-
2
-
-
0024366602
-
Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie
-
Bruce M.E., P.A. McBride and C.F. Farquhar. 1989. Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie. Neurosci. Lett. 102:1.
-
(1989)
Neurosci. Lett.
, vol.102
, pp. 1
-
-
Bruce, M.E.1
McBride, P.A.2
Farquhar, C.F.3
-
3
-
-
0345654322
-
Neuronal apoptosis in Creutzfeldt-Jakob disease
-
Gray F., F. Chretien, H. Adle-Biassette, A. Dorandeu, T. Ereau, M. B. Delisle, N. Kopp, J.W. Ironside and C. Vital. 1999. Neuronal apoptosis in Creutzfeldt-Jakob disease. J. Neuropathol. Exp. Neurol. 58:3.
-
(1999)
J. Neuropathol. Exp. Neurol.
, vol.58
, pp. 3
-
-
Gray, F.1
Chretien, F.2
Adle-Biassette, H.3
Dorandeu, A.4
Ereau, T.5
Delisle, M.B.6
Kopp, N.7
Ironside, J.W.8
Vital, C.9
-
4
-
-
0024802065
-
PrPSc in scrapie-infected hamster brain is spatially and temporally related to histopathology and infectivity titer
-
De Armond S.J., M. Gonzales, W.C. Mobley, A.A. Kon, H. Sern and S.B. Prusiner. 1989. PrPSc in scrapie-infected hamster brain is spatially and temporally related to histopathology and infectivity titer. Prog. Clin. Biol. Res. 317:601.
-
(1989)
Prog. Clin. Biol. Res.
, vol.317
, pp. 601
-
-
De Armond, S.J.1
Gonzales, M.2
Mobley, W.C.3
Kon, A.A.4
Sern, H.5
Prusiner, S.B.6
-
5
-
-
0034237389
-
Intracellular mechanisms mediating the neuronal death and astrogliosis induced by the prion protein fragment 106-126
-
Thellung S., T. Florio, A. Corsaro, et al. 2000. Intracellular mechanisms mediating the neuronal death and astrogliosis induced by the prion protein fragment 106-126. Int. J. Dev. Neurosi. 18:481.
-
(2000)
Int. J. Dev. Neurosi.
, vol.18
, pp. 481
-
-
Thellung, S.1
Florio, T.2
Corsaro, A.3
-
6
-
-
0036176506
-
p38 MAP kinase mediates the cell death induced by PrP106-126 in the SH-SY5Y neuroblastoma cells
-
Thellung S., V. Villa, A. Corsaro, et al. 2002. p38 MAP kinase mediates the cell death induced by PrP106-126 in the SH-SY5Y neuroblastoma cells. Neurobiol. Dis. 9:69.
-
(2002)
Neurobiol. Dis.
, vol.9
, pp. 69
-
-
Thellung, S.1
Villa, V.2
Corsaro, A.3
-
7
-
-
0034916581
-
Prion diseases of humans and animals: Their causes and molecular basis
-
Collinge J. 2001. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24:519.
-
(2001)
Annu. Rev. Neurosci.
, vol.24
, pp. 519
-
-
Collinge, J.1
-
8
-
-
14844322442
-
-
S. B. Prusiner, ed. Cold Spring Harbor Laboratory New York
-
Gambetti P., R.B. Petersen, P. Parchi, et al. 1999. In Prion Biology and Diseases. S. B. Prusiner, ed. Cold Spring Harbor Laboratory New York, p. 1.
-
(1999)
Prion Biology and Diseases
, pp. 1
-
-
Gambetti, P.1
Petersen, R.B.2
Parchi, P.3
-
9
-
-
0031754291
-
Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity
-
Piccardo P., S.R. Dlouhy, P.M.J. Lievens, et al. 1998. Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity. J. Neuropathol. and Exp. Neurol. 57:979.
