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606 results on '"Aebi, U"'

1. Nuclear Pore Complex Architecture and Functional Dynamics

Author

Fahrenkrog, B., Stoffler, D., Aebi, U., Compans, R. W., editor, Cooper, M., editor, Ito, Y., editor, Koprowski, H., editor, Melchers, F., editor, Oldstone, M., editor, Olsnes, S., editor, Potter, M., editor, Vogt, P. K., editor, Wagner, H., editor, Hauber, Joachim, editor, and Vogt, Peter K., editor

Published
2001
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15. Freie mitteilungen

Author

Krähenmann, F., Weidmann, B., Brühwiler, H., Weidmann, B., Krähenmann, F., Brühwiler, H., Bacheland, O., Santos-Eggiman, B., Paccaud, F., Berger-Menz, E., Hänggi, W., Junod, M., Schneider, H., Fink, St., Hänggi, W., Aebi, U., Lachat, R., Schneider, H., Schlatter-Messerli, P., Dürig, P., Rüdeberg, A., Khan, G., Zimmermann, R., Huch, R., Huch, A., Fink, D., Schär, G., Perucchini, D., Helfenstein, U., Haller, U., Jörimann, H., Stoll, W., Peschers, U., Zen-Ruffinen, F., Hess, Th., Schär, G., Schüssler, B., Keller, M., Florek, P., Perucchini, D., Schär, G., Fink, D., and Haller, U.

Published
1995
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17. A giant nucleopore protein that binds Ran/TC4

Author

Yokoyama, N., Hayashi, N., Seki, T., Pante, N., Ohba, T., Nishii, K., Kuma, K., Hayashida, T., Miyata, T., Aebi, U., Fukui, M., and Nishimoto, T.

Subjects
Proteins -- Analysis, Carrier proteins -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

The protein RanBP2, which binds to the nuclear G protein Ran/TC4, contains 3,224 residues and is comprised of a leucine-rich amino-terminal region, four domains homologous to RanBP1, eight zinc-finger motifs and a carboxy terminus similar to cyclophilin. Studies show that RanBP2 is a part of the nuclear pore complex and is probably present on both sides of the pore. Ran/TC4 is necessary for the import of proteins containing NLS.

Published
1995

18. STEM Analysis of Caenorhabditis elegans muscle thick filaments: evidence for microdifferentiated substructures

Author

Muller, S. A, Haner, M, Ortiz, I, Aebi, U, and Epstein, H. F

Subjects
Life Sciences (General)
Abstract

In the thick filaments of body muscle in Caenorhabditis elegans, myosin A and myosin B isoforms and a subpopulation of paramyosin, a homologue of myosin heavy chain rods, are organized about a tubular core. As determined by scanning transmission electron microscopy, the thick filaments show a continuous decrease in mass-per-length (MPL) from their central zones to their polar regions. This is consistent with previously reported morphological studies and suggests that both their content and structural organization are microdifferentiated as a function of position. The cores are composed of a second distinct subpopulation of paramyosin in association with the alpha, beta, and gamma-filagenins. MPL measurements suggest that cores are formed from seven subfilaments containing four strands of paramyosin molecules, rather than the two originally proposed. The periodic locations of the filagenins within different regions and the presence of a central zone where myosin A is located, implies that the cores are also microdifferentiated with respect to molecular content and structure. This differentiation may result from a novel "induced strain" assembly mechanism based upon the interaction of the filagenins, paramyosin and myosin A. The cores may then serve as "differentiated templates" for the assembly of myosin B and paramyosin in the tapering, microdifferentiated polar regions of the thick filaments.

Published
2001
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29. Neue Bücher

Author

Zurhrügg, Chr, Aebi, U., Bleuler, Manfred, Ammann, A., Grischott, G., OMS, Wieltschnig, E., and Gutzwiller, F.

Published
1978
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31. EMBO WORKSHOP REPORT An eclipse over the cell nucleus Functional organization of the cell nucleus Prague, August 9–12, 1999

Author

Raška, I., Aebi, U., and Earnshaw, W.C.

