메뉴 건너뛰기




Volumn 102, Issue 2, 2012, Pages 245-265

Mass spectrometry studies of protein folding

Author keywords

Hydrogen deuterium exchange; Macromolecular assembly; Mass spectrometry; Protein folding and aggregation

Indexed keywords


EID: 84864807757     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (208)
  • 1
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J. and Wright, P. E., Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol., 2002, 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 2
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded? Eur
    • Uversky, V. N., What does it mean to be natively unfolded? Eur. J. Biochem., 2002, 269, 2-12.
    • (2002) J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 3
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A. L., Natively unfolded proteins. Curr. Opin. Struct. Biol., 2005, 15, 35-41.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 4
    • 0015597839 scopus 로고
    • Nucleation, rapid folding, and globular intrachain regions in proteins
    • Wetlaufer, D. B., Nucleation, rapid folding, and globular intrachain regions in proteins. Proc. Natl. Acad. Sci. USA, 1973, 70, 697-701.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1
  • 5
    • 0015243226 scopus 로고
    • Analysis of the code relating sequence to conformation in proteins: possible implications for the mechanism of formation of helical regions
    • Robson, B. and Pain, R. H., Analysis of the code relating sequence to conformation in proteins: possible implications for the mechanism of formation of helical regions. J. Mol. Biol., 1971, 58, 237-259.
    • (1971) J. Mol. Biol. , vol.58 , pp. 237-259
    • Robson, B.1    Pain, R.H.2
  • 6
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K. A., Theory for the folding and stability of globular proteins. Biochemistry, 1985, 24, 1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 7
    • 0028944346 scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • Gutin, A. M., Abkevich, V. I. and Shakhnovich, E. I., Is burst hydrophobic collapse necessary for protein folding? Biochemistry, 1995, 34, 3066-3076.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 8
    • 0015920746 scopus 로고
    • Stages in the mechanism of self-organization of protein molecules
    • Ptitsyn, O. B., Stages in the mechanism of self-organization of protein molecules. Dokl. Akad. Nauk SSSR, 1973, 210, 1213-1215.
    • (1973) Dokl. Akad. Nauk SSSR , vol.210 , pp. 1213-1215
    • Ptitsyn, O.B.1
  • 9
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P. S. and Baldwin, R. L., Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem., 1982, 51, 459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 10
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • Udgaonkar, J. B. and Baldwin, R. L., NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature, 1988, 335, 694-699.
    • (1988) Nature , vol.335 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 11
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleationcondensation mechanism for protein folding
    • Itzhaki, L. S., Otzen, D. E. and Fersht, A. R., The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleationcondensation mechanism for protein folding. J. Mol. Biol., 1995, 254, 260-288.
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 12
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications
    • Fersht, A. R., Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. USA, 1995, 92, 10869-10873.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 13
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding? Trends Biochem
    • Daggett, V. and Fersht, A. R., Is there a unifying mechanism for protein folding? Trends Biochem. Sci., 2003, 28, 18-25.
    • (2003) Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 14
    • 0343368213 scopus 로고
    • The stabilities of globular proteins
    • Dill, K. A., The stabilities of globular proteins. Protein Eng., 1987, 16, 187-192.
    • (1987) Protein Eng. , vol.16 , pp. 187-192
    • Dill, K.A.1
  • 16
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. and Chan, H. S., From Levinthal to pathways to funnels. Nature Struct. Biol., 1997, 4, 10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 17
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold? Fold
    • Jackson, S. E., How do small single-domain proteins fold? Fold. Des., 1998, 3, R81-R91.
    • (1998) Des. , vol.3
    • Jackson, S.E.1
  • 18
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sanchez, I. E. and Kiefhaber, T., Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol., 2003, 325, 367-376.
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 19
    • 33748675500 scopus 로고    scopus 로고
    • Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states
    • Korzhnev, D. M., Neudecker, P., Zarrine-Afsar, A., Davidson, A. R. and Kay, L. E., Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states. Biochemistry, 2006, 45, 10175-10183.
    • (2006) Biochemistry , vol.45 , pp. 10175-10183
    • Korzhnev, D.M.1    Neudecker, P.2    Zarrine-Afsar, A.3    Davidson, A.R.4    Kay, L.E.5
  • 20
    • 61649112900 scopus 로고    scopus 로고
    • Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase
    • Wani, A. H. and Udgaonkar, J. B., Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase. J. Mol. Biol., 2009, 387, 348-362.
    • (2009) J. Mol. Biol. , vol.387 , pp. 348-362
    • Wani, A.H.1    Udgaonkar, J.B.2
  • 22
    • 0035965128 scopus 로고    scopus 로고
    • Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9
    • Gorski, S. A., Capaldi, A. P., Kleanthous, C. and Radford, S. E., Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9. J. Mol. Biol., 2001, 312, 849-863.
    • (2001) J. Mol. Biol. , vol.312 , pp. 849-863
    • Gorski, S.A.1    Capaldi, A.P.2    Kleanthous, C.3    Radford, S.E.4
  • 23
    • 33748774168 scopus 로고    scopus 로고
    • HX-ESI-MS and optical studies of the unfolding of thioredoxin indicate stabilization of a partially unfolded, aggregation-competent intermediate at low pH
    • Wani, A. H. and Udgaonkar, J. B., HX-ESI-MS and optical studies of the unfolding of thioredoxin indicate stabilization of a partially unfolded, aggregation-competent intermediate at low pH. Biochemistry, 2006, 45, 11226-11238.
    • (2006) Biochemistry , vol.45 , pp. 11226-11238
    • Wani, A.H.1    Udgaonkar, J.B.2
  • 24
    • 48249140760 scopus 로고    scopus 로고
    • Multiple routes and structural heterogeneity in protein folding
    • Udgaonkar, J. B., Multiple routes and structural heterogeneity in protein folding. Annu. Rev. Biophys., 2008, 37, 489-510.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 489-510
    • Udgaonkar, J.B.1
  • 26
    • 0037614975 scopus 로고    scopus 로고
    • Quaternary structure of aldolase leads to differences in folding and unfolding intermediates
    • Pan, H. and Smith, D. L., Quaternary structure of aldolase leads to differences in folding and unfolding intermediates. Biochemistry, 2003, 42, 5713-5721.
    • (2003) Biochemistry , vol.42 , pp. 5713-5721
    • Pan, H.1    Smith, D.L.2
  • 28
    • 70350492887 scopus 로고    scopus 로고
    • Linear quadrupoles in mass spectrometry
    • Douglas, D. J., Linear quadrupoles in mass spectrometry. Mass Spectrom. Rev., 2009, 28, 937-960.
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 937-960
    • Douglas, D.J.1
  • 29
    • 68949157005 scopus 로고    scopus 로고
    • Mass spectrometry: from proteomics to metabolomics and lipidomics
    • Griffiths, W. J. and Wang, Y., Mass spectrometry: from proteomics to metabolomics and lipidomics. Chem. Soc. Rev., 2009, 38, 1882-1896.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 1882-1896
    • Griffiths, W.J.1    Wang, Y.2
  • 31
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: approaches, advances, and applications
    • Yates, J. R., Ruse, C. I. and Nakorchevsky, A., Proteomics by mass spectrometry: approaches, advances, and applications. Annu. Rev. Biomed. Eng., 2009, 11, 49-79.
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 32
    • 0033557450 scopus 로고    scopus 로고
    • Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/ protein interactions
    • Ehring, H., Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/ protein interactions. Anal. Biochem., 1999, 267, 252-259.
    • (1999) Anal. Biochem. , vol.267 , pp. 252-259
    • Ehring, H.1
  • 33
    • 33750602591 scopus 로고    scopus 로고
    • Ions of the interactome: the role of MS in the study of protein interactions in proteomics and structural biology
    • Downard, K. M., Ions of the interactome: the role of MS in the study of protein interactions in proteomics and structural biology. Proteomics, 2006, 6, 5374-5384.
    • (2006) Proteomics , vol.6 , pp. 5374-5384
    • Downard, K.M.1
  • 35
    • 33744542891 scopus 로고    scopus 로고
    • Protein interactions probed with mass spectrometry
    • Kaveti, S. and Engen, J. R., Protein interactions probed with mass spectrometry. Methods Mol. Biol., 2006, 316, 179-197.
    • (2006) Methods Mol. Biol. , vol.316 , pp. 179-197
    • Kaveti, S.1    Engen, J.R.2
  • 36
    • 49149112494 scopus 로고    scopus 로고
    • Identification of proteins based on MS/MS spectra and location of posttranslational modifications
    • Stone, K. L., Crawford, M., McMurray, W., Williams, N. and Williams, K. R., Identification of proteins based on MS/MS spectra and location of posttranslational modifications. Methods Mol. Biol., 2007, 386, 57-77.
    • (2007) Methods Mol. Biol. , vol.386 , pp. 57-77
    • Stone, K.L.1    Crawford, M.2    McMurray, W.3    Williams, N.4    Williams, K.R.5
  • 37
    • 55949131766 scopus 로고    scopus 로고
    • Identification of four novel types of in vitro protein modifications
    • Xing, G., Zhang, J., Chen, Y. and Zhao, Y., Identification of four novel types of in vitro protein modifications. J. Proteome Res., 2008, 7, 4603-4608.
