-
1
-
-
0033621165
-
Amyloid diseases: Abnormal protein aggregation in neurodegeneration
-
Koo, E. H., Lansbury, P. T. Jr & Kelly, J. W. Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc. Natl Acad. Sci. USA 96, 9989-9990 (1999).
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 9989-9990
-
-
Koo, E.H.1
Lansbury Jr., P.T.2
Kelly, J.W.3
-
2
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson, C. M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24, 329-332 (1999).
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
3
-
-
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. Nature Struct. Biol. 8, 211-214 (2001).
-
(2001)
Nature Struct. Biol.
, vol.8
, pp. 211-214
-
-
Liu, Y.1
Gotte, G.2
Libonati, M.3
Eisenberg, D.4
-
4
-
-
0031592945
-
Common core structure of amyloid fibrils by synchrotron X-ray diffraction
-
Sunde, M. et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273, 729-739 (1997).
-
(1997)
J. Mol. Biol.
, vol.273
, pp. 729-739
-
-
Sunde, M.1
-
5
-
-
0015859467
-
Principles that govern the folding of protein chains
-
Anfinsen, C. B. Principles that govern the folding of protein chains. Science 181, 223-230 (1973).
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
6
-
-
0001611370
-
Electron microscopic observations on a fibrous component in amyloid of diverse origins
-
Cohen, A. A. & Calkins, E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183, 1202-1203 (1959).
-
(1959)
Nature
, vol.183
, pp. 1202-1203
-
-
Cohen, A.A.1
Calkins, E.2
-
7
-
-
0042847751
-
Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
-
Jimenez, J. L. et al. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18, 815-821 (1999).
-
(1999)
EMBO J.
, vol.18
, pp. 815-821
-
-
Jimenez, J.L.1
-
8
-
-
0037047118
-
The protofilament structure of insulin amyloid fibrils
-
Jimenez, J. L. et al. The protofilament structure of insulin amyloid fibrils. Proc. Natl Acad. Sci. USA 99, 9196-9201 (2002).
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 9196-9201
-
-
Jimenez, J.L.1
-
9
-
-
1242340413
-
β-Helix is a likely core structure of yeast prion Sup amyloid fibrils
-
Kishimoto, A. et al. β-Helix is a likely core structure of yeast prion Sup amyloid fibrils. Biochem. Biophys. Res. Commun. 315, 739-745 (2004).
-
(2004)
Biochem. Biophys. Res. Commun.
, vol.315
, pp. 739-745
-
-
Kishimoto, A.1
-
10
-
-
2942616602
-
Evidence for assembly of prions with left-handed β-helices into trimers
-
Govaerts, C., Wille, H., Prusiner, S. B. & Cohen, F. E. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl Acad. Sci. USA 101, 8342-8347 (2004).
-
(2004)
Proc. Natl Acad. Sci. USA
, vol.101
, pp. 8342-8347
-
-
Govaerts, C.1
Wille, H.2
Prusiner, S.B.3
Cohen, F.E.4
-
11
-
-
0037117519
-
Amyloid fibrils are water-filled nanotubes
-
Perutz, M. F., Finch, J. T., Berriman, J. & Lesk, A. Amyloid fibrils are water-filled nanotubes. Proc. Natl Acad. Sci. USA 99, 5591-5595 (2002).
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 5591-5595
-
-
Perutz, M.F.1
Finch, J.T.2
Berriman, J.3
Lesk, A.4
-
12
-
-
0037313696
-
A primordial structure underlying amyloid
-
Pickersgill, R. W. A primordial structure underlying amyloid. Structure 11, 137-138 (2003).
-
(2003)
Structure
, vol.11
, pp. 137-138
-
-
Pickersgill, R.W.1
-
13
-
-
0036052739
-
Ideas of order for amyloid fibril structure
-
Wetzel, R. Ideas of order for amyloid fibril structure. Structure 10, 1031-1036 (2002).
-
(2002)
Structure
, vol.10
, pp. 1031-1036
-
-
Wetzel, R.1
-
14
-
-
2942748436
-
Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin
-
Eakin, C. M., Attenello, F. J., Morgan, C. J. & Miranker, A. D. Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin. Biochemistry 43, 7808-7815 (2004).
