-
1
-
-
0035066332
-
Alzheimer's disease: Genes, proteins, and therapy
-
Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741-766.
-
(2001)
Physiol. Rev.
, vol.81
, pp. 741-766
-
-
Selkoe, D.J.1
-
2
-
-
0037135111
-
The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
-
Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 297:2002;353-356.
-
(2002)
Science
, vol.297
, pp. 353-356
-
-
Hardy, J.1
Selkoe, D.J.2
-
4
-
-
0033592877
-
Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans
-
Scott M.R., Robert W., Ironside J., Nguyen H.-O.B., Tremblay P., DeArmond S.J., Prusiner S.B. Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans. Proc. Natl. Acad. Sci. U.S.A. 96:1999;15137-15142.
-
(1999)
Proc. Natl. Acad. Sci. U.S.A.
, vol.96
, pp. 15137-15142
-
-
Scott, M.R.1
Robert, W.2
Ironside, J.3
Nguyen, H.-O.B.4
Tremblay, P.5
DeArmond, S.J.6
Prusiner, S.B.7
-
5
-
-
0033865052
-
Review: Amyloidogenesis - unquestioned answers and unanswered questions
-
Kisilevsky R. Review: Amyloidogenesis - unquestioned answers and unanswered questions. J. Struct. Biol. 130:2000;99-108.
-
(2000)
J. Struct. Biol.
, vol.130
, pp. 99-108
-
-
Kisilevsky, R.1
-
6
-
-
11544279355
-
Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
-
Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., Morgan T.E., Rozovsky I., Trommer B., Viola K.L. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U.S.A. 95:1998;6448-6453.
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 6448-6453
-
-
Lambert, M.P.1
Barlow, A.K.2
Chromy, B.A.3
Edwards, C.4
Freed, R.5
Liosatos, M.6
Morgan, T.E.7
Rozovsky, I.8
Trommer, B.9
Viola, K.L.10
-
7
-
-
0033520461
-
Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
-
Walsh D.M., Hartley D.M., Kusumoto Y., Fezoui Y., Condron M.M., Lomakin A., Benedek G.B., Selkoe D.J., Teplow D.B. Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274:1999;25945-25952.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 25945-25952
-
-
Walsh, D.M.1
Hartley, D.M.2
Kusumoto, Y.3
Fezoui, Y.4
Condron, M.M.5
Lomakin, A.6
Benedek, G.B.7
Selkoe, D.J.8
Teplow, D.B.9
-
8
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
9
-
-
0033616575
-
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
-
Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., Dobson C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. U.S.A. 96:1999;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
Ramponi, G.6
Dobson, C.M.7
-
11
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
It is shown that species that form early in the aggregation of proteins (SH3 domain and bovine phosphatidyl-inositol 3′ kinase) that are not associated with known diseases may be inherently cytotoxic. A clear implication of this study is that natural proteins have evolved not only to fold to the desired folded state but also to avoid aggregation.
-
Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:2002;507-511 It is shown that species that form early in the aggregation of proteins (SH3 domain and bovine phosphatidyl-inositol 3′ kinase) that are not associated with known diseases may be inherently cytotoxic. A clear implication of this study is that natural proteins have evolved not only to fold to the desired folded state but also to avoid aggregation.
-
(2002)
Nature
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
Giannoni, E.2
Chiti, F.3
Baroni, F.4
Formigli, L.5
Zurdo, J.6
Taddei, N.7
Ramponi, G.8
Dobson, C.M.9
Stefani, M.10
-
12
-
-
0029981197
-
Alternative conformations of amyloidogenic proteins govern their behavior
-
Kelly J.W. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6:1996;11-17.
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 11-17
-
-
Kelly, J.W.1
-
13
-
-
0032006678
-
The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
-
Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8:1998;101-106.
-
(1998)
Curr. Opin. Struct. Biol.
, vol.8
, pp. 101-106
-
-
Kelly, J.W.1
-
14
-
-
0031932169
-
Protein aggregation: Folding aggregates, inclusion bodies and amyloid
-
Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des. 3:1998;R9-R23.
-
(1998)
Fold Des
, vol.3
-
-
Fink, A.L.1
-
15
-
-
0025276708
-
Sickle cell hemoglobin polymerization
-
Eaton W.A., Hofrichter J. Sickle cell hemoglobin polymerization. Adv. Protein Chem. 40:1990;63-279.