    • (2008) J. Proteome Res. , vol.7 , pp. 4603-4608
    • Xing, G.1    Zhang, J.2    Chen, Y.3    Zhao, Y.4
  • 38
    • 67650303382 scopus 로고    scopus 로고
    • A complex assembly landscape for the 30S ribosomal subunit
    • Sykes, M. T. and Williamson, J. R., A complex assembly landscape for the 30S ribosomal subunit. Annu. Rev. Biophys., 2009, 38, 197-215.
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 197-215
    • Sykes, M.T.1    Williamson, J.R.2
  • 39
    • 77957235518 scopus 로고    scopus 로고
    • Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif
    • Marcsisin, S. R. and Engen, J. R., Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif. J. Mol. Biol., 2010, 402, 892-904.
    • (2010) J. Mol. Biol. , vol.402 , pp. 892-904
    • Marcsisin, S.R.1    Engen, J.R.2
  • 40
    • 79959452019 scopus 로고    scopus 로고
    • Capturing protein structural kinetics by mass spectrometry
    • Ben-Nissan, G. and Sharon, M., Capturing protein structural kinetics by mass spectrometry. Chem. Soc. Rev., 2011, 40, 3627-3637.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 3627-3637
    • Ben-Nissan, G.1    Sharon, M.2
  • 42
    • 0025411841 scopus 로고
    • Effect of reducing disulfide-containing proteins on electrospray ionization mass spectra
    • Loo, J. A., Edmonds, C. G., Udseth, H. R. and Smith, R. D., Effect of reducing disulfide-containing proteins on electrospray ionization mass spectra. Anal. Chem., 1990, 62, 693-698.
    • (1990) Anal. Chem. , vol.62 , pp. 693-698
    • Loo, J.A.1    Edmonds, C.G.2    Udseth, H.R.3    Smith, R.D.4
  • 43
    • 0026134908 scopus 로고
    • Conformational changes in proteins probed by hydrogen-exchange electrospray-ionization mass spectrometry
    • Katta, V. and Chait, B. T., Conformational changes in proteins probed by hydrogen-exchange electrospray-ionization mass spectrometry. Rapid Commun. Mass Spectrom., 1991, 5, 214-217.
    • (1991) Rapid Commun. Mass Spectrom. , vol.5 , pp. 214-217
    • Katta, V.1    Chait, B.T.2
  • 44
    • 0001510590 scopus 로고
    • Ion formation from charged droplets: roles of geometry, energy and time
    • Fenn, J. B., Ion formation from charged droplets: roles of geometry, energy and time. J. Am. Soc. Mass Spectrom., 1993, 4, 524-535.
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 524-535
    • Fenn, J.B.1
  • 45
    • 0030827122 scopus 로고    scopus 로고
    • Acid-induced unfolding of cytochrome c at different methanol concentrations: electrospray ionization mass spectrometry specifically monitors changes in the tertiary structure
    • Konermann, L. and Douglas, D. J., Acid-induced unfolding of cytochrome c at different methanol concentrations: electrospray ionization mass spectrometry specifically monitors changes in the tertiary structure. Biochemistry, 1997, 36, 12296-12302.
    • (1997) Biochemistry , vol.36 , pp. 12296-12302
    • Konermann, L.1    Douglas, D.J.2
  • 46
    • 16544379725 scopus 로고    scopus 로고
    • Interpreting conformational effects in protein nano-ESI-MS spectra
    • Samalikova, M., Matecko, I., Muller, N. and Grandori, R., Interpreting conformational effects in protein nano-ESI-MS spectra. Anal. Bioanal. Chem., 2004, 378, 1112-1123.
    • (2004) Anal. Bioanal. Chem. , vol.378 , pp. 1112-1123
    • Samalikova, M.1    Matecko, I.2    Muller, N.3    Grandori, R.4
  • 47
    • 0030919476 scopus 로고    scopus 로고
    • Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry
    • Konermann, L., Rosell, F. I., Mauk, A. G. and Douglas, D. J., Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry. Biochemistry, 1997, 36, 6448-6454.
    • (1997) Biochemistry , vol.36 , pp. 6448-6454
    • Konermann, L.1    Rosell, F.I.2    Mauk, A.G.3    Douglas, D.J.4
  • 48
    • 0034727681 scopus 로고    scopus 로고
    • Methanol-induced conformations of myoglobin at pH 4.0
    • Babu, K. R. and Douglas, D. J., Methanol-induced conformations of myoglobin at pH 4.0. Biochemistry, 2002, 39, 14702-14710.
    • (2002) Biochemistry , vol.39 , pp. 14702-14710
    • Babu, K.R.1    Douglas, D.J.2
  • 49
    • 0035563698 scopus 로고    scopus 로고
    • The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: a study by electrospray ionization mass spectrometry
    • Babu, K. R., Moradian, A. and Douglas, D. J., The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: a study by electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom., 2001, 12, 317-328.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 317-328
    • Babu, K.R.1    Moradian, A.2    Douglas, D.J.3
  • 50
    • 0037544036 scopus 로고    scopus 로고
    • Interlobe communication in human serum transferrin: metal binding and conformational dynamics investigated by electrospray ionization mass spectrometry
    • Gumerov, D. R., Mason, A. B. and Kaltashov, I. A., Interlobe communication in human serum transferrin: metal binding and conformational dynamics investigated by electrospray ionization mass spectrometry. Biochemistry, 2003, 42, 5421-5428.
    • (2003) Biochemistry , vol.42 , pp. 5421-5428
    • Gumerov, D.R.1    Mason, A.B.2    Kaltashov, I.A.3
  • 51
    • 0030069246 scopus 로고    scopus 로고
    • Study of the new stability properties induced by amino acid replacement of tyrosine 64 in cytochrome C553 from Desulfovibrio vulgaris Hildenborough using electrospray ionization mass spectrometry
    • Guy, P., Remigy, H., Jaquinod, M., Bersch, B., Blanchard, L., Dolla, A. and Forest, E., Study of the new stability properties induced by amino acid replacement of tyrosine 64 in cytochrome C553 from Desulfovibrio vulgaris Hildenborough using electrospray ionization mass spectrometry. Biochem. Biophys. Res. Commun., 1996, 218, 97-103.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 97-103
    • Guy, P.1    Remigy, H.2    Jaquinod, M.3    Bersch, B.4    Blanchard, L.5    Dolla, A.6    Forest, E.7
  • 52
    • 0041471397 scopus 로고    scopus 로고
    • Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry
    • Griffith, W. P. and Kaltashov, I. A., Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry. Biochemistry, 2003, 42, 10024-10033.
    • (2003) Biochemistry , vol.42 , pp. 10024-10033
    • Griffith, W.P.1    Kaltashov, I.A.2
  • 53
    • 78649605961 scopus 로고    scopus 로고
    • Observation of symmetric denaturation of hemoglobin subunits by electrospray ionization mass spectrometry
    • Wang, X., Zhao, W., Lin, X., Su, B. and Liu, J., Observation of symmetric denaturation of hemoglobin subunits by electrospray ionization mass spectrometry. Mass Spectrom. Rev., 2010, 45, 1306-1311.
    • (2010) Mass Spectrom. Rev. , vol.45 , pp. 1306-1311
    • Wang, X.1    Zhao, W.2    Lin, X.3    Su, B.4    Liu, J.5
  • 54
    • 0031918412 scopus 로고    scopus 로고
    • Equilibrium unfolding of proteins monitored by electrospray ionization mass spectrometry: distinguishing two-state from multi-state transitions
    • Konermann, L. and Douglas, D. J., Equilibrium unfolding of proteins monitored by electrospray ionization mass spectrometry: distinguishing two-state from multi-state transitions. Rapid Commun. Mass Spectrom., 1998, 12, 435-442.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 435-442
    • Konermann, L.1    Douglas, D.J.2
  • 55
    • 79952159609 scopus 로고    scopus 로고
    • Manipulation of protein charge states through continuous flow-extractive desorption electrospray ionization: a new ambient ionization technique
    • Yang, S. H., Wijeratne, A. B., Li, L., Edwards, B. L. and Schug, K. A., Manipulation of protein charge states through continuous flow-extractive desorption electrospray ionization: a new ambient ionization technique. Anal. Chem., 2011, 83, 643-647.
    • (2011) Anal. Chem. , vol.83 , pp. 643-647
    • Yang, S.H.1    Wijeratne, A.B.2    Li, L.3    Edwards, B.L.4    Schug, K.A.5
  • 56
    • 77956253029 scopus 로고    scopus 로고
    • Electrospray droplet exposure to gaseous acids for the manipulation of protein charge state distributions
    • Kharlamova, A., Prentice, B. M., Huang, T. Y. and McLuckey, S. A., Electrospray droplet exposure to gaseous acids for the manipulation of protein charge state distributions. Anal. Chem., 2010, 82, 7422-7429.
    • (2010) Anal. Chem. , vol.82 , pp. 7422-7429
    • Kharlamova, A.1    Prentice, B.M.2    Huang, T.Y.3    McLuckey, S.A.4
  • 57
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L. and Englander, S. W., Primary structure effects on peptide group hydrogen exchange. Proteins, 1993, 17, 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 58
    • 35648957285 scopus 로고    scopus 로고
    • Scope and utility of hydrogen exchange as a tool for mapping landscapes
    • Jaswal, S. S. and Miranker, A. D., Scope and utility of hydrogen exchange as a tool for mapping landscapes. Protein Sci., 2007, 16, 2378-2390.
