Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Ludovic R. Otterbein"'
Autor:
Roberto Dominguez, Renne C. Lu, Guanming Wu, Lakshmi A. Palecanda, Mohammed Terrak, Ludovic R. Otterbein
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:1882-1885
Mlc1p is a calmodulin-like protein from the budding yeast Saccharomyces cerevisiae, where it has been identified as a subunit of a class V myosin, Myo2p, and a binding partner of an IQGAP-like protein, Iqg1p. Through its interactions with these two p
Autor:
Carlos Witte-Hoffmann, C.-L. Albert Wang, Ludovic R. Otterbein, Jolanta Kordowska, Roberto Dominguez
Publikováno v:
Structure. 10:557-567
S100A6 is a member of the S100 family of Ca 2+ binding proteins, which have come to play an important role in the diagnosis of cancer due to their overexpression in various tumor cells. We have determined the crystal structures of human S100A6 in the
Actin is the most abundant protein in eukaryotic cells, but its release from cells into blood vessels can be lethal, being associated with clinical situations including hepatic necrosis and septic shock. A homeostatic mechanism, termed the actin-scav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::820249c8caec9c27bb6c6b1941b016ad
https://europepmc.org/articles/PMC123010/
https://europepmc.org/articles/PMC123010/
Autor:
Ludovic R, Otterbein, Jolanta, Kordowska, Carlos, Witte-Hoffmann, C-L Albert, Wang, Roberto, Dominguez
Publikováno v:
Structure (London, England : 1993). 10(4)
S100A6 is a member of the S100 family of Ca(2+) binding proteins, which have come to play an important role in the diagnosis of cancer due to their overexpression in various tumor cells. We have determined the crystal structures of human S100A6 in th
Publikováno v:
Science (New York, N.Y.). 293(5530)
The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine 5′-triphosphate (ATP) by a mechanism that remains to be elucidated. Actin modified to block polymerization was crystallize