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Volumn 102, Issue 11, 2012, Pages 2595-2604

Characterizing intermolecular interactions that initiate native-like protein aggregation

Author keywords

[No Author keywords available]

Indexed keywords

ACID ANHYDRIDE HYDROLASE; ACYLPHOSPHATASE; AMIDE;

EID: 84861872576     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.03.057     Document Type: Article
Times cited : (27)

References (29)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 33749864323 scopus 로고    scopus 로고
    • Sequence and structural determinants of amyloid fibril formation
    • F. Bemporad, and G. Calloni F. Chiti Sequence and structural determinants of amyloid fibril formation Acc. Chem. Res. 39 2006 620 627
    • (2006) Acc. Chem. Res. , vol.39 , pp. 620-627
    • Bemporad, F.1    Calloni, G.2    Chiti, F.3
  • 3
    • 0034725535 scopus 로고    scopus 로고
    • The protofilament substructure of amyloid fibrils
    • L.C. Serpell, and M. Sunde P.E. Fraser The protofilament substructure of amyloid fibrils J. Mol. Biol. 300 2000 1033 1039
    • (2000) J. Mol. Biol. , vol.300 , pp. 1033-1039
    • Serpell, L.C.1    Sunde, M.2    Fraser, P.E.3
  • 4
    • 0036220131 scopus 로고    scopus 로고
    • Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
    • D. Canet, and A.M. Last C.M. Dobson Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme Nat. Struct. Biol. 9 2002 308 315
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 308-315
    • Canet, D.1    Last, A.M.2    Dobson, C.M.3
  • 5
    • 77951990084 scopus 로고    scopus 로고
    • Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates
    • K. Pagano, and F. Bemporad A. Corazza Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates J. Biol. Chem. 285 2010 14689 14700
    • (2010) J. Biol. Chem. , vol.285 , pp. 14689-14700
    • Pagano, K.1    Bemporad, F.2    Corazza, A.3
  • 6
    • 1242316998 scopus 로고    scopus 로고
    • Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy
    • A. Olofsson, and J.H. Ippel A. Ohman Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy J. Biol. Chem. 279 2004 5699 5707
    • (2004) J. Biol. Chem. , vol.279 , pp. 5699-5707
    • Olofsson, A.1    Ippel, J.H.2    Ohman, A.3
  • 7
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • A. Quintas, and D.C. Vaz R.M. Brito Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants J. Biol. Chem. 276 2001 27207 27213
    • (2001) J. Biol. Chem. , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Brito, R.M.3
  • 8
    • 0038442784 scopus 로고    scopus 로고
    • Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
    • J.S. Elam, and A.B. Taylor P.J. Hart Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS Nat. Struct. Biol. 10 2003 461 467
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 461-467
    • Elam, J.S.1    Taylor, A.B.2    Hart, P.J.3
  • 9
    • 33744905543 scopus 로고    scopus 로고
    • Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus
    • G. Plakoutsi, and F. Bemporad F. Chiti Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus Structure 14 2006 993 1001
    • (2006) Structure , vol.14 , pp. 993-1001
    • Plakoutsi, G.1    Bemporad, F.2    Chiti, F.3
  • 10
    • 30344478570 scopus 로고    scopus 로고
    • Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus
    • A. Corazza, and C. Rosano P. Viglino Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus Proteins 62 2006 64 79
    • (2006) Proteins , vol.62 , pp. 64-79
    • Corazza, A.1    Rosano, C.2    Viglino, P.3
  • 11
    • 68649095591 scopus 로고    scopus 로고
    • "Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications
    • F. Bemporad, and F. Chiti "Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications FEBS Lett. 583 2009 2630 2638
    • (2009) FEBS Lett. , vol.583 , pp. 2630-2638
    • Bemporad, F.1    Chiti, F.2
  • 12
    • 1842790837 scopus 로고    scopus 로고
    • Aggregation of the acylphosphatase from Sulfolobus solfataricus: The folded and partially unfolded states can both be precursors for amyloid formation
    • G. Plakoutsi, and N. Taddei F. Chiti Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation J. Biol. Chem. 279 2004 14111 14119
    • (2004) J. Biol. Chem. , vol.279 , pp. 14111-14119
    • Plakoutsi, G.1    Taddei, N.2    Chiti, F.3
  • 13
    • 23444447864 scopus 로고    scopus 로고
    • Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    • G. Plakoutsi, and F. Bemporad F. Chiti Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates J. Mol. Biol. 351 2005 910 922
    • (2005) J. Mol. Biol. , vol.351 , pp. 910-922
    • Plakoutsi, G.1    Bemporad, F.2    Chiti, F.3
  • 14
    • 54549095709 scopus 로고    scopus 로고
    • A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state
    • F. Bemporad, and T. Vannocci F. Chiti A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state Biochim. Biophys. Acta 1784 2008 1986 1996
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1986-1996
