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Olga Perisic

Researcher at Laboratory of Molecular Biology

Publications -  66
Citations -  9774

Olga Perisic is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Protein subunit & ESCRT. The author has an hindex of 43, co-authored 65 publications receiving 9005 citations. Previous affiliations of Olga Perisic include Medical Research Council & Boston College.

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Structural Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, LY294002, Quercetin, Myricetin, and Staurosporine

TL;DR: Interestingly, LY294002 and the lead compound on which it was designed, quercetin, as well as the closely related flavonoid myricetin bind PI3K in remarkably different orientations that are related to each other by 180 degrees rotations.
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Crystal Structure and Functional Analysis of Ras Binding to Its Effector Phosphoinositide 3-Kinase γ

TL;DR: Ras activation of phosphoinositide 3-kinase (PI3K) is important for survival of transformed cells and it is found that PI3Kgamma is strongly and directly activated by H-Ras G12V in vivo or by GTPgammaS-loaded H- Ras in vitro.
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Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta.

TL;DR: The 2.4-Å structure of phospholipase Cδ1 reveals a multidomain protein incorporating modules shared by many signalling proteins that suggests a mechanism for membrane attachment and Ca2+ -dependent hydrolysis of second-messenger precursors.
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Phosphoinositide 3-Kinase δ Gene Mutation Predisposes to Respiratory Infection and Airway Damage

TL;DR: Activated PI3K-δ syndrome (APDS), a PID associated with a dominant gain-of-function mutation in which lysine replaced glutamic acid at residue 1021 (E1021K) in the p110δ protein, the catalytic subunit of phosphoinositide 3-kinase δ (PI3Kδ), encoded by the PIK3CD gene is described.
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Structural insights into phosphoinositide 3-kinase catalysis and signalling.

TL;DR: The 2.2 Å X-ray crystallographic structure of the catalytic subunit of PI3Kγ, the class I enzyme that is activated by heterotrimeric G-protein βγ subunits and Ras is reported.