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Volumn 54, Issue 28, 2015, Pages 4285-4296

Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ASSOCIATION REACTIONS; IONS; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MONOMERS; OLIGOMERS; PROTEINS; SPECTROMETRY;

EID: 84937576786     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00478     Document Type: Article
Times cited : (28)

References (82)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on huntingtons-disease chromosomes
    • The Huntington's Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on huntingtons-disease chromosomes Cell 72, 971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 2
    • 0030919726 scopus 로고    scopus 로고
    • CAG repeat number governs the development rate of pathology in Huntington's disease
    • Penney, J. B., Vonsattel, J. P., MacDonald, M. E., Gusella, J. F., and Myers, R. H. (1997) CAG repeat number governs the development rate of pathology in Huntington's disease Ann. Neurol. 41, 689-692
    • (1997) Ann. Neurol. , vol.41 , pp. 689-692
    • Penney, J.B.1    Vonsattel, J.P.2    MacDonald, M.E.3    Gusella, J.F.4    Myers, R.H.5
  • 5
    • 84856226648 scopus 로고    scopus 로고
    • Slow Amyloid Nucleation via alpha-Helix-Rich Oligomeric Intermediates in Short Polyglutamine-Containing Huntingtin Fragments
    • Jayaraman, M., Kodali, R., Sahoo, B., Thakur, A. K., Mayasundari, A., Mishra, R., Peterson, C. B., and Wetzel, R. (2012) Slow Amyloid Nucleation via alpha-Helix-Rich Oligomeric Intermediates in Short Polyglutamine-Containing Huntingtin Fragments J. Mol. Biol. 415, 881-899
    • (2012) J. Mol. Biol. , vol.415 , pp. 881-899
    • Jayaraman, M.1    Kodali, R.2    Sahoo, B.3    Thakur, A.K.4    Mayasundari, A.5    Mishra, R.6    Peterson, C.B.7    Wetzel, R.8
  • 6
    • 84902164061 scopus 로고    scopus 로고
    • Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations
    • n/a-n/a
    • Coîté, S., Wei, G., and Mousseau, N. (2014) Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations Proteins: Struct., Funct., Bioinf. n/a-n/a
    • (2014) Proteins: Struct., Funct., Bioinf.
    • Coîté, S.1    Wei, G.2    Mousseau, N.3
  • 7
    • 84873381579 scopus 로고    scopus 로고
    • Membrane Interactions of the Amphipathic Amino Terminus of Huntingtin
    • Michalek, M., Salnikov, E. S., Werten, S., and Bechinger, B. (2013) Membrane Interactions of the Amphipathic Amino Terminus of Huntingtin Biochemistry 52, 847-858
    • (2013) Biochemistry , vol.52 , pp. 847-858
    • Michalek, M.1    Salnikov, E.S.2    Werten, S.3    Bechinger, B.4
  • 8
    • 84878217830 scopus 로고    scopus 로고
    • The Interaction of Polyglutamine Peptides with Lipid Membranes is Regulated by Flanking Sequences Associated with Huntingtin
    • Burke, K. A., Kauffman, K. J., Umbaugh, C. S., Frey, S. L., and Legleiter, J. (2013) The Interaction of Polyglutamine Peptides With Lipid Membranes is Regulated by Flanking Sequences Associated with Huntingtin J. Biol. Chem. 288, 14993-5005
    • (2013) J. Biol. Chem. , vol.288 , pp. 14993-15005
    • Burke, K.A.1    Kauffman, K.J.2    Umbaugh, C.S.3    Frey, S.L.4    Legleiter, J.5
  • 9
    • 84874787234 scopus 로고    scopus 로고
    • An N-terminal Nuclear Export Signal Regulates Trafficking and Aggregation of Huntingtin (Htt) Protein Exon 1
    • Zheng, Z. Q., Li, A. M., Holmes, B. B., Marasa, J. C., and Diamond, M. I. (2013) An N-terminal Nuclear Export Signal Regulates Trafficking and Aggregation of Huntingtin (Htt) Protein Exon 1 J. Biol. Chem. 288, 6063-6071
    • (2013) J. Biol. Chem. , vol.288 , pp. 6063-6071
    • Zheng, Z.Q.1    Li, A.M.2    Holmes, B.B.3    Marasa, J.C.4    Diamond, M.I.5