-
(2004)
Biochemistry
, vol.43
, pp. 7808-7815
-
-
Eakin, C.M.1
Attenello, F.J.2
Morgan, C.J.3
Miranker, A.D.4
-
15
-
-
0030770294
-
Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
-
Schlunegger, M. P., Bennett, M. J. & Eisenberg, D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50, 61-122 (1997).
-
(1997)
Adv. Protein Chem.
, vol.50
, pp. 61-122
-
-
Schlunegger, M.P.1
Bennett, M.J.2
Eisenberg, D.3
-
16
-
-
0035069135
-
Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping
-
Janowski, R. et al. Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nature Struct. Biol. 8, 316-320 (2001).
-
(2001)
Nature Struct. Biol.
, vol.8
, pp. 316-320
-
-
Janowski, R.1
-
17
-
-
2642567686
-
Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: Use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C
-
Nilsson, M. et al. Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C. J. Biol. Chem. 279, 24236-24245 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 24236-24245
-
-
Nilsson, M.1
-
18
-
-
0345869697
-
Cystatin forms a tetramer through structural rearrangement of domain-swapped dinners prior to amyloidogenesis
-
Sanders, A. et al. Cystatin forms a tetramer through structural rearrangement of domain-swapped dinners prior to amyloidogenesis. J. Mol. Biol. 336, 165-178 (2004).
-
(2004)
J. Mol. Biol.
, vol.336
, pp. 165-178
-
-
Sanders, A.1
-
19
-
-
0035801540
-
Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
-
Staniforth, R. A. et al. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20, 4774-4781 (2001).
-
(2001)
EMBO J.
, vol.20
, pp. 4774-4781
-
-
Staniforth, R.A.1
-
20
-
-
0000505830
-
Reductive cleavage of disulfide bridges in ribonuclease
-
Sela, M., White, F. H. & Anfinsen, C. B. Reductive cleavage of disulfide bridges in ribonuclease. Science 125, 691-692 (1957).
-
(1957)
Science
, vol.125
, pp. 691-692
-
-
Sela, M.1
White, F.H.2
Anfinsen, C.B.3
-
21
-
-
0001036527
-
Properties and conformation of the histidine residues at the active site of ribonuclease
-
Crestfield, A. M., Stein, W. H. & Moore, S. Properties and conformation of the histidine residues at the active site of ribonuclease. J. Biol. Chem. 228, 2421-2428 (1963).
-
(1963)
J. Biol. Chem.
, vol.228
, pp. 2421-2428
-
-
Crestfield, A.M.1
Stein, W.H.2
Moore, S.3
-
22
-
-
0001483424
-
Structural versatility of bovine ribonuclease A. Distinct conformers of trimeric and tetrameric aggregates of the enzyme
-
Gotte, G., Bertoldi, M. & Libonati, M. Structural versatility of bovine ribonuclease A. Distinct conformers of trimeric and tetrameric aggregates of the enzyme. Eur. J. Biochem. 265, 680-687 (1999).
-
(1999)
Eur. J. Biochem.
, vol.265
, pp. 680-687
-
-
Gotte, G.1
Bertoldi, M.2
Libonati, M.3
-
23
-
-
20444440728
-
Structure of the amyloid spine
-
Nelson, R. et al. Structure of the amyloid spine. Nature 435, 773-777 (2005).
-
(2005)
Nature
, vol.435
, pp. 773-777
-
-
Nelson, R.1
-
24
-
-
0036108484
-
3D domain swapping: As domains continue to swap
-
Liu, Y. & Eisenberg, D. 3D domain swapping: as domains continue to swap. Protein Sci. 11, 1285-1299 (2002).
-
(2002)
Protein Sci.
, vol.11
, pp. 1285-1299
-
-
Liu, Y.1
Eisenberg, D.2
-
25
-
-
0031056829
-
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
-
Booth, D. R. et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787-793 (1997).
-
(1997)
Nature
, vol.385
, pp. 787-793
-
-
Booth, D.R.1
-
26
-
-
0028865843
-
3D domain swapping: A mechanism for oligomer assembly
-
Bennett, M. J., Schlunegger, M. P. & Eisenberg, D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4, 2455-2468 (1995).
-
(1995)
Protein Sci.
, vol.4
, pp. 2455-2468
-
-
Bennett, M.J.1
Schlunegger, M.P.2
Eisenberg, D.3
|