메뉴 건너뛰기




Volumn 10, Issue 6, 2014, Pages

Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARAGINE; PROTEIN VARIANT; AMYLOID; AMYLOID BETA PROTEIN; FUNGAL PROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; HET-S PROTEIN, PODOSPORA ANSERINA; MUTANT PROTEIN; PEPTIDE FRAGMENT; PRION; PRND PROTEIN, HUMAN;

EID: 84903464851     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004158     Document Type: Article
Times cited : (43)

References (83)
  • 1
    • 68049114613 scopus 로고    scopus 로고
    • Self-propagating beta-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world
    • Maury CP, (2009) Self-propagating beta-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world. Orig Life Evol Biosph 39: 141-150.
    • (2009) Orig Life Evol Biosph , vol.39 , pp. 141-150
    • Maury, C.P.1
  • 2
    • 77957782470 scopus 로고    scopus 로고
    • Biology of amyloid: structure, function, and regulation
    • Greenwald J, Riek R, (2010) Biology of amyloid: structure, function, and regulation. Structure 18: 1244-1260.
    • (2010) Structure , vol.18 , pp. 1244-1260
    • Greenwald, J.1    Riek, R.2
  • 3
    • 84864288105 scopus 로고    scopus 로고
    • On the possible amyloid origin of protein folds
    • Greenwald J, Riek R, (2012) On the possible amyloid origin of protein folds. J Mol Biol 421: 417-426.
    • (2012) J Mol Biol , vol.421 , pp. 417-426
    • Greenwald, J.1    Riek, R.2
  • 4
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • Eichner T, Radford SE, (2011) A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 43: 8-18.
    • (2011) Mol Cell , vol.43 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 5
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • Monsellier E, Chiti F, (2007) Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep 8: 737-742.
    • (2007) EMBO Rep , vol.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 7
    • 79955761085 scopus 로고    scopus 로고
    • Structural insights into functional and pathological amyloid
    • Shewmaker F, McGlinchey RP, Wickner RB, (2011) Structural insights into functional and pathological amyloid. J Biol Chem 286: 16533-16540.
    • (2011) J Biol Chem , vol.286 , pp. 16533-16540
    • Shewmaker, F.1    McGlinchey, R.P.2    Wickner, R.B.3
  • 8
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM, (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 9
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M, (2012) The amyloid state of proteins in human diseases. Cell 148: 1188-1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 10
    • 0028025483 scopus 로고
    • Mechanism of scrapie replication
    • Lansbury PT, (1994) Mechanism of scrapie replication. Science 265: 1510.
    • (1994) Science , vol.265 , pp. 1510
    • Lansbury, P.T.1
  • 11
    • 84866893801 scopus 로고    scopus 로고
    • Corruption and spread of pathogenic proteins in neurodegenerative diseases
    • Walker LC, LeVine H 3rd, (2012) Corruption and spread of pathogenic proteins in neurodegenerative diseases. J Biol Chem 287: 33109-33115.
    • (2012) J Biol Chem , vol.287 , pp. 33109-33115
    • Walker, L.C.1    LeVine 3rd, H.2
  • 12
    • 80053563923 scopus 로고    scopus 로고
    • Misfolded protein aggregates: mechanisms, structures and potential for disease transmission
    • Moreno-Gonzalez I, Soto C, (2011) Misfolded protein aggregates: mechanisms, structures and potential for disease transmission. Semin Cell Dev Biol 22: 482-487.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 482-487
    • Moreno-Gonzalez, I.1    Soto, C.2
  • 13
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: conformational diversity and consequences
    • Toyama BH, Weissman JS, (2011) Amyloid structure: conformational diversity and consequences. Annu Rev Biochem 80: 557-585.
    • (2011) Annu Rev Biochem , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 16
    • 80053569870 scopus 로고    scopus 로고
    • The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility
    • Saupe SJ, (2011) The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility. Semin Cell Dev Biol 22: 460-468.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 460-468
    • Saupe, S.J.1
  • 17
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • Coustou V, Deleu C, Saupe S, Begueret J, (1997) The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci U S A 94: 9773-9778.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 20
    • 84883216859 scopus 로고    scopus 로고
    • The Transcriptional Response to Nonself in the Fungus Podospora anserina
    • Bidard F, Clave C, Saupe SJ, (2013) The Transcriptional Response to Nonself in the Fungus Podospora anserina. G3 (Bethesda) 3: 1015-1030.