-
(1990)
Adv. Protein Chem.
, vol.40
, pp. 63-279
-
-
Eaton, W.A.1
Hofrichter, J.2
-
16
-
-
0030908095
-
Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of time-dependent stability of amyloid proteins
-
Harper J.D., Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of time-dependent stability of amyloid proteins. Annu. Rev. Biochem. 66:1997;385-407.
-
(1997)
Annu. Rev. Biochem.
, vol.66
, pp. 385-407
-
-
Harper, J.D.1
Lansbury, P.T.2
-
17
-
-
0028997297
-
Non-genetic propagation of strain-specific properties of scrapie prion protein
-
Bessen R.A., Kocisko D.A., Raymond G.J., Nandan S., Lansbury P.T., Caughey B. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature. 375:1995;698-700.
-
(1995)
Nature
, vol.375
, pp. 698-700
-
-
Bessen, R.A.1
Kocisko, D.A.2
Raymond, G.J.3
Nandan, S.4
Lansbury, P.T.5
Caughey, B.6
-
18
-
-
0029831213
-
Molecular analysis of prion strain variation and the etiology of new variant CJD
-
Collinge J., Sidle K.C., Meads J., Ironside J., Hill A.F. Molecular analysis of prion strain variation and the etiology of new variant CJD. Nature. 383:1996;685-690.
-
(1996)
Nature
, vol.383
, pp. 685-690
-
-
Collinge, J.1
Sidle, K.C.2
Meads, J.3
Ironside, J.4
Hill, A.F.5
-
19
-
-
0031720905
-
Sc molecules with different conformations
-
Sc molecules with different conformations. Nat. Med. 4:1998;1157-1165.
-
(1998)
Nat. Med.
, vol.4
, pp. 1157-1165
-
-
Safar, J.1
Wille, H.2
Itri, V.3
Groth, D.4
Serban, H.5
Torchia, M.6
Cohen, F.E.7
Prusiner, S.B.8
-
20
-
-
0028804827
-
Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
-
Lansbury P.T., Costa P.R., Griffiths J.M., Simon E.J., Auger M., Halverson K., Kocisko D.A., Hendsch Z.S., Ashburn T.T., Spencer R.et al. Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat. Struct. Biol. 2:1995;990-998.
-
(1995)
Nat. Struct. Biol.
, vol.2
, pp. 990-998
-
-
Lansbury, P.T.1
Costa, P.R.2
Griffiths, J.M.3
Simon, E.J.4
Auger, M.5
Halverson, K.6
Kocisko, D.A.7
Hendsch, Z.S.8
Ashburn, T.T.9
Spencer, R.10
-
21
-
-
0034706014
-
Structure of the β-amyloid(10-35) fibril
-
10-35 peptides.
-
10-35 peptides.
-
(2000)
J. Am. Chem. Soc.
, vol.122
, pp. 7883-7889
-
-
Burkoth, T.S.1
Benzinger, T.2
Urban, V.3
Morgan, D.M.4
Gregory, D.M.5
Thiyagarajan, P.6
Botto, R.E.7
Meredith, S.C.8
Lynn, D.G.9
-
22
-
-
0033776959
-
Solid-state NMR as a probe of amyloid fibril structure
-
Tycko R. Solid-state NMR as a probe of amyloid fibril structure. Curr. Opin. Chem. Biol. 4:2000;500-506.
-
(2000)
Curr. Opin. Chem. Biol.
, vol.4
, pp. 500-506
-
-
Tycko, R.1
-
23
-
-
0034700129
-
Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils
-
1-40 peptides are arranged as parallel β sheets in amyloid fibrils.
-
1-40 peptides are arranged as parallel β sheets in amyloid fibrils.
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 13045-13050
-
-
Antzutkin, O.N.1
Balbach, J.J.2
Leapman, R.D.3
Rizzo, N.W.4
Reed, J.5
Tycko, R.6
-
24
-
-
0033551440
-
Assembly of Aβ amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
-
Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Assembly of Aβ amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry. 38:1999;8972-8980.
