-
1
-
-
0347357617
-
Protein folding and misfolding
-
Dobson CM, (2003) Protein folding and misfolding. Nature 426: 884-890.
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
Dobson, C.M.1
-
2
-
-
71749113077
-
Low micromolar zinc accelerates the fibrillization of human Tau via bridging of Cys-291 and Cys-322
-
Mo ZY, Zhu YZ, Zhu HL, Fan JB, Chen J, et al. (2009) Low micromolar zinc accelerates the fibrillization of human Tau via bridging of Cys-291 and Cys-322. J Biol Chem 284: 34648-34657.
-
(2009)
J Biol Chem
, vol.284
, pp. 34648-34657
-
-
Mo, Z.Y.1
Zhu, Y.Z.2
Zhu, H.L.3
Fan, J.B.4
Chen, J.5
-
3
-
-
77950473768
-
Quantitative characterization of heparin binding to Tau protein. Implication for inducer-mediated Tau filament formation
-
Zhu HL, Fernández C, Fan JB, Shewmaker F, Chen J, et al. (2010) Quantitative characterization of heparin binding to Tau protein. Implication for inducer-mediated Tau filament formation. J Biol Chem 285: 3592-3599.
-
(2010)
J Biol Chem
, vol.285
, pp. 3592-3599
-
-
Zhu, H.L.1
Fernández, C.2
Fan, J.B.3
Shewmaker, F.4
Chen, J.5
-
4
-
-
80053144801
-
Fibrillization of human Tau is accelerated by exposure to lead via interaction with His-330 and His-362
-
Zhu HL, Meng SR, Fan JB, Chen J, Liang Y, (2011) Fibrillization of human Tau is accelerated by exposure to lead via interaction with His-330 and His-362. PLoS One 6: e25020.
-
(2011)
PLoS One
, vol.6
-
-
Zhu, H.L.1
Meng, S.R.2
Fan, J.B.3
Chen, J.4
Liang, Y.5
-
5
-
-
33746813983
-
How can biochemical reactions within cells differ from those in test tubes?
-
Minton AP, (2006) How can biochemical reactions within cells differ from those in test tubes? J Cell Sci 119: 2863-2869.
-
(2006)
J Cell Sci
, vol.119
, pp. 2863-2869
-
-
Minton, A.P.1
-
6
-
-
0035253217
-
Macromolecular crowding: an important but neglected aspect of the intracellular environment
-
Ellis RJ, (2001) Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr Opin Struct Biol 11: 114-119.
-
(2001)
Curr Opin Struct Biol
, vol.11
, pp. 114-119
-
-
Ellis, R.J.1
-
7
-
-
41049090929
-
Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences
-
Zhou HX, Rivas G, Minton AP, (2008) Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 37: 375-397.
-
(2008)
Annu Rev Biophys
, vol.37
, pp. 375-397
-
-
Zhou, H.X.1
Rivas, G.2
Minton, A.P.3
-
8
-
-
80052720461
-
From water and ions to crowded biomacromolecules: in vivo structuring of a prokaryotic cell
-
Spitzer J, (2011) From water and ions to crowded biomacromolecules: in vivo structuring of a prokaryotic cell. Microbiol Mol Biol Rev 75: 491-506.
-
(2011)
Microbiol Mol Biol Rev
, vol.75
, pp. 491-506
-
-
Spitzer, J.1
-
9
-
-
11244296161
-
Mixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme: implications for protein folding in intracellular environments
-
Zhou BR, Liang Y, Du F, Zhou Z, Chen J, (2004) Mixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme: implications for protein folding in intracellular environments. J Biol Chem 279: 55109-55116.
-
(2004)
J Biol Chem
, vol.279
, pp. 55109-55116
-
-
Zhou, B.R.1
Liang, Y.2
Du, F.3
Zhou, Z.4
Chen, J.5
-
10
-
-
33750806263
-
Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments
-
Du F, Zhou Z, Mo ZY, Shi JZ, Chen J, et al. (2006) Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments. J Mol Biol 364: 469-482.