    • (2007) Protein Sci. , vol.16 , pp. 2378-2390
    • Jaswal, S.S.1    Miranker, A.D.2
  • 59
    • 33644528769 scopus 로고    scopus 로고
    • Automated extraction of backbone deuteration levels from amide H/2H mass spectrometry experiments
    • Hotchko, M., Anand, G. S., Komives, E. A., and Ten Eyck, L. F., Automated extraction of backbone deuteration levels from amide H/2H mass spectrometry experiments. Protein Sci., 2006, 15, 583-601.
    • (2006) Protein Sci. , vol.15 , pp. 583-601
    • Hotchko, M.1    Anand, G.S.2    Komives, E.A.3    Ten Eyck, L.F.4
  • 60
    • 33749326831 scopus 로고    scopus 로고
    • Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis
    • Weis, D. D., Wales, T. E., Engen, J. R., Hotchko, M. and Ten Eyck, L. F., Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis. J. Am. Soc. Mass Spectrom., 2006, 17, 1498-1509.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1498-1509
    • Weis, D.D.1    Wales, T.E.2    Engen, J.R.3    Hotchko, M.4    Ten Eyck, L.F.5
  • 62
    • 62149090281 scopus 로고    scopus 로고
    • HD desktop: an integrated platform for the analysis and visualization of H/D exchange data
    • Pascal, B. D., Chalmers, M. J., Busby, S. A. and Griffin, P. R., HD desktop: an integrated platform for the analysis and visualization of H/D exchange data. J. Am. Soc. Mass Spectrom., 2009, 20, 601-610.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 601-610
    • Pascal, B.D.1    Chalmers, M.J.2    Busby, S.A.3    Griffin, P.R.4
  • 63
    • 53349173099 scopus 로고    scopus 로고
    • 'TOF2H': a precision toolbox for rapid, high density/high coverage hydrogen-deuterium exchange mass spectrometry via an LC-MALDI approach, covering the data pipeline from spectral acquisition to HDX rate analysis
    • Nikamanon, P., Pun, E., Chou, W., Koter, M. D. and Gershon, P. D., 'TOF2H': a precision toolbox for rapid, high density/high coverage hydrogen-deuterium exchange mass spectrometry via an LC-MALDI approach, covering the data pipeline from spectral acquisition to HDX rate analysis. BMC Bioinformatics, 2008, 9, 387.
    • (2008) BMC Bioinformatics , vol.9 , pp. 387
    • Nikamanon, P.1    Pun, E.2    Chou, W.3    Koter, M.D.4    Gershon, P.D.5
  • 65
    • 79951518978 scopus 로고    scopus 로고
    • HDX-analyser: a novel package for statistical analysis of protein structure dynamics
    • Liu, S. et al., HDX-analyser: a novel package for statistical analysis of protein structure dynamics. BMC Bioinformatics (Suppl. 1), 2011, 12, S43.
    • (2011) BMC Bioinformatics , vol.12 , Issue.SUPPL. 1
    • Liu, S.1
  • 66
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation
    • Zhang, Z. and Smith, D. L., Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci., 1993, 2, 522-531.
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 67
    • 0035326304 scopus 로고    scopus 로고
    • Investigating protein structure and dynamics by hydrogen exchange MS
    • Engen, J. R. and Smith, D. L., Investigating protein structure and dynamics by hydrogen exchange MS. Anal. Chem., 2001, 73, 256A-265A.
    • (2001) Anal. Chem. , vol.73
    • Engen, J.R.1    Smith, D.L.2
  • 68
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: optimization of digestion conditions
    • Wang, L., Pan, H. and Smith, D. L., Hydrogen exchange-mass spectrometry: optimization of digestion conditions. Mol. Cell Proteomics, 2002, 1, 132-138.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 70
    • 57449107282 scopus 로고    scopus 로고
    • Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry
    • Zhang, H. M., Kazazic, S., Schaub, T. M., Tipton, J. D., Emmett, M. R. and Marshall, A. G., Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem., 2008, 80, 9034-9041.
    • (2008) Anal. Chem. , vol.80 , pp. 9034-9041
    • Zhang, H.M.1    Kazazic, S.2    Schaub, T.M.3    Tipton, J.D.4    Emmett, M.R.5    Marshall, A.G.6
  • 71
    • 0035840988 scopus 로고    scopus 로고
    • Sitespecific amide hydrogen/deuterium exchange in E. coli thioredoxins measured by electrospray ionization mass spectrometry
    • Kim, M. Y., Maier, C. S., Reed, D. J. and Deinzer, M. L., Sitespecific amide hydrogen/deuterium exchange in E. coli thioredoxins measured by electrospray ionization mass spectrometry. J. Am. Chem. Soc., 2001, 123, 9860-9866.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9860-9866
    • Kim, M.Y.1    Maier, C.S.2    Reed, D.J.3    Deinzer, M.L.4
  • 72
    • 1542289847 scopus 로고    scopus 로고
    • Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of Staphylococcus aureus aldolase
    • Pan, H. and Smith, D. L., Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of Staphylococcus aureus aldolase. Methods Enzymol., 2004, 380, 285-308.
    • (2004) Methods Enzymol. , vol.380 , pp. 285-308
    • Pan, H.1    Smith, D.L.2
  • 73
    • 4143057003 scopus 로고    scopus 로고
    • Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry
    • Rojsajjakul, T., Wintrode, P., Vadrevu, R., Robert Matthews, C. and Smith, D. L., Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry. J. Mol. Biol., 2004, 341, 241-253.
    • (2004) J. Mol. Biol. , vol.341 , pp. 241-253
    • Rojsajjakul, T.1    Wintrode, P.2    Vadrevu, R.3    Robert Matthews, C.4    Smith, D.L.5
  • 74
    • 33947593231 scopus 로고    scopus 로고
    • Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus
    • Gu, Z., Zitzewitz, J. A. and Matthews, C. R., Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus. J. Mol. Biol., 2007, 368, 582-594.
    • (2007) J. Mol. Biol. , vol.368 , pp. 582-594
    • Gu, Z.1    Zitzewitz, J.A.2    Matthews, C.R.3
  • 75
    • 15244354756 scopus 로고    scopus 로고
    • An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein
    • Wintrode, P. L., Rojsajjakul, T., Vadrevu, R., Matthews, C. R. and Smith, D. L., An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein. J. Mol. Biol., 2005, 347, 911-919.
    • (2005) J. Mol. Biol. , vol.347 , pp. 911-919
    • Wintrode, P.L.1    Rojsajjakul, T.2    Vadrevu, R.3    Matthews, C.R.4    Smith, D.L.5
  • 76
    • 33645073892 scopus 로고    scopus 로고
    • Partial unfolding of diverse SH3 domains on a wide timescale
    • Wales, T. E. and Engen, J. R., Partial unfolding of diverse SH3 domains on a wide timescale. J. Mol. Biol., 2006, 357, 1592-1604.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1592-1604
    • Wales, T.E.1    Engen, J.R.2
  • 77
    • 73949098098 scopus 로고    scopus 로고
    • Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration
    • Wani, A. H. and Udgaonkar, J. B., Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration. Proc. Natl. Acad. Sci. USA, 2009, 106, 20711-20716.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20711-20716
    • Wani, A.H.1    Udgaonkar, J.B.2
  • 78
    • 0032485916 scopus 로고    scopus 로고
    • Identification of unfolding domains in large proteins by their unfolding rates
    • Deng, Y. and Smith, D. L., Identification of unfolding domains in large proteins by their unfolding rates. Biochemistry, 1998, 37, 6256-6262.
    • (1998) Biochemistry , vol.37 , pp. 6256-6262
    • Deng, Y.1    Smith, D.L.2
  • 79
    • 0030046197 scopus 로고    scopus 로고
    • Amide hydrogen exchange determined by mass spectrometry: application to rabbit muscle aldolase
    • Zhang, Z., Post, C. B. and Smith, D. L., Amide hydrogen exchange determined by mass spectrometry: application to rabbit muscle aldolase. Biochemistry, 1996, 35, 779-791.
    • (1996) Biochemistry , vol.35 , pp. 779-791
    • Zhang, Z.1    Post, C.B.2    Smith, D.L.3
  • 80
    • 0036290571 scopus 로고    scopus 로고
    • Crossing the phase boundary to study protein dynamics and function: combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase
    • Kaltashov, I. A. and Eyles, S. J., Crossing the phase boundary to study protein dynamics and function: combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase. J. Mass Spectrom., 2002, 37, 557-565.
    • (2002) J. Mass Spectrom. , vol.37 , pp. 557-565
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 81
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann, L., Pan, J. and Liu, Y. H., Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem. Soc. Rev., 2011, 40, 1224-1234.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 82
    • 77958068942 scopus 로고    scopus 로고
    • Characterizing short-lived protein folding intermediates by top-down hydrogen exchange mass spectrometry
    • Pan, J., Han, J., Borchers, C. H. and Konermann, L., Characterizing short-lived protein folding intermediates by top-down hydrogen exchange mass spectrometry. Anal. Chem., 2010, 82, 8591-8597.