-
(1999)
Biochemistry
, vol.38
, pp. 8972-8980
-
-
Harper, J.D.1
Wong, S.S.2
Lieber, C.M.3
Lansbury, P.T.4
-
25
-
-
0037047118
-
The protofilament structure of insulin amyloid fibrils
-
Jimenez J.L., Nettleton E.J., Bouchard M., Robinson C.V., Dobson C.M., Saibil H.R. The protofilament structure of insulin amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 99:2002;9196-9201.
-
(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 9196-9201
-
-
Jimenez, J.L.1
Nettleton, E.J.2
Bouchard, M.3
Robinson, C.V.4
Dobson, C.M.5
Saibil, H.R.6
-
26
-
-
0034716942
-
Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid
-
Serpell J.C., Smith J.M. Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid. J. Mol. Biol. 299:2000;225-231.
-
(2000)
J. Mol. Biol.
, vol.299
, pp. 225-231
-
-
Serpell, J.C.1
Smith, J.M.2
-
27
-
-
0037195098
-
10-35): Sequence effects
-
MD simulations were used to assess the stabilities of Aβ peptides. By comparing the stabilities of different arrangements of peptides in the fibril, the authors have proposed a novel structural model for aggregates of Aβ peptides.
-
10-35): sequence effects. Proc. Natl. Acad. Sci. U.S.A. 99:2002;14126-14131 MD simulations were used to assess the stabilities of Aβ peptides. By comparing the stabilities of different arrangements of peptides in the fibril, the authors have proposed a novel structural model for aggregates of Aβ peptides.
-
(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 14126-14131
-
-
Ma, B.1
Nussinov, R.2
-
28
-
-
0037041426
-
Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
-
Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416:2002;535-539.
-
(2002)
Nature
, vol.416
, pp. 535-539
-
-
Walsh, D.M.1
Klyubin, I.2
Fadeeva, J.V.3
Cullen, W.K.4
Anwyl, R.5
Wolfe, M.S.6
Rowan, M.J.7
Selkoe, D.J.8
-
29
-
-
0035812658
-
Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
-
One of the first studies to describe the pathways in the assembly of Aβ peptides into fibrils. By studying the assembly kinetics of 18 different Aβ peptides, the authors suggest that fibril formation is preceded by the transient population of on-pathway α-helical intermediates.
-
Kirkitadze M.D., Condron M.M., Teplow D.B. Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis. J. Mol. Biol. 312:2001;1103-1119 One of the first studies to describe the pathways in the assembly of Aβ peptides into fibrils. By studying the assembly kinetics of 18 different Aβ peptides, the authors suggest that fibril formation is preceded by the transient population of on-pathway α-helical intermediates.
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 1103-1119
-
-
Kirkitadze, M.D.1
Condron, M.M.2
Teplow, D.B.3
-
30
-
-
0037337271
-
16-22 amyloid peptides into antiparallel β-sheets
-
16-22 peptides form antiparallel β-sheet structures. Even in this system, α-helical intermediates are transiently populated. This led the authors to propose that fibril formation by Aβ peptides, which occurs by maximizing the number of salt bridges and hydrophobic interactions, must involve oligomers with high α-helical content.
-
16-22 peptides form antiparallel β-sheet structures. Even in this system, α-helical intermediates are transiently populated. This led the authors to propose that fibril formation by Aβ peptides, which occurs by maximizing the number of salt bridges and hydrophobic interactions, must involve oligomers with high α-helical content.
-
(2003)
Structure
, vol.11
, pp. 295-307
-
-
Klimov, D.K.1
Thirumalai, D.2
-
33
-
-
0037022563
-
Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
-
This novel study illustrates the general strategies that naturally occurring β sheets use to avoid aggregation. The principles that emerge from this paper are not only relevant to the prediction of regions in proteins that are susceptible to aggregation, but also are important in the de novo design of proteins with β-sheet architecture.
-
Richardson J.S., Richardson D.C. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. U.S.A. 99:2002;2754-2759 This novel study illustrates the general strategies that naturally occurring β sheets use to avoid aggregation. The principles that emerge from this paper are not only relevant to the prediction of regions in proteins that are susceptible to aggregation, but also are important in the de novo design of proteins with β-sheet architecture.