  • 10
    • 84881409549 scopus 로고    scopus 로고
    • Structure and Topology of the Huntingtin 1 17 Membrane Anchor by a Combined Solution and Solid-State NMR Approach
    • Michalek, M., Salnikov, E. S., and Bechinger, B. (2013) Structure and Topology of the Huntingtin 1 17 Membrane Anchor by a Combined Solution and Solid-State NMR Approach Biophys. J. 105, 699-710
    • (2013) Biophys. J. , vol.105 , pp. 699-710
    • Michalek, M.1    Salnikov, E.S.2    Bechinger, B.3
  • 11
    • 80053259405 scopus 로고    scopus 로고
    • Conformations of the Huntingtin N-term in aqueous solution from atomistic simulations
    • Rossetti, G., Cossio, P., Laio, A., and Carloni, P. (2011) Conformations of the Huntingtin N-term in aqueous solution from atomistic simulations FEBS Lett. 585, 3086-3089
    • (2011) FEBS Lett. , vol.585 , pp. 3086-3089
    • Rossetti, G.1    Cossio, P.2    Laio, A.3    Carloni, P.4
  • 12
    • 77649271684 scopus 로고    scopus 로고
    • Modulation of Polyglutamine Conformations and Dimer Formation by the N-Terminus of Huntingtin
    • Williamson, T. E., Vitalis, A., Crick, S. L., and Pappu, R. V. (2010) Modulation of Polyglutamine Conformations and Dimer Formation by the N-Terminus of Huntingtin J. Mol. Biol. 396, 1295-1309
    • (2010) J. Mol. Biol. , vol.396 , pp. 1295-1309
    • Williamson, T.E.1    Vitalis, A.2    Crick, S.L.3    Pappu, R.V.4
  • 14
    • 84868200854 scopus 로고    scopus 로고
    • Serine Phosphorylation Suppresses Huntingtin Amyloid Accumulation by Altering Protein Aggregation Properties
    • Mishra, R., Hoop, C. L., Kodali, R., Sahoo, B., van der Wel, P. C. A., and Wetzel, R. (2012) Serine Phosphorylation Suppresses Huntingtin Amyloid Accumulation by Altering Protein Aggregation Properties J. Mol. Biol. 424, 1-14
    • (2012) J. Mol. Biol. , vol.424 , pp. 1-14
    • Mishra, R.1    Hoop, C.L.2    Kodali, R.3    Sahoo, B.4    Van Der Wel, P.C.A.5    Wetzel, R.6
  • 17
    • 84908300165 scopus 로고    scopus 로고
    • Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state NMR
    • Hoop, C. L., Lin, H.-K., Kar, K., Hou, Z., Poirier, M. A., Wetzel, R., and van der Wel, P. C. A. (2014) Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state NMR Biochemistry 10.1021/bi501010q
    • (2014) Biochemistry
    • Hoop, C.L.1    Lin, H.-K.2    Kar, K.3    Hou, Z.4    Poirier, M.A.5    Wetzel, R.6    Van Der Wel, P.C.A.7
  • 19
    • 0029841917 scopus 로고    scopus 로고
    • Gas-Phase Conformation of Biological Molecules: Bradykinin
    • Wyttenbach, T., von Helden, G., and Bowers, M. T. (1996) Gas-Phase Conformation of Biological Molecules: Bradykinin J. Am. Chem. Soc. 118, 8355-8364
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8355-8364
    • Wyttenbach, T.1    Von Helden, G.2    Bowers, M.T.3
  • 20
    • 0036558161 scopus 로고    scopus 로고
    • Cis-Trans Signatures of Proline-Containing Tryptic Peptides in the Gas Phase
    • Counterman, A. E. and Clemmer, D. E. (2002) Cis-Trans Signatures of Proline-Containing Tryptic Peptides in the Gas Phase Anal. Chem. 74, 1946-1951
    • (2002) Anal. Chem. , vol.74 , pp. 1946-1951
    • Counterman, A.E.1    Clemmer, D.E.2
  • 21
    • 0035814755 scopus 로고    scopus 로고
    • Large anhydrous polyalanine ions: Substitution of Na+ for H+ destabilizes folded states
    • Taraszka, J. A., Counterman, A. E., and Clemmer, D. E. (2001) Large anhydrous polyalanine ions: substitution of Na+ for H+ destabilizes folded states Int. J. Mass Spectrom. 204, 87-100
    • (2001) Int. J. Mass Spectrom. , vol.204 , pp. 87-100
    • Taraszka, J.A.1    Counterman, A.E.2    Clemmer, D.E.3
  • 22
    • 0033620367 scopus 로고    scopus 로고
