Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Annemarie Scherbarth"'
Autor:
Martin K Schwarz, Annemarie Scherbarth, Rolf Sprengel, Johann Engelhardt, Patrick Theer, Guenter Giese
Publikováno v:
PLoS ONE, Vol 10, Iss 5, p e0124650 (2015)
In order to observe and quantify long-range neuronal connections in intact mouse brain by light microscopy, it is first necessary to clear the brain, thus suppressing refractive-index variations. Here we describe a method that clears the brain and pr
Externí odkaz:
https://doaj.org/article/02b22ab34ad042fea247e183048e19fb
Okadaic acid co-induces vimentin expression and cell cycle arrest in MPC-11 mouse plasmacytoma cells
Publikováno v:
Journal of Cellular Physiology
The effect of the tumor promoter okadaic acid on cell cycle progression and on vimentin expression in MPC-11 mouse plasmacytoma cells was compared with that of the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA). Cell cycle progression of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1125ee2c3e1f68f85cc9729f59be704
https://hdl.handle.net/11858/00-001M-0000-0019-A9A2-711858/00-001M-0000-002D-2468-0
https://hdl.handle.net/11858/00-001M-0000-0019-A9A2-711858/00-001M-0000-002D-2468-0
Publikováno v:
Journal of Biomolecular Structure and Dynamics
Guanine-rich polynucleotides such as poly(dG), oligo(dG)12-18 or poly(rG) were shown to exert a strong inhibitory effect on vimentin filament assembly and also to cause disintegration of preformed filaments in vitro. Gold-labeled oligo(dG)25 was pref
Publikováno v:
Journal of Molecular Biology (London)
In order to demonstrate that the nucleic acid-binding activities of vimentin are dictated by its Arg-rich N-terminal head domain, this was cut off at position Lys96 with lysine-specific endoproteinase and analysed for its capacity to associate with a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4389c5b261759744d32850e906948fab
https://hdl.handle.net/21.11116/0000-0000-5F30-021.11116/0000-0000-5F2E-4
https://hdl.handle.net/21.11116/0000-0000-5F30-021.11116/0000-0000-5F2E-4
Publikováno v:
Journal of Cell Science
Previous studies have shown that the non-alpha-helical, amino-terminal head region of vimentin is essential for the formation and stability of vimentin intermediate filaments (IFs). In order to specify its target site on companion protein subunits, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f72a302acc3bd1fb634bb7e2ad4b0857
https://hdl.handle.net/21.11116/0000-0000-6069-E21.11116/0000-0000-6067-0
https://hdl.handle.net/21.11116/0000-0000-6069-E21.11116/0000-0000-6067-0
Publikováno v:
Journal of Cell Science
Using immunofluorescence and immunoblotting techniques, we have examined the composition of the nuclear lamina in murine plasmacytoma cells, MPC-11, exposed to the phorbol ester TPA as well as in two cell lines devoid of cytoplasmic intermediate fila
Publikováno v:
FEBS Letters. 193:217-221
Vimentin enriched in cytoskeletal frameworks by Triton X-100 extraction of Ehrlich ascites tumor cells and purified from a low ionic strength extract of the cell residues by (NH4)2SO4 precipitation and DEAE-Sepharose and ssDNA-cellulose chromatograph
Publikováno v:
Journal of Biological Chemistry. 261:10558-10568
The interaction of nonepithelial intermediate filament (IF) proteins with vesicles produced from total Ehrlich ascites tumor cell lipids results in the formation of complexes which in sucrose density gradient centrifugation attain positions distinctl
Publikováno v:
The Journal of Biological Chemistry
The ability of the intermediate filament subunit protein vimentin to bind synthetic oligonucleotide telomere models containing repeat sequences from Oxytricha (T4G4), Saccharomyces (TGTGTG3), or Tetrahymena (T2G4) was investigated in vitro with a fil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65aebb0cae17dfcf4096b5434d7e7fc4
http://www.jbc.org/content/263/35/18744.abstract?maxtoshow%3D%26HITS%3D10%26hits%3D10%26RESULTFORMAT%3D%26fulltext%3Din%2Bvitro%2Bof%26searchid%3D1113896081545_593%26stored_search%3D%26FIRSTINDEX%3D0%26volume%3D263%26issue%3D35%26journalcode%3Djbc
http://www.jbc.org/content/263/35/18744.abstract?maxtoshow%3D%26HITS%3D10%26hits%3D10%26RESULTFORMAT%3D%26fulltext%3Din%2Bvitro%2Bof%26searchid%3D1113896081545_593%26stored_search%3D%26FIRSTINDEX%3D0%26volume%3D263%26issue%3D35%26journalcode%3Djbc
Publikováno v:
Zeitschrift fur Naturforschung. C, Journal of biosciences. 42(1-2)
Non-epithelial intermediate filament (IF) subunit proteins show a high and specific affinity for core histones at physiological ionic strength. When IF proteins are titrated with a mixture of core histones and linker histone H1, in general the latter