    • (2013) G3 (Bethesda) , vol.3 , pp. 1015-1030
    • Bidard, F.1    Clave, C.2    Saupe, S.J.3
  • 21
    • 84859506059 scopus 로고    scopus 로고
    • Genomic Clustering and Homology between HET-S and the NWD2 STAND Protein in Various Fungal Genomes
    • Daskalov A, Paoletti M, Ness F, Saupe SJ, (2012) Genomic Clustering and Homology between HET-S and the NWD2 STAND Protein in Various Fungal Genomes. Plos One 7: e34854.
    • (2012) Plos One , vol.7
    • Daskalov, A.1    Paoletti, M.2    Ness, F.3    Saupe, S.J.4
  • 22
    • 70549098240 scopus 로고    scopus 로고
    • Fungal incompatibility: evolutionary origin in pathogen defense?
    • Paoletti M, Saupe SJ, (2009) Fungal incompatibility: evolutionary origin in pathogen defense? Bioessays 31: 1201-1210.
    • (2009) Bioessays , vol.31 , pp. 1201-1210
    • Paoletti, M.1    Saupe, S.J.2
  • 23
    • 0001771763 scopus 로고
    • Incompatibilité cellulaire et interactions nucléocytoplamsiques dans les phénomènes de barrage chez le Podospora anserina
    • Beisson-Schecroun J, (1962) Incompatibilité cellulaire et interactions nucléocytoplamsiques dans les phénomènes de barrage chez le Podospora anserina. Ann Genet 4: 3-50.
    • (1962) Ann Genet , vol.4 , pp. 3-50
    • Beisson-Schecroun, J.1
  • 25
    • 0038219626 scopus 로고    scopus 로고
    • Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
    • Balguerie A, Dos Reis S, Ritter C, Chaignepain S, Coulary-Salin B, et al. (2003) Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. Embo J 22: 2071-2081.
    • (2003) Embo J , vol.22 , pp. 2071-2081
    • Balguerie, A.1    Dos Reis, S.2    Ritter, C.3    Chaignepain, S.4    Coulary-Salin, B.5
  • 27
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structural elements and infectivity of the HET-s prion
    • Ritter C, Maddelein ML, Siemer AB, Luhrs T, Ernst M, et al. (2005) Correlation of structural elements and infectivity of the HET-s prion. Nature 435: 844-848.
    • (2005) Nature , vol.435 , pp. 844-848
    • Ritter, C.1    Maddelein, M.L.2    Siemer, A.B.3    Luhrs, T.4    Ernst, M.5
  • 28
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy
    • Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, et al. (2010) Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc 132: 13765-13775.
    • (2010) J Am Chem Soc , vol.132 , pp. 13765-13775
    • Van Melckebeke, H.1    Wasmer, C.2    Lange, A.3    Ab, E.4    Loquet, A.5
  • 29
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, et al. (2008) Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319: 1523-1526.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5
  • 30
    • 84871682946 scopus 로고    scopus 로고
    • The mechanism of toxicity in HET-S/HET-s prion incompatibility
    • Seuring C, Greenwald J, Wasmer C, Wepf R, Saupe SJ, et al. (2012) The mechanism of toxicity in HET-S/HET-s prion incompatibility. PLoS Biol 10: e1001451.
    • (2012) PLoS Biol , vol.10
    • Seuring, C.1    Greenwald, J.2    Wasmer, C.3    Wepf, R.4    Saupe, S.J.5
  • 31
    • 84863666574 scopus 로고    scopus 로고
    • The [Het-s] Prion, an Amyloid Fold as a Cell Death Activation Trigger
    • Saupe SJ, Daskalov A, (2012) The [Het-s] Prion, an Amyloid Fold as a Cell Death Activation Trigger. PLoS Pathog 8: e1002687.
    • (2012) PLoS Pathog , vol.8
    • Saupe, S.J.1    Daskalov, A.2
  • 32
    • 84856790302 scopus 로고    scopus 로고
    • Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity
    • Mathur V, Seuring C, Riek R, Saupe SJ, Liebman SW, (2012) Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity. Mol Cell Biol 32: 139-153.
    • (2012) Mol Cell Biol , vol.32 , pp. 139-153
    • Mathur, V.1    Seuring, C.2    Riek, R.3    Saupe, S.J.4    Liebman, S.W.5
  • 33
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like Polymerization Underlies Signal Transduction in Antiviral Immune Defense and Inflammasome Activation
    • Cai X, Chen J, Xu H, Liu S, Jiang QX, et al. (2014) Prion-like Polymerization Underlies Signal Transduction in Antiviral Immune Defense and Inflammasome Activation. Cell 156: 1207-1222.