    • Thermal Unfolding of Unsolvated Cytochrome c: Experiment and Molecular Dynamics Simulations
    • Mao, Y., Woenckhaus, J., Kolafa, J., Ratner, M. A., and Jarrold, M. F. (1999) Thermal Unfolding of Unsolvated Cytochrome c: Experiment and Molecular Dynamics Simulations J. Am. Chem. Soc. 121, 2712-2721
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2712-2721
    • Mao, Y.1    Woenckhaus, J.2    Kolafa, J.3    Ratner, M.A.4    Jarrold, M.F.5
  • 23
    • 84865788284 scopus 로고    scopus 로고
    • Structural modeling of heteromeric protein complexes from disassembly pathways and ion mobility-mass spectrometry
    • Hall, Z., Politis, A., and Robinson, C. V. (2012) Structural modeling of heteromeric protein complexes from disassembly pathways and ion mobility-mass spectrometry Structure 20, 1596-1609
    • (2012) Structure , vol.20 , pp. 1596-1609
    • Hall, Z.1    Politis, A.2    Robinson, C.V.3
  • 24
    • 77957784477 scopus 로고    scopus 로고
    • Integrating Ion Mobility Mass Spectrometry with Molecular Modelling to Determine the Architecture of Multiprotein Complexes
    • Politis, A., Park, A. Y., Hyung, S.-J., Barsky, D., Ruotolo, B. T., and Robinson, C. V. (2010) Integrating Ion Mobility Mass Spectrometry with Molecular Modelling to Determine the Architecture of Multiprotein Complexes PLoS One 5, e12080
    • (2010) PLoS One , vol.5 , pp. e12080
    • Politis, A.1    Park, A.Y.2    Hyung, S.-J.3    Barsky, D.4    Ruotolo, B.T.5    Robinson, C.V.6
  • 25
    • 35648957210 scopus 로고    scopus 로고
    • Ion Mobility-Mass Spectrometry Reveals Long-Lived, Unfolded Intermediates in the Dissociation of Protein Complexes
    • Ruotolo, B. T., Hyung, S.-J., Robinson, P. M., Giles, K., Bateman, R. H., and Robinson, C. V. (2007) Ion Mobility-Mass Spectrometry Reveals Long-Lived, Unfolded Intermediates in the Dissociation of Protein Complexes Angew. Chem., Int. Ed. 46, 8001-8004
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 8001-8004
    • Ruotolo, B.T.1    Hyung, S.-J.2    Robinson, P.M.3    Giles, K.4    Bateman, R.H.5    Robinson, C.V.6
  • 26
    • 0037212630 scopus 로고    scopus 로고
    • Application of ion mobility to the gas-phase conformational analysis of polyhedral oligomeric silsesquioxanes (POSS)
    • Gidden, J., Kemper, P. R., Shammel, E., Fee, D. P., Anderson, S., and Bowers, M. T. (2003) Application of ion mobility to the gas-phase conformational analysis of polyhedral oligomeric silsesquioxanes (POSS) Int. J. Mass Spectrom. 222, 63-73
    • (2003) Int. J. Mass Spectrom. , vol.222 , pp. 63-73
    • Gidden, J.1    Kemper, P.R.2    Shammel, E.3    Fee, D.P.4    Anderson, S.5    Bowers, M.T.6
  • 27
    • 80054892557 scopus 로고    scopus 로고
    • Structural Stability from Solution to the Gas Phase: Native Solution Structure of Ubiquitin Survives Analysis in a Solvent-Free Ion Mobility-Mass Spectrometry Environment
    • Wyttenbach, T. and Bowers, M. T. (2011) Structural Stability from Solution to the Gas Phase: Native Solution Structure of Ubiquitin Survives Analysis in a Solvent-Free Ion Mobility-Mass Spectrometry Environment J. Phys. Chem. B 115, 12266-12275
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12266-12275
    • Wyttenbach, T.1    Bowers, M.T.2
  • 28
    • 80052326593 scopus 로고    scopus 로고
    • Number of Solution States of Bradykinin from Ion Mobility and Mass Spectrometry Measurements
    • Pierson, N. A., Chen, L., Valentine, S. J., Russell, D. H., and Clemmer, D. E. (2011) Number of Solution States of Bradykinin from Ion Mobility and Mass Spectrometry Measurements J. Am. Chem. Soc. 133, 13810-13813
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13810-13813
    • Pierson, N.A.1    Chen, L.2    Valentine, S.J.3    Russell, D.H.4    Clemmer, D.E.5