    • Bemporad, F.1    Vannocci, T.2    Chiti, F.3
  • 15
    • 41549161190 scopus 로고    scopus 로고
    • The degree of structural protection at the edge β-strands determines the pathway of amyloid formation in globular proteins
    • G. Soldi, F. Bemporad, and F. Chiti The degree of structural protection at the edge β-strands determines the pathway of amyloid formation in globular proteins J. Am. Chem. Soc. 130 2008 4295 4302
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 4295-4302
    • Soldi, G.1    Bemporad, F.2    Chiti, F.3
  • 16
    • 84855438639 scopus 로고    scopus 로고
    • Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility
    • A. De Simone, and A. Dhulesia C.M. Dobson Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility Proc. Natl. Acad. Sci. USA 108 2011 21057 21062
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 21057-21062
    • De Simone, A.1    Dhulesia, A.2    Dobson, C.M.3
  • 17
    • 3142745308 scopus 로고    scopus 로고
    • Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily
    • F. Bemporad, and C. Capanni F. Chiti Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily Biochemistry 43 2004 9116 9126
    • (2004) Biochemistry , vol.43 , pp. 9116-9126
    • Bemporad, F.1    Capanni, C.2    Chiti, F.3
  • 18
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of α-synuclein fibrils studied by site-directed spin labeling
    • A. Der-Sarkissian, and C.C. Jao R. Langen Structural organization of α-synuclein fibrils studied by site-directed spin labeling J. Biol. Chem. 278 2003 37530 37535
    • (2003) J. Biol. Chem. , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Langen, R.3
  • 19
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
    • F.A. Mulder, and D. Schipper R. Boelens Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins J. Mol. Biol. 292 1999 111 123
    • (1999) J. Mol. Biol. , vol.292 , pp. 111-123
    • Mulder, F.A.1    Schipper, D.2    Boelens, R.3
  • 20
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Y. Bai, and J.S. Milne S.W. Englander Primary structure effects on peptide group hydrogen exchange Proteins 17 1993 75 86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Englander, S.W.3
  • 21
  • 22
    • 84855416769 scopus 로고    scopus 로고
    • Energy landscape of the prion protein helix 1 probed by metadynamics and NMR
    • C. Camilloni, and D. Schaal A. De Simone Energy landscape of the prion protein helix 1 probed by metadynamics and NMR Biophys. J. 102 2012 158 167
    • (2012) Biophys. J. , vol.102 , pp. 158-167
    • Camilloni, C.1    Schaal, D.2    De Simone, A.3
  • 23
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • F. Chiti, and C.M. Dobson Amyloid formation by globular proteins under native conditions Nat. Chem. Biol. 5 2009 15 22
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 24
    • 27744607600 scopus 로고    scopus 로고
    • Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution
    • L. Banci, and I. Bertini J.S. Valentine Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution J. Biol. Chem. 280 2005 35815 35821
    • (2005) J. Biol. Chem. , vol.280 , pp. 35815-35821
    • Banci, L.1    Bertini, I.2    Valentine, J.S.3
  • 25
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Z. Lai, W. Colón, and J.W. Kelly The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid Biochemistry 35 1996 6470 6482
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colón, W.2    Kelly, J.W.3
  • 26
    • 33144467755 scopus 로고    scopus 로고
    • Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
    • T.R. Jahn, and M.J. Parker S.E. Radford Amyloid formation under physiological conditions proceeds via a native-like folding intermediate Nat. Struct. Mol. Biol. 13 2006 195 201
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 195-201
    • Jahn, T.R.1    Parker, M.J.2    Radford, S.E.3
  • 27
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • C.M. Eakin, A.J. Berman, and A.D. Miranker A native to amyloidogenic transition regulated by a backbone trigger Nat. Struct. Mol. Biol. 13 2006 202 208
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 28
    • 78649728415 scopus 로고    scopus 로고
    • Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution
    • A. Dhulesia, and N. Cremades C.M. Dobson Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution J. Am. Chem. Soc. 132 2010 15580 15588
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15580-15588
    • Dhulesia, A.1    Cremades, N.2    Dobson, C.M.3
  • 29
    • 33746365408 scopus 로고    scopus 로고
    • Identification of the core structure of lysozyme amyloid fibrils by proteolysis
    • E. Frare, and M.F. Mossuto A. Fontana Identification of the core structure of lysozyme amyloid fibrils by proteolysis J. Mol. Biol. 361 2006 551 561
    • (2006) J. Mol. Biol. , vol.361 , pp. 551-561
    • Frare, E.1    Mossuto, M.F.2    Fontana, A.3


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