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1    Chen, J.2    Xu, H.3    Liu, S.4    Jiang, Q.X.5
  • 34
    • 79952772833 scopus 로고    scopus 로고
    • Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy
    • Mizuno N, Baxa U, Steven AC, (2011) Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy. Proc Natl Acad Sci U S A 108: 3252-3257.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3252-3257
    • Mizuno, N.1    Baxa, U.2    Steven, A.C.3
  • 36
    • 80855134303 scopus 로고    scopus 로고
    • Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids
    • Gendoo DM, Harrison PM, (2011) Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids. Plos One 6: e27342.
    • (2011) Plos One , vol.6
    • Gendoo, D.M.1    Harrison, P.M.2
  • 37
    • 83355166788 scopus 로고    scopus 로고
    • Two structurally similar fungal prions efficiently cross-seed in vivo but form distinct polymers when coexpressed
    • Benkemoun L, Ness F, Sabate R, Ceschin J, Breton A, et al. (2011) Two structurally similar fungal prions efficiently cross-seed in vivo but form distinct polymers when coexpressed. Mol Microbiol 82: 1392-1405.
    • (2011) Mol Microbiol , vol.82 , pp. 1392-1405
    • Benkemoun, L.1    Ness, F.2    Sabate, R.3    Ceschin, J.4    Breton, A.5
  • 38
    • 77956782713 scopus 로고    scopus 로고
    • Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity
    • Wasmer C, Zimmer A, Sabate R, Soragni A, Saupe SJ, et al. (2010) Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity. J Mol Biol 402: 311-325.
    • (2010) J Mol Biol , vol.402 , pp. 311-325
    • Wasmer, C.1    Zimmer, A.2    Sabate, R.3    Soragni, A.4    Saupe, S.J.5
  • 39
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307: 262-265.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5
  • 40
    • 70349768853 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids
    • Wasmer C, Benkemoun L, Sabate R, Steinmetz MO, Coulary-Salin B, et al. (2009) Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids. Angew Chem Int Ed Engl 48: 4858-4860.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 4858-4860
    • Wasmer, C.1    Benkemoun, L.2    Sabate, R.3    Steinmetz, M.O.4    Coulary-Salin, B.5
  • 42
    • 53549129515 scopus 로고    scopus 로고
    • Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra
    • Wasmer C, Soragni A, Sabate R, Lange A, Riek R, et al. (2008) Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra. Angew Chem Int Ed Engl 47: 5839-5841.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 5839-5841
    • Wasmer, C.1    Soragni, A.2    Sabate, R.3    Lange, A.4    Riek, R.5
  • 43
    • 84885650263 scopus 로고    scopus 로고
    • Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289)
    • Wan W, Bian W, McDonald M, Kijac A, Wemmer DE, et al. (2013) Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289). J Biol Chem 288: 29604-29612.
    • (2013) J Biol Chem , vol.288 , pp. 29604-29612
    • Wan, W.1    Bian, W.2    McDonald, M.3    Kijac, A.4    Wemmer, D.E.5
  • 44
    • 84861135685 scopus 로고    scopus 로고
    • Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold
    • Wan W, Wille H, Stohr J, Baxa U, Prusiner SB, et al. (2012) Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold. Biophys J 102: 2339-2344.
    • (2012) Biophys J , vol.102 , pp. 2339-2344
    • Wan, W.1    Wille, H.2    Stohr, J.3    Baxa, U.4    Prusiner, S.B.5
  • 46
    • 33644818046 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability
    • Williams AD, Shivaprasad S, Wetzel R, (2006) Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability. J Mol Biol 357: 1283-1294.
    • (2006) J Mol Biol , vol.357 , pp. 1283-1294
    • Williams, A.D.1    Shivaprasad, S.2    Wetzel, R.3
  • 49
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS, (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 50
    • 84878872010 scopus 로고    scopus 로고
    • Structural Definition Is Important for the Propagation of the Yeast [PSI(+)] Prion
    • Marchante R, Rowe M, Zenthon J, Howard MJ, Tuite MF, (2013) Structural Definition Is Important for the Propagation of the Yeast [PSI(+)] Prion. Mol Cell 50: 675-685.