  • 30
    • 84858327195 scopus 로고    scopus 로고
    • Conformation Types of Ubiquitin M+8H (8+) Ions from Water:Methanol Solutions: Evidence for the N and A States in Aqueous Solution
    • Shi, H. L., Pierson, N. A., Valentine, S. J., and Clemmer, D. E. (2012) Conformation Types of Ubiquitin M+8H (8+) Ions from Water:Methanol Solutions: Evidence for the N and A States in Aqueous Solution J. Phys. Chem. B 116, 3344-3352
    • (2012) J. Phys. Chem. B , vol.116 , pp. 3344-3352
    • Shi, H.L.1    Pierson, N.A.2    Valentine, S.J.3    Clemmer, D.E.4
  • 31
    • 84907486653 scopus 로고    scopus 로고
    • Characterizing Intermediates Along the Transition from Polyproline i to Polyproline II Using Ion Mobility Spectrometry-Mass Spectrometry
    • Shi, L., Holliday, A. E., Shi, H., Zhu, F., Ewing, M. A., Russell, D. H., and Clemmer, D. E. (2014) Characterizing Intermediates Along the Transition from Polyproline I to Polyproline II Using Ion Mobility Spectrometry-Mass Spectrometry J. Am. Chem. Soc. 136, 12702-11
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 12702-12711
    • Shi, L.1    Holliday, A.E.2    Shi, H.3    Zhu, F.4    Ewing, M.A.5    Russell, D.H.6    Clemmer, D.E.7
  • 32
    • 0000837469 scopus 로고    scopus 로고
    • High resolution ion mobility measurements for gas phase proteins: Correlation between solution phase and gas phase conformations
    • Hudgins, R. R., Woenckhaus, J., and Jarrold, M. F. (1997) High resolution ion mobility measurements for gas phase proteins: correlation between solution phase and gas phase conformations Int. J. Mass Spectrom. 165-166, 497-507
    • (1997) Int. J. Mass Spectrom. , vol.165-166 , pp. 497-507
    • Hudgins, R.R.1    Woenckhaus, J.2    Jarrold, M.F.3
  • 33
    • 0028855096 scopus 로고
    • Naked Protein Conformations: Cytochrome c in the Gas Phase
    • Clemmer, D. E., Hudgins, R. R., and Jarrold, M. F. (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
  • 34
    • 84887736083 scopus 로고    scopus 로고
    • Ion Mobility Spectrometry Reveals the Mechanism of Amyloid Formation of A beta(25-35) and Its Modulation by Inhibitors at the Molecular Level: Epigallocatechin Gallate and Scyllo-inositol
    • Bleiholder, C., Do, T. D., Wu, C., Economou, N. J., Bernstein, S. S., Buratto, S. K., Shea, J. E., and Bowers, M. T. (2013) Ion Mobility Spectrometry Reveals the Mechanism of Amyloid Formation of A beta(25-35) and Its Modulation by Inhibitors at the Molecular Level: Epigallocatechin Gallate and Scyllo-inositol J. Am. Chem. Soc. 135, 16926-16937
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 16926-16937
    • Bleiholder, C.1    Do, T.D.2    Wu, C.3    Economou, N.J.4    Bernstein, S.S.5    Buratto, S.K.6    Shea, J.E.7    Bowers, M.T.8
  • 35
    • 84874640131 scopus 로고    scopus 로고
    • Carbohydrate Structure Characterization by Tandem Ion Mobility Mass Spectrometry (IMMS)2
    • Li, H., Bendiak, B., Siems, W. F., Gang, D. R., and Hill, H. H. (2013) Carbohydrate Structure Characterization by Tandem Ion Mobility Mass Spectrometry (IMMS)2 Anal. Chem. 85, 2760-2769
    • (2013) Anal. Chem. , vol.85 , pp. 2760-2769
    • Li, H.1    Bendiak, B.2    Siems, W.F.3    Gang, D.R.4    Hill, H.H.5
  • 36
    • 79952006474 scopus 로고    scopus 로고
    • Ion Mobility Separation Coupled with MS Detects Two Structural States of Alzheimer's Disease A beta 1-40 Peptide Oligomers
    • Kloniecki, M., Jablonowska, A., Poznanski, J., Langridge, J., Hughes, C., Campuzano, I., Giles, K., and Dadlez, M. (2011) Ion Mobility Separation Coupled with MS Detects Two Structural States of Alzheimer's Disease A beta 1-40 Peptide Oligomers J. Mol. Biol. 407, 110-124