    • (2010) Anal. Chem. , vol.82 , pp. 8591-8597
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 83
    • 69849083391 scopus 로고    scopus 로고
    • Hydrogen/ deuterium exchange mass spectrometry with top-down electron capture dissociation for characterizing structural transitions of a 17 kDa protein
    • Pan, J., Han, J., Borchers, C. H. and Konermann, L., Hydrogen/ deuterium exchange mass spectrometry with top-down electron capture dissociation for characterizing structural transitions of a 17 kDa protein. J. Am. Chem. Soc., 2009, 131, 12801-12808.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12801-12808
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 84
    • 0033473768 scopus 로고    scopus 로고
    • Comparison of continuous and pulsed labelling amide hydrogen exchange/mass spectrometry for studies of protein dynamics
    • Deng, Y., Zhang, Z. and Smith, D. L., Comparison of continuous and pulsed labelling amide hydrogen exchange/mass spectrometry for studies of protein dynamics. J. Am. Soc. Mass Spectrom., 1999, 10, 675-684.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 675-684
    • Deng, Y.1    Zhang, Z.2    Smith, D.L.3
  • 85
    • 0029643523 scopus 로고
    • Protein folding intermediates: native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L. and Englander, S. W., Protein folding intermediates: native-state hydrogen exchange. Science, 1995, 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 88
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander, S. W., Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct., 2000, 29, 213-328.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 213-328
    • Englander, S.W.1
  • 89
    • 67449100204 scopus 로고    scopus 로고
    • Functional unfolding of alpha 1-antitrypsin probed by hydrogen-deuterium exchange coupled with mass spectrometry
    • Baek, J. H., Yang, W. S., Lee, C. and Yu, M. H., Functional unfolding of alpha 1-antitrypsin probed by hydrogen-deuterium exchange coupled with mass spectrometry. Mol. Cell Proteomics, 2009, 8, 1072-1078.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 1072-1078
    • Baek, J.H.1    Yang, W.S.2    Lee, C.3    Yu, M.H.4
  • 90
    • 1642452920 scopus 로고    scopus 로고
    • Hydrogen/ deuterium exchange studies of native rabbit MM-CK dynamics
    • Mazon, H., Marcillat, O., Forest, E. and Vial, C., Hydrogen/ deuterium exchange studies of native rabbit MM-CK dynamics. Protein Sci., 2004, 13, 476-486.
    • (2004) Protein Sci. , vol.13 , pp. 476-486
    • Mazon, H.1    Marcillat, O.2    Forest, E.3    Vial, C.4
  • 91
    • 0032512423 scopus 로고    scopus 로고
    • Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild-type and constitutively active mutants of MAP kinase kinase-1
    • Resing, K. A. and Ahn, N. G., Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild-type and constitutively active mutants of MAP kinase kinase-1. Biochemistry, 1998, 37, 463-475.
    • (1998) Biochemistry , vol.37 , pp. 463-475
    • Resing, K.A.1    Ahn, N.G.2
  • 92
    • 19444384291 scopus 로고    scopus 로고
    • Transient structural disorder as a facilitator of protein-ligand binding: native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I
    • Xiao, H. and Kaltashov, I. A., Transient structural disorder as a facilitator of protein-ligand binding: native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I. J. Am. Soc. Mass Spectrom., 2005, 16, 869-879.
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 869-879
    • Xiao, H.1    Kaltashov, I.A.2
  • 93
    • 0030696119 scopus 로고    scopus 로고
    • Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry
    • Engen, J. R., Smithgall, T. E., Gmeiner, W. H. and Smith, D. L., Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry. Biochemistry, 1997, 36, 14384-14391.
    • (1997) Biochemistry , vol.36 , pp. 14384-14391
    • Engen, J.R.1    Smithgall, T.E.2    Gmeiner, W.H.3    Smith, D.L.4
  • 94
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F. and Dobson, C. M., Amyloid formation by globular proteins under native conditions. Nature Chem. Biol., 2009, 5, 15-22.
    • (2009) Nature Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 95
    • 3342900252 scopus 로고    scopus 로고
    • Localized nature of the transition-state structure in goat alphalactalbumin folding
    • Saeki, K., Arai, M., Yoda, T., Nakao, M. and Kuwajima, K., Localized nature of the transition-state structure in goat alphalactalbumin folding. J. Mol. Biol., 2004, 341, 589-604.
    • (2004) J. Mol. Biol. , vol.341 , pp. 589-604
    • Saeki, K.1    Arai, M.2    Yoda, T.3    Nakao, M.4    Kuwajima, K.5
  • 96
    • 52949124053 scopus 로고    scopus 로고
    • Folding mechanism of reduced cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide
    • Latypov, R. F., Maki, K., Cheng, H., Luck, S. D. and Roder, H., Folding mechanism of reduced cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide. J. Mol. Biol., 2008, 383, 437-453.
    • (2008) J. Mol. Biol. , vol.383 , pp. 437-453
    • Latypov, R.F.1    Maki, K.2    Cheng, H.3    Luck, S.D.4    Roder, H.5
  • 97
    • 0036177471 scopus 로고    scopus 로고
    • Detecting equilibrium cytochrome c folding intermediates by electrospray ionisation mass spectrometry: two partially folded forms populate the molten-globule state
    • Grandori, R., Detecting equilibrium cytochrome c folding intermediates by electrospray ionisation mass spectrometry: two partially folded forms populate the molten-globule state. Protein Sci., 2002, 11, 453-458.
    • (2002) Protein Sci. , vol.11 , pp. 453-458
    • Grandori, R.1
  • 98
    • 0032232233 scopus 로고    scopus 로고
    • Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes
    • Konermann, L. and Douglas, D. J., Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes. J. Am. Soc. Mass Spectrom., 1998, 9, 1248-1254.
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 1248-1254
    • Konermann, L.1    Douglas, D.J.2
  • 99
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • Ghaemmaghami, S. and Oas, T. G., Quantitative protein stability measurement in vivo. Nat. Struct. Biol., 2001, 8, 879-882.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 100
    • 33750370331 scopus 로고    scopus 로고
    • A mass spectrometry-based probe of equilibrium intermediates in protein-folding reactions
    • Dai, S. Y. and Fitzgerald, M. C., A mass spectrometry-based probe of equilibrium intermediates in protein-folding reactions. Biochemistry, 2006, 45, 12890-12897.
    • (2006) Biochemistry , vol.45 , pp. 12890-12897
    • Dai, S.Y.1    Fitzgerald, M.C.2
  • 101
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • Raschke, T. M. and Marqusee, S., The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Struct. Biol., 1997, 4, 298-304.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 102
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectrometry
    • Miranker, A., Robinson, C. V., Radford, S. E., Aplin, R. T. and Dobson, C. M., Detection of transient protein folding populations by mass spectrometry. Science, 1993, 262, 896-900.
    • (1993) Science , vol.262 , pp. 896-900
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 103
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin-1 beta
    • Heidary, D. K., Gross, L. A., Roy, M. and Jennings, P. A., Evidence for an obligatory intermediate in the folding of interleukin-1 beta. Nature Struct. Biol., 1997, 4, 725-731.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 725-731
    • Heidary, D.K.1    Gross, L.A.2    Roy, M.3    Jennings, P.A.4
  • 104
    • 0032901420 scopus 로고    scopus 로고
    • Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate
    • Tsui, V., Garcia, C., Cavagnero, S., Siuzdak, G., Dyson, H. J. and Wright, P. E., Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate. Protein Sci., 1999, 8, 45-49.
    • (1999) Protein Sci. , vol.8 , pp. 45-49
    • Tsui, V.1    Garcia, C.2    Cavagnero, S.3    Siuzdak, G.4    Dyson, H.J.5    Wright, P.E.6
  • 105
    • 28844466085 scopus 로고    scopus 로고
    • Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin
    • Nishimura, C., Dyson, H. J. and Wright, P. E., Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin. J. Mol. Biol., 2006, 355, 139-156.
    • (2006) J. Mol. Biol. , vol.355 , pp. 139-156
    • Nishimura, C.1    Dyson, H.J.2    Wright, P.E.3
  • 106
    • 77957265050 scopus 로고    scopus 로고
    • Rapid collapse into molten globule is followed by simple two-state kinetics in the folding of lysozyme from bacteriophage ?
    • Di Paolo, A., Balbeur, D., De Pauw, E., Redfield, C. and Matagne, A., Rapid collapse into molten globule is followed by simple two-state kinetics in the folding of lysozyme from bacteriophage ?. Biochemistry, 2010, 49, 8644-8657.
    • (2010) Biochemistry , vol.49 , pp. 8644-8657
    • Di Paolo, A.1    Balbeur, D.2    De Pauw, E.3    Redfield, C.4    Matagne, A.5
  • 107
    • 1242294469 scopus 로고    scopus 로고
    • Equilibrium and kinetic folding of rabbit muscle triosephosphate isomerase by hydrogen exchange mass spectrometry
    • Pan, H., Raza, A. S. and Smith, D. L., Equilibrium and kinetic folding of rabbit muscle triosephosphate isomerase by hydrogen exchange mass spectrometry. J. Mol. Biol., 2004, 336, 1251-1263.
    • (2004) J. Mol. Biol. , vol.336 , pp. 1251-1263
    • Pan, H.1    Raza, A.S.2    Smith, D.L.3
  • 108
    • 20544458613 scopus 로고    scopus 로고
    • Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments: implications for ubiquitin folding
    • Pan, J., Wilson, D. J. and Konermann, L., Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments: implications for ubiquitin folding. Biochemistry, 2005, 44, 8627-8633.
