7 RESULTS
COMMENT This is an important paper, demonstrating that detailed molecular structural information about Aβ fibrils can be obtained from cryoEM. Other labs have attempted this in earlier publications, but with less success. The success of this work by Gremer et al. ...
COMMENT "Amplification bias" is certainly an issue that needs to be considered when fibril structures from brain tissue are amplified by seeded growth. Certain structures may self-propagate more efficiently than others, depending on the precise details ...
COMMENT This structural model for Aβ42 fibrils is surprisingly different from existing models for Aβ40 fibrils. The peptide backbone conformation is different, and the contacts between amino acid side chains are different. For example, most Aβ40 fibrils have ...
COMMENT In response to Dr. Kennedy's comments: 1. Our structural model for Aβ40 fibrils from patient 1, described in this paper, was calculated with Xplor-NIH software using 197 NMR-based experimental structural restraints (4.925 restraints per residue on ...
COMMENT This paper from the Eisenberg group suggests several molecular structural models for fibrils formed by full-length β amyloid peptides, based on their crystal structures of segments of the full-length peptide that reveal the details of intermolecular ...
COMMENT 1. Before comparing structural studies of Aβ fibrils from different laboratories, it is crucially important to compare the conditions under which the fibrils were grown, as our own solid-state NMR and electron microscopy studies have shown that Aβ fibril ...
COMMENT Novel experiments by David Teplow, George Benedek, and their colleagues provide important new information about the nature of oligomeric aggregates that form rapidly in aqueous solutions of the β-amyloid peptides, prior to the formation of protofibrils ...
