Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Adelajda Zorba"'
Autor:
Warintra Pitsawong, Vanessa Buosi, Renee Otten, Roman V Agafonov, Adelajda Zorba, Nadja Kern, Steffen Kutter, Gunther Kern, Ricardo AP Pádua, Xavier Meniche, Dorothee Kern
Publikováno v:
eLife, Vol 7 (2018)
Protein kinases are major drug targets, but the development of highly-selective inhibitors has been challenging due to the similarity of their active sites. The observation of distinct structural states of the fully-conserved Asp-Phe-Gly (DFG) loop h
Externí odkaz:
https://doaj.org/article/539402f8e5bf4f61a9b4fed6f3529b41
Autor:
Adelajda Zorba, Vanessa Buosi, Steffen Kutter, Nadja Kern, Francesco Pontiggia, Young-Jin Cho, Dorothee Kern
Publikováno v:
eLife, Vol 3 (2014)
We elucidate the molecular mechanisms of two distinct activation strategies (autophosphorylation and TPX2-mediated activation) in human Aurora A kinase. Classic allosteric activation is in play where either activation loop phosphorylation or TPX2 bin
Externí odkaz:
https://doaj.org/article/778cc46f09144da3a8447e979851d695
Autor:
Adelajda Zorba, Shohei Koide, Marc Hoemberger, Akiko Koide, Chansik Kim, Vy Nguyen, Dorothee Kern, Yuejiao Zheng, Steffen Kutter
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 116(28)
Despite being the subject of intense effort and scrutiny, kinases have proven to be consistently challenging targets in inhibitor drug design. A key obstacle has been promiscuity and consequent adverse effects of drugs targeting the ATP binding site.
Autor:
Suman Luthra, Graham M. West, Jeremy T. Starr, Matthew Frank Brown, Matthew F. Calabrese, Jinshan Chen, Hongyao Zhu, Xiayang Qiu, Daniel P. Uccello, Matthew Merrill Hayward, Jeanne S. Chang, Jotham Wadsworth Coe, Kathleen A. Farley, Kris A. Borzilleri, Mark C. Noe, Justin I. Montgomery, Adam M. Gilbert, Veerabahu Shanmugasundaram, Lara C. Czabaniuk, Robert M. Oliver, Carmen N. Garcia-Irrizary, Brandon P. Schuff, Chuong Nguyen, Yingrong Xu, James Schiemer, Jaymin C. Shah, Xidong Feng, Mark Niosi, Jennifer A. Young, WeiDong Ding, Ayman El-Kattan, Adelajda Zorba, James F. Smith
Proteolysis targeting chimeras (PROTACs) are heterobifunctional small molecules that simultaneously bind to a target protein and an E3 ligase, thereby leading to ubiquitination and subsequent degradation of the target. They present an exciting opport
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf434de63be490efb6416cf59a222839
https://europepmc.org/articles/PMC6077745/
https://europepmc.org/articles/PMC6077745/
Autor:
Roman V. Agafonov, Xavier Meniche, Adelajda Zorba, Nadja Kern, Warintra Pitsawong, Ricardo Ap Pádua, Renee Otten, Gunther Kern, Vanessa Buosi, Dorothee Kern, Steffen Kutter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ecf9e22cd46a2f3e0233b3870aee7cf8
https://doi.org/10.7554/elife.36656.040
https://doi.org/10.7554/elife.36656.040
Autor:
Roman V. Agafonov, Dorothee Kern, Xavier Meniche, Vanessa Buosi, Steffen Kutter, Gunther Kern, Warintra Pitsawong, Renee Otten, Adelajda Zorba, Nadja Kern, Ricardo Ap Pádua
Publikováno v:
eLife
eLife, Vol 7 (2018)
eLife, Vol 7 (2018)
Protein kinases are major drug targets, but the development of highly-selective inhibitors has been challenging due to the similarity of their active sites. The observation of distinct structural states of the fully-conserved Asp-Phe-Gly (DFG) loop h
Autor:
Warintra Pitsawong, Vanessa Buosi, Renee Otten, Roman V. Agafonov, Adelajda Zorba, Nadja Kern, Steffen Kutter, Gunther Kern, Ricardo A. P. Pádua, Xavier Meniche, Dorothee Kern
Protein kinases are major drug targets, but the development of highly-selective inhibitors has been challenging due to the similarity of their active sites. The observation of distinct structural states of the fully-conserved Asp-Phe-Gly (DFG) loop h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7b0872372260ae60e8eea19c9a44fc4
Autor:
Douglas L. Theobald, Dorothee Kern, D. Waterman, Christine D. Wilson, Jackson C. Halpin, Vanessa Buosi, Steffen Kutter, Marc Hoemberger, Roman V. Agafonov, Renee Otten, Adelajda Zorba
Publikováno v:
Science. 347:882-886
Macromolecular function is rooted in energy landscapes, where sequence determines not a single structure but an ensemble of conformations. Hence, evolution modifies a protein’s function by altering its energy landscape. Here, we recreate the evolut
Autor:
Young-Jin Cho, Vanessa Buosi, Francesco Pontiggia, Dorothee Kern, Adelajda Zorba, Nadja Kern, Steffen Kutter
Publikováno v:
eLife
eLife, Vol 3 (2014)
eLife, Vol 3 (2014)
We elucidate the molecular mechanisms of two distinct activation strategies (autophosphorylation and TPX2-mediated activation) in human Aurora A kinase. Classic allosteric activation is in play where either activation loop phosphorylation or TPX2 bin