Vachet, R.W.2
  • 152
    • 77955636430 scopus 로고    scopus 로고
    • Cleavable cross-linker for protein structure analysis: reliable identification of cross-linking products by tandem MS
    • Müller MQ, Dreiocker F, Ihling CH, Schäfer M, Sinz A (2010) Cleavable cross-linker for protein structure analysis: reliable identification of cross-linking products by tandem MS. Anal Chem 82: 6958–6968
    • (2010) Anal Chem , vol.82 , pp. 6958-6968
    • Müller, M.Q.1    Dreiocker, F.2    Ihling, C.H.3    Schäfer, M.4    Sinz, A.5
  • 153
    • 0000916259 scopus 로고
    • High pressure mass spectrometric study of alkanes 1
    • Munson MSB, Franklin JL, Field FH (1964) High pressure mass spectrometric study of alkanes 1. J Phys Chem 68: 3098–3107
    • (1964) J Phys Chem , vol.68 , pp. 3098-3107
    • Munson, M.S.B.1    Franklin, J.L.2    Field, F.H.3
  • 154
    • 33947334687 scopus 로고
    • Chemical ionization mass spectrometry. I. General introduction
    • Munson MSB, Field FH (1966) Chemical ionization mass spectrometry. I. General introduction. J Am Chem Soc 88: 2621–2630
    • (1966) J Am Chem Soc , vol.88 , pp. 2621-2630
    • Munson, M.S.B.1    Field, F.H.2
  • 157
    • 84887151962 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry of intact protein–ligand complexes for pharmaceutical drug discovery and development
    • Niu S, Rabuck JN, Ruotolo BT (2013) Ion mobility-mass spectrometry of intact protein–ligand complexes for pharmaceutical drug discovery and development. Curr Opin Chem Biol 17: 809–817
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 809-817
    • Niu, S.1    Rabuck, J.N.2    Ruotolo, B.T.3
  • 158
    • 84902533278 scopus 로고    scopus 로고
    • Unravelling the structural and mechanistic basis of CRISPR–Cas systems
    • van der Oost J, Westra ER, Jackson RN, Wiedenheft B (2014) Unravelling the structural and mechanistic basis of CRISPR–Cas systems. Nat Rev Micro 12: 479–492
    • (2014) Nat Rev Micro , vol.12 , pp. 479-492
    • van der Oost, J.1    Westra, E.R.2    Jackson, R.N.3    Wiedenheft, B.4
  • 159
    • 84958181515 scopus 로고    scopus 로고
    • Protein species-specific characterization of conformational change induced by multisite phosphorylation
    • Pan J, Zhang S, Borchers CH (2016) Protein species-specific characterization of conformational change induced by multisite phosphorylation. J Proteomics 134: 138–143
    • (2016) J Proteomics , vol.134 , pp. 138-143
    • Pan, J.1    Zhang, S.2    Borchers, C.H.3
  • 161
    • 0039219978 scopus 로고
    • Electromagnetic traps for charged and neutral particles
    • Paul W (1990) Electromagnetic traps for charged and neutral particles. Rev Mod Phys 62: 531–540
    • (1990) Rev Mod Phys , vol.62 , pp. 531-540
    • Paul, W.1
  • 162
    • 84920070787 scopus 로고    scopus 로고
    • Making proteomics data accessible and reusable: current state of proteomics databases and repositories
    • Perez-Riverol Y, Alpi E, Wang R, Hermjakob H, Vizcaíno JA (2015) Making proteomics data accessible and reusable: current state of proteomics databases and repositories. Proteomics 15: 930–950
    • (2015) Proteomics , vol.15 , pp. 930-950
    • Perez-Riverol, Y.1    Alpi, E.2    Wang, R.3    Hermjakob, H.4    Vizcaíno, J.A.5
  • 163
    • 78149438179 scopus 로고    scopus 로고
    • Crosslinking combined with mass spectrometry for structural proteomics
    • Petrotchenko EV, Borchers CH (2010) Crosslinking combined with mass spectrometry for structural proteomics. Mass Spectrom Rev 29: 862–876
    • (2010) Mass Spectrom Rev , vol.29 , pp. 862-876
    • Petrotchenko, E.V.1    Borchers, C.H.2
  • 164
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring–based proteomics: workflows, potential, pitfalls and future directions
    • Picotti P, Aebersold R (2012) Selected reaction monitoring–based proteomics: workflows, potential, pitfalls and future directions. Nat Meth 9: 555–566
    • (2012) Nat Meth , vol.9 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 165