-
(2006)
J Mol Biol
, vol.364
, pp. 469-482
-
-
Du, F.1
Zhou, Z.2
Mo, Z.Y.3
Shi, J.Z.4
Chen, J.5
-
11
-
-
71049123175
-
Crowded cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding
-
Zhou Z, Fan JB, Zhu HL, Shewmaker F, Yan X, et al. (2009) Crowded cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding. J Biol Chem 284: 30148-30158.
-
(2009)
J Biol Chem
, vol.284
, pp. 30148-30158
-
-
Zhou, Z.1
Fan, J.B.2
Zhu, H.L.3
Shewmaker, F.4
Yan, X.5
-
12
-
-
77955699308
-
Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria
-
Jiao M, Li HT, Chen J, Minton AP, Liang Y, (2010) Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria. Biophys J 99: 914-923.
-
(2010)
Biophys J
, vol.99
, pp. 914-923
-
-
Jiao, M.1
Li, H.T.2
Chen, J.3
Minton, A.P.4
Liang, Y.5
-
13
-
-
80053106666
-
Fibril formation of the rabbit/human/bovine prion proteins
-
Zhou Z, Yan X, Pan K, Chen J, Xie ZS, et al. (2011) Fibril formation of the rabbit/human/bovine prion proteins. Biophys J 101: 1483-1492.
-
(2011)
Biophys J
, vol.101
, pp. 1483-1492
-
-
Zhou, Z.1
Yan, X.2
Pan, K.3
Chen, J.4
Xie, Z.S.5
-
14
-
-
50149096820
-
Guiding protein aggregation with macromolecular crowding
-
Munishkina LA, Ahmad A, Fink AL, Uversky VN, (2008) Guiding protein aggregation with macromolecular crowding. Biochemistry 47: 8993-9006.
-
(2008)
Biochemistry
, vol.47
, pp. 8993-9006
-
-
Munishkina, L.A.1
Ahmad, A.2
Fink, A.L.3
Uversky, V.N.4
-
15
-
-
79951841821
-
Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching
-
Johansen D, Jeffries CM, Hammouda B, Trewhella J, Goldenberg DP, (2011) Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching. Biophys J 100: 1120-1128.
-
(2011)
Biophys J
, vol.100
, pp. 1120-1128
-
-
Johansen, D.1
Jeffries, C.M.2
Hammouda, B.3
Trewhella, J.4
Goldenberg, D.P.5
-
17
-
-
0027420369
-
Tau protein and the neurofibrillary pathology of Alzheimer's disease
-
Goedert M, (1993) Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends Neurosci 16: 460-465.
-
(1993)
Trends Neurosci
, vol.16
, pp. 460-465
-
-
Goedert, M.1
-
18
-
-
80155157847
-
The seeds of neurodegeneration: prion-like spreading in ALS
-
Polymenidou M, Cleveland DW, (2011) The seeds of neurodegeneration: prion-like spreading in ALS. Cell 147: 498-508.
-
(2011)
Cell
, vol.147
, pp. 498-508
-
-
Polymenidou, M.1
Cleveland, D.W.2
-
19
-
-
0033520987
-
Posttranslational quality control: folding, refolding, and degrading proteins
-
Wickner S, Maurizi MR, Gottesman S, (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286: 1888-1893.
-
(1999)
Science
, vol.286
, pp. 1888-1893
-
-
Wickner, S.1
Maurizi, M.R.2
Gottesman, S.3
-
20
-
-
78649907008
-
Cell-to-cell transmission of non-prion protein aggregates
-
Lee SJ, Desplats P, Sigurdson C, Tsigelny I, Masliah E, (2010) Cell-to-cell transmission of non-prion protein aggregates. Nat Rev Neurol 6: 702-706.