-
(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 2754-2759
-
-
Richardson, J.S.1
Richardson, D.C.2
-
34
-
-
0033863220
-
Activation barriers to structural transition determine deposition rates of Alzheimer's disease
-
Esler W.P., Stimson E.R., Lachenmann M.J., Ghilardi J.R., Lu Y., Vinters H.V., Mantyh P.W., Lee J.P., Maggio J.E. Activation barriers to structural transition determine deposition rates of Alzheimer's disease. J. Struct. Biol. 130:2000;174-183.
-
(2000)
J. Struct. Biol.
, vol.130
, pp. 174-183
-
-
Esler, W.P.1
Stimson, E.R.2
Lachenmann, M.J.3
Ghilardi, J.R.4
Lu, Y.5
Vinters, H.V.6
Mantyh, P.W.7
Lee, J.P.8
Maggio, J.E.9
-
35
-
-
0034235515
-
Oligomerization of β-amyloid of the Alzheimer's and the dutch-cerebral-haemorrhage
-
Sian A.K., Frears E.R., El-Agnaf O.A., Patel B.P., Manca M.F., Siligardi G., Hussain R., Austen B.M. Oligomerization of β-amyloid of the Alzheimer's and the dutch-cerebral-haemorrhage. Biochem. J. 349:2000;299-308.
-
(2000)
Biochem. J.
, vol.349
, pp. 299-308
-
-
Sian, A.K.1
Frears, E.R.2
El-Agnaf, O.A.3
Patel, B.P.4
Manca, M.F.5
Siligardi, G.6
Hussain, R.7
Austen, B.M.8
-
37
-
-
0031467313
-
Heparin-binding properties of the amyloidogenic peptides Aβ and amylin
-
Watson D.J., Landers A.D., Selkoe D.J. Heparin-binding properties of the amyloidogenic peptides Aβ and amylin. J. Biol. Chem. 272:1997;31617-31624.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 31617-31624
-
-
Watson, D.J.1
Landers, A.D.2
Selkoe, D.J.3
-
38
-
-
0034282630
-
Substitutions at codon 22 of Alzheimer's Aβ peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
-
Miravalle L., Tokuda T., Chiarle R., Giaccone G., Bugiani O., Ragliavini F., Frangione B., Ghiso J. Substitutions at codon 22 of Alzheimer's Aβ peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. J. Biol. Chem. 275:2000;27110-27116.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 27110-27116
-
-
Miravalle, L.1
Tokuda, T.2
Chiarle, R.3
Giaccone, G.4
Bugiani, O.5
Ragliavini, F.6
Frangione, B.7
Ghiso, J.8
-
39
-
-
0035133048
-
Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution
-
Massi F., Peng J.W., Lee J.P., Straub J.E. Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution. Biophys. J. 80:2001;31-44.
-
(2001)
Biophys. J.
, vol.80
, pp. 31-44
-
-
Massi, F.1
Peng, J.W.2
Lee, J.P.3
Straub, J.E.4
-
40
-
-
0034901811
-
Probing the origins of increased activity of the E22Q Dutch mutant of the Alzheimer's β-amyloid peptide
-
Massi F., Straub J.E. Probing the origins of increased activity of the E22Q Dutch mutant of the Alzheimer's β-amyloid peptide. Biophys. J. 81:2001;697-709.
-
(2001)
Biophys. J.
, vol.81
, pp. 697-709
-
-
Massi, F.1
Straub, J.E.2
-
41
-
-
0036081257
-
Charged states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant
-
To test the hypothesis that differences in the tendency to form β strands may explain the variations in the deposition rates of wild-type Aβ and the E22Q mutant, the authors performed a series of MD simulations. They showed that the desolvation penalty, rather than intrinsic preferences for β structure, explains the differences in the fibrillization kinetics.
-
Massi F., Klimov D., Thirumalai D., Straub J.E. Charged states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant. Protein Sci. 11:2002;1639-1647 To test the hypothesis that differences in the tendency to form β strands may explain the variations in the deposition rates of wild-type Aβ and the E22Q mutant, the authors performed a series of MD simulations. They showed that the desolvation penalty, rather than intrinsic preferences for β structure, explains the differences in the fibrillization kinetics.
-
(2002)
Protein Sci.