    • 84920474229 scopus 로고    scopus 로고
    • Applications of hydrogen/deuterium exchange MS from 2012 to 2014
    • Pirrone GF, Iacob RE, Engen JR (2015) Applications of hydrogen/deuterium exchange MS from 2012 to 2014. Anal Chem 87: 99–118
    • (2015) Anal Chem , vol.87 , pp. 99-118
    • Pirrone, G.F.1    Iacob, R.E.2    Engen, J.R.3
  • 167
    • 84989038957 scopus 로고
    • The modern mass spectrometer—a complete chemical laboratory
    • Porter CJ, Beynon JH, Ast T (1981) The modern mass spectrometer—a complete chemical laboratory. Org Mass Spectrom 16: 101–114
    • (1981) Org Mass Spectrom , vol.16 , pp. 101-114
    • Porter, C.J.1    Beynon, J.H.2    Ast, T.3
  • 169
    • 0034650492 scopus 로고    scopus 로고
    • A generic strategy to analyze the spatial organization of multi-protein complexes by cross-linking and mass spectrometry
    • Rappsilber J, Siniossoglou S, Hurt EC, Mann M (2000) A generic strategy to analyze the spatial organization of multi-protein complexes by cross-linking and mass spectrometry. Anal Chem 72: 267–275
    • (2000) Anal Chem , vol.72 , pp. 267-275
    • Rappsilber, J.1    Siniossoglou, S.2    Hurt, E.C.3    Mann, M.4
  • 173
    • 84953713244 scopus 로고    scopus 로고
    • Phosphoproteomics in the age of rapid and deep proteome profiling
    • Riley NM, Coon JJ (2016) Phosphoproteomics in the age of rapid and deep proteome profiling. Anal Chem 88: 74–94
    • (2016) Anal Chem , vol.88 , pp. 74-94
    • Riley, N.M.1    Coon, J.J.2
  • 175
    • 33747190864 scopus 로고    scopus 로고
    • Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics
    • Robinette D, Neamati N, Tomer KB, Borchers CH (2006) Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics. Expert Rev Proteomics 3: 399–408
    • (2006) Expert Rev Proteomics , vol.3 , pp. 399-408
    • Robinette, D.1    Neamati, N.2    Tomer, K.B.3    Borchers, C.H.4
  • 179
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff P, Fohlman J (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed Mass Spectrom 11: 601
    • (1984) Biomed Mass Spectrom , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 180
    • 84889806552 scopus 로고    scopus 로고
    • In-depth qualitative and quantitative analysis of composite glycosylation profiles and other micro-heterogeneity on intact monoclonal antibodies by high-resolution native mass spectrometry using a modified Orbitrap
    • Rosati S, van den Bremer ETJ, Schuurman J, Parren PWHI, Kamerling JP, Heck AJR (2013) In-depth qualitative and quantitative analysis of composite glycosylation profiles and other micro-heterogeneity on intact monoclonal antibodies by high-resolution native mass spectrometry using a modified Orbitrap. mAbs 5: 917–924
    • (2013) mAbs , vol.5 , pp. 917-924
    • Rosati, S.1    van den Bremer, E.T.J.2    Schuurman, J.3    Parren, P.W.H.I.4    Kamerling, J.P.5    Heck, A.J.R.6
  • 181
    • 84897142414 scopus 로고    scopus 로고
    • Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry
    • Rosati S, Yang Y, Barendregt A, Heck AJR (2014) Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry. Nat Protoc 9: 967–976
    • (2014) Nat Protoc , vol.9 , pp. 967-976
    • Rosati, S.1    Yang, Y.2    Barendregt, A.3    Heck, A.J.R.4
  • 182
    • 84869033783 scopus 로고    scopus 로고
    • High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies
    • Rose RJ, Damoc E, Denisov E, Makarov A, Heck AJR (2012) High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies. Nat Meth 9: 1084–1086
    • (2012) Nat Meth , vol.9 , pp. 1084-1086
    • Rose, R.J.1    Damoc, E.2    Denisov, E.3    Makarov, A.4    Heck, A.J.R.5
  • 189
    • 84872614213 scopus 로고    scopus 로고
    • Structure and function of the initially transcribing RNA polymerase II–TFIIB complex
    • Sainsbury S, Niesser J, Cramer P (2012) Structure and function of the initially transcribing RNA polymerase II–TFIIB complex. Nature 493: 437–440