    • (2005) Biochemistry , vol.44 , pp. 8627-8633
    • Pan, J.1    Wilson, D.J.2    Konermann, L.3
  • 109
    • 0037065802 scopus 로고    scopus 로고
    • Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-line isotopic pulse labelling
    • Simmons, D. A. and Konermann, L., Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-line isotopic pulse labelling. Biochemistry, 2002, 41, 1906-1914.
    • (2002) Biochemistry , vol.41 , pp. 1906-1914
    • Simmons, D.A.1    Konermann, L.2
  • 110
    • 33644663381 scopus 로고    scopus 로고
    • Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange
    • Pan, J., Rintala-Dempsey, A. C., Li, Y., Shaw, G. S. and Konermann, L., Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange. Biochemistry, 2006, 45, 3005-3013.
    • (2006) Biochemistry , vol.45 , pp. 3005-3013
    • Pan, J.1    Rintala-Dempsey, A.C.2    Li, Y.3    Shaw, G.S.4    Konermann, L.5
  • 111
    • 0030787174 scopus 로고    scopus 로고
    • Multiple intermediates and transition states during protein unfolding
    • Zaidi, F. N., Nath, U. and Udgaonkar, J. B., Multiple intermediates and transition states during protein unfolding. Nature Struct. Biol., 1997, 4, 1016-1024.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 1016-1024
    • Zaidi, F.N.1    Nath, U.2    Udgaonkar, J.B.3
  • 112
    • 0032560593 scopus 로고    scopus 로고
    • Multiple kinetic intermediates accumulate during the unfolding of horse cytochrome c in the oxidized state
    • Bhuyan, A. K. and Udgaonkar, J. B., Multiple kinetic intermediates accumulate during the unfolding of horse cytochrome c in the oxidized state. Biochemistry, 1998, 37, 9147-9155.
    • (1998) Biochemistry , vol.37 , pp. 9147-9155
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 113
    • 0036220131 scopus 로고    scopus 로고
    • Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
    • Canet, D. et al., Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nature Struct. Biol., 2002, 4, 308-315.
    • (2002) Nature Struct. Biol. , vol.4 , pp. 308-315
    • Canet, D.1
  • 114
    • 0038810081 scopus 로고    scopus 로고
    • Protein structure change studied by hydrogen-deuterium exchange, functional labelling, and mass spectrometry
    • Englander, J. J. et al., Protein structure change studied by hydrogen-deuterium exchange, functional labelling, and mass spectrometry. Proc. Natl. Acad. Sci. USA, 2003, 100, 7057-7062.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7057-7062
    • Englander, J.J.1
  • 115
    • 8744221645 scopus 로고    scopus 로고
    • Subunit disassembly and unfolding kinetics of hemoglobin studied by time-resolved electrospray mass spectrometry
    • Simmons, D. A., Wilson, D. J., Lajoie, G. A., Doherty-Kirby, A. and Konermann, L., Subunit disassembly and unfolding kinetics of hemoglobin studied by time-resolved electrospray mass spectrometry. Biochemistry, 2004, 43, 14792-14801.
    • (2004) Biochemistry , vol.43 , pp. 14792-14801
    • Simmons, D.A.1    Wilson, D.J.2    Lajoie, G.A.3    Doherty-Kirby, A.4    Konermann, L.5
  • 116
    • 67749108049 scopus 로고    scopus 로고
    • Detection of early unfolding events in a dimeric protein by amide proton exchange and native electrospray mass spectrometry
    • Mobley, J. A. and Pollakov, A., Detection of early unfolding events in a dimeric protein by amide proton exchange and native electrospray mass spectrometry. Protein Sci., 2009, 18, 1620-1627.
    • (2009) Protein Sci. , vol.18 , pp. 1620-1627
    • Mobley, J.A.1    Pollakov, A.2
  • 118
    • 65549094060 scopus 로고    scopus 로고
    • Painting proteins with covalent labels: what is the picture? J
    • Fitzgerald, M. C. and West, G. M., Painting proteins with covalent labels: what is the picture? J. Am. Soc. Mass Spectrom., 2009, 20, 1193-1206.
    • (2009) Am. Soc. Mass Spectrom. , vol.20 , pp. 1193-1206
    • Fitzgerald, M.C.1    West, G.M.2
  • 119
    • 79955565663 scopus 로고    scopus 로고
    • Mass spectrometry- and lysine amidination-based protocol for thermodynamic analysis of proteins and ligand binding interactions
    • Xu, Y., Falk, I. N., Hallen, M. A. and Fitzergerald, M. C., Mass spectrometry- and lysine amidination-based protocol for thermodynamic analysis of proteins and ligand binding interactions. Anal. Chem., 2011, 83, 3555-3562.
    • (2011) Anal. Chem. , vol.83 , pp. 3555-3562
    • Xu, Y.1    Falk, I.N.2    Hallen, M.A.3    Fitzergerald, M.C.4
  • 120
    • 0035900542 scopus 로고    scopus 로고
    • On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin
    • Feng, Z., Butler, M. C., Alam, S. L. and Loh, S. N., On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin. J. Mol. Biol., 2001, 314, 153-166.
    • (2001) J. Mol. Biol. , vol.314 , pp. 153-166
    • Feng, Z.1    Butler, M.C.2    Alam, S.L.3    Loh, S.N.4
  • 121
    • 79954516745 scopus 로고    scopus 로고
    • Cysteine tagging for MSbased proteomics
    • Giron, P., Dayon, L. and Sanchez, J. C., Cysteine tagging for MSbased proteomics. Mass Spectrom. Rev., 2011, 30, 366-395.
    • (2011) Mass Spectrom. Rev. , vol.30 , pp. 366-395
    • Giron, P.1    Dayon, L.2    Sanchez, J.C.3
  • 122
    • 38049108092 scopus 로고    scopus 로고
    • Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labelling and mass spectrometry
    • Jha, S. K. and Udgaonkar, J. B., Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labelling and mass spectrometry. J. Biol. Chem., 2007, 282, 37479-37491.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37479-37491
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 123
    • 79953906735 scopus 로고    scopus 로고
    • Identification of multiple folding pathways of monellin using pulsed thiol labelling and mass spectrometry
    • Jha, S. K., Dasgupta, A., Malhotra, P. and Udgaonkar, J. B., Identification of multiple folding pathways of monellin using pulsed thiol labelling and mass spectrometry. Biochemistry, 2011, 50, 3062-3074.
    • (2011) Biochemistry , vol.50 , pp. 3062-3074
    • Jha, S.K.1    Dasgupta, A.2    Malhotra, P.3    Udgaonkar, J.B.4
  • 124
    • 0028022793 scopus 로고
    • Analysis of RNase A refolding intermediates by electrospray/mass spectrometry
    • Torella, C., Ruoppolo, M., Marino, G. and Pucci, P., Analysis of RNase A refolding intermediates by electrospray/mass spectrometry. FEBS Lett., 1994, 352, 301-306.
    • (1994) FEBS Lett. , vol.352 , pp. 301-306
    • Torella, C.1    Ruoppolo, M.2    Marino, G.3    Pucci, P.4
  • 125
  • 126
    • 0031954924 scopus 로고    scopus 로고
    • Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry
    • Wu, J., Yang, Y. and Watson, J. T., Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry. Protein Sci., 1998, 7, 1017-1028.
    • (1998) Protein Sci. , vol.7 , pp. 1017-1028
    • Wu, J.1    Yang, Y.2    Watson, J.T.3
  • 127
    • 3042758481 scopus 로고    scopus 로고
    • Integration of hydrogen/deuterium exchange and cyanylation-based methodology for conformational studies of cystinyl proteins
    • Li, X., Chou, Y. T., Husain, R. and Watson, J. T., Integration of hydrogen/deuterium exchange and cyanylation-based methodology for conformational studies of cystinyl proteins. Anal. Biochem., 2004, 331, 130-137.
    • (2004) Anal. Biochem. , vol.331 , pp. 130-137
    • Li, X.1    Chou, Y.T.2    Husain, R.3    Watson, J.T.4
  • 128
    • 78650717220 scopus 로고    scopus 로고
    • Future directions of structural mass spectrometry using hydroxyl radical footprinting
    • Kiselar, J. G. and Chance, M. R., Future directions of structural mass spectrometry using hydroxyl radical footprinting. Mass Spectrom. Rev., 2010, 45, 1373-1382.
    • (2010) Mass Spectrom. Rev. , vol.45 , pp. 1373-1382
    • Kiselar, J.G.1    Chance, M.R.2
  • 129
    • 0036006581 scopus 로고    scopus 로고
    • Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry
    • Maleknia, S. D., Kiselar, J. G. and Downard, K. M., Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry. Rapid Commun. Mass Spectrom., 2002, 16, 53-61.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 53-61
    • Maleknia, S.D.1    Kiselar, J.G.2    Downard, K.M.3
  • 130
    • 0035719748 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry
    • Maleknia, S. D. and Downard, K. M., Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry. Eur. J. Biochem., 2001, 268, 5578-5588.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5578-5588
    • Maleknia, S.D.1    Downard, K.M.2
  • 131
    • 79957681753 scopus 로고    scopus 로고
    • Temporal development of protein structure during S100A11 folding and dimerization probed by oxidative labelling and mass spectrometry
    • Stocks, B. B., Rezvanpour, A., Shaw, G. S. and Konermann, L., Temporal development of protein structure during S100A11 folding and dimerization probed by oxidative labelling and mass spectrometry. J. Mol. Biol., 2011, 409, 669-679.