, vol.11
, pp. 1639-1647
-
-
Massi, F.1
Klimov, D.2
Thirumalai, D.3
Straub, J.E.4
-
43
-
-
0027258525
-
The carboxy terminus of β amyloid protein in critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
-
Jarrett J.T., Berger E.P., Lansbury P.T. The carboxy terminus of β amyloid protein in critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry. 32:1993;4693-4697.
-
(1993)
Biochemistry
, vol.32
, pp. 4693-4697
-
-
Jarrett, J.T.1
Berger, E.P.2
Lansbury, P.T.3
-
44
-
-
0028987233
-
1H NMR of Aβ amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence
-
1H NMR of Aβ amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence Biochemistry. 34:1995;5191-5200.
-
(1995)
Biochemistry
, vol.34
, pp. 5191-5200
-
-
Lee, J.P.1
Stimson, E.R.2
Ghilardi, J.R.3
Mantyh, P.W.4
Lu, Y.A.5
Felix, A.M.6
Llanos, W.7
Behbin, A.8
Cummings, M.9
Criekinge, M.V.10
-
46
-
-
0030781922
-
PH-dependent stability and conformation of the recombinant human prion protein PrP(90-231)
-
Swietnicki W., Petersen R., Gambetti P., Surewicz W.K. pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J. Biol. Chem. 272:1997;27517-27520.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 27517-27520
-
-
Swietnicki, W.1
Petersen, R.2
Gambetti, P.3
Surewicz, W.K.4
-
47
-
-
0032568592
-
A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH
-
Hornemann S., Glockshuber R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc. Natl. Acad. Sci. U.S.A. 95:1998;6010-6014.
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 6010-6014
-
-
Hornemann, S.1
Glockshuber, R.2
-
49
-
-
0030050614
-
A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
-
Lorimer G.H. A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. FASEB J. 10:1996;5-9.
-
(1996)
FASEB J.
, vol.10
, pp. 5-9
-
-
Lorimer, G.H.1
-
50
-
-
0015859467
-
Principles that govern the folding of protein chains
-
Anfinsen C.B. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
51
-
-
0032718386
-
Salt-induced detour through compact regions of the protein folding landscape
-
Otzen D.E., Oliveberg M. Salt-induced detour through compact regions of the protein folding landscape. Proc. Natl. Acad. Sci. U.S.A. 96:1999;11746-11751.
-
(1999)
Proc. Natl. Acad. Sci. U.S.A.
, vol.96
, pp. 11746-11751
-
-
Otzen, D.E.1
Oliveberg, M.2
-
52
-
-
0034730203
-
Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly
-
This is the first study that used mutational analysis to investigate the factors that prevent wild-type S6 from aggregation. The experiments were used to introduce a key idea - natural proteins use charged gatekeeper residues (ones that are not involved in directing the folding process) to prevent intermolecular association.
-
Otzen D.E., Kristensen O., Oliveberg M. Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly. Proc. Natl. Acad. Sci. U.S.A. 97:2000;9907-9912 This is the first study that used mutational analysis to investigate the factors that prevent wild-type S6 from aggregation. The experiments were used to introduce a key idea - natural proteins use charged gatekeeper residues (ones that are not involved in directing the folding process) to prevent intermolecular association.
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 9907-9912
-
-
Otzen, D.E.1
Kristensen, O.2
Oliveberg, M.3
-
53
-
-
0037117519
-
Amyloid fibers are water-filled nanotubes
-
Using available experimental data and novel modeling methods, this study suggests that amyloid fibrils may have a near 'universal' structure.
-
Perutz M.F., Finch J.T., Berriman J., Lesk A. Amyloid fibers are water-filled nanotubes. Proc. Natl. Acad. Sci. U.S.A. 99:2002;5591-5595 Using available experimental data and novel modeling methods, this study suggests that amyloid fibrils may have a near 'universal' structure.
-
(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 5591-5595
-
-
Perutz, M.F.1
Finch, J.T.2
Berriman, J.3
Lesk, A.4
-
54
-
-
0028304962
-
Satisfying hydrogen bonding potential in proteins
-
McDonald I., Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:1994;777-793.
-
(1994)
J. Mol. Biol.
, vol.238
, pp. 777-793
-
-
McDonald, I.1
Thornton, J.M.2
-
55
-
-
0037018932
-
Alpha-helix structure in Alzheimer's disease aggregates of tau-protein
-
This study challenges the commonly held belief that all amyloid fibrils comprise β-sheet structures. Using CD and FTIR spectroscopy, the authors suggest that, in the PHFs, the tau protein adopts an α-helical conformation.