    • (2012) Nature , vol.493 , pp. 437-440
    • Sainsbury, S.1    Niesser, J.2    Cramer, P.3
  • 190
    • 84923804845 scopus 로고    scopus 로고
    • Structural basis of transcription initiation by RNA polymerase II
    • Sainsbury S, Bernecky C, Cramer P (2015) Structural basis of transcription initiation by RNA polymerase II. Nat Rev Mol Cell Biol 16: 129–143
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 129-143
    • Sainsbury, S.1    Bernecky, C.2    Cramer, P.3
  • 192
    • 84862219287 scopus 로고    scopus 로고
    • Investigation of protein-RNA interactions by mass spectrometry–Techniques and applications
    • Schmidt C, Kramer K, Urlaub H (2012) Investigation of protein-RNA interactions by mass spectrometry–Techniques and applications. J Proteomics 75: 3478–3494
    • (2012) J Proteomics , vol.75 , pp. 3478-3494
    • Schmidt, C.1    Kramer, K.2    Urlaub, H.3
  • 193
    • 84879967659 scopus 로고    scopus 로고
    • Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation
    • Schmidt C, Zhou M, Marriott H, Morgner N, Politis A, Robinson CV (2013) Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation. Nat Commun 4: 1985
    • (2013) Nat Commun , vol.4 , pp. 1985
    • Schmidt, C.1    Zhou, M.2    Marriott, H.3    Morgner, N.4    Politis, A.5    Robinson, C.V.6
  • 194
    • 84960799533 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited
    • Schuller JM, Beck F, Lössl P, Heck AJR, Förster F (2016) Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited. FEBS Lett 590: 595–604
    • (2016) FEBS Lett , vol.590 , pp. 595-604
    • Schuller, J.M.1    Beck, F.2    Lössl, P.3    Heck, A.J.R.4    Förster, F.5
  • 195
    • 77955952166 scopus 로고    scopus 로고
    • Molecular imaging by mass spectrometry — looking beyond classical histology
    • Schwamborn K, Caprioli RM (2010) Molecular imaging by mass spectrometry — looking beyond classical histology. Nat Rev Cancer 10: 639–646
    • (2010) Nat Rev Cancer , vol.10 , pp. 639-646
    • Schwamborn, K.1    Caprioli, R.M.2
  • 196
    • 0001051186 scopus 로고
    • Observation of noncovalent complexes to the avidin tetramer by electrospray ionization mass spectrometry
    • Schwartz BL, Light-Wahl KJ, Smith RD (1994) Observation of noncovalent complexes to the avidin tetramer by electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 5: 201–204
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 201-204
    • Schwartz, B.L.1    Light-Wahl, K.J.2    Smith, R.D.3
  • 203
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz A (2003) Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J Mass Spectrom 38: 1225–1237
    • (2003) J Mass Spectrom , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 205
    • 0039901639 scopus 로고
    • Ionization and dissociation of polyatomic molecules by electron impact I. Methane
    • Smith LG (1937) Ionization and dissociation of polyatomic molecules by electron impact I. Methane. Phys Rev 51: 263–275
    • (1937) Phys Rev , vol.51 , pp. 263-275
    • Smith, L.G.1
  • 206
    • 84904342151 scopus 로고    scopus 로고
    • Analytical approaches for size and mass analysis of large protein assemblies
    • Snijder J, Heck AJR (2014) Analytical approaches for size and mass analysis of large protein assemblies. Annu Rev Anal Chem 7: 43–64
    • (2014) Annu Rev Anal Chem , vol.7 , pp. 43-64
    • Snijder, J.1    Heck, A.J.R.2
  • 208
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott F, Hernández H, McCammon MG, Tito MA, Robinson CV (2002) A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal Chem 74: 1402–1407
    • (2002) Anal Chem , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernández, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 209
    • 33845310551 scopus 로고    scopus 로고
    • Collision-induced dissociative chemical cross-linking reagents and methodology: applications to protein structural characterization using tandem mass spectrometry analysis