-
(2010)
Nat Rev Neurol
, vol.6
, pp. 702-706
-
-
Lee, S.J.1
Desplats, P.2
Sigurdson, C.3
Tsigelny, I.4
Masliah, E.5
-
21
-
-
79952449094
-
Prion hypothesis: the end of the controversy?
-
Soto C, (2011) Prion hypothesis: the end of the controversy? Trends Biochem Sci 36: 151-158.
-
(2011)
Trends Biochem Sci
, vol.36
, pp. 151-158
-
-
Soto, C.1
-
22
-
-
78651246462
-
Genetic Creutzfeldt-Jakob disease and fatal familial insomnia: insights into phenotypic variability and disease pathogenesis
-
Capellari S, Strammiello R, Saverioni D, Kretzschmar H, Parchi P, (2011) Genetic Creutzfeldt-Jakob disease and fatal familial insomnia: insights into phenotypic variability and disease pathogenesis. Acta Neuropathol 121: 21-37.
-
(2011)
Acta Neuropathol
, vol.121
, pp. 21-37
-
-
Capellari, S.1
Strammiello, R.2
Saverioni, D.3
Kretzschmar, H.4
Parchi, P.5
-
23
-
-
48349090111
-
Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival
-
Wang Q, Johnson JL, Agar NYR, Agar JN, (2008) Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival. PLoS Biol 6: e170.
-
(2008)
PLoS Biol
, vol.6
-
-
Wang, Q.1
Johnson, J.L.2
Agar, N.Y.R.3
Agar, J.N.4
-
24
-
-
79958070512
-
ALS-causing SOD1 mutations promote production of copper-deficient misfolded species
-
Ip P, Mulligan VK, Chakrabartty A, (2011) ALS-causing SOD1 mutations promote production of copper-deficient misfolded species. J Mol Biol 409: 839-852.
-
(2011)
J Mol Biol
, vol.409
, pp. 839-852
-
-
Ip, P.1
Mulligan, V.K.2
Chakrabartty, A.3
-
25
-
-
0037301367
-
Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform
-
Vorberg I, Groschup MH, Pfaff E, Priola SA, (2003) Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J Virol 77: 2003-2009.
-
(2003)
J Virol
, vol.77
, pp. 2003-2009
-
-
Vorberg, I.1
Groschup, M.H.2
Pfaff, E.3
Priola, S.A.4
-
26
-
-
77953315370
-
Residues surrounding the glycosylphosphatidylinositol anchor attachment site of PrP modulate prion infection: insight from the resistance of rabbits to prion disease
-
Nisbet RM, Harrison CF, Lawson VA, Masters CL, Cappai R, et al. (2010) Residues surrounding the glycosylphosphatidylinositol anchor attachment site of PrP modulate prion infection: insight from the resistance of rabbits to prion disease. J Virol 84: 6678-6686.
-
(2010)
J Virol
, vol.84
, pp. 6678-6686
-
-
Nisbet, R.M.1
Harrison, C.F.2
Lawson, V.A.3
Masters, C.L.4
Cappai, R.5
-
27
-
-
80051903352
-
Lysozyme: A model protein for amyloid research
-
Swaminathan R, Ravi VK, Kumar S, Kumar MVS, Chandra N, (2011) Lysozyme: A model protein for amyloid research. Adv Protein Chem Struct Biol 84: 63-111.
-
(2011)
Adv Protein Chem Struct Biol
, vol.84
, pp. 63-111
-
-
Swaminathan, R.1
Ravi, V.K.2
Kumar, S.3
Kumar, M.V.S.4
Chandra, N.5
-
28
-
-
22844445324
-
Purification of recombinant Tau protein and preparation of Alzheimer-paired helical filaments in vitro
-
Barghorn S, Biernat J, Mandelkow E, (2005) Purification of recombinant Tau protein and preparation of Alzheimer-paired helical filaments in vitro. Methods Mol Biol 299: 35-51.