-
Sadqi M., Hernandez F., Pan U.M., Perez M., Schaeberle M.D., Avila J., Munoz V. Alpha-helix structure in Alzheimer's disease aggregates of tau-protein. Biochemistry. 41:2002;7150-7155 This study challenges the commonly held belief that all amyloid fibrils comprise β-sheet structures. Using CD and FTIR spectroscopy, the authors suggest that, in the PHFs, the tau protein adopts an α-helical conformation.
-
(2002)
Biochemistry
, vol.41
, pp. 7150-7155
-
-
Sadqi, M.1
Hernandez, F.2
Pan, U.M.3
Perez, M.4
Schaeberle, M.D.5
Avila, J.6
Munoz, V.7
-
56
-
-
0036228167
-
Exploring protein aggregation and self-propagation using lattice models: Phase diagram and kinetics
-
The authors use lattice models to describe various scenarios for protein aggregation. They use a toy model to verify the templated aggregation model for prion propagation [77].
-
Dima R.I., Thirumalai D. Exploring protein aggregation and self-propagation using lattice models: phase diagram and kinetics. Protein Sci. 11:2002;1036-1049 The authors use lattice models to describe various scenarios for protein aggregation. They use a toy model to verify the templated aggregation model for prion propagation [77].
-
(2002)
Protein Sci.
, vol.11
, pp. 1036-1049
-
-
Dima, R.I.1
Thirumalai, D.2
-
59
-
-
0034691149
-
Native topology determines force-induced unfolding pathways in globular proteins
-
Klimov D.K., Thirumalai D. Native topology determines force-induced unfolding pathways in globular proteins. Proc. Natl. Acad. Sci. U.S.A. 97:2000;7254-7259.
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 7254-7259
-
-
Klimov, D.K.1
Thirumalai, D.2
-
60
-
-
0033613188
-
De novo amyloid proteins from designed combinatorial libraries
-
West M.W., Wang W., Patterson J., Mancias J.D., Beasley J.R., Hecht M.H. De novo amyloid proteins from designed combinatorial libraries. Proc. Natl. Acad. Sci. U.S.A. 96:1999;11211-11216.
-
(1999)
Proc. Natl. Acad. Sci. U.S.A.
, vol.96
, pp. 11211-11216
-
-
West, M.W.1
Wang, W.2
Patterson, J.3
Mancias, J.D.4
Beasley, J.R.5
Hecht, M.H.6
-
61
-
-
0035055990
-
Frequencies of amino acid string in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues
-
Schwartz R., Istrail S., King J. Frequencies of amino acid string in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues. Protein Sci. 10:2001;1023-1031.
-
(2001)
Protein Sci.
, vol.10
, pp. 1023-1031
-
-
Schwartz, R.1
Istrail, S.2
King, J.3
-
62
-
-
0027291015
-
Prediction of protein secondary structure at better than 70% accuracy
-
Rost B., Sander C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:1993;584-599.
-
(1993)
J. Mol. Biol.
, vol.232
, pp. 584-599
-
-
Rost, B.1
Sander, C.2
-
63
-
-
0033957834
-
The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
-
Bairoch A., Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acid Res. 28:2000;275-284.
-
(2000)
Nucleic Acid Res.
, vol.28
, pp. 275-284
-
-
Bairoch, A.1
Apweiler, R.2
-
64
-
-
0017868338
-
Empirical predictions of protein conformation
-
Chou P.Y., Fasman G.D. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47:1978;251-276.
-
(1978)
Annu. Rev. Biochem.
, vol.47
, pp. 251-276
-
-
Chou, P.Y.1
Fasman, G.D.2
-
65
-
-
0033215478
-
Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel
-
Moore R.C., Lee I.Y., Silverman G.L., Harrison P.M., Strome R., Heinrich C., Karunaratne A., Pasternak S.H., Chishti M.A., Liang Y.et al. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel. J. Mol. Biol. 292:1999;797-817.