    • Soderblom EJ, Goshe MB (2006) Collision-induced dissociative chemical cross-linking reagents and methodology: applications to protein structural characterization using tandem mass spectrometry analysis. Anal Chem 78: 8059–8068
    • (2006) Anal Chem , vol.78 , pp. 8059-8068
    • Soderblom, E.J.1    Goshe, M.B.2
  • 212
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen H, Mann M (2004) The ABC's (and XYZ's) of peptide sequencing. Nat Rev Mol Cell Biol 5: 699–711
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 213
    • 85006218273 scopus 로고    scopus 로고
    • Mass spectra
    • In, Linstrom PJ, Mallard WG, (eds)., Gaithersburg, MD, National Institute of Standards and Technology, (accessed March 3, 2016)
    • Stein SE (2016) Mass spectra. In NIST chemistry webbook: NIST standard reference database number 69, Linstrom PJ, Mallard WG (eds). Gaithersburg, MD: National Institute of Standards and Technology, http://webbook.nist.gov (accessed: March 3, 2016)
    • (2016) NIST chemistry webbook: NIST standard reference database number 69
    • Stein, S.E.1
  • 214
    • 12044260066 scopus 로고
    • Matrix-assisted laser desorption ionization mass spectrometry of proteins electroblotted after polyacrylamide gel electrophoresis
    • Strupat K, Karas M, Hillenkamp F, Eckerskorn C, Lottspeich F (1994) Matrix-assisted laser desorption ionization mass spectrometry of proteins electroblotted after polyacrylamide gel electrophoresis. Anal Chem 66: 464–470
    • (1994) Anal Chem , vol.66 , pp. 464-470
    • Strupat, K.1    Karas, M.2    Hillenkamp, F.3    Eckerskorn, C.4    Lottspeich, F.5
  • 216
    • 0016171640 scopus 로고
    • Topography of ribosomal proteins of the Escherichia coli 30S subunit as studied with the reversible cross-linking reagent methyl 4-mercaptobutyrimidate
    • Sun TT, Bollen A, Kahan L, Traut RR (1974) Topography of ribosomal proteins of the Escherichia coli 30S subunit as studied with the reversible cross-linking reagent methyl 4-mercaptobutyrimidate. Biochemistry 13: 2334–2340
    • (1974) Biochemistry , vol.13 , pp. 2334-2340
    • Sun, T.T.1    Bollen, A.2    Kahan, L.3    Traut, R.R.4
  • 217
    • 33846269339 scopus 로고    scopus 로고
    • Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors
    • Swaney DL, McAlister GC, Wirtala M, Schwartz JC, Syka JEP, Coon JJ (2007) Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors. Anal Chem 79: 477–485
    • (2007) Anal Chem , vol.79 , pp. 477-485
    • Swaney, D.L.1    McAlister, G.C.2    Wirtala, M.3    Schwartz, J.C.4    Syka, J.E.P.5    Coon, J.J.6
  • 219
    • 33749240797 scopus 로고    scopus 로고
    • Probing genuine strong interactions and post-translational modifications in the heterogeneous yeast exosome protein complex
    • Synowsky SA, van den Heuvel RHH, Mohammed S, Pijnappel PWWM, Heck AJR (2006) Probing genuine strong interactions and post-translational modifications in the heterogeneous yeast exosome protein complex. Mol Cell Proteomics 5: 1581–1592
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1581-1592
    • Synowsky, S.A.1    van den Heuvel, R.H.H.2    Mohammed, S.3    Pijnappel, P.W.W.M.4    Heck, A.J.R.5
  • 220
    • 0037133237 scopus 로고    scopus 로고
    • Top-down mass spectrometry of a 29-kDa protein for characterization of any post-translational modification to within one residue
    • Sze SK, Ge Y, Oh H, McLafferty FW (2002) Top-down mass spectrometry of a 29-kDa protein for characterization of any post-translational modification to within one residue. Proc Natl Acad Sci USA 99: 1774–1779
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1774-1779
    • Sze, S.K.1    Ge, Y.2    Oh, H.3    McLafferty, F.W.4
  • 221
    • 84885675848 scopus 로고    scopus 로고
    • Quality assessment for clinical proteomics
    • Tabb DL (2013) Quality assessment for clinical proteomics. Clin Biochem 46: 411–420
    • (2013) Clin Biochem , vol.46 , pp. 411-420
    • Tabb, D.L.1
  • 224
    • 0001442182 scopus 로고
    • Cathode rays
