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Iva Navratilova
Researcher at University of Dundee
Publications - 31
Citations - 1373
Iva Navratilova is an academic researcher from University of Dundee. The author has contributed to research in topics: Drug discovery & Surface plasmon resonance. The author has an hindex of 17, co-authored 29 publications receiving 1193 citations. Previous affiliations of Iva Navratilova include Schrödinger & Pfizer.
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Journal ArticleDOI
Mechanism of ubiquitylation by dimeric RING ligase RNF4
Anna Plechanovová,Ellis Jaffray,Stephen A. McMahon,Kenneth A. Johnson,Iva Navratilova,James H. Naismith,Ronald T. Hay +6 more
TL;DR: D dimeric RING ligases facilitate ubiquitin transfer by preferentially binding the E2~ubiquitin thioester across the dimer and activating the thioesters bond for catalysis.
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ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressor.
Elton Zeqiraj,Beatrice M. Filippi,Simon Goldie,Iva Navratilova,Jérôme Boudeau,Maria Deak,Dario R. Alessi,Daan M. F. van Aalten +7 more
TL;DR: The conformation of the pseudokinase STRADα, which is regulated by binding to ATP and to the scaffolding protein MO25α, is key to the activiation of the LKB1 tumor suppressor complex.
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Fragment screening by surface plasmon resonance.
TL;DR: In this paper, a method for biosensor-based fragment screening using surface plasmon resonance (SPR) was proposed to eliminate all nonspecific (false positive) binders.
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MO25 is a master regulator of SPAK/OSR1 and MST3/MST4/YSK1 protein kinases
Beatrice M. Filippi,Paola de los Heros,Youcef Mehellou,Iva Navratilova,Robert Gourlay,Maria Deak,Lorna Plater,Rachel Toth,Elton Zeqiraj,Dario R. Alessi +9 more
TL;DR: Mouse protein‐25 (MO25) isoforms bind to the STRAD pseudokinase and stabilise it in a conformation that can activate the LKB1 tumour suppressor kinase, demonstrating that by binding to several STE20 family kinases, MO25 has roles beyond controlling L KB1.
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O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
Marianne Schimpl,Xiaowei Zheng,Vladimir S. Borodkin,D.E. Blair,Andrew T. Ferenbach,Alexander W. Schüttelkopf,Iva Navratilova,Tonia Aristotelous,Osama Albarbarawi,David A. Robinson,Megan A. Macnaughtan,Daan M. F. van Aalten +11 more
TL;DR: This work defines how human O-GlcNAc transferase recognizes the sugar donor and acceptor peptide and employs a novel catalytic mechanism of glycosyl transfer, involving the sugar donors α-phosphate as the catalytic base, as well as an essential lysine.