-
(2005)
Methods Mol Biol
, vol.299
, pp. 35-51
-
-
Barghorn, S.1
Biernat, J.2
Mandelkow, E.3
-
29
-
-
12544257523
-
In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc
-
Bocharova OV, Breydo L, Parfenov AS, Salnikov VV, Baskakov IV, (2005) In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc. J Mol Biol 346: 645-659.
-
(2005)
J Mol Biol
, vol.346
, pp. 645-659
-
-
Bocharova, O.V.1
Breydo, L.2
Parfenov, A.S.3
Salnikov, V.V.4
Baskakov, I.V.5
-
30
-
-
57749100302
-
Initiation and elongation in fibrillation of ALS-linked superoxide dismutase
-
Chattopadhyay M, Durazo A, Sohn SH, Strong CD, Gralla EB, et al. (2008) Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc Natl Acad Sci USA 105: 18663-18668.
-
(2008)
Proc Natl Acad Sci USA
, vol.105
, pp. 18663-18668
-
-
Chattopadhyay, M.1
Durazo, A.2
Sohn, S.H.3
Strong, C.D.4
Gralla, E.B.5
-
31
-
-
0031796990
-
Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: the "phantom" subunit and the possible role of Lys7p
-
Lyons TJ, Nersissian A, Goto JJ, Zhu H, Gralla EB, et al. (1998) Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: the "phantom" subunit and the possible role of Lys7p. J Biol Inorg Chem 3: 650-662.
-
(1998)
J Biol Inorg Chem
, vol.3
, pp. 650-662
-
-
Lyons, T.J.1
Nersissian, A.2
Goto, J.J.3
Zhu, H.4
Gralla, E.B.5
-
32
-
-
11244340520
-
Thermally induced fibrillar aggregation of hen egg white lysozyme
-
Arnaudov LN, de Vries R, (2005) Thermally induced fibrillar aggregation of hen egg white lysozyme. Biophys J 88: 515-526.
-
(2005)
Biophys J
, vol.88
, pp. 515-526
-
-
Arnaudov, L.N.1
de Vries, R.2
-
33
-
-
33646857025
-
The core of Tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis
-
von Bergen M, Barghorn S, Müller SA, Pickhardt M, Biernat J, et al. (2006) The core of Tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis. Biochemistry 45: 6446-6457.
-
(2006)
Biochemistry
, vol.45
, pp. 6446-6457
-
-
von Bergen, M.1
Barghorn, S.2
Müller, S.A.3
Pickhardt, M.4
Biernat, J.5
-
34
-
-
37549058441
-
Highly promiscuous nature of prion polymerization
-
Makarava N, Lee CI, Ostapchenko VG, Baskakov IV, (2007) Highly promiscuous nature of prion polymerization. J Biol Chem 282: 36704-36713.
-
(2007)
J Biol Chem
, vol.282
, pp. 36704-36713
-
-
Makarava, N.1
Lee, C.I.2
Ostapchenko, V.G.3
Baskakov, I.V.4
-
35
-
-
0034647438
-
Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain
-
Krebs MRH, Wilkins DK, Chung EW, Pitkeathly MC, Chamberlain AK, et al. (2000) Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain. J Mol Biol 300: 541-549.
-
(2000)
J Mol Biol
, vol.300
, pp. 541-549
-
-
Krebs, M.R.H.1
Wilkins, D.K.2
Chung, E.W.3
Pitkeathly, M.C.4
Chamberlain, A.K.5
-
36
-
-
70349195971
-
The consequences of pathogenic mutations to the human prion protein
-
van der Kamp MW, Daggett V, (2009) The consequences of pathogenic mutations to the human prion protein. Protein Eng Des Sel 22: 461-468.
-
(2009)
Protein Eng Des Sel
, vol.22
, pp. 461-468
-
-
van der Kamp, M.W.1
Daggett, V.2
-
37
-
-
0037795635
-
Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro
-
Stathopulos PB, Rumfeldt JA, Scholz GA, Irani RA, Frey HE, et al. (2003) Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. Proc Natl Acad Sci USA 100: 7021-7026.
