-
1
-
-
0001193811
-
A reductionist view of Alzheimer's disease
-
1. Lansbury, P.T. Jr (1996) A reductionist view of Alzheimer's disease. Acc. Chem. Res. 29, 317-321.
-
(1996)
Acc. Chem. Res.
, vol.29
, pp. 317-321
-
-
Lansbury P.T., Jr.1
-
2
-
-
0029895147
-
Brain amyloid - A physicochemical perspective
-
2. Maggio, J.E. & Mantyh, P.W. (1996) Brain amyloid - a physicochemical perspective. Brain Pathol. 6, 147-162.
-
(1996)
Brain Pathol.
, vol.6
, pp. 147-162
-
-
Maggio, J.E.1
Mantyh, P.W.2
-
3
-
-
0020511509
-
Ultrastructural morphology of amyloid fibrils from neuritic and amyloid plaques
-
3. Merz, P.A., Wisniewski, H.M., Sommerville, R.A., Bobin, S.A., Masters, C.L. & Iqbal, K. (1983) Ultrastructural morphology of amyloid fibrils from neuritic and amyloid plaques. Acta Neuropathol. 60, 113-124.
-
(1983)
Acta Neuropathol.
, vol.60
, pp. 113-124
-
-
Merz, P.A.1
Wisniewski, H.M.2
Sommerville, R.A.3
Bobin, S.A.4
Masters, C.L.5
Iqbal, K.6
-
4
-
-
0026453127
-
Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid β-protein
-
4. Fraser, P.E., Nguyen, J.T., Inouye, H., Surewicz, W.K., Selkoe, D.J., Podlisny, M.B. & Kirschner, D.A. (1992) Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid β-protein. Biochemistry 31, 10716-10723.
-
(1992)
Biochemistry
, vol.31
, pp. 10716-10723
-
-
Fraser, P.E.1
Nguyen, J.T.2
Inouye, H.3
Surewicz, W.K.4
Selkoe, D.J.5
Podlisny, M.B.6
Kirschner, D.A.7
-
5
-
-
0028063590
-
Conformation and fibrillogenesis of Alzheimer Aβ peptides with selected substitution of charged residues
-
5. Fraser, P.E., McLachlan, D.R., Surewicz, W.K., Mizzen, C.A., Snow, A.D., Nguyen, J.T. & Kirschner, D.A. (1994) Conformation and fibrillogenesis of Alzheimer Aβ peptides with selected substitution of charged residues. J. Mol. Biol. 244, 64-73.
-
(1994)
J. Mol. Biol.
, vol.244
, pp. 64-73
-
-
Fraser, P.E.1
McLachlan, D.R.2
Surewicz, W.K.3
Mizzen, C.A.4
Snow, A.D.5
Nguyen, J.T.6
Kirschner, D.A.7
-
6
-
-
0014098295
-
High resolution electron microscopic analysis of the amyloid fibril
-
6. Shirahama, T. & Cohen, A.S. (1967) High resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol. 33, 679-706.
-
(1967)
J. Cell Biol.
, vol.33
, pp. 679-706
-
-
Shirahama, T.1
Cohen, A.S.2
-
7
-
-
0014413467
-
Cross-β conformation in proteins
-
7. Geddes, A.J., Parker, K.D., Atkins, E.D.T. & Beighton, E. (1968) Cross-β conformation in proteins. J. Mol. Biol. 32, 343-358.
-
(1968)
J. Mol. Biol.
, vol.32
, pp. 343-358
-
-
Geddes, A.J.1
Parker, K.D.2
Atkins, E.D.T.3
Beighton, E.4
-
8
-
-
38349006853
-
An investigation of the structure of silk fibroin
-
8. Marsh, R.E., Corey, R.B. & Pauling, L. (1955) An investigation of the structure of silk fibroin. Biochim. Biophys. Acta 16, 1-34.
-
(1955)
Biochim. Biophys. Acta
, vol.16
, pp. 1-34
-
-
Marsh, R.E.1
Corey, R.B.2
Pauling, L.3
-
9
-
-
0026320119
-
An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: Application of solid-state NMR to the determination of protein secondary structure
-
9. Spenser, R.G.S., Halverson, K.J., Auger, M., McDermott, A.E., Griffin, R.G. & Lansbury, P.T. Jr (1991) An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Biochemistry 30, 10382-10387.
-
(1991)
Biochemistry
, vol.30
, pp. 10382-10387
-
-
Spenser, R.G.S.1
Halverson, K.J.2
Auger, M.3
McDermott, A.E.4
Griffin, R.G.5
Lansbury P.T., Jr.6
-
10
-
-
0000666695
-
Rotational resonance solid-state NMR elucidates a structural model of pancreatic amyloid
-
10. Griffiths, J.M., Ashburn, T.T., Auger, M., Costa, P.R., Griffin, R.G. & Lansbury, P.T. Jr (1995) Rotational resonance solid-state NMR elucidates a structural model of pancreatic amyloid. J. Am. Chem. Soc. 117, 3539-3546.