-
(1999)
J. Mol. Biol.
, vol.292
, pp. 797-817
-
-
Moore, R.C.1
Lee, I.Y.2
Silverman, G.L.3
Harrison, P.M.4
Strome, R.5
Heinrich, C.6
Karunaratne, A.7
Pasternak, S.H.8
Chishti, M.A.9
Liang, Y.10
-
66
-
-
0033049539
-
A mouse prion protein transgene rescues mice deficient for the prion protein gene from Purkinje cell degeneration and demyelination
-
Nishida N., Tremblay P., Sugimoto T., Shigematsu K., Shirabe S., Petromilli C., Erpel S.P., Nakaoke R., Atarashi R., Houtani T.et al. A mouse prion protein transgene rescues mice deficient for the prion protein gene from Purkinje cell degeneration and demyelination. Lab. Invest. 79:1999;689-697.
-
(1999)
Lab. Invest.
, vol.79
, pp. 689-697
-
-
Nishida, N.1
Tremblay, P.2
Sugimoto, T.3
Shigematsu, K.4
Shirabe, S.5
Petromilli, C.6
Erpel, S.P.7
Nakaoke, R.8
Atarashi, R.9
Houtani, T.10
-
67
-
-
0035957003
-
Two different neurodegenerative diseases caused by proteins with similar structures
-
Mo H., Moore R.C., Cohen F.E., Westaway D., Prusiner S.B., Wright P.E., Dyson H.J. Two different neurodegenerative diseases caused by proteins with similar structures. Proc. Natl. Acad. Sci. U.S.A. 98:2001;2352-2357.
-
(2001)
Proc. Natl. Acad. Sci. U.S.A.
, vol.98
, pp. 2352-2357
-
-
Mo, H.1
Moore, R.C.2
Cohen, F.E.3
Westaway, D.4
Prusiner, S.B.5
Wright, P.E.6
Dyson, H.J.7
-
69
-
-
0034869693
-
Crystal structure of the human prion protein reveals a mechanism for oligomerization
-
Sc, shows that the dimer forms by a domain-swap mechanism.
-
Sc, shows that the dimer forms by a domain-swap mechanism.
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 770-774
-
-
Knaus, K.J.1
Morillas, M.2
Swietnicki, W.3
Malone, M.4
Surewicz, W.K.5
Yee, V.C.6
-
70
-
-
0035127031
-
A domain-swapped RNase A dimer with implications for amyloid formation
-
Liu Y., Gotte G., Libonati M., Eisenberg D. A domain-swapped RNase A dimer with implications for amyloid formation. Nat. Struct. Biol. 8:2002;211-214.
-
(2002)
Nat. Struct. Biol.
, vol.8
, pp. 211-214
-
-
Liu, Y.1
Gotte, G.2
Libonati, M.3
Eisenberg, D.4
-
73
-
-
0034649352
-
16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR
-
16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR. Biochemistry. 39:2000;13748-13759.
-
(2000)
Biochemistry
, vol.39
, pp. 13748-13759
-
-
Balbach, J.J.1
Ishii, Y.2
Antzutkin, O.N.3
Leapman, R.D.4
Rizzo, N.W.5
Dyda, F.6
Reed, J.7
Tycko, R.8
-
74
-
-
0036784617
-
Molecular dynamics simulations of alanine rich β-sheet oligomers: Insight into amyloid formation
-
Ma B., Nussinov R. Molecular dynamics simulations of alanine rich β-sheet oligomers: insight into amyloid formation. Protein Sci. 11:2002;2335-2350.
-
(2002)
Protein Sci.
, vol.11
, pp. 2335-2350
-
-
Ma, B.1
Nussinov, R.2
-
75
-
-
0028170411
-
Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
-
Schweer O., Schonbrunn-Hanebeck E., Marx A., Mandelkow E. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. J. Biol. Chem. 269:1994;24290-24297.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 24290-24297
-
-
Schweer, O.1
Schonbrunn-Hanebeck, E.2
Marx, A.3
Mandelkow, E.4
-
76
-
-
0037137228
-
The conformations of filamentous and soluble tau associated with Alzheimer paired helical filaments
-
••].
-
••].
-
(2002)
Biochemistry
, vol.41
, pp. 13798-13806
-
-
Goux, W.J.1
-
77
-
-
0014190760
-
Self-replication and scrapie
-
Griffith J.S. Self-replication and scrapie. Nature. 215:1967;1043-1044.