    • (2011) J. Mol. Biol. , vol.409 , pp. 669-679
    • Stocks, B.B.1    Rezvanpour, A.2    Shaw, G.S.3    Konermann, L.4
  • 132
    • 78149244661 scopus 로고    scopus 로고
    • Temperature jump and fast photochemical oxidation probe submillisecond protein folding
    • Chen, J., Rempel, D. L. and Gross, M. L., Temperature jump and fast photochemical oxidation probe submillisecond protein folding. J. Am. Chem. Soc., 2010, 10, 15502-15504.
    • (2010) J. Am. Chem. Soc. , vol.10 , pp. 15502-15504
    • Chen, J.1    Rempel, D.L.2    Gross, M.L.3
  • 133
    • 78649807441 scopus 로고    scopus 로고
    • Analytical biochemistry: weighing up protein folding
    • Grurbele, M., Analytical biochemistry: weighing up protein folding. Nature, 2010, 468, 640-641.
    • (2010) Nature , vol.468 , pp. 640-641
    • Grurbele, M.1
  • 134
    • 77951765288 scopus 로고    scopus 로고
    • Time-dependent changes in side-chain solvent accessibility during cytochrome c folding probed by pulsed oxidative labelling and mass spectrometry
    • Stocks, B. B. and Konermann, L., Time-dependent changes in side-chain solvent accessibility during cytochrome c folding probed by pulsed oxidative labelling and mass spectrometry. J. Mol. Biol., 2010, 398, 362-373.
    • (2010) J. Mol. Biol. , vol.398 , pp. 362-373
    • Stocks, B.B.1    Konermann, L.2
  • 135
    • 79959456892 scopus 로고    scopus 로고
    • Advances in mass spectrometry of membrane proteins: from individual proteins to intact complexes
    • Barrera, N. P. and Robinson, C. V., Advances in mass spectrometry of membrane proteins: from individual proteins to intact complexes. Annu. Rev. Biochem., 2011, 80, 34.1-34.25.
    • (2011) Annu. Rev. Biochem. , vol.80
    • Barrera, N.P.1    Robinson, C.V.2
  • 136
    • 70449687854 scopus 로고    scopus 로고
    • Mapping the structure of an integral membrane protein under semi-denaturing conditions by laser-induced oxidative labelling and mass spectrometry
    • Pan, Y., Brown, L. and Konermann, L., Mapping the structure of an integral membrane protein under semi-denaturing conditions by laser-induced oxidative labelling and mass spectrometry. J. Mol. Biol., 2009, 394, 968-981.
    • (2009) J. Mol. Biol. , vol.394 , pp. 968-981
    • Pan, Y.1    Brown, L.2    Konermann, L.3
  • 137
    • 77958198646 scopus 로고    scopus 로고
    • Site-directed mutagenesis combined with oxidative methionine labelling for probing structural transitions of a membrane protein by mass spectrometry
    • Pan, Y., Brown, L. and Konermann, L., Site-directed mutagenesis combined with oxidative methionine labelling for probing structural transitions of a membrane protein by mass spectrometry. J. Am. Soc. Mass Spectrom., 2010, 21, 1947-1956.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1947-1956
    • Pan, Y.1    Brown, L.2    Konermann, L.3
  • 138
    • 79958755721 scopus 로고    scopus 로고
    • Kinetic folding mechanism of an integral membrane protein examined by pulsed oxidative labelling and mass spectrometry
    • Pan, Y., Brown, L. and Konermann, L., Kinetic folding mechanism of an integral membrane protein examined by pulsed oxidative labelling and mass spectrometry. J. Mol. Biol., 2011, 410, 146-158.
    • (2011) J. Mol. Biol. , vol.410 , pp. 146-158
    • Pan, Y.1    Brown, L.2    Konermann, L.3
  • 139
    • 33644554831 scopus 로고    scopus 로고
    • Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics
    • Ellison, P. A. and Cavagnero, S., Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics. Protein Sci., 2006, 15, 564-582.
    • (2006) Protein Sci. , vol.15 , pp. 564-582
    • Ellison, P.A.1    Cavagnero, S.2
  • 140
    • 35448932093 scopus 로고    scopus 로고
    • Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways
    • Patra, A. K. and Udgaonkar, J. B., Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways. Biochemistry, 2007, 46, 11727-11743.
    • (2007) Biochemistry , vol.46 , pp. 11727-11743
    • Patra, A.K.1    Udgaonkar, J.B.2
  • 141
    • 0031933290 scopus 로고    scopus 로고
    • Parallel pathways in the folding of a short-term denatured scFv fragment of an antibody
    • Freund, C., Gehrig, P., Baici, A., Holak, T. A. and Pluckthun, A., Parallel pathways in the folding of a short-term denatured scFv fragment of an antibody. Fold. Des., 1998, 3, 39-49.
    • (1998) Fold. Des. , vol.3 , pp. 39-49
    • Freund, C.1    Gehrig, P.2    Baici, A.3    Holak, T.A.4    Pluckthun, A.5
  • 142
    • 0342264617 scopus 로고    scopus 로고
    • Direct evidence by H/D exchange and ESI-MS for transient unproductive domain interaction in the refolding of an antibody scFv fragment
    • Jager, M. and Pluckthun, A., Direct evidence by H/D exchange and ESI-MS for transient unproductive domain interaction in the refolding of an antibody scFv fragment. Protein Sci., 2000, 9, 552-563.
    • (2000) Protein Sci. , vol.9 , pp. 552-563
    • Jager, M.1    Pluckthun, A.2
  • 143
    • 0035913902 scopus 로고    scopus 로고
    • Dual function of protein confinement in chaperonin-assisted protein folding
    • Brinker, A., Pfeifer, G., Kerner, M. J., Naylor, D. J., Hartl, F. U. and Hayer-Hartl, M., Dual function of protein confinement in chaperonin-assisted protein folding. Cell, 2001, 107, 223-233.
    • (2001) Cell , vol.107 , pp. 223-233
    • Brinker, A.1    Pfeifer, G.2    Kerner, M.J.3    Naylor, D.J.4    Hartl, F.U.5    Hayer-Hartl, M.6
  • 144
    • 0346438814 scopus 로고    scopus 로고
    • Chaperonins as protein folding machines
    • Bhutani, N. and Udgaonkar, J. B., Chaperonins as protein folding machines. Curr. Sci., 2002, 83, 1337-1351.
    • (2002) Curr. Sci. , vol.83 , pp. 1337-1351
    • Bhutani, N.1    Udgaonkar, J.B.2
  • 145
    • 33646907087 scopus 로고    scopus 로고
    • GroEL-GroESmediated protein folding
    • Horwich, A. L., Farr, G. W. and Fenton, W. A., GroEL-GroESmediated protein folding. Chem. Rev., 2006, 106, 1917-1930.
    • (2006) Chem. Rev. , vol.106 , pp. 1917-1930
    • Horwich, A.L.1    Farr, G.W.2    Fenton, W.A.3
  • 146
    • 33646897305 scopus 로고    scopus 로고
    • Structural features of the GroEL-GroES nanocage required for rapid folding of encapsulated protein
    • Tang, Y. C. et al., Structural features of the GroEL-GroES nanocage required for rapid folding of encapsulated protein. Cell, 2006, 125, 903-914.
    • (2006) Cell , vol.125 , pp. 903-914
    • Tang, Y.C.1
  • 147
    • 33847635621 scopus 로고    scopus 로고
    • Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner
    • Kipnis, Y., Papo, N., Haran, G. and Horovitz, A., Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner. Proc. Natl. Acad. Sci. USA, 2007, 104, 3119-3124.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3119-3124
    • Kipnis, Y.1    Papo, N.2    Haran, G.3    Horovitz, A.4
  • 148
    • 41149089882 scopus 로고    scopus 로고
    • Monitoring protein conformation along the pathway of chaperonin-assisted folding
    • Sharma, S. et al., Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell, 2008, 133, 142-153.
    • (2008) Cell , vol.133 , pp. 142-153
    • Sharma, S.1
  • 149
    • 0028670568 scopus 로고
    • Conformation of GroEL-bound alphalactalbumin probed by mass spectrometry
    • Robinson, C. V. et al., Conformation of GroEL-bound alphalactalbumin probed by mass spectrometry. Nature, 1994, 372, 646-651.
    • (1994) Nature , vol.372 , pp. 646-651
    • Robinson, C.V.1
  • 150
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: folding by forced unfolding
    • Shtilerman, M., Lorimer, G. H. and Englander, S. W., Chaperonin function: folding by forced unfolding. Science, 1999, 284, 822-825.