    • (2013) Mol Cell , vol.50 , pp. 675-685
    • Marchante, R.1    Rowe, M.2    Zenthon, J.3    Howard, M.J.4    Tuite, M.F.5
  • 51
    • 0032711226 scopus 로고    scopus 로고
    • Mutational analysis of the [Het-s] prion analog of Podospora anserina. A short N-terminal peptide allows prion propagation
    • Coustou V, Deleu C, Saupe SJ, Begueret J, (1999) Mutational analysis of the [Het-s] prion analog of Podospora anserina. A short N-terminal peptide allows prion propagation. Genetics 153: 1629-1640.
    • (1999) Genetics , vol.153 , pp. 1629-1640
    • Coustou, V.1    Deleu, C.2    Saupe, S.J.3    Begueret, J.4
  • 52
    • 0027234098 scopus 로고
    • A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina
    • Deleu C, Clave C, Begueret J, (1993) A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina. Genetics 135: 45-52.
    • (1993) Genetics , vol.135 , pp. 45-52
    • Deleu, C.1    Clave, C.2    Begueret, J.3
  • 54
    • 33745622856 scopus 로고    scopus 로고
    • Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity
    • Benkemoun L, Sabate R, Malato L, Dos Reis S, Dalstra H, et al. (2006) Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity. Methods 39: 61-67.
    • (2006) Methods , vol.39 , pp. 61-67
    • Benkemoun, L.1    Sabate, R.2    Malato, L.3    Dos Reis, S.4    Dalstra, H.5
  • 55
    • 37049025592 scopus 로고    scopus 로고
    • Role of Hsp104 in the propagation and inheritance of the [Het-s] prion
    • Malato L, Dos Reis S, Benkemoun L, Sabate R, Saupe SJ, (2007) Role of Hsp104 in the propagation and inheritance of the [Het-s] prion. Mol Biol Cell 18: 4803-4812.
    • (2007) Mol Biol Cell , vol.18 , pp. 4803-4812
    • Malato, L.1    Dos Reis, S.2    Benkemoun, L.3    Sabate, R.4    Saupe, S.J.5
  • 56
    • 18044391103 scopus 로고    scopus 로고
    • High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation
    • Siemer AB, Ritter C, Ernst M, Riek R, Meier BH, (2005) High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation. Angew Chem Int Ed Engl 44: 2441-2444.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 2441-2444
    • Siemer, A.B.1    Ritter, C.2    Ernst, M.3    Riek, R.4    Meier, B.H.5
  • 58
    • 0038131734 scopus 로고    scopus 로고
    • Surface salt bridges, double-mutant cycles, and protein stability: an experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein l9
    • Luisi DL, Snow CD, Lin JJ, Hendsch ZS, Tidor B, et al. (2003) Surface salt bridges, double-mutant cycles, and protein stability: an experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein l9. Biochemistry 42: 7050-7060.
    • (2003) Biochemistry , vol.42 , pp. 7050-7060
    • Luisi, D.L.1    Snow, C.D.2    Lin, J.J.3    Hendsch, Z.S.4    Tidor, B.5
  • 59
    • 0028574137 scopus 로고
    • Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor
    • Marqusee S, Sauer RT, (1994) Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor. Protein Sci 3: 2217-2225.
    • (1994) Protein Sci , vol.3 , pp. 2217-2225
    • Marqusee, S.1    Sauer, R.T.2
  • 60
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • Schreiber G, Fersht AR, (1995) Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J Mol Biol 248: 478-486.
    • (1995) J Mol Biol , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 61
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW, (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 63
    • 0035933338 scopus 로고    scopus 로고
    • The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins
    • Whitten ST, Wooll JO, Razeghifard R, Garcia-Moreno EB, Hilser VJ, (2001) The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins. J Mol Biol 309: 1165-1175.
    • (2001) J Mol Biol , vol.309 , pp. 1165-1175
    • Whitten, S.T.1    Wooll, J.O.2    Razeghifard, R.3    Garcia-Moreno, E.B.4    Hilser, V.J.5
  • 64
    • 33845311853 scopus 로고    scopus 로고
    • Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains
    • Batey S, Clarke J, (2006) Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains. Proc Natl Acad Sci U S A 103: 18113-18118.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18113-18118
    • Batey, S.1    Clarke, J.2
  • 65
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM, (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 4: 2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 66
    • 77952305367 scopus 로고    scopus 로고
    • Beta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrils
    • Kajava AV, Baxa U, Steven AC, (2010) Beta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrils. FASEB J 24: 1311-1319.
    • (2010) FASEB J , vol.24 , pp. 1311-1319
    • Kajava, A.V.1    Baxa, U.2    Steven, A.C.3
  • 67
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka M, Collins SR, Toyama BH, Weissman JS, (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442: 585-589.
