Alzheimer's amyloid fibrils: structure and assembly Export

@article{citeulike:3727446, abstract = {Structural studies of Alzheimer\&\#x2019;s amyloid fibrils have revealed information about the structure at different levels. The amyloid-\&\#x3b2; peptide has been examined in various solvents and conditions and this has led to a model by which a conformational switching occurs from \&\#x3b1;-helix or random coil, to a \&\#x3b2;-sheet structure. Amyloid fibril assembly proceeds by a nucleation dependent pathway leading to elongation of the fibrils. Along this pathway small oligomeric intermediates and short fibrillar structures (protofibrils) have been observed. In cross-section the fibril appears to be composed of several subfibrils or protofilaments. Each of these protofilaments is composed of \&\#x3b2;-sheet structure in which hydrogen bonding occurs along the length of the fibre and the \&\#x3b2;-strands run perpendicular to the fibre axis. This hierarchy of structure is discussed in this review.}, author = {Serpell, L.}, citeulike-article-id = {3727446}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0925-4439(00)00029-6}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0925-4439(00)00029-6}, day = {26}, doi = {10.1016/S0925-4439(00)00029-6}, issn = {09254439}, journal = {Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease}, keywords = {amyloids}, month = {July}, number = {1}, pages = {16--30}, posted-at = {2009-05-07 10:23:36}, priority = {2}, title = {Alzheimer's amyloid fibrils: structure and assembly}, url = {http://dx.doi.org/10.1016/S0925-4439(00)00029-6}, volume = {1502}, year = {2000} }

TY - JOUR ID - citeulike:3727446 L3 - citeulike-article-id:3727446 N2 - Structural studies of Alzheimer’s amyloid fibrils have revealed information about the structure at different levels. The amyloid-β peptide has been examined in various solvents and conditions and this has led to a model by which a conformational switching occurs from α-helix or random coil, to a β-sheet structure. Amyloid fibril assembly proceeds by a nucleation dependent pathway leading to elongation of the fibrils. Along this pathway small oligomeric intermediates and short fibrillar structures (protofibrils) have been observed. In cross-section the fibril appears to be composed of several subfibrils or protofilaments. Each of these protofilaments is composed of β-sheet structure in which hydrogen bonding occurs along the length of the fibre and the β-strands run perpendicular to the fibre axis. This hierarchy of structure is discussed in this review. IS - 1 JF - Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease SN - 09254439 EP - 30 TI - Alzheimer's amyloid fibrils: structure and assembly VL - 1502 SP - 16 KW - amyloids AU - Serpell, L PY - 2000/07/26/ UR - http://dx.doi.org/10.1016/S0925-4439(00)00029-6 ER -