    • (2011) J. Mol. Biol. , vol.407 , pp. 110-124
    • Kloniecki, M.1    Jablonowska, A.2    Poznanski, J.3    Langridge, J.4    Hughes, C.5    Campuzano, I.6    Giles, K.7    Dadlez, M.8
  • 37
    • 80053577933 scopus 로고    scopus 로고
    • Ion Mobility-Mass Spectrometry Reveals Conformational Changes in Charge Reduced Multiprotein Complexes
    • Bornschein, R. E., Hyung, S. J., and Ruotolo, B. T. (2011) Ion Mobility-Mass Spectrometry Reveals Conformational Changes in Charge Reduced Multiprotein Complexes J. Am. Soc. Mass Spectrom. 22, 1690-1698
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1690-1698
    • Bornschein, R.E.1    Hyung, S.J.2    Ruotolo, B.T.3
  • 39
    • 33646801627 scopus 로고    scopus 로고
    • Characterizing the structures and folding of free proteins using 2-D gas-phase separations: Observation of multiple unfolded conformers
    • Shvartsburg, A. A., Li, F. M., Tang, K. Q., and Smith, R. D. (2006) Characterizing the structures and folding of free proteins using 2-D gas-phase separations: Observation of multiple unfolded conformers Anal. Chem. 78, 3304-3315
    • (2006) Anal. Chem. , vol.78 , pp. 3304-3315
    • Shvartsburg, A.A.1    Li, F.M.2    Tang, K.Q.3    Smith, R.D.4
  • 40
    • 77749322503 scopus 로고    scopus 로고
    • Structural Characterization of Phospholipids and Peptides Directly from Tissue Sections by MALDI Traveling-Wave Ion Mobility-Mass Spectrometry
    • Ridenour, W. B., Kliman, M., McLean, J. A., and Caprioli, R. M. (2010) Structural Characterization of Phospholipids and Peptides Directly from Tissue Sections by MALDI Traveling-Wave Ion Mobility-Mass Spectrometry Anal. Chem. 82, 1881-1889
    • (2010) Anal. Chem. , vol.82 , pp. 1881-1889
    • Ridenour, W.B.1    Kliman, M.2    McLean, J.A.3    Caprioli, R.M.4
  • 41
    • 84862909014 scopus 로고    scopus 로고
    • Structural Characterization of Drug-like Compounds by Ion Mobility Mass Spectrometry: Comparison of Theoretical and Experimentally Derived Nitrogen Collision Cross Sections
    • Campuzano, I., Bush, M. F., Robinson, C. V., Beaumont, C., Richardson, K., Kim, H., and Kim, H. I. (2011) Structural Characterization of Drug-like Compounds by Ion Mobility Mass Spectrometry: Comparison of Theoretical and Experimentally Derived Nitrogen Collision Cross Sections Anal. Chem. 84, 1026-1033
    • (2011) Anal. Chem. , vol.84 , pp. 1026-1033
    • Campuzano, I.1    Bush, M.F.2    Robinson, C.V.3    Beaumont, C.4    Richardson, K.5    Kim, H.6    Kim, H.I.7
  • 42
    • 0032093224 scopus 로고    scopus 로고
    • Three-Dimensional Ion Mobility/TOFMS Analysis of Electrosprayed Biomolecules
    • Hoaglund, C. S., Valentine, S. J., Sporleder, C. R., Reilly, J. P., and Clemmer, D. E. (1998) Three-Dimensional Ion Mobility/TOFMS Analysis of Electrosprayed Biomolecules Anal. Chem. 70, 2236-2242
    • (1998) Anal. Chem. , vol.70 , pp. 2236-2242
    • Hoaglund, C.S.1    Valentine, S.J.2    Sporleder, C.R.3    Reilly, J.P.4    Clemmer, D.E.5
  • 43
    • 0032403450 scopus 로고    scopus 로고
    • Electrospray Ionization High-Resolution Ion Mobility Spectrometry-Mass Spectrometry
    • Wu, C., Siems, W. F., Asbury, G. R., and Hill, H. H. (1998) Electrospray Ionization High-Resolution Ion Mobility Spectrometry-Mass Spectrometry Anal. Chem. 70, 4929-4938
    • (1998) Anal. Chem. , vol.70 , pp. 4929-4938
    • Wu, C.1    Siems, W.F.2    Asbury, G.R.3    Hill, H.H.4
  • 44
    • 84856212436 scopus 로고    scopus 로고
    • Inhibiting the Nucleation of Amyloid Structure in a Huntingtin Fragment by Targeting alpha-Helix-Rich Oligomeric Intermediates
