Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Klavs B. Hendil"'
Autor:
Rasmus Hartmann-Petersen, Yasushi Saeki, Michael Seeger, Keiji Tanaka, Anne-Marie B. Lauridsen, Klavs B. Hendil, Franziska Kriegenburg
Publikováno v:
Cell. 135:355-365
SummaryIt has been suggested that degradation of polyubiquitylated proteins is coupled to dissociation of 26S proteasomes. In contrast, using several independent types of experiments, we find that mammalian proteasomes can degrade polyubiquitylated p
Autor:
Shigeo Murata, Toshihiko Kishimoto, Klavs B. Hendil, Shun-ichiro Iemura, Shin-ichiro Niwa, Masanori Kasahara, Hidemi Hayashi, Keiji Tanaka, Tohru Natsume, Yuko Hirano
Publikováno v:
Molecular Cell. 24:977-984
The 20S proteasome is a catalytic core of the 26S proteasome, a central enzyme in the degradation of ubiquitin-conjugated proteins. It is composed of 14 distinct gene products that form four stacked rings of seven subunits each, alpha(1-7)beta(1-7)be
Autor:
Wei Ping Gai, Peter Højrup, Rasmus Beedholm, Poul Henning Jensen, Torben Moos, Klavs B. Hendil, Evo Lindersson
Publikováno v:
Lindersson, E, Beedholm, R, Højrup, P, Moos, T, Gai, W P, Hendil, K B & Jensen, P H 2004, ' Proteasomal inhibition by a-synuclein filaments and oligomers. ', Journal of Biological Chemistry, vol. 279, pp. 12924-12934 . https://doi.org/10.1074/jbc.M306390200
Lindersson, E, Beedholm, R, Højrup, P, Moos, T, Gai, W, Hendil, K B & Jensen, P H 2004, ' Proteasomal inhibition by alpha-synuclein filaments and oligomers ', Journal of Biological Chemistry, vol. 279, no. 13, pp. 12924-34 . https://doi.org/10.1074/jbc.M306390200
Lindersson, E, Beedholm, R, Højrup, P, Moos, T, Gai, W, Hendil, K B & Jensen, P H 2004, ' Proteasomal inhibition by alpha-synuclein filaments and oligomers ', Journal of Biological Chemistry, vol. 279, no. 13, pp. 12924-34 . https://doi.org/10.1074/jbc.M306390200
Udgivelsesdato: 2004-Mar-26 A unifying feature of many neurodegenerative disorders is the accumulation of polyubiquitinated protein inclusions in dystrophic neurons, e.g. containing alpha-synuclein, which is suggestive of an insufficient proteasomal
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 35:629-636
The ubiquitin-proteasome pathway for intracellular proteolysis is involved in a series of cellular and molecular functions, including the degradation of bulk proteins, cell cycle control, DNA repair, antigen presentation, vesicle transport and the re
Autor:
Ahmed Ouali, Lothar Kuehn, Didier Levieux, Klavs B. Hendil, D. Dutaud, Laurent Aubry, Laurent Henry, Jean Paul Bureau
Publikováno v:
Journal of Immunological Methods. 260:183-193
Because quantification of the 20S proteasome by functional activity measurements is difficult and inaccurate, we have developed an indirect sandwich enzyme-linked immunosorbent assays (ELISA) for quantification of the 20S proteasome in human plasma.
Publikováno v:
Journal of Molecular Biology. 315:627-636
Most proteins in eukaryotic cells are degraded by 26-S proteasomes, usually after being conjugated to ubiquitin. In the absence of ATP, 26-S proteasomes fall apart into their two sub-complexes, 20-S proteasomes and PA700, which reassemble upon additi
Publikováno v:
Biochemical Journal. 352:611-615
Proteasomes are complex multisubunit proteases which play a critical role in intracellular proteolysis. Immunoproteasomes, which contain three γ-interferon-inducible subunits, are a subset of proteasomes which have a specialized function in antigen
Autor:
Keiji Tanaka, Yasuko Murakami, Naoki Shimbara, Nobuyuki Tanahashi, Yasufumi Minami, Klavs B. Hendil
Publikováno v:
Journal of Biological Chemistry. 275:14336-14345
Eukaryotic cells contain various types of proteasomes. Core 20 S proteasomes (abbreviated 20 S below) have two binding sites for the regulatory particles, PA700 and PA28. PA700–20 S-PA700 complexes are known as 26 S proteasomes and are ATP-dependen
Autor:
Mariangela Conconi, Bertrand Friguet, Wolfgang Uerkvitz, Klavs B. Hendil, Lisa Djavadi-Ohaniance
Publikováno v:
Archives of Biochemistry and Biophysics. 362:325-328
Proteasomes interact with a variety of macromolecular ligands that modulate their ability to degrade peptide and protein substrates. The effector PA28 increases the peptidase activities of proteasomes whereas HSP90 and alpha-crystallin inhibit a pept
Autor:
Line Jørgensen, Klavs B. Hendil
Publikováno v:
Molecular Biology Reports. 26:119-123
20 S Proteasomes are large proteinase complexes found in eukaryotic cells where they degrade cell proteins in an ATP-dependent manner. Proteasomes consist of 14 different subunits. One of them, zeta, was found in HeLa cells at a concentration of 890