-
(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 7021-7026
-
-
Stathopulos, P.B.1
Rumfeldt, J.A.2
Scholz, G.A.3
Irani, R.A.4
Frey, H.E.5
-
38
-
-
77955249021
-
Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c
-
Christiansen A, Wang Q, Samiotakis A, Cheung MS, Wittung-Stafshede P, (2010) Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c. Biochemistry 49: 6519-6530.
-
(2010)
Biochemistry
, vol.49
, pp. 6519-6530
-
-
Christiansen, A.1
Wang, Q.2
Samiotakis, A.3
Cheung, M.S.4
Wittung-Stafshede, P.5
-
39
-
-
48349137105
-
The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity
-
Meiering EM, (2008) The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity. PLoS Biol 6: e193.
-
(2008)
PLoS Biol
, vol.6
-
-
Meiering, E.M.1
-
40
-
-
0028998411
-
On the structure of microtubules, tau, and paired helical filaments
-
Mandelkow E, Song YH, Schweers O, Marx A, Mandelkow EM, (1995) On the structure of microtubules, tau, and paired helical filaments. Neurobiol Aging 16: 347-354.
-
(1995)
Neurobiol Aging
, vol.16
, pp. 347-354
-
-
Mandelkow, E.1
Song, Y.H.2
Schweers, O.3
Marx, A.4
Mandelkow, E.M.5
-
42
-
-
0034185689
-
Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype
-
Peoc'h K, Manivet P, Beaudry P, Attane F, Besson G, et al. (2000) Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype. Hum Mutat 15: 482.
-
(2000)
Hum Mutat
, vol.15
, pp. 482
-
-
Peoc'h, K.1
Manivet, P.2
Beaudry, P.3
Attane, F.4
Besson, G.5
-
43
-
-
0032553530
-
Familial mutations and the thermodynamic stability of the recombinant human prion protein
-
Swietnicki W, Petersen RB, Gambetti P, Surewicz WK, (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J Biol Chem 273: 31048-31052.
-
(1998)
J Biol Chem
, vol.273
, pp. 31048-31052
-
-
Swietnicki, W.1
Petersen, R.B.2
Gambetti, P.3
Surewicz, W.K.4
-
44
-
-
79952308169
-
Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS
-
Vassall KA, Stubbs HR, Primmer HA, Tong MS, Sullivan SM, et al. (2011) Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS. Proc Natl Acad Sci USA 108: 2210-2215.
-
(2011)
Proc Natl Acad Sci USA
, vol.108
, pp. 2210-2215
-
-
Vassall, K.A.1
Stubbs, H.R.2
Primmer, H.A.3
Tong, M.S.4
Sullivan, S.M.5
-
45
-
-
39049119728
-
Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size
-
Sun Y, Makarava N, Lee CI, Laksanalamai P, Robb FT, et al. (2008) Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J Mol Biol 376: 1155-1167.
-
(2008)
J Mol Biol
, vol.376
, pp. 1155-1167
-
-
Sun, Y.1
Makarava, N.2
Lee, C.I.3
Laksanalamai, P.4
Robb, F.T.5
-
46
-
-
0034681163
-
Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
-
Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, et al. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy. Proc Natl Acad Sci USA 97: 571-576.
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 571-576
-
-
Conway, K.A.1
Lee, S.J.2
Rochet, J.C.3
Ding, T.T.4
Williamson, R.E.5
-
47
-
-
0242668337
-
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
-
Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489.
-
(2003)
Science
, vol.300
, pp. 486-489
-
-
Kayed, R.1
Head, E.2
Thompson, J.L.3
McIntire, T.M.4
Milton, S.C.5
-
48
-
-
24644448839
-
The most infectious prion protein particles
-
Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, et al. (2005) The most infectious prion protein particles. Nature 437: 257-261.
-
(2005)
Nature
, vol.437
, pp. 257-261
-
-
Silveira, J.R.1
Raymond, G.J.2
Hughson, A.G.3
Race, R.E.4
Sim, V.L.5
|