    • Mishra, R., Jayaraman, M., Roland, B. P., Landrum, E., Fullam, T., Kodali, R., Thakur, A. K., Arduini, I., and Wetzel, R. (2012) Inhibiting the Nucleation of Amyloid Structure in a Huntingtin Fragment by Targeting alpha-Helix-Rich Oligomeric Intermediates J. Mol. Biol. 415, 900-917
    • (2012) J. Mol. Biol. , vol.415 , pp. 900-917
    • Mishra, R.1    Jayaraman, M.2    Roland, B.P.3    Landrum, E.4    Fullam, T.5    Kodali, R.6    Thakur, A.K.7    Arduini, I.8    Wetzel, R.9
  • 46
    • 84863011516 scopus 로고    scopus 로고
    • A beta(39-42) Modulates A beta Oligomerization but Not Fibril Formation
    • Gessel, M. M., Wu, C., Li, H. Y., Bitan, G., Shea, J. E., and Bowers, M. T. (2012) A beta(39-42) Modulates A beta Oligomerization but Not Fibril Formation Biochemistry 51, 108-117
    • (2012) Biochemistry , vol.51 , pp. 108-117
    • Gessel, M.M.1    Wu, C.2    Li, H.Y.3    Bitan, G.4    Shea, J.E.5    Bowers, M.T.6
  • 47
    • 79251631002 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to beta-sheet in amyloid fibril formation
    • Bleiholder, C., Dupuis, N. F., Wyttenbach, T., and Bowers, M. T. (2011) Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to beta-sheet in amyloid fibril formation Nat. Chem. 3, 172-177
    • (2011) Nat. Chem. , vol.3 , pp. 172-177
    • Bleiholder, C.1    Dupuis, N.F.2    Wyttenbach, T.3    Bowers, M.T.4
  • 48
    • 13944282886 scopus 로고    scopus 로고
    • Amyloid beta-protein: Monomer structure and early aggregation states of A beta 42 and its Pro(19) alloform
    • Bernstein, S. L., Wyttenbach, T., Baumketner, A., Shea, J. E., Bitan, G., Teplow, D. B., and Bowers, M. T. (2005) Amyloid beta-protein: Monomer structure and early aggregation states of A beta 42 and its Pro(19) alloform J. Am. Chem. Soc. 127, 2075-2084
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2075-2084
    • Bernstein, S.L.1    Wyttenbach, T.2    Baumketner, A.3    Shea, J.E.4    Bitan, G.5    Teplow, D.B.6    Bowers, M.T.7
  • 49
    • 77449095000 scopus 로고    scopus 로고
    • Structure of the Preamyloid Dimer of beta-2-Microglobulin from Covalent Labeling and Mass Spectrometry
    • Mendoza, V. L., Antwi, K., Baron-Rodriguez, M. A., Blanco, C., and Vachet, R. W. (2010) Structure of the Preamyloid Dimer of beta-2-Microglobulin from Covalent Labeling and Mass Spectrometry Biochemistry 49, 1522-1532
    • (2010) Biochemistry , vol.49 , pp. 1522-1532
    • Mendoza, V.L.1    Antwi, K.2    Baron-Rodriguez, M.A.3    Blanco, C.4    Vachet, R.W.5
  • 50
    • 79961041262 scopus 로고    scopus 로고
    • Structural Insights into the Pre-Amyloid Tetramer of beta-2-Microglobulin from Covalent Labeling and Mass Spectrometry
    • Mendoza, V. L., Baron-Rodriguez, M. A., Blanco, C., and Vachet, R. W. (2011) Structural Insights into the Pre-Amyloid Tetramer of beta-2-Microglobulin from Covalent Labeling and Mass Spectrometry Biochemistry 50, 6711-6722
    • (2011) Biochemistry , vol.50 , pp. 6711-6722
    • Mendoza, V.L.1    Baron-Rodriguez, M.A.2    Blanco, C.3    Vachet, R.W.4
  • 51
    • 79957681753 scopus 로고    scopus 로고
    • Temporal Development of Protein Structure during S100A11 Folding and Dimerization Probed by Oxidative Labeling and Mass Spectrometry
    • Stocks, B. B., Rezvanpour, A., Shaw, G. S., and Konermann, L. (2011) Temporal Development of Protein Structure during S100A11 Folding and Dimerization Probed by Oxidative Labeling and Mass Spectrometry J. Mol. Biol. 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
  • 52
    • 84921649003 scopus 로고    scopus 로고
    • Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation
    • Arndt, J. R., Brown, R. J., Burke, K. A., Legleiter, J., and Valentine, S. J. (2015) Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation J. Mass Spectrom. 50, 117-126