    • Thomson JJ (1897) Cathode rays. Philos Mag 44: 293–316
    • (1897) Philos Mag , vol.44 , pp. 293-316
    • Thomson, J.J.1
  • 225
    • 0000331003 scopus 로고
    • XXVI. Rays of positive electricity
    • Thomson JJ (1911) XXVI. Rays of positive electricity. Philos Mag 21: 225–249
    • (1911) Philos Mag , vol.21 , pp. 225-249
    • Thomson, J.J.1
  • 227
    • 84940985057 scopus 로고    scopus 로고
    • Conformational analysis of large and highly disulfide-stabilized proteins by integrating online electrochemical reduction into an optimized H/D exchange mass spectrometry workflow
    • Trabjerg E, Jakobsen RU, Mysling S, Christensen S, Jørgensen TJD, Rand KD (2015) Conformational analysis of large and highly disulfide-stabilized proteins by integrating online electrochemical reduction into an optimized H/D exchange mass spectrometry workflow. Anal Chem 87: 8880–8888
    • (2015) Anal Chem , vol.87 , pp. 8880-8888
    • Trabjerg, E.1    Jakobsen, R.U.2    Mysling, S.3    Christensen, S.4    Jørgensen, T.J.D.5    Rand, K.D.6
  • 228
    • 68049099249 scopus 로고    scopus 로고
    • Multiplexed size separation of intact proteins in solution phase for mass spectrometry
    • Tran JC, Doucette AA (2009) Multiplexed size separation of intact proteins in solution phase for mass spectrometry. Anal Chem 81: 6201–6209
    • (2009) Anal Chem , vol.81 , pp. 6201-6209
    • Tran, J.C.1    Doucette, A.A.2
  • 230
    • 84937245669 scopus 로고    scopus 로고
    • Proteomics beyond trypsin
    • Tsiatsiani L, Heck AJR (2015) Proteomics beyond trypsin. FEBS J 282: 2612–2626
    • (2015) FEBS J , vol.282 , pp. 2612-2626
    • Tsiatsiani, L.1    Heck, A.J.R.2
  • 232
  • 235
    • 84959558618 scopus 로고    scopus 로고
    • Load-dependent destabilization of the γ-rotor shaft in F O F 1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry
    • Vahidi S, Bi Y, Dunn SD, Konermann L (2016) Load-dependent destabilization of the γ-rotor shaft in F O F 1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry. Proc Natl Acad Sci USA 113: 2412–2417
    • (2016) Proc Natl Acad Sci USA , vol.113 , pp. 2412-2417
    • Vahidi, S.1    Bi, Y.2    Dunn, S.D.3    Konermann, L.4
  • 236
    • 84875249328 scopus 로고    scopus 로고
    • A structural perspective on RNA polymerase I and RNA polymerase III transcription machineries
    • Vannini A (2013) A structural perspective on RNA polymerase I and RNA polymerase III transcription machineries. BBA-Gene Regul Mech 1829: 258–264
    • (2013) BBA-Gene Regul Mech , vol.1829 , pp. 258-264
    • Vannini, A.1
  • 238
    • 84868575176 scopus 로고    scopus 로고
    • Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment
    • Walters BT, Ricciuti A, Mayne L, Englander SW (2012) Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment. J Am Soc Mass Spectrom 23: 2132–2139
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 2132-2139
    • Walters, B.T.1    Ricciuti, A.2    Mayne, L.3    Englander, S.W.4
  • 240
    • 0035019857 scopus 로고    scopus 로고
    • Detecting structural changes in viral capsids by hydrogen exchange and mass spectrometry
    • Wang L, Lane LC, Smith DL (2001) Detecting structural changes in viral capsids by hydrogen exchange and mass spectrometry. Protein Sci 10: 1234–1243
    • (2001) Protein Sci , vol.10 , pp. 1234-1243
    • Wang, L.1    Lane, L.C.2    Smith, D.L.3
  • 241
    • 0141958921 scopus 로고    scopus 로고
    • Influence of solution and gas phase processes on protein−carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry
    • Wang W, Kitova EN, Klassen JS (2003) Influence of solution and gas phase processes on protein−carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 75: 4945–4955
    • (2003) Anal Chem , vol.75 , pp. 4945-4955
    • Wang, W.1    Kitova, E.N.2    Klassen, J.S.3
  • 243
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR III (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19: 242–247
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 245