-
(1998)
J. Neuropathol. and Exp. Neurol.
, vol.57
, pp. 979
-
-
Piccardo, P.1
Dlouhy, S.R.2
Lievens, P.M.J.3
-
10
-
-
0034974318
-
Prion proteins with different conformations accumulate in Gerstmann-Straussler-Scheinker disease caused by A117V and F198S mutations
-
Piccardo P., J.J. Liepnieks, A. William, et al. 2001. Prion proteins with different conformations accumulate in Gerstmann-Straussler-Scheinker disease caused by A117V and F198S mutations. Am. J. Pathol. 158:2201.
-
(2001)
Am. J. Pathol.
, vol.158
, pp. 2201
-
-
Piccardo, P.1
Liepnieks, J.J.2
William, A.3
-
11
-
-
0031456947
-
Structure of the recombinant full-length hamster prion protein PrP (29-231): The N terminus is highly flexible
-
Donne G.D., J.H. Viles, D. Groth, I. Mehlhorn, T.L. James, F.E. Cohen, S.B. Prusiner, P.E. Wright and H.J. Dyson. 1997. Structure of the recombinant full-length hamster prion protein PrP (29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. U.S.A. 94:13452.
-
(1997)
Proc. Natl. Acad. Sci. U.S.A.
, vol.94
, pp. 13452
-
-
Donne, G.D.1
Viles, J.H.2
Groth, D.3
Mehlhorn, I.4
James, T.L.5
Cohen, F.E.6
Prusiner, S.B.7
Wright, P.E.8
Dyson, H.J.9
-
12
-
-
0032578451
-
Prion protein NMR structure and familial human spongiform encephalopathies
-
Riek R., G. Wider, M. Billeter, S. Hornemann, R. Glockshuber and K. Wuthrich. 1998. Prion protein NMR structure and familial human spongiform encephalopathies Proc. Natl. Acad. Sci. U.S.A. 95:11667.
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 11667
-
-
Riek, R.1
Wider, G.2
Billeter, M.3
Hornemann, S.4
Glockshuber, R.5
Wuthrich, K.6
-
15
-
-
0026705377
-
Prion protein preamyloid and amyloid deposits in Gerstmann-Straussler- Scheinker disease, Indiana kindred
-
Giacconne G., L. Verga, O. Bugiani, et al. 1992. Prion protein preamyloid and amyloid deposits in Gerstmann-Straussler-Scheinker disease, Indiana kindred. Proc. Natl. Acad. Sci. U. S. A. 89:9349.
-
(1992)
Proc. Natl. Acad. Sci. U. S. A.
, vol.89
, pp. 9349
-
-
Giacconne, G.1
Verga, L.2
Bugiani, O.3
-
16
-
-
0025944507
-
Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
-
Caughey B. W., A. Dong, K. S. Bhat, D. Ernst, S. F. Hayes and W. S. Caughey. 1991. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochem. 30:7672.
-
(1991)
Biochem.
, vol.30
, pp. 7672
-
-
Caughey, B.W.1
Dong, A.2
Bhat, K.S.3
Ernst, D.4
Hayes, S.F.5
Caughey, W.S.6
-
17
-
-
0027388993
-
Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
-
Gasset M., M. A. Baldwin, R. J. Fletterick and S. B. Prusiner. 1993. Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc. Natl. Acad. Sci. U. S. A. 90:1.
-
(1993)
Proc. Natl. Acad. Sci. U. S. A.
, vol.90
, pp. 1
-
-
Gasset, M.1
Baldwin, M.A.2
Fletterick, R.J.3
Prusiner, S.B.4
-
18
-
-
0036708438
-
Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignments
-
Dima R. I. and D. Thirumalai. 2002. Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignments. Biophys. J. 83:1268.
-
(2002)
Biophys. J.
, vol.83
, pp. 1268
-
-
Dima, R.I.1
Thirumalai, D.2
-
19
-
-
0027204024
-
Helix stop signals in proteins and peptides: The capping box
-
Harper E. T. and G. D. Rose. 1993. Helix stop signals in proteins and peptides: the capping box. Biochemistry 32:7605.