-
(1995)
J. Am. Chem. Soc.
, vol.117
, pp. 3539-3546
-
-
Griffiths, J.M.1
Ashburn, T.T.2
Auger, M.3
Costa, P.R.4
Griffin, R.G.5
Lansbury P.T., Jr.6
-
11
-
-
0028804827
-
Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
-
11. Lansbury, P.T. Jr, Costa, P.R., Griffiths, J.M., Simon, E.J., Auger, M., Halversen, K.J., Kocisko, D.A., Hendsch, Z.S., Ashburn, T.T., Spenser, R.G.S., Tidor, B. & Griffin, R.G. (1995) Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nature Struct. Biol. 2, 990-998.
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 990-998
-
-
Lansbury P.T., Jr.1
Costa, P.R.2
Griffiths, J.M.3
Simon, E.J.4
Auger, M.5
Halversen, K.J.6
Kocisko, D.A.7
Hendsch, Z.S.8
Ashburn, T.T.9
Spenser, R.G.S.10
Tidor, B.11
Griffin, R.G.12
-
12
-
-
0030668710
-
Determination of peptide amide configuration in a model amyloid fibril by solid-state NMR
-
12. Costa, P.R., Kocisko, D.A., Sun, B.Q., Lansbury, P.T. Jr & Griffin, R.G. (1997) Determination of peptide amide configuration in a model amyloid fibril by solid-state NMR. J. Am. Chem. Soc. 119, 10487-10493.
-
(1997)
J. Am. Chem. Soc.
, vol.119
, pp. 10487-10493
-
-
Costa, P.R.1
Kocisko, D.A.2
Sun, B.Q.3
Lansbury P.T., Jr.4
Griffin, R.G.5
-
13
-
-
0029670277
-
The nanometer-scale structure of amyloid-β visualized by atomic force microscopy
-
13. Stine, W.B., Snyder, S.W., Ladror, U.S., Wade, W.S., Miller, M.F., Perun, T.J., Holtzman, T.F. & Krafft, G.A. (1996) The nanometer-scale structure of amyloid-β visualized by atomic force microscopy. J. Protein Chem. 15, 193-202.
-
(1996)
J. Protein Chem.
, vol.15
, pp. 193-202
-
-
Stine, W.B.1
Snyder, S.W.2
Ladror, U.S.3
Wade, W.S.4
Miller, M.F.5
Perun, T.J.6
Holtzman, T.F.7
Krafft, G.A.8
-
14
-
-
0030614627
-
Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
-
14. Harper, J.D., Wong, S.S., Lieber, C.M. & Lansbury, P.T. Jr (1997) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
-
(1997)
Chem. Biol.
, vol.4
, pp. 119-125
-
-
Harper, J.D.1
Wong, S.S.2
Lieber, C.M.3
Lansbury P.T., Jr.4
-
15
-
-
0031444010
-
Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
-
15. Harper, J.D., Lieber, C.M. & Lansbury, P.T. Jr (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem. Biol. 4, 951-959.
-
(1997)
Chem. Biol.
, vol.4
, pp. 951-959
-
-
Harper, J.D.1
Lieber, C.M.2
Lansbury P.T., Jr.3
-
16
-
-
0032539573
-
Amyloid fibrils may be assembled from β-helical protofibrils
-
16. Lazo, N.D. & Downing, D.T. (1998) Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry 37, 1731-1735.
-
(1998)
Biochemistry
, vol.37
, pp. 1731-1735
-
-
Lazo, N.D.1
Downing, D.T.2
-
17
-
-
0025275241
-
Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments
-
17. Halverson, K., Fraser, P.E., Kirschner, D.A. & Lansbury, P.T. Jr (1990) Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistiy 29, 2639-2644.
-
(1990)
Biochemistiy
, vol.29
, pp. 2639-2644
-
-
Halverson, K.1
Fraser, P.E.2
Kirschner, D.A.3
Lansbury P.T., Jr.4
-
18
-
-
0027949973
-
A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation
-
18. Kelly, J.W. & Lansbury, P.T. Jr (1994) A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation. Amyloid: Int. J. Exp. Clin. Invest. 1, 186-205.
-
(1994)
Amyloid: Int. J. Exp. Clin. Invest.
, vol.1
, pp. 186-205
-
-
Kelly, J.W.1
Lansbury P.T., Jr.2
-
19
-
-
0031019984
-
Circular dichroism of model peptides emulating the amphipathic α-helical regions of intermediate filaments
-
19. Lazo, N.D. & Downing, D.T. (1997) Circular dichroism of model peptides emulating the amphipathic α-helical regions of intermediate filaments. Biochemistry 36, 2559-2565.
-
(1997)
Biochemistry
, vol.36
, pp. 2559-2565
-
-
Lazo, N.D.1
Downing, D.T.2
-
20
-
-
0022503457
-
Calculation of protein conformation from circular dichroism
-
20. Yang, J.T., Wu, C.-S.C. & Martinez, H.M. (1986) Calculation of protein conformation from circular dichroism. Meth Enzymol. 130, 208-269.
-
(1986)
Meth Enzymol.