    • (2015) J. Mass Spectrom. , vol.50 , pp. 117-126
    • Arndt, J.R.1    Brown, R.J.2    Burke, K.A.3    Legleiter, J.4    Valentine, S.J.5
  • 53
    • 69849100869 scopus 로고    scopus 로고
    • Probing protein structure by amino acid-specific covalent labeling and mass spectrometry
    • Mendoza, V. L. and Vachet, R. W. (2009) Probing protein structure by amino acid-specific covalent labeling and mass spectrometry Mass Spec. Rev. 28, 785-815
    • (2009) Mass Spec. Rev. , vol.28 , pp. 785-815
    • Mendoza, V.L.1    Vachet, R.W.2
  • 54
    • 42349091083 scopus 로고    scopus 로고
    • Protein Surface Mapping Using Diethylpyrocarbonate with Mass Spectrometric Detection
    • Mendoza, V. L. and Vachet, R. W. (2008) Protein Surface Mapping Using Diethylpyrocarbonate with Mass Spectrometric Detection Anal. Chem. 80, 2895-2904
    • (2008) Anal. Chem. , vol.80 , pp. 2895-2904
    • Mendoza, V.L.1    Vachet, R.W.2
  • 56
    • 84919949421 scopus 로고    scopus 로고
    • Combining Ion Mobility Spectrometry with Hydrogen-Deuterium Exchange and Top-Down MS for Peptide Ion Structure Analysis
    • Khakinejad, M., Kondalaji, S. G., Maleki, H., Arndt, J. R., Donohoe, G. C., and Valentine, S. J. (2014) Combining Ion Mobility Spectrometry with Hydrogen-Deuterium Exchange and Top-Down MS for Peptide Ion Structure Analysis J. Am. Soc. Mass Spectrom. 25, 2103-2115
    • (2014) J. Am. Soc. Mass Spectrom. , vol.25 , pp. 2103-2115
    • Khakinejad, M.1    Kondalaji, S.G.2    Maleki, H.3    Arndt, J.R.4    Donohoe, G.C.5    Valentine, S.J.6
  • 59
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges - The RESP model
    • Bayly, C. I., Cieplak, P., Cornell, W. D., and Kollman, P. A. (1993) A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges-the RESP model J. Phys. Chem. 97, 10269-10280
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 62
    • 0029841917 scopus 로고    scopus 로고
    • Gas-phase conformation of biological molecules: Bradykinin
    • Wyttenbach, T., vonHelden, G., and Bowers, M. T. (1996) Gas-phase conformation of biological molecules: Bradykinin J. Am. Chem. Soc. 118, 8355-8364
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8355-8364
    • Wyttenbach, T.1    Vonhelden, G.2    Bowers, M.T.3
  • 65
    • 33748887803 scopus 로고    scopus 로고
    • Structural Information from Ion Mobility Measurements: Effects of the Long-Range Potential
    • Mesleh, M. F., Hunter, J. M., Shvartsburg, A. A., Schatz, G. C., and Jarrold, M. F. (1996) Structural Information from Ion Mobility Measurements: Effects of the Long-Range Potential J. Phys. Chem. 100, 16082-16086
    • (1996) J. Phys. Chem. , vol.100 , pp. 16082-16086
    • Mesleh, M.F.1    Hunter, J.M.2    Shvartsburg, A.A.3    Schatz, G.C.4    Jarrold, M.F.5
  • 66
    • 84924908297 scopus 로고    scopus 로고
    • Ion Mobility Spectrometry-Hydrogen Deuterium Exchange Mass Spectrometry of Anions: Part 1. Peptides to Proteins
    • Donohoe, G., Khakinejad, M., and Valentine, S. (2015) Ion Mobility Spectrometry-Hydrogen Deuterium Exchange Mass Spectrometry of Anions: Part 1. Peptides to Proteins J. Am. Soc. Mass Spectrom. 26, 564-576
    • (2015) J. Am. Soc. Mass Spectrom. , vol.26 , pp. 564-576
    • Donohoe, G.1    Khakinejad, M.2    Valentine, S.3
  • 69
    • 84866419575 scopus 로고    scopus 로고
    • Structural Features and Domain Organization of Huntingtin Fibrils
    • Bugg, C. W., Isas, J. M., Fischer, T., Patterson, P. H., and Langen, R. (2012) Structural Features and Domain Organization of Huntingtin Fibrils J. Biol. Chem. 287, 31739-31746
    • (2012) J. Biol. Chem. , vol.287 , pp. 31739-31746
    • Bugg, C.W.1    Isas, J.M.2    Fischer, T.3    Patterson, P.H.4    Langen, R.5
