10201 RESULTS
COMMENT I am familiar with the Aβ*56 story and read the original Nature paper with interest. I also recall talking to several colleagues about this paper. I have not followed the story carefully, but am aware that this Aβ oligomer species has been difficult to co
COMMENT This is terrible news! However, I think the implications the Science piece is suggesting are somewhat overblown. The Lesne/Ashe paper had far less effect on the direction of the field than the Science article claims. I think the Aβ*56 work was just one pa
COMMENT Clearly, science is a continuous discussion of the relevance of published results. Hence, it is of utmost importance to see data replicated and verified by other research groups. This is especially the case in such a competitive field as Alzheimer’s disea
COMMENT I am speechless about these allegations. This damages the reputation of the oligomer research field, where much good work is being done. Regarding Aβ56*, we were skeptical about the data from the beginning, and our lab never started a project on it. chris
COMMENT I have never thought this paper was important, and I don’t think I have ever cited it. “Oligomer” toxicity has never been satisfactorily demonstrated in any system. It is too bad if these papers involve deceit, and journals and institutions need to crack
COMMENT Aβ, also known as “the peptide from hell,” is very difficult to work with, because of its high degree of hydrophobicity and aggregability. We first described oligomers of Aβ in 1985 (A-8 dimers, A-16 tetramers, etc.; Masters et al., 1985). There have been
COMMENT In my own group, we tried replicating the Aβ *56 western blots for about a year, without success. We then moved on to other things. Our later work on soluble Aβ aggregates/oligomers from human brain tissue indicated that they are considerably larger than
COMMENT There is a large body of evidence that soluble Aβ aggregates, either formed in the test tube or in the brain, can be toxic to neurons. However, a wide variety of aggregates of different sizes and structures can be formed during the aggregation of Aβ in th
COMMENT times suggests. I did submit a quite long comment on this paper back in 2006 in Alzforum, where I voiced
COMMENT Aβ oligomers are a very successful concept, most importantly in comparison and in contrast to the previous concepts that were totally limited to pure plaque pathology. Characterization and description of Aβ oligomers, however, is terribly difficult, becau
COMMENT There are many layers of disappointment, dismay, and anger to disentangle if these strongly supported allegations of scientific fraud attributed to a member of the AD field are true. On a broader scale, it makes me question how a protein associated with A
COMMENT This is shocking. I have always been suspicious about the quality of the data supporting the oligomer “soup” hypothesis (see Benilova et al., 2012). It is a pity that this scandal also undermines all the decent work in our field. Aβ undoubtedly plays an
COMMENT Various studies from many laboratories suggest that the most toxic forms of Aβ are not the fibrils found in plaques, but rather the soluble lower-molecular-weight species known as Aβ oligomers and protofibrils (Walsh et al., 1997; Nilsberth et al., 2001;
COMMENT I was interviewed by the investigative reporter and saw some of the forensic analyses of the images. In 2006, a number of us considered it unlikely that there was one favored oligomer causing synaptotoxicity. I feel this problem is most unfortunate for ge
COMMENT I am responding to this story not with regard to these specific allegations, but because I have broader concerns regarding the use of Aβ oligomers as a tool to induce toxicity resembling a process that matters to AD pathogenesis. To my mind, it is irrelev
