Zobrazeno 1 - 2
of 2
pro vyhledávání: '"drug effects [Biocatalysis]"'
Autor:
Laura J. Blair, Piotr Wysoczanski, Chung-Tien Lee, Romina V. Hofele, Pijush Chakraborty, Chad A. Dickey, Markus Zweckstetter, Henning Urlaub, Ángel Pérez-Lara, Jacek Biernat, Jeremy D. Baker, Bliss J. Chang, Javier Oroz, Eckhard Mandelkow
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nature Communications
Nature Communications 9(1), 4532 (2018). doi:10.1038/s41467-018-06880-0
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Communications
Nature Communications 9(1), 4532 (2018). doi:10.1038/s41467-018-06880-0
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
13 pags, 6 figs
The molecular chaperone Hsp90 is critical for the maintenance of cellular homeostasis and represents a promising drug target. Despite increasing knowledge on the structure of Hsp90, the molecular basis of substrate recognition an
The molecular chaperone Hsp90 is critical for the maintenance of cellular homeostasis and represents a promising drug target. Despite increasing knowledge on the structure of Hsp90, the molecular basis of substrate recognition an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c144d3a1bf30d26c48ef53e76c19a76
http://link.springer.com/article/10.1038/s41467-018-06880-0
http://link.springer.com/article/10.1038/s41467-018-06880-0
Autor:
Stefan F. Lichtenthaler, Qing-Xiang Amy Sang, Taheera Ferdous, Robert M. Petrovich, Bart De Strooper, Marcia L. Moss, Ina Tesseur, Gary Powell, Colin Dingwall, Jörg W. Bartsch, Bin Qi, Douglas A. Lauffenburger, Julia Li Zhong, Uwe Schlomann, Linda G. Griffith, Miles A. Miller, Mara Taverna, Lori L. Edwards, Pei Zhou
Publikováno v:
American Society for Biochemistry and Molecular Biology
The journal of biological chemistry 286(47), 40443-40451 (2011). doi:10.1074/jbc.M111.280495
The journal of biological chemistry 286(47), 40443-40451 (2011). doi:10.1074/jbc.M111.280495
Prodomains of A disintegrin and metalloproteinase (ADAM) metallopeptidases can act as highly specific intra- and intermolecular inhibitors of ADAM catalytic activity. The mouse ADAM9 prodomain (proA9; amino acids 24–204), expressed and characterize
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33f46250ec6dfd62cdd977af30f72776
http://hdl.handle.net/1721.1/76196
http://hdl.handle.net/1721.1/76196
