Zobrazeno 1 - 10
of 15
pro vyhledávání: '"T. E. Kreis"'
Publikováno v:
International review of cytology. 195
This review focuses on the roles of coat proteins in regulating the membrane traffic of eukaryotic cells. Coat proteins are recruited to the donor organelle membrane from a cytosolic pool by specific small GTP-binding proteins and are required for th
Autor:
J, Scheel, T E, Kreis
Publikováno v:
Methods in enzymology. 298
Publikováno v:
Methods in enzymology. 298
Publikováno v:
European journal of cell biology. 71(1)
Our goal was to engineer a Golgi glycosyltransferase epitope-tagged on its cytoplasmically exposed, short, N-terminal domain that gave normal subcellular localization. Partial replacement of the cytoplasmic tail of human alpha-2,6-sialyltransferase (
Autor:
D. Hennig, Robert G. Parton, Rainer Pepperkok, J. E. Rickard, P. I. Karecla, J. Scheel, B. Joggerst-Thomalla, T. E. Kreis, A. Sawyer, Philippe Pierre
Publikováno v:
Molecular Mechanisms of Membrane Traffic ISBN: 9783662029305
Microtubules play a key role in the dynamic spatial organization of the cytoplasmic matrix. They are involved in regulating the structure and positioning of intracellular organelles like the Golgi apparatus and endosomes, and they provide the tracks
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b97dc4a1ced1027429f0b76546cba43
https://doi.org/10.1007/978-3-662-02928-2_29
https://doi.org/10.1007/978-3-662-02928-2_29
Autor:
B. Joggerst-Thomalla, H. Horstmann, B. Storrie, J. Scheel, R. Duden, G. Griffiths, T. E. Kreis, R. Pepperkok, A. Sawyer
Publikováno v:
Molecular Mechanisms of Membrane Traffic ISBN: 9783662029305
The Golgi complex is a polarized cytoplasmic organelle that is generally considered to be built up of at least three functionally distinct, membrane bounded subcompartments, the cis-Golgi network (CGN), the stacked Golgi cisternae and the trans-Golgi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59c0d2ecd196f49a38353514fbadc07f
https://doi.org/10.1007/978-3-662-02928-2_26
https://doi.org/10.1007/978-3-662-02928-2_26
Autor:
P I, Karecla, T E, Kreis
Publikováno v:
European journal of cell biology. 57(2)
We have developed an in vitro assay for characterizing the binding of elements of the Golgi complex to microtubules. The binding assay comprises three distinct components, Golgi elements purified from Vero cells by subcellular fractionation, taxol-po
Publikováno v:
The Journal of biological chemistry. 266(31)
Previous studies have shown that nuclear lamin B binds specifically to the C-terminal domains of type III intermediate filament (IF) proteins under in vitro conditions. To further explore such site-specific interactions, we have used a two-step anti-
Autor:
J, Scheel, T E, Kreis
Publikováno v:
The Journal of biological chemistry. 266(27)
We have established an in vitro assay to characterize the binding of endocytic carrier vesicles to microtubules. Magnetic beads coated with microtubules were used as an affinity matrix. A fraction from nocodazole-treated cells enriched in endocytic c
Autor:
J E, Rickard, T E, Kreis
Publikováno v:
The Journal of biological chemistry. 266(26)
We have used a monoclonal antibody affinity column to purify from HeLa cells a protein of molecular weight 170,000 (designated pp170) which we previously identified as a nucleotide-sensitive microtubule-binding protein (Rickard, J. E., and Kreis, T.