, vol.130
, pp. 208-269
-
-
Yang, J.T.1
Wu, C.-S.C.2
Martinez, H.M.3
-
21
-
-
0028864109
-
Molecular modeling indicates that homodimers form the basis for intermediate filament assembly from human and mouse epidermal keratins
-
21. Downing, D.T. (1995) Molecular modeling indicates that homodimers form the basis for intermediate filament assembly from human and mouse epidermal keratins. Proteins: Struct. Func. Genet. 23, 204-217.
-
(1995)
Proteins: Struct. Func. Genet.
, vol.23
, pp. 204-217
-
-
Downing, D.T.1
-
22
-
-
0029902083
-
Chemical cross-linking between lysine groups in vimentin oligomers is dependent on local peptide conformations
-
22. Downing, D.T. (1996) Chemical cross-linking between lysine groups in vimentin oligomers is dependent on local peptide conformations. Proteins: Struct. Func. Genet. 25, 215-224.
-
(1996)
Proteins: Struct. Func. Genet.
, vol.25
, pp. 215-224
-
-
Downing, D.T.1
-
23
-
-
0030443369
-
Molecular modeling of vimentin filament assembly
-
23. Downing, D.T. (1996) Molecular modeling of vimentin filament assembly. Proteins: Struct. Func. Genet. 26, 472-478.
-
(1996)
Proteins: Struct. Func. Genet.
, vol.26
, pp. 472-478
-
-
Downing, D.T.1
-
25
-
-
0031907944
-
Stabilization of amphipathic α-helical and β-helical conformations in synthetic peptides in the presence and absence of ionic interactions
-
25. Lazo, N.D. & Downing, D.T. (1998) Stabilization of amphipathic α-helical and β-helical conformations in synthetic peptides in the presence and absence of ionic interactions. J. Peptide Res. 51, 85-89.
-
(1998)
J. Peptide Res.
, vol.51
, pp. 85-89
-
-
Lazo, N.D.1
Downing, D.T.2
-
26
-
-
0029081224
-
Circular dichroism of the parallel β-helical proteins pectate lyase C and E
-
26. Sieber, V., Jumak, F. & Moe, G.R. (1995) Circular dichroism of the parallel β-helical proteins pectate lyase C and E. Proteins: Struct. Func. Genet. 23, 32-37.
-
(1995)
Proteins: Struct. Func. Genet.
, vol.23
, pp. 32-37
-
-
Sieber, V.1
Jumak, F.2
Moe, G.R.3
-
27
-
-
0028885682
-
Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro
-
27. Pike, C.J., Overman, M.J. & Cotman, C.W. (1995) Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro. J. Biol. Chem. 270, 23895-23898.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 23895-23898
-
-
Pike, C.J.1
Overman, M.J.2
Cotman, C.W.3
-
28
-
-
0027329090
-
New domain motif: The structure of pectate lyase c, a secreted plant virulence factor
-
28. Yoder, M.D., Keen, N.T. & Jurnak, F. (1993) New domain motif: the structure of pectate lyase c, a secreted plant virulence factor. Science 260, 1503-1507.
-
(1993)
Science
, vol.260
, pp. 1503-1507
-
-
Yoder, M.D.1
Keen, N.T.2
Jurnak, F.3
-
29
-
-
0028095571
-
Crystal structure of p22 tailspike protein: Interdigitated subunits in a thermostable trimer
-
29. Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R. & Reinemer, P. (1994) Crystal structure of p22 tailspike protein: interdigitated subunits in a thermostable trimer. Science 265, 383-386.
-
(1994)
Science
, vol.265
, pp. 383-386
-
-
Steinbacher, S.1
Seckler, R.2
Miller, S.3
Steipe, B.4
Huber, R.5
Reinemer, P.6
-
30
-
-
0028844306
-
A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase
-
30. Raetz, C.R.H. & Roderick, S.L. (1995) A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270, 997-1000.
-
(1995)
Science
, vol.270
, pp. 997-1000
-
-
Raetz, C.R.H.1
Roderick, S.L.2
-
31
-
-
0030908095
-
Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
-
31. Harper, J.D. & Lansbury, P.T. Jr (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66, 385-407.
-
(1997)
Annu. Rev. Biochem.
, vol.66
, pp. 385-407
-
-
Harper, J.D.1
Lansbury P.T., Jr.2
-
32
-
-
0028845988
-
Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs
-
32. Serpell, L.C., Sunde, M., Fraser, P.E., Luther, P.K., Morris, E.P. Sangren, O., Lundgren, E. & Blake, C.C.F. (1995) Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254, 113-118.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 113-118
-
-
Serpell, L.C.1
Sunde, M.2
Fraser, P.E.3
Luther, P.K.4
Morris, E.P.5
Sangren, O.6
Lundgren, E.7
Blake, C.C.F.8
-
33
-
-
0030586945
-
Synchrotron X-ray studies suggest that the core of the transthyretin amyoid fibril is a continuous β-sheet helix
-
33. Blake, C. & Serpell, L. (1996) Synchrotron X-ray studies suggest that the core of the transthyretin amyoid fibril is a continuous β-sheet helix. Structure 4, 989-998.
-
(1996)
Structure
, vol.4
, pp. 989-998
-
-
Blake, C.1
Serpell, L.2
|