-
(1993)
Biochemistry
, vol.32
, pp. 7605
-
-
Harper, E.T.1
Rose, G.D.2
-
20
-
-
0030824202
-
The conserved N-capping box in the Hydrophobic core of glutathione S-transferase P1-1 isessential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability
-
Dragani, B., G. Stenberg, S. Melino, R. Petruzzelli, B. Mannervik and A. Aceto. 1997. The conserved N-capping box in the Hydrophobic core of glutathione S-transferase P1-1 isessential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability. J. Biol. Chem. 272:25518.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 25518
-
-
Dragani, B.1
Stenberg, G.2
Melino, S.3
Petruzzelli, R.4
Mannervik, B.5
Aceto, A.6
-
22
-
-
0034665733
-
Structures of thermolabile mutants of human glutathione transferase P1-1
-
Rossjohn J., W. J. McKinstry, A. J. Oakley, et al. 2000. Structures of thermolabile mutants of human glutathione transferase P1-1. J. Mol. Biol. 302:295.
-
(2000)
J. Mol. Biol.
, vol.302
, pp. 295
-
-
Rossjohn, J.1
McKinstry, W.J.2
Oakley, A.J.3
-
23
-
-
0027212028
-
Design of helix ends, amino acid preferences, hydrogen bonding and electrostatic interactions
-
Dasgupta S. and J.A. Bell. 1993. Design of helix ends, Amino acid preferences, hydrogen bonding and electrostatic interactions. Int. J. Pept. Protein Res. 41:499.
-
(1993)
Int. J. Pept. Protein Res.
, vol.41
, pp. 499
-
-
Dasgupta, S.1
Bell, J.A.2
-
24
-
-
0024290472
-
Amino acid preferences for specific locations at the ends of alpha helices
-
Richardson J.S. and D.C. Richardson. 1988. Amino acid preferences for specific locations at the ends of alpha helices. Science 240:1632.
-
(1988)
Science
, vol.240
, pp. 1632
-
-
Richardson, J.S.1
Richardson, D.C.2
-
25
-
-
0027946254
-
Amino acid preferences for specific locations at the ends of alpha helices
-
Jimenez M.A., V. Munoz, M. Rico and L. Serrano. 1994. Amino acid preferences for specific locations at the ends of alpha helices. J. Mol. Biol. 242:487.
-
(1994)
J. Mol. Biol.
, vol.242
, pp. 487
-
-
Jimenez, M.A.1
Munoz, V.2
Rico, M.3
Serrano, L.4
-
26
-
-
0029009067
-
The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding
-
Munoz V., F. J. Blanco and L. Serrano. 1995. The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding. Nature (London) 2:380.
-
(1995)
Nature (London)
, vol.2
, pp. 380
-
-
Munoz, V.1
Blanco, F.J.2
Serrano, L.3
-
27
-
-
0034616347
-
A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1
-
Stenberg G., B. Dragani, R. Cocco, B. Mannervik and A. Aceto. 2000. A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1. J. Biol. Chem. 275:10421.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 10421
-
-
Stenberg, G.1
Dragani, B.2
Cocco, R.3
Mannervik, B.4
Aceto, A.5
-
28
-
-
0035943609
-
The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif
-
Cocco R., G. Stenberg, B. Dragani, et al. 2001. The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif. J. Biol. Chem. 276:32177.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 32177
-
-
Cocco, R.1
Stenberg, G.2
Dragani, B.3
-
29
-
-
0037428487
-
Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1
-
Kong G.K., G. Polekhina, W.J. McKinstry, et al. 2003. Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1. J. Biol. Chem. 278:1291.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 1291
-
-
Kong, G.K.1
Polekhina, G.2
McKinstry, W.J.3
-
30
-
-
14844292799
-
-
G. M. Haddock, ed. Churchill Livingstone Edinburgh United Kingdom
-
Parchi P., P. Gambetti, P. Piccardo and B. Ghetti. 1998. In Progress in Pathology IV. G. M. Haddock, ed. Churchill Livingstone Edinburgh United Kingdom, p.1.