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 151
    • 0034880923 scopus 로고    scopus 로고
    • Folding of malate dehydrogenase inside the GroEL-GroES cavity
    • Chen, J., Walter, S., Horwich, A. L. and Smith, D. L., Folding of malate dehydrogenase inside the GroEL-GroES cavity. Nature Struct. Biol., 2001, 8, 721-728.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 721-728
    • Chen, J.1    Walter, S.2    Horwich, A.L.3    Smith, D.L.4
  • 152
    • 33646045893 scopus 로고    scopus 로고
    • Tandem mass spectrometry of intact GroELsubstrate complexes reveals substrate-specific conformational changes in the trans ring
    • van Duijn, E. et al., Tandem mass spectrometry of intact GroELsubstrate complexes reveals substrate-specific conformational changes in the trans ring. J. Am. Chem. Soc., 2006, 128, 4694-4702.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4694-4702
    • van Duijn, E.1
  • 153
    • 62049084010 scopus 로고    scopus 로고
    • Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine
    • Graf, C., Stankiewicz, M., Kramer, G. and Mayer, M. P., Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J., 2009, 28, 602-613.
    • (2009) EMBO J. , vol.28 , pp. 602-613
    • Graf, C.1    Stankiewicz, M.2    Kramer, G.3    Mayer, M.P.4
  • 154
    • 33745183353 scopus 로고    scopus 로고
    • Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation
    • Rist, W., Graf, C., Bukau, B. and Mayer, M. P., Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. J. Biol. Chem., 2006, 281, 16493-16501.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16493-16501
    • Rist, W.1    Graf, C.2    Bukau, B.3    Mayer, M.P.4
  • 155
    • 55549133282 scopus 로고    scopus 로고
    • Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry
    • Cheng, G., Basha, E., Wysocki, V. H. and Vierling, E., Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem., 2008, 283, 26634-26642.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26634-26642
    • Cheng, G.1    Basha, E.2    Wysocki, V.H.3    Vierling, E.4
  • 156
    • 76649084269 scopus 로고    scopus 로고
    • Quaternary dynamics and plasticity underlie small heat shock protein chaperon function
    • Stengel, F. et al., Quaternary dynamics and plasticity underlie small heat shock protein chaperon function. Proc. Natl. Acad. Sci. USA, 2010, 107, 2007-2012.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2007-2012
    • Stengel, F.1
  • 157
    • 33847769109 scopus 로고    scopus 로고
    • Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion
    • Kumar, S., Mohanty, S. K. and Udgaonkar, J. B., Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion. J. Mol. Biol., 2007, 367, 1186-1204.
    • (2007) J. Mol. Biol. , vol.367 , pp. 1186-1204
    • Kumar, S.1    Mohanty, S.K.2    Udgaonkar, J.B.3
  • 158
    • 84864817964 scopus 로고    scopus 로고
    • Mechanisms of amyloid fibril formation by proteins
    • Kumar, S. and Udgaonkar, J. B., Mechanisms of amyloid fibril formation by proteins. Curr. Sci., 2010, 96, 1053-1070.
    • (2010) Curr. Sci. , vol.96 , pp. 1053-1070
    • Kumar, S.1    Udgaonkar, J.B.2
  • 159
    • 51349098137 scopus 로고    scopus 로고
    • Evidence for stepwise formation of amyloid fibrils by the mouse prion protein
    • Jain, S. and Udgaonkar, J. B., Evidence for stepwise formation of amyloid fibrils by the mouse prion protein. J. Mol. Biol., 2008, 382, 1228-1241.
    • (2008) J. Mol. Biol. , vol.382 , pp. 1228-1241
    • Jain, S.1    Udgaonkar, J.B.2
  • 160
    • 0033849738 scopus 로고    scopus 로고
    • Review: history of the amyloid fibril
    • Sipe, J. D. and Cohen, A. S., Review: history of the amyloid fibril. J. Struct. Biol., 2000, 130, 88-98.
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 161
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C. M., Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem., 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 162
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B. and Lansbury, P. T., Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci., 2003, 26, 267-298.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 163
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E. and Glabe, C. G., Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem., 2004, 279, 46363-46366.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 164
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: a common structural link for protein-misfolding disease
    • Quist, A. et al., Amyloid ion channels: a common structural link for protein-misfolding disease. Proc. Natl. Acad. Sci. USA, 2005, 102, 10427-10432.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10427-10432
    • Quist, A.1
  • 165
    • 0011246323 scopus 로고    scopus 로고
    • Electron microscopy of prefibrillar structures and amyloid fibrils
    • Nielsen, E. H., Nybo, M. and Svehag, S. E., Electron microscopy of prefibrillar structures and amyloid fibrils. Methods Enzymol., 1999, 309, 491-496.
    • (1999) Methods Enzymol. , vol.309 , pp. 491-496
    • Nielsen, E.H.1    Nybo, M.2    Svehag, S.E.3
  • 166
    • 0032857176 scopus 로고    scopus 로고
    • Analysis of amyloid-beta assemblies using tapping mode atomic force microscopy under ambient conditions
    • Ding, T. T. and Harper, J. D., Analysis of amyloid-beta assemblies using tapping mode atomic force microscopy under ambient conditions. Methods Enzymol., 1999, 309, 510-225.
    • (1999) Methods Enzymol. , vol.309 , pp. 510-225
    • Ding, T.T.1    Harper, J.D.2
  • 167
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri, S., Khurana, R. and Fink, A. L., Fourier transform infrared spectroscopy in analysis of protein deposits. Methods Enzymol., 1999, 309, 559-576.
    • (1999) Methods Enzymol. , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 168
    • 0032879438 scopus 로고    scopus 로고
    • X-ray fiber diffraction of amyloid fibrils
    • Serpell, L. C., Fraser, P. E. and Sunde, M., X-ray fiber diffraction of amyloid fibrils. Methods Enzymol., 1999, 309, 526-536.
    • (1999) Methods Enzymol. , vol.309 , pp. 526-536
    • Serpell, L.C.1    Fraser, P.E.2    Sunde, M.3
  • 170
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen, S., Ferrone, F. A. and Wetzel, R., Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc. Natl. Acad. Sci. USA, 2002, 99, 11884-11889.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 171
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: insights from solid-state NMR
    • Tycko, R., Molecular structure of amyloid fibrils: insights from solid-state NMR. Q. Rev. Biophys., 2006, 39, 1-55.
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 1-55
    • Tycko, R.1
  • 172
    • 33749838193 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry -a window into amyloid structure
    • Kheterpal, I. and Wetzel, R., Hydrogen/deuterium exchange mass spectrometry -a window into amyloid structure. Acc. Chem. Res., 2006, 39, 584-593.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 584-593
    • Kheterpal, I.1    Wetzel, R.2
  • 173
    • 79954460138 scopus 로고    scopus 로고
    • The use of mass spectrometry to study amyloid-ß peptides
    • Grasso, G., The use of mass spectrometry to study amyloid-ß peptides. Mass Spectrom. Rev., 2011, 30, 347-365.
    • (2011) Mass Spectrom. Rev. , vol.30 , pp. 347-365
    • Grasso, G.1
  • 174
    • 18844427273 scopus 로고    scopus 로고
    • Structural properties of Abeta protofibrils stabilized by a small-molecule
    • Williams, A. D. et al., Structural properties of Abeta protofibrils stabilized by a small-molecule. Proc. Natl. Acad. Sci. USA, 2005, 102, 7115-7120.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7115-7120
    • Williams, A.D.1
  • 175
    • 33746781304 scopus 로고    scopus 로고
    • Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation
    • Kheterpal, I., Chen, M., Cook, K. D. and Wetzel, R., Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation. J. Mol. Biol., 2006, 361, 785-795.
    • (2006) J. Mol. Biol. , vol.361 , pp. 785-795
    • Kheterpal, I.1    Chen, M.2    Cook, K.D.3    Wetzel, R.4
  • 176
    • 61549108314 scopus 로고    scopus 로고
    • Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/ deuterium exchange
    • Zhang, A., Qi, W., Good, T. A. and Fernandez, E. J., Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/ deuterium exchange. Biophys. J., 2009, 96, 1091-1104.
    • (2009) Biophys. J. , vol.96 , pp. 1091-1104
    • Zhang, A.1    Qi, W.2    Good, T.A.3    Fernandez, E.J.4
  • 177
    • 79955406741 scopus 로고    scopus 로고
    • Aß40 and Aß42 amyloid fibrils exhibit distinct molecular recycling properties
    • Sánchez, L. et al., Aß40 and Aß42 amyloid fibrils exhibit distinct molecular recycling properties. J. Am. Chem. Soc., 2011, 133, 6505-6508.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6505-6508
    • Sánchez, L.1
  • 178
    • 23144459082 scopus 로고    scopus 로고
    • Molecular recycling within amyloid fibrils
    • Carulla, N. et al., Molecular recycling within amyloid fibrils. Nature, 2005, 436, 554-558.
    • (2005) Nature , vol.436 , pp. 554-558
    • Carulla, N.1
  • 179
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton, E. J., Tito, P. Sunde, M., Bouchard, M., Dobson, C. M. and Robinson, C. V. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys J., 2000, 79, 1053-1065.