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 68
    • 34447639732 scopus 로고    scopus 로고
    • Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes
    • Legname G, Nguyen HO, Peretz D, Cohen FE, DeArmond SJ, et al. (2006) Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci U S A 103: 19105-19110.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19105-19110
    • Legname, G.1    Nguyen, H.O.2    Peretz, D.3    Cohen, F.E.4    DeArmond, S.J.5
  • 70
    • 84893724428 scopus 로고    scopus 로고
    • Wild type and mutants of the HET-s(218-289) prion show different flexibility at fibrillar ends: A simulation study
    • Friedman R, Caflisch A, (2013) Wild type and mutants of the HET-s(218-289) prion show different flexibility at fibrillar ends: A simulation study. Proteins 82: 399-404.
    • (2013) Proteins , vol.82 , pp. 399-404
    • Friedman, R.1    Caflisch, A.2
  • 71
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • Chiti F, Webster P, Taddei N, Clark A, Stefani M, et al. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci U S A 96: 3590-3594.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3590-3594
    • Chiti, F.1    Webster, P.2    Taddei, N.3    Clark, A.4    Stefani, M.5
  • 72
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models of amyloid fibril structure
    • Nelson R, Eisenberg D, (2006) Recent atomic models of amyloid fibril structure. Curr Opin Struct Biol 16: 260-265.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 73
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-beta spine of amyloid-like fibrils
    • Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, et al. (2005) Structure of the cross-beta spine of amyloid-like fibrils. Nature 435: 773-778.
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.O.4    Riekel, C.5
  • 74
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447: 453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5
  • 75
    • 33846002029 scopus 로고    scopus 로고
    • Side chain-dependent stacking modulates tau filament structure
    • Margittai M, Langen R, (2006) Side chain-dependent stacking modulates tau filament structure. J Biol Chem 281: 37820-37827.
    • (2006) J Biol Chem , vol.281 , pp. 37820-37827
    • Margittai, M.1    Langen, R.2
  • 76
    • 0037044732 scopus 로고    scopus 로고
    • Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides
    • Tjernberg L, Hosia W, Bark N, Thyberg J, Johansson J, (2002) Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides. J Biol Chem 277: 43243-43246.
    • (2002) J Biol Chem , vol.277 , pp. 43243-43246
    • Tjernberg, L.1    Hosia, W.2    Bark, N.3    Thyberg, J.4    Johansson, J.5
  • 77
    • 0038274079 scopus 로고    scopus 로고
    • The sequence dependence of fiber organization. A comparative molecular dynamics study of the islet amyloid polypeptide segments 22-27 and 22-29
    • Zanuy D, Nussinov R, (2003) The sequence dependence of fiber organization. A comparative molecular dynamics study of the islet amyloid polypeptide segments 22-27 and 22-29. J Mol Biol 329: 565-584.
    • (2003) J Mol Biol , vol.329 , pp. 565-584
    • Zanuy, D.1    Nussinov, R.2
  • 78
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L, (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 22: 1302-1306.
    • (2004) Nat Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 80
    • 33845978790 scopus 로고    scopus 로고
    • Insight into the structure of amyloid fibrils from the analysis of globular proteins
    • Trovato A, Chiti F, Maritan A, Seno F, (2006) Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comput Biol 2: e170.
    • (2006) PLoS Comput Biol , vol.2
    • Trovato, A.1    Chiti, F.2    Maritan, A.3    Seno, F.4
  • 81
    • 41149088659 scopus 로고    scopus 로고
    • Gene deletion and allelic replacement in the filamentous fungus Podospora anserina
    • El-Khoury R, Sellem CH, Coppin E, Boivin A, Maas MF, et al. (2008) Gene deletion and allelic replacement in the filamentous fungus Podospora anserina. Curr Genet 53: 249-258.
    • (2008) Curr Genet , vol.53 , pp. 249-258
    • El-Khoury, R.1    Sellem, C.H.2    Coppin, E.3    Boivin, A.4    Maas, M.F.5
  • 82
    • 0000953276 scopus 로고    scopus 로고
    • 13C-1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • Takegoshi K, Nakamura S, Terao T, (2001) 13C-1H dipolar-assisted rotational resonance in magic-angle spinning NMR. Phys Lett 344: 631-637.
    • (2001) Phys Lett , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 83
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: development of a software pipeline
    • Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, et al. (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59: 687-696.
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevens, T.J.3    Fogh, R.H.4    Pajon, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.