TY - JOUR
T1 - On the structure of microtubules, tau, and paired helical filaments
AU - Mandelkow, E.
AU - Song, Y. H.
AU - Schweers, O.
AU - Marx, A.
AU - Mandelkow, E. M.
N1 - Funding Information:
We thank K. Kosik (Harvard Medical School) for the clone of kinesin, and M. Goedert (MRC Cambridge) for the clones of tau. Brain tissue was generously provided by the Bryan Alzheimer Disease Research Center (Duke University Medical Center, Durham, NC), the Brain Tissue Resource Center (McLean Hospital/Harvard Medical School, Belmont, MA), and the Alzheimer Research Center (University of Rochester Medical School, Rochester, NY). This work was supported by Bundes-ministerium fiir Forschung und Technologie (BMFT) and the Deutsche Forschungsgemeinschaft (DFG).
Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.
PY - 1995
Y1 - 1995
N2 - Microtubules and their associated proteins form the basis of axonal transport; they are degraded during the neuronal degeneration in Alzheimer's disease. This article surveys recent results on the structure of microtubules, tau protein, and PHFs. Microtubules have been investigated by electron microscopy and image processing after labeling them with the head domain of the motor protein kinesin. This reveals the arrangement of tubulin subunits in microtubules and the shape of the tubulin-motor complex. Tau protein was studied by electron microscopy, solution X-ray scattering, and spectroscopic methods. It appears as an elongated molecule (about 35 nm) without recognizable secondary structure. Alzheimer PHFs were examined by FTIR and X-ray diffraction; they, too, show evidence for secondary structure such as β sheets.
AB - Microtubules and their associated proteins form the basis of axonal transport; they are degraded during the neuronal degeneration in Alzheimer's disease. This article surveys recent results on the structure of microtubules, tau protein, and PHFs. Microtubules have been investigated by electron microscopy and image processing after labeling them with the head domain of the motor protein kinesin. This reveals the arrangement of tubulin subunits in microtubules and the shape of the tubulin-motor complex. Tau protein was studied by electron microscopy, solution X-ray scattering, and spectroscopic methods. It appears as an elongated molecule (about 35 nm) without recognizable secondary structure. Alzheimer PHFs were examined by FTIR and X-ray diffraction; they, too, show evidence for secondary structure such as β sheets.
UR - http://www.scopus.com/inward/record.url?scp=0028998411&partnerID=8YFLogxK
U2 - 10.1016/0197-4580(95)00026-B
DO - 10.1016/0197-4580(95)00026-B
M3 - Journal articles
C2 - 7566344
AN - SCOPUS:0028998411
SN - 0197-4580
VL - 16
SP - 347
EP - 354
JO - Neurobiology of Aging
JF - Neurobiology of Aging
IS - 3
ER -