Norman Foster
Center for Alzheimer's Care, Imaging and ResearchSalt Lake City, United States
329938 RESULTS
Center for Alzheimer's Care, Imaging and ResearchSalt Lake City, United States
PAPER Do CB, Tung JY, Dorfman E, Kiefer AK, Drabant EM, Francke U, Mountain JL, Goldman SM, Tanner CM, Langston JW, Wojcicki A, Eriksson N
PAPER
Merck Sharpe & DohmeWest Point, United States
COMMENT This is a great finding. We have all along suspected that there may be a transport mechanism for Aβ through the blood-brain barrier. In our previous article, we thought that impaired clearance of Aβ may be responsible for late-onset AD through impaired tr
COMMENT Dr. Krohn and colleagues have identified another Aβ transporter at the CNS-blood barrier, ABCC1. Interestingly, this particular transporter is highly expressed at the choroid plexus, suggesting that, in addition to playing a role at the blood-brain barrie
PAPER Bartels AL, Kortekaas R, Bart J, Willemsen AT, de Klerk OL, de Vries JJ, van Oostrom JC, Leenders KL
PAPER Bartels AL, Willemsen AT, Kortekaas R, de Jong BM, de Vries R, de Klerk O, van Oostrom JC, Portman A, Leenders KL
PAPER Kortekaas R, Leenders KL, van Oostrom JC, Vaalburg W, Bart J, Willemsen AT, Hendrikse NH
COMMENT As an insulin research scientist of many decades, it is of interest to read the article showing alterations in brain function by nasal insulin. For many years, it has been believed that brain tissue as an obligatory glucose consumer does not require insul
COMMENT We should learn from the success of the vaccination against cervical cancer. 0 saido
COMMENT This is an important paper. 0 saido
COMMENT What about plasmin and plasminogen activators? 0 saido
COMMENT Comment by Sascha Weggen, Thorsten Jumpertz, Andreas Rennhack, Bruno Bulic Despite substantial progress in the chemical and preclinical development of γ-secretase modulators (GSMs), the molecular mechanism and target of GSMs have remained controversial. T
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 inter
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