Subjects
Articles
Abstract

The EMBO workshop ‘Functional Organization of the Cell Nucleus’ held in Prague at the Hotel of the Postgraduate School of Medicine was attended by 110 participants (49 invited speakers and 61 selected participants) from 22 countries. Such a full range of topics devoted to the cell biology of the nucleus has not been discussed previously in such an intimate meeting in Europe. The workshop not only offered an opportunity for junior scientists to benefit from having an international meeting within Europe and a chance to discuss their work with internationally recognized experts, but it also offered a unique opportunity for interactions among the more established investigators. The fruits of a number of presentations are gathered together in a Special Issue of the Journal of Structural Biology which appeared in spring 2000. Last but not least, it is worth mentioning that while stepping through a packed scientific program, the participants did find the time to observe the solar eclipse just before the lunch break of August 11.

Published
2000

32. Domain analysis of cortexillin I: actin bundling, PIP2-binding and the rescue of cytokinesis

Author

Stock, A., Steinmetz, M.O., Janmey, P.A., Aebi, U., Gerisch, G., Kammerer, R.A., Weber, Igor, and Faix, J.

Subjects
macromolecular substances
Abstract

Cortexillins are actin-bundling proteins that form a parallel two-stranded coiled-coil rod. Actin-binding domains of the alpha-actinin/spectrin type are located N-terminal to the rod and unique sequence elements are found in the C-terminal region. Domain analysis ill vitro revealed that the N-terminal domains are not responsible for the strong actin-filament bundling activity of cortexillin I. The strongest activity resides in the C-terminal region. Phosphatidylinositol 4, 5-bisphosphate (PIP2) suppresses this bundling activity by binding to a C-terminal nonapeptide sequence. These data define a new PIP2-regulated actin-bundling site. In vivo the PIP2-binding motif enhances localization of a C-terminal cortexillin I fragment to the cell cortex and improves the rescue of cytokinesis. This motif is not required, however, for translocation to the cleavage furrow. A model is presented proposing that cortexillin translocation is based on a mitotic cycle of polar actin polymerization and midzone depolymerization.

Published
1999

34. The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis

Author

von Bergen, Martin, Barghorn, S., Müller, S.A., Pickhardt, M., Biernat, J., Mandelkow, E.-M., Davies, P., Aebi, U., Mandelkow, E., von Bergen, Martin, Barghorn, S., Müller, S.A., Pickhardt, M., Biernat, J., Mandelkow, E.-M., Davies, P., Aebi, U., and Mandelkow, E.

Abstract

In Alzheimer's disease and frontotemporal dementias the microtubule-associated protein tau forms intracellular paired helical filaments (PHFs). The filaments formed in vivo consist mainly of full-length molecules of the six different isoforms present in adult brain. The substructure of the PHF core is still elusive. Here we applied scanning transmission electron microscopy (STEM) and limited proteolysis to probe the mass distribution of PHFs and their surface exposure. Tau filaments assembled from the three repeat domain have a mass per length (MPL) of ~60 kDa/nm and filaments from full-length tau (htau40K280 mutant) have ~160 kDa/nm, compared with ~130 kDa/nm for PHFs from Alzheimer's brain. Polyanionic cofactors such as heparin accelerate assembly but are not incorporated into PHFs. Limited proteolysis combined with N-terminal sequencing and mass spectrometry of fragments reveals a protease-sensitive N-terminal half and semiresistant PHF core starting in the first repeat and reaching to the C-terminus of tau. Continued proteolysis leads to a fragment starting at the end of the first repeat and ending in the fourth repeat. PHFs from tau isoforms with four repeats revealed an additional cleavage site within the middle of the second repeat. Probing the PHFs with antibodies detecting epitopes either over longer stretches in the C-terminal half of tau or in the fourth repeat revealed that they grow in a polar manner. These data describe the physical parameters of the PHFs and enabled us to build a model of the molecular arrangement within the filamentous structures.

Published
2006

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