-
(1998)
Progress in Pathology IV
, pp. 1
-
-
Parchi, P.1
Gambetti, P.2
Piccardo, P.3
Ghetti, B.4
-
31
-
-
0030822582
-
Prion diseases and the BSE crisis
-
Prusiner S. B. 1997. Prion diseases and the BSE crisis. Science 278:245.
-
(1997)
Science
, vol.278
, pp. 245
-
-
Prusiner, S.B.1
-
32
-
-
0032496419
-
Protein folding and protein evolution: Common folding nucleus in different subfamilies of c-type cytochromes?
-
Ptitsyn O.B. 1998. Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?. J. Mol. Biol. 278:655.
-
(1998)
J. Mol. Biol.
, vol.278
, pp. 655
-
-
Ptitsyn, O.B.1
-
33
-
-
0033588067
-
Non-functional conserved residues in globins and their possible role as a folding nucleus
-
Ptitsyn O.B. and K.H. Ting. 1999. Non-functional conserved residues in globins and their possible role as a folding nucleus. J. Mol. Biol. 291:671.
-
(1999)
J. Mol. Biol.
, vol.291
, pp. 671
-
-
Ptitsyn, O.B.1
Ting, K.H.2
-
34
-
-
0031043161
-
Nucleation mechanisms in protein folding
-
Fersht A.R. 1997. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7:3.
-
(1997)
Curr. Opin. Struct. Biol.
, vol.7
, pp. 3
-
-
Fersht, A.R.1
-
36
-
-
0037380980
-
Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic
-
Florio T., D. Paludi, V. Villa, et al. 2003. Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic. J. Neurochem. 85:62.
-
(2003)
J. Neurochem.
, vol.85
, pp. 62
-
-
Florio, T.1
Paludi, D.2
Villa, V.3
-
37
-
-
0016169865
-
Determination of the helix and B form of proteins in aqueous solution by circular dichroism
-
Chen Y.H., J.T. Yang and K.H. Chau. 1974. Determination of the helix and B form of Proteins in aqueous solution by circular dichroism. Biochem. 13:3350.
-
(1974)
Biochem.
, vol.13
, pp. 3350
-
-
Chen, Y.H.1
Yang, J.T.2
Chau, K.H.3
-
38
-
-
0018118041
-
Circular dichroic analysis of protein conformation: Inclusion of the beta-turns
-
Chang C.T., C.S.C. Wu and J.T. Yang. 1978. Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Anal. Biochem. 91:13.
-
(1978)
Anal. Biochem.
, vol.91
, pp. 13
-
-
Chang, C.T.1
Wu, C.S.C.2
Yang, J.T.3
-
39
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UN1X pipes
-
Delaglio F., S. Grzesiek, G.W. Vuister, G. Zhu, J. Pfeifer and A. Bax. 1995. NMRPipe: a multidimensional spectral processing system based on UN1X pipes. J. Biomol. NMR 6:277.
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277
-
-
Delaglio, F.1
Grzesiek, S.2
Vuister, G.W.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
40
-
-
34249765651
-
A computer program for the visualization and analysis of NMR data
-
Johnson B. A. and R. A. J. Blevins. 1994. A computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:603.
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 603
-
-
Johnson, B.A.1
Blevins, R.A.J.2
-
41
-
-
5144233105
-
MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
-
Bax A. and D.G. Davis. 1985. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:355.
-
(1985)
J. Magn. Reson.
, vol.65
, pp. 355
-
-
Bax, A.1
Davis, D.G.2
-
42
-
-
0027787894
-
2O in protein NMR. Application to sensitivity enhancement and NOE measurements
-
2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115:12593.