  • 70
    • 71449084004 scopus 로고    scopus 로고
    • The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
    • Tam, S., Spiess, C., Auyeung, W., Joachimiak, L., Chen, B., Poirier, M. A., and Frydman, J. (2009) The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation Nat. Struct. Mol. Biol. 16, 1279-U1298
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. U1279-U1298
    • Tam, S.1    Spiess, C.2    Auyeung, W.3    Joachimiak, L.4    Chen, B.5    Poirier, M.A.6    Frydman, J.7
  • 72
    • 80053923210 scopus 로고    scopus 로고
    • Secondary Structures of Native and Pathogenic Huntingtin N-Terminal Fragments
    • Dlugosz, M. and Trylska, J. (2011) Secondary Structures of Native and Pathogenic Huntingtin N-Terminal Fragments J. Phys. Chem.B 115, 11597-11608
    • (2011) J. Phys. Chem.B , vol.115 , pp. 11597-11608
    • Dlugosz, M.1    Trylska, J.2
  • 73
    • 80053259405 scopus 로고    scopus 로고
    • Conformations of the Huntingtin N-term in aqueous solution from atomistic simulations
    • Rossetti, G., Cossio, P., Laio, A., and Carloni, P. (2011) Conformations of the Huntingtin N-term in aqueous solution from atomistic simulations FEBS Lett. 585, 3086-3089
    • (2011) FEBS Lett. , vol.585 , pp. 3086-3089
    • Rossetti, G.1    Cossio, P.2    Laio, A.3    Carloni, P.4
  • 74
    • 67349278762 scopus 로고    scopus 로고
    • The Predicted Structure of the Headpiece of the Huntingtin Protein and Its Implications on Huntingtin Aggregation
    • Kelley, N. W., Huang, X., Tam, S., Spiess, C., Frydman, J., and Pande, V. S. (2009) The Predicted Structure of the Headpiece of the Huntingtin Protein and Its Implications on Huntingtin Aggregation J. Mol. Biol. 388, 919-927
    • (2009) J. Mol. Biol. , vol.388 , pp. 919-927
    • Kelley, N.W.1    Huang, X.2    Tam, S.3    Spiess, C.4    Frydman, J.5    Pande, V.S.6
  • 76
    • 84908509758 scopus 로고    scopus 로고
    • Role of the Coiled-Coil Structural Motif in Polyglutamine Aggregation
    • Kokona, B., Rosenthal, Z. P., and Fairman, R. (2014) Role of the Coiled-Coil Structural Motif in Polyglutamine Aggregation Biochemistry 53, 6738-6746
    • (2014) Biochemistry , vol.53 , pp. 6738-6746
    • Kokona, B.1    Rosenthal, Z.P.2    Fairman, R.3
  • 80
    • 84867267823 scopus 로고    scopus 로고
    • Post-aggregation Oxidation of Mutant Huntingtin Controls the Interactions between Aggregates
    • Mitomi, Y., Nomura, T., Kurosawa, M., Nukina, N., and Furukawa, Y. (2012) Post-aggregation Oxidation of Mutant Huntingtin Controls the Interactions between Aggregates J. Biol. Chem. 287, 34764-34775
    • (2012) J. Biol. Chem. , vol.287 , pp. 34764-34775
    • Mitomi, Y.1    Nomura, T.2    Kurosawa, M.3    Nukina, N.4    Furukawa, Y.5
  • 81
    • 84890288534 scopus 로고    scopus 로고
    • Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation
    • Crick, S. L., Ruff, K. M., Garai, K., Frieden, C., and Pappu, R. V. (2013) Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation Proc. Nat. Acad. Sci. U.S.A. 110, 20075-20080
    • (2013) Proc. Nat. Acad. Sci. U.S.A. , vol.110 , pp. 20075-20080
    • Crick, S.L.1    Ruff, K.M.2    Garai, K.3    Frieden, C.4    Pappu, R.V.5
  • 82
    • 84902970753 scopus 로고    scopus 로고
    • The Effects of Flanking Sequences in the Interaction of Polyglutamine Peptides with a Membrane Bilayer
    • Nagarajan, A., Jawahery, S., and Matysiak, S. (2014) The Effects of Flanking Sequences in the Interaction of Polyglutamine Peptides with a Membrane Bilayer J. Phys. Chem. B 118, 6368-6379
    • (2014) J. Phys. Chem. B , vol.118 , pp. 6368-6379
    • Nagarajan, A.1    Jawahery, S.2    Matysiak, S.3


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