Amyloid fibrils may be assembled from β-helical protofibrils

[1] Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix [J]. STRUCTURE, 1996, 4 (08) : 989 - 998

[2] Downing DT, 1996, PROTEINS, V25, P215, DOI 10.1002/(SICI)1097-0134(199606)25:2<215::AID-PROT7>3.0.CO

[3] 2-G

[4] Downing DT, 1996, PROTEINS, V26, P472, DOI 10.1002/(SICI)1097-0134(199612)26:4<472::AID-PROT8>3.0.CO

[5] 2-D

[6] MOLECULAR MODELING INDICATES THAT HOMODIMERS FORM THE BASIS FOR INTERMEDIATE FILAMENT ASSEMBLY FROM HUMAN AND MOUSE EPIDERMAL KERATINS [J]. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1995, 23 (02): : 204 - 217

[7] CONFORMATION AND FIBRILLOGENESIS OF ALZHEIMER A-BETA PEPTIDES WITH SELECTED SUBSTITUTION OF CHARGED RESIDUES [J]. JOURNAL OF MOLECULAR BIOLOGY, 1994, 244 (01) : 64 - 73

[8] The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid [J]. BIOCHEMISTRY, 1996, 35 (20) : 6470 - 6482

[9] IN PURSUIT OF THE MOLECULAR-STRUCTURE OF AMYLOID PLAQUE - NEW TECHNOLOGY PROVIDES UNEXPECTED AND CRITICAL INFORMATION [J]. BIOCHEMISTRY, 1992, 31 (30) : 6865 - 6870

[10] STRUCTURAL MODEL FOR THE BETA-AMYLOID FIBRIL BASED ON INTERSTRAND ALIGNMENT OF AN ANTIPARALLEL-SHEET COMPRISING A C-TERMINAL PEPTIDE [J]. NATURE STRUCTURAL BIOLOGY, 1995, 2 (11): : 990 - 998

[1] Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix [J]. STRUCTURE, 1996, 4 (08) : 989 - 998

[2] Downing DT, 1996, PROTEINS, V25, P215, DOI 10.1002/(SICI)1097-0134(199606)25:2<215::AID-PROT7>3.0.CO

[3] 2-G

[4] Downing DT, 1996, PROTEINS, V26, P472, DOI 10.1002/(SICI)1097-0134(199612)26:4<472::AID-PROT8>3.0.CO

[5] 2-D

[6] MOLECULAR MODELING INDICATES THAT HOMODIMERS FORM THE BASIS FOR INTERMEDIATE FILAMENT ASSEMBLY FROM HUMAN AND MOUSE EPIDERMAL KERATINS [J]. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1995, 23 (02): : 204 - 217

[7] CONFORMATION AND FIBRILLOGENESIS OF ALZHEIMER A-BETA PEPTIDES WITH SELECTED SUBSTITUTION OF CHARGED RESIDUES [J]. JOURNAL OF MOLECULAR BIOLOGY, 1994, 244 (01) : 64 - 73

[8] The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid [J]. BIOCHEMISTRY, 1996, 35 (20) : 6470 - 6482

[9] IN PURSUIT OF THE MOLECULAR-STRUCTURE OF AMYLOID PLAQUE - NEW TECHNOLOGY PROVIDES UNEXPECTED AND CRITICAL INFORMATION [J]. BIOCHEMISTRY, 1992, 31 (30) : 6865 - 6870

[10] STRUCTURAL MODEL FOR THE BETA-AMYLOID FIBRIL BASED ON INTERSTRAND ALIGNMENT OF AN ANTIPARALLEL-SHEET COMPRISING A C-TERMINAL PEPTIDE [J]. NATURE STRUCTURAL BIOLOGY, 1995, 2 (11): : 990 - 998