-
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 12593
-
-
Grzesiek, S.1
Bax, A.2
-
43
-
-
0000762913
-
Sensitivity-enhanced correlation of 15N and 1H chemical
-
Bax A., R.H. Griffey and B.L. Hawkins. 1983. Sensitivity-enhanced correlation of 15N and 1H chemical. J. Am. Chem. Soc. 105:7188.
-
(1983)
J. Am. Chem. Soc.
, vol.105
, pp. 7188
-
-
Bax, A.1
Griffey, R.H.2
Hawkins, B.L.3
-
44
-
-
0344448273
-
Coherence transfer by isotopic mixing: Application to proton correlation spectroscopy
-
Braunschweiler L. and R.R. Ernst. 1983. Coherence transfer by isotopic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53:521.
-
(1983)
J. Magn. Reson.
, vol.53
, pp. 521
-
-
Braunschweiler, L.1
Ernst, R.R.2
-
45
-
-
5144229966
-
Practical aspects of two-dimensional transverse NOE spectroscopy
-
Bax A. and D.G. Davis. 1985. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63:207.
-
(1985)
J. Magn. Reson.
, vol.63
, pp. 207
-
-
Bax, A.1
Davis, D.G.2
-
47
-
-
0021114895
-
Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
-
Marion D. and K. Wuthrich. 1983. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113:967.
-
(1983)
Biochem. Biophys. Res. Commun.
, vol.113
, pp. 967
-
-
Marion, D.1
Wuthrich, K.2
-
48
-
-
0023645325
-
Protein structures in solution by nuclea'r magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
-
Wagner G., W. Braun, T. F. Havel, T. Schaumann, N. Go and K. J. Wüthrich. 1987. Protein structures in solution by nuclea'r magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. Mol. Biol. 196:611.
-
(1987)
Mol. Biol.
, vol.196
, pp. 611
-
-
Wagner, G.1
Braun, W.2
Havel, T.F.3
Schaumann, T.4
Go, N.5
Wüthrich, K.J.6
-
49
-
-
14844337186
-
-
Brunger A.T. 1993. Yale University Press New Haven CT, p. 1
-
Brunger A.T. 1993. Yale University Press New Haven CT, p. 1.
-
-
-
-
50
-
-
0031013382
-
The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode
-
Omichinski J.G., P.V. Pedone, G. Felsenfeld and G.M. Clore. 1997. The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode. Nat. Struct. Biol. 4:122.
-
(1997)
Nat. Struct. Biol.
, vol.4
, pp. 122
-
-
Omichinski, J.G.1
Pedone, P.V.2
Felsenfeld, G.3
Clore, G.M.4
-
51
-
-
0026410969
-
Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
-
Wishart D.S., B.D. Sykes and F.M. Richards. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:311.
-
(1991)
J. Mol. Biol.
, vol.222
, pp. 311
-
-
Wishart, D.S.1
Sykes, B.D.2
Richards, F.M.3
-
52
-
-
0023122030
-
Tests of the helix dipole model for stabilization of alpha-helices
-
Shoemaker K.R P.S. Kim, E.J. York, J.M. Stewart, and R.L. Baldwin. 1987. Tests of the helix dipole model for stabilization of alpha-helices. Nature 326:563.
-
(1987)
Nature
, vol.326
, pp. 563
-
-
Kim, S.K.R.P.S.1
York, E.J.2
Stewart, J.M.3
Baldwin, R.L.4
-
53
-
-
0037073678
-
Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form
-
Vanik D.L. and W. K. Surewicz. 2002. Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form. J. Biol. Chem. 277:49065.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 49065
-
-
Vanik, D.L.1
Surewicz, W.K.2
-
54
-
-
0034721767
-
Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases
-
Zhang Y., W. Swietnicki, M. G. Zagorski, W. K. Surewicz and F.D. Sonnichsen. 2000. Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J. Biol. Chem. 275:33650.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 33650
-
-
Zhang, Y.1
Swietnicki, W.2
Zagorski, M.G.3
Surewicz, W.K.4
Sonnichsen, F.D.5
|