Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Vincent Guénebaut"'
Publikováno v:
Nature Cell Biology. 2:365-370
The γ-tubulin ring complex (γTuRC) is a protein complex of relative molecular mass ~2.2 × 106 that nucleates microtubules at the centrosome. Here we use electron-microscopic tomography and metal shadowing to examine the structure of isolated Droso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a23c38b556263fad7420855a37af035
https://doi.org/10.1038/35014058
https://doi.org/10.1038/35014058
Autor:
Hanns Weiss, Ulrich Schulte, Dierk Scheide, Kevin Leonard, Tim Rasmussen, Thorsten Friedrich, Angela Schlitt, Anke Abelmann, Vincent Guénebaut, Lars Kintscher, Benedikt Brors
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1365(1-2):215-219
The proton-pumping NADH:ubiquinone oxidoreductase is the first complex in the respiratory chains of many purple bacteria and of mitochondria of most eucaryotes. The bacterial complex consists of 14 different subunits. The mitochondrial complex contai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::151cfdf607f00912fdbd66d6339e052f
Publikováno v:
Journal of Molecular Biology. 276:105-112
Respiratory chains of bacteria and mitochondria contain closely related forms of the proton-pumping NADH:ubiquinone oxidoreductase (complex I). In bacteria the complex has a molecular mass of approximately 530 kDa and consists of 14 different subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e1ec9e7ad9b4f526c63ad28eec97711
https://doi.org/10.1006/jmbi.1997.1518
https://doi.org/10.1006/jmbi.1997.1518
Publikováno v:
Journal of Molecular Biology. 265:409-418
NADH-dehydrogenase (Complex I) is the first complex of the mitochondrial respiratory chain. It is an amphipatic molecule located in the inner mitochondrial membrane and is composed of at least 35 unique subunits encoded by both mitochondrial and nucl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb869e0aa35d09507557c1923af01430
https://doi.org/10.1006/jmbi.1996.0753
https://doi.org/10.1006/jmbi.1996.0753
Autor:
Vincent Guénebaut, David A. Agard, Frederick Cohen, Stanley B. Prusiner, Ana Serban, Holger Wille, Surachai Supattapone, Melissa D. Michelitsch
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 99(6)
Because the insolubility of the scrapie prion protein (PrP Sc ) has frustrated structural studies by x-ray crystallography or NMR spectroscopy, we used electron crystallography to characterize the structure of two infectious variants of the prion pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5167c5de66053b820da803e586e851a
https://pubmed.ncbi.nlm.nih.gov/11891310
https://pubmed.ncbi.nlm.nih.gov/11891310