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PI(3,5)P2 Controls the Signaling Activity of Class I PI3K
Structural Basis for Highly Selective Class II Alpha Phosphoinositide-3-Kinase Inhibition
Journal of Medicinal Chemistry 2023
online lesenDevelopment of selective inhibitors of phosphatidylinositol 3-kinase C2α
Nature Chemical Biology 2023
online lesenAntagonistic control of active surface integrins by myotubularin and phosphatidylinositol 3-kinase C2β in a myotubular myopathy model
Proceedings of the National Academy of Sciences 2022
online lesenPhosphoinositide Conversion Inactivates R‐RAS and Drives Metastases in Breast Cancer
Advanced Science 2022
online lesenStructural basis of phosphatidylinositol 3-kinase C2α function
Nature Structural & Molecular Biology 2022
online lesenmTORC1 activity repression by late endosomal phosphatidylinositol 3,4-bisphosphate
Science 2017
online lesenLipid-mediated PX-BAR domain recruitment couples local membrane constriction to endocytic vesicle fission
Nature Communications 2017
online lesenA Coincidence Detection Mechanism Controls PX-BAR Domain-Mediated Endocytic Membrane Remodeling via an Allosteric Structural Switch
Developmental Cell 2017
online lesenNon-targeting siRNA induces NPGPx expression to cooperate with exoribonuclease XRN2 for releasing the stress
Nucleic Acids Research 2012
online lesenLoss of the Oxidative Stress Sensor NPGPx Compromises GRP78 Chaperone Activity and Induces Systemic Disease
Molecular Cell 2012
online lesenDas Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) gehört zum Forschungsverbund Berlin e.V. (FVB), einem Zusammenschluss von sieben natur-, lebens- und umweltwissenschaftlichen Instituten in Berlin. Die Einrichtungen sind Mitglieder der Leibniz-Gemeinschaft.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Deutschland