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Victoria Lunz - Genuinely Passionate about Research

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[February 2017] Photo credited to OÖ Nachrichten ...  more of Victoria Lunz - Genuinely Passionate about Research (Titel)

Tