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Gitte Neubauer
Researcher at European Bioinformatics Institute
Publications - 48
Citations - 14123
Gitte Neubauer is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Phosphorylation & Spliceosome. The author has an hindex of 30, co-authored 48 publications receiving 13629 citations.
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Journal Article
A comprehensive biochemical and genetic analysis of the yeast U1 snRNP reveals five novel proteins.
Alexander Gottschalk,Jie Tang,Oscar Puig,Josefa Salgado,Gitte Neubauer,Hildur V. Colot,Matthias Mann,Bertrand Séraphin,Michael Rosbash,Reinhard Lührmann,Patrizia Fabrizio +10 more
TL;DR: The U1 snRNP is essential for recognition of the pre-mRNA 5'-splice site and the subsequent assembly of the spliceosome and it is shown that Nam8p/Mud15p contributes to the stability of U1snRNP.
Journal Article
Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry.
TL;DR: A fifth protein in the H complex peak, corresponding to hnRNP P2, is shown to be the product of the TLS/FUS gene, which was originally identified as a chimeric oncogene formed by the chromosome translocation t(12;16) that is responsible for myxoid liposarcoma.
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A selective inhibitor reveals PI3Kγ dependence of T H 17 cell differentiation
Giovanna Bergamini,Kathryn Bell,Satoko Shimamura,Thilo Werner,Andrew Cansfield,Katrin Müller,Jessica Perrin,Christina Rau,Katie Ellard,Carsten Hopf,Carola Doce,Daniel Leggate,Raffaella Mangano,Toby Mathieson,Alison O'Mahony,Ivan Plavec,Faiza Rharbaoui,Friedrich B M Reinhard,Mikhail M. Savitski,Nigel Ramsden,Emilio Hirsch,Gerard Drewes,Oliver Rausch,Marcus Bantscheff,Gitte Neubauer +24 more
TL;DR: High-throughput chemoproteomics method enabled multiplexed screening of 16,000 compounds against native protein and lipid kinases in cell extracts resulted in CZC24832, which is to the authors' knowledge the first selective inhibitor of phosphoinositide 3-kinase γ (PI3Kγ) with efficacy in in vitro and in vivo models of inflammation.
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Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
John C. Williams,J. P. Zeelen,Gitte Neubauer,Gert Vriend,Jan Backmann,Paul A.M. Michels,Anne-Marie Lambeir,Rik K. Wierenga +7 more
TL;DR: This mutation to glutamine in the E65Q variant of leishmania TIM results in much higher stability; for example, at pH 7, the apparent melting temperature increases by 26 degrees C and this mutation does not affect the kinetic properties, showing that even point mutations can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power at the Mesophilic temperature.
Journal ArticleDOI
The Commonly Used PI3-Kinase Probe LY294002 Is an Inhibitor of BET Bromodomains
Antje Dittmann,Thilo Werner,Chun-wa Chung,Mikhail M. Savitski,Maria Fälth Savitski,Paola Grandi,Carsten Hopf,Matthew J Lindon,Gitte Neubauer,Rab K. Prinjha,Marcus Bantscheff,Gerard Drewes +11 more
TL;DR: Quantitative chemoproteomic profiling shows that LY294002 and LY303511 inhibit the BET bromodomain proteins BRD2, BRD3, and BRD4 that comprise a family of targets structurally unrelated to PI3K.