    • (2000) Biophys J. , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 180
    • 33846811599 scopus 로고    scopus 로고
    • Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/ deuterium exchange
    • Lu, X., Wintrode, P. L. and Surewicz, W. K., Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/ deuterium exchange. Proc. Natl. Acad. Sci. USA, 2007, 104, 1510-1515.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 181
    • 33846847762 scopus 로고    scopus 로고
    • A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis
    • Wilson, L. M. et al., A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis. J. Mol. Biol., 2007, 366, 1639-1651.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1639-1651
    • Wilson, L.M.1
  • 183
    • 77951081386 scopus 로고    scopus 로고
    • Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
    • Smith, D. P., Radford, S. E. and Ashcroft, A. E., Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc. Natl. Acad. Sci. USA, 2010, 107, 6794-6798.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6794-6798
    • Smith, D.P.1    Radford, S.E.2    Ashcroft, A.E.3
  • 184
    • 79954556420 scopus 로고    scopus 로고
    • Direct monitoring of heat-stressed biopolymers with temperature-controlled electrospray ionization mass spectrometry
    • Wang, G., Abzalimov, R. R. and Kaltashov, I. A., Direct monitoring of heat-stressed biopolymers with temperature-controlled electrospray ionization mass spectrometry. Anal. Chem., 2011, 15, 2870-2876.
    • (2011) Anal. Chem. , vol.15 , pp. 2870-2876
    • Wang, G.1    Abzalimov, R.R.2    Kaltashov, I.A.3
  • 185
    • 33745934794 scopus 로고    scopus 로고
    • Characterization of systemic amyloid deposits by mass spectrometry
    • Murphy, C. L., Wang, S., Williams, T., Weiss, D. T. and Solomon, A., Characterization of systemic amyloid deposits by mass spectrometry. Methods Enzymol., 2006, 412, 48-62.
    • (2006) Methods Enzymol. , vol.412 , pp. 48-62
    • Murphy, C.L.1    Wang, S.2    Williams, T.3    Weiss, D.T.4    Solomon, A.5
  • 188
    • 67849106670 scopus 로고    scopus 로고
    • Amloid-ß protein oligimerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
    • Bernstein, S. L. et al., Amloid-ß protein oligimerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nature Chem., 2009, 1, 326-331.
    • (2009) Nature Chem. , vol.1 , pp. 326-331
    • Bernstein, S.L.1
  • 189
    • 78049239444 scopus 로고    scopus 로고
    • Defining the mechanism of polymerization in the sepinopathies
    • Ekeowa, U. I. et al., Defining the mechanism of polymerization in the sepinopathies. Proc. Natl. Acad. Sci. USA, 2010, 107, 17146-17151.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17146-17151
    • Ekeowa, U.I.1
  • 190
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon, M. and Robinson, C. V., The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem., 2007, 76, 167-193.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 191
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott, F., Hernandez, H., McCammon, M. G., Tito, M. A. and Robinson, C. V., A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal. Chem., 2002, 74, 1402-1407.
    • (2002) Anal. Chem. , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 192
    • 20444427617 scopus 로고    scopus 로고
    • Heptameric (L12)6/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria
    • Ilag, L. L., Videler, H., McKay, A. R., Sobott, F., Fucini, P., Nierhaus, K. H. and Robinson, C. V., Heptameric (L12)6/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria. Proc. Natl. Acad. Sci. USA, 2005, 102, 8192-8197.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8192-8197
    • Ilag, L.L.1    Videler, H.2    McKay, A.R.3    Sobott, F.4    Fucini, P.5    Nierhaus, K.H.6    Robinson, C.V.7
  • 193
    • 1542723081 scopus 로고    scopus 로고
    • Collisional cooling of large ions in electrospray mass spectrometry
    • Chernushevich, I. V. and Thomson, B. A., Collisional cooling of large ions in electrospray mass spectrometry. Anal. Chem., 2004, 76, 1754-1760.
    • (2004) Anal. Chem. , vol.76 , pp. 1754-1760
    • Chernushevich, I.V.1    Thomson, B.A.2
  • 194
    • 0034687748 scopus 로고    scopus 로고
    • Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry
    • Fandrich, M., Tito, M. A., Leroux, M. R., Rostom, A. A., Hartl, F. U., Dobson, C. M. and Robinson, C. V., Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry. Proc. Natl. Acad. Sci. USA, 2000, 97, 14151-14155.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14151-14155
    • Fandrich, M.1    Tito, M.A.2    Leroux, M.R.3    Rostom, A.A.4    Hartl, F.U.5    Dobson, C.M.6    Robinson, C.V.7
  • 195
    • 34547132331 scopus 로고    scopus 로고
    • Mass spectrometry reveals the missing links in the assembly pathway of the bacterial 20 S proteasome
    • Sharon, M., Witt, S., Glasmacher, E., Baumeister, W. and Robinson, C. V., Mass spectrometry reveals the missing links in the assembly pathway of the bacterial 20 S proteasome. J. Biol. Chem., 2007, 282, 18448-18457.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18448-18457
    • Sharon, M.1    Witt, S.2    Glasmacher, E.3    Baumeister, W.4    Robinson, C.V.5
  • 197
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • Talkington, M. W., Siuzdak, G. and Williamson, J. R., An assembly landscape for the 30S ribosomal subunit. Nature, 2005, 438, 628-632.
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.W.1    Siuzdak, G.2    Williamson, J.R.3
  • 198
    • 58149112770 scopus 로고    scopus 로고
    • Quantitative ESI-TOF analysis of macromolecular assembly kinetics
    • Bunner, A. E., Trauger, S. A., Siuzdak, G. and Williamson, J. R., Quantitative ESI-TOF analysis of macromolecular assembly kinetics. Anal. Chem., 2008, 80, 9397-9386.
    • (2008) Anal. Chem. , vol.80 , pp. 9397-9386
    • Bunner, A.E.1    Trauger, S.A.2    Siuzdak, G.3    Williamson, J.R.4
  • 199
    • 70349267528 scopus 로고    scopus 로고
    • Stable isotope pulse-chase monitored by quantitative mass spectrometry applied to E. coli 30s ribosome assembly kinetics
    • Bunner, A. E. and Williamson, J. R., Stable isotope pulse-chase monitored by quantitative mass spectrometry applied to E. coli 30s ribosome assembly kinetics. Methods, 2009, 49, 136-141.
    • (2009) Methods , vol.49 , pp. 136-141
    • Bunner, A.E.1    Williamson, J.R.2
  • 200
    • 67650303382 scopus 로고    scopus 로고
    • A complex assembly landscape for the 30S ribosomal subunit
    • Sykes, M. T. and Williamson, J. R., A complex assembly landscape for the 30S ribosomal subunit. Annu. Rev. Biophys., 2009, 38, 197-215.
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 197-215
    • Sykes, M.T.1    Williamson, J.R.2
  • 201
    • 77950410654 scopus 로고    scopus 로고
    • Kinetic cooperativity in Escherichia coli 30S ribosomal subunit reconstitution reveals additional complexity in the assembly landscape
    • Bunner, A. E., Beck, A. H. and Williamson, J. R., Kinetic cooperativity in Escherichia coli 30S ribosomal subunit reconstitution reveals additional complexity in the assembly landscape. Proc. Natl. Acad. Sci. USA, 2010, 107, 5417-5422.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5417-5422
    • Bunner, A.E.1    Beck, A.H.2    Williamson, J.R.3
  • 203
    • 34547132331 scopus 로고    scopus 로고
    • Mass spectrometry reveals the missing links in the assembly pathway of the bacterial 20S proteosome
    • Sharon, M., Witt, S., Glasmacher, E., Baumeister, W. and Robinson, C. V., Mass spectrometry reveals the missing links in the assembly pathway of the bacterial 20S proteosome. J. Biol. Chem., 2007, 282, 18448-18457.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18448-18457
    • Sharon, M.1    Witt, S.2    Glasmacher, E.3    Baumeister, W.4    Robinson, C.V.5
  • 204
    • 33745827710 scopus 로고    scopus 로고
    • Proteasome assembly triggers a switch required for active-site maturation
    • Witt, S. et al., Proteasome assembly triggers a switch required for active-site maturation. Structure, 2006, 14, 1179-1188.
    • (2006) Structure , vol.14 , pp. 1179-1188
    • Witt, S.1
  • 205
    • 77951582169 scopus 로고    scopus 로고
    • Ion mobility mass spectrometry of proteins and protein assemblies
    • Utrech, C., Rose, R. J., van Duijn, E., Lorenzen, K. and Heck, A. J., Ion mobility mass spectrometry of proteins and protein assemblies. Chem. Soc. Rev., 2010, 39, 1633-1655.
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 1633-1655
    • Utrech, C.1    Rose, R.J.2    van Duijn, E.3    Lorenzen, K.4    Heck, A.J.5
  • 206
    • 78649712290 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals the influence of subunit packing and charge on the dissociation of multiprotein complexes
    • Boeri Erba, E., Ruotolo, B. T., Barsky, D. and Robinson, C. V., Ion mobility-mass spectrometry reveals the influence of subunit packing and charge on the dissociation of multiprotein complexes. Anal. Chem., 2010, 82, 9702-9710.
    • (2010) Anal. Chem. , vol.82 , pp. 9702-9710
    • Boeri Erba, E.1    Ruotolo, B.T.2    Barsky, D.3    Robinson, C.V.4
  • 208
    • 78449304111 scopus 로고    scopus 로고
    • Gas-phase compaction and unfolding of protein structures
    • Michaelevski, I., Eisenstein, M. and Sharon, M., Gas-phase compaction and unfolding of protein structures. Anal. Chem., 2010, 82, 9484-9491.
    • (2010) Anal. Chem. , vol.82 , pp. 9484-9491
    • Michaelevski, I.1    Eisenstein, M.2    Sharon, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.