-
(1967)
Nature
, vol.215
, pp. 1043-1044
-
-
Griffith, J.S.1
-
78
-
-
0035079856
-
Conformational propagation with prion-like characteristics in a simple model of protein folding
-
Harrison P.M., Chan H.S., Prusiner S.B., Cohen F.E. Conformational propagation with prion-like characteristics in a simple model of protein folding. Protein Sci. 10:2001;819-835.
-
(2001)
Protein Sci.
, vol.10
, pp. 819-835
-
-
Harrison, P.M.1
Chan, H.S.2
Prusiner, S.B.3
Cohen, F.E.4
-
79
-
-
0035254995
-
Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation
-
The authors have proposed several schemes for the kinetics of fibril formation by Aβ peptides. By using the analogy with the energy landscape perspective of protein folding, many new predictions are made for the assembly of amyloid fibrils.
-
Massi F., Straub J.E. Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation. Proteins. 42:2001;217-229 The authors have proposed several schemes for the kinetics of fibril formation by Aβ peptides. By using the analogy with the energy landscape perspective of protein folding, many new predictions are made for the assembly of amyloid fibrils.
-
(2001)
Proteins
, vol.42
, pp. 217-229
-
-
Massi, F.1
Straub, J.E.2
-
81
-
-
0034714351
-
Nucleated conformational conversion and the replication of conformational information by a prion determinant
-
+] production from Sup35 in S. cerevisiae, the authors proposed a novel model that incorporate elements of the templated assembly and nucleation-growth mechanisms. It is likely that recent studies on Aβ aggregation provide additional examples of the NCC model.
-
+] production from Sup35 in S. cerevisiae, the authors proposed a novel model that incorporate elements of the templated assembly and nucleation-growth mechanisms. It is likely that recent studies on Aβ aggregation provide additional examples of the NCC model.
-
(2000)
Science
, vol.289
, pp. 1317-1321
-
-
Serio, T.R.1
Cashikar, A.G.2
Kowal, A.S.3
Sawicki, G.J.4
Moslehi, J.J.5
Serpell, L.6
Arnsdorf, M.F.7
Lindquist, S.L.8
-
82
-
-
0034255027
-
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
-
Ramirez-Alvarado M., Merkel J.S., Regan L. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. U.S.A. 97:2000;8979-8984.
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 8979-8984
-
-
Ramirez-Alvarado, M.1
Merkel, J.S.2
Regan, L.3
-
83
-
-
0029008481
-
The biophysics of sickle cell hydroxyurea therapy
-
Eaton W.A., Hofrichter J. The biophysics of sickle cell hydroxyurea therapy. Science. 268:1995;1142-1143.
-
(1995)
Science
, vol.268
, pp. 1142-1143
-
-
Eaton, W.A.1
Hofrichter, J.2
-
84
-
-
0026244229
-
MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
-
Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
-
(1991)
J. Appl. Crystallogr.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
85
-
-
0029881007
-
Molmol: A program for display and analysis of macromolecular structures
-
Koradi R., Billeter M., Wuthrich K. Molmol: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
-
(1996)
J. Mol. Graph
, vol.14
, pp. 51-55
-
-
Koradi, R.1
Billeter, M.2
Wuthrich, K.3
-
86
-
-
0037422540
-
Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
-
Bitan G., Kirkitadze M.A., Lomakin A., Vollers S.S., Benedeck G.B., Teplow D.B. Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. U.S.A. 100:2003;330-335.
-
(2003)
Proc. Natl. Acad. Sci. U.S.A.
, vol.100
, pp. 330-335
-
-
Bitan, G.1
Kirkitadze, M.A.2
Lomakin, A.3
Vollers, S.S.4
Benedeck, G.B.5
Teplow, D.B.6
-
87
-
-
0037473750
-
Prevention of transthyretin amyloid disease by changing protein misfolding energetics
-
Hammarstrom P., Wiseman R.L., Powers E.T., Kelly J.W. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science. 299:2003;713-716.
-
(2003)
Science
, vol.299
, pp. 713-716
-
-
Hammarstrom, P.1
Wiseman, R.L.2
Powers, E.T.3
Kelly, J.W.4
|