On the structure of microtubules, tau, and paired helical filaments

E. Mandelkow; Y. H. Song; O. Schweers; A. Marx; E. M. Mandelkow

doi:10.1016/0197-4580(95)00026-B

On the structure of microtubules, tau, and paired helical filaments

E. Mandelkow, Y. H. Song, O. Schweers, A. Marx, E. M. Mandelkow^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Physik

Max Planck Advanced Study Group

52 Zitate (Scopus)

Abstract

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.

Originalsprache	Englisch
Zeitschrift	Neurobiology of Aging
Jahrgang	16
Ausgabenummer	3
Seiten (von - bis)	347-354
Seitenumfang	8
ISSN	0197-4580
DOIs	https://doi.org/10.1016/0197-4580(95)00026-B
Publikationsstatus	Veröffentlicht - 1995

Fördermittel

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).

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10.1016/0197-4580(95)00026-B

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title = "On the structure of microtubules, tau, and paired helical filaments",

abstract = "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.",

author = "E. Mandelkow and Song, \{Y. H.\} and O. Schweers and A. Marx and Mandelkow, \{E. M.\}",

note = "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.",

year = "1995",

doi = "10.1016/0197-4580(95)00026-B",

language = "English",

volume = "16",

pages = "347--354",

journal = "Neurobiology of Aging",

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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 - https://www.scopus.com/pages/publications/0028998411

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 -

On the structure of microtubules, tau, and paired helical filaments

Abstract

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