    • 84875913034 scopus 로고    scopus 로고
    • In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy
    • Weisbrod CR, Chavez JD, Eng JK, Yang L, Zheng C, Bruce JE (2013) In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy. J Proteome Res 12: 1569–1579
    • (2013) J Proteome Res , vol.12 , pp. 1569-1579
    • Weisbrod, C.R.1    Chavez, J.D.2    Eng, J.K.3    Yang, L.4    Zheng, C.5    Bruce, J.E.6
  • 249
    • 84878105806 scopus 로고    scopus 로고
    • Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly
    • Woods LA, Radford SE, Ashcroft AE (2013) Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly. Biochim Biophys Acta 1834: 1257–1268
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1257-1268
    • Woods, L.A.1    Radford, S.E.2    Ashcroft, A.E.3
  • 250
    • 84954214717 scopus 로고    scopus 로고
    • Biology and applications of CRISPR systems: harnessing nature's toolbox for genome engineering
    • Wright AV, Nuñez JK, Doudna JA (2016) Biology and applications of CRISPR systems: harnessing nature's toolbox for genome engineering. Cell 164: 29–44
    • (2016) Cell , vol.164 , pp. 29-44
    • Wright, A.V.1    Nuñez, J.K.2    Doudna, J.A.3
  • 254
    • 84890453080 scopus 로고    scopus 로고
    • Analyzing protein micro-heterogeneity in chicken ovalbumin by high-resolution native mass spectrometry exposes qualitatively and semi-quantitatively 59 proteoforms
    • Yang Y, Barendregt A, Kamerling JP, Heck AJR (2013) Analyzing protein micro-heterogeneity in chicken ovalbumin by high-resolution native mass spectrometry exposes qualitatively and semi-quantitatively 59 proteoforms. Anal Chem 85: 12037–12045
    • (2013) Anal Chem , vol.85 , pp. 12037-12045
    • Yang, Y.1    Barendregt, A.2    Kamerling, J.P.3    Heck, A.J.R.4
  • 255
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • Young MM, Tang N, Hempel JC, Oshiro CM, Taylor EW, Kuntz ID, Gibson BW, Dollinger G (2000) High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc Natl Acad Sci USA 97: 5802–5806
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5802-5806
    • Young, M.M.1    Tang, N.2    Hempel, J.C.3    Oshiro, C.M.4    Taylor, E.W.5    Kuntz, I.D.6    Gibson, B.W.7    Dollinger, G.8
  • 256
    • 67749127567 scopus 로고    scopus 로고
    • Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution
    • Zehl M, Rand KD, Jensen ON, Jørgensen TJD (2008) Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution. J Am Chem Soc 130: 17453–17459
    • (2008) J Am Chem Soc , vol.130 , pp. 17453-17459
    • Zehl, M.1    Rand, K.D.2    Jensen, O.N.3    Jørgensen, T.J.D.4
  • 258
    • 84876148755 scopus 로고    scopus 로고
    • Protein analysis by shotgun/bottom-up proteomics
    • Zhang Y, Fonslow BR, Shan B, Baek M, Yates JR III (2013) Protein analysis by shotgun/bottom-up proteomics. Chem Rev 113: 2343–2394
    • (2013) Chem Rev , vol.113 , pp. 2343-2394
    • Zhang, Y.1    Fonslow, B.R.2    Shan, B.3    Baek, M.4    Yates, J.R.5
  • 261
    • 84898915327 scopus 로고    scopus 로고
    • Surface induced dissociation: dissecting noncovalent protein complexes in the gas phase
    • Zhou M, Wysocki VH (2014) Surface induced dissociation: dissecting noncovalent protein complexes in the gas phase. Acc Chem Res 47: 1010–1018
    • (2014) Acc Chem Res , vol.47 , pp. 1010-1018
    • Zhou, M.1    Wysocki, V.H.2
  • 262
    • 1242351309 scopus 로고    scopus 로고
    • Electron-capture dissociation tandem mass spectrometry
    • Zubarev RA (2004) Electron-capture dissociation tandem mass spectrometry. Curr Opin Biotech 15: 12–16
    • (2004) Curr Opin Biotech , vol.15 , pp. 12-16
    • Zubarev, R.A.1
  • 263
    • 84878633937 scopus 로고    scopus 로고
    • Orbitrap mass spectrometry
    • Zubarev RA, Makarov A (2013) Orbitrap mass spectrometry. Anal Chem 85: 5288–5296
    • (2013) Anal Chem , vol.85 , pp. 5288-5296
    • Zubarev, R.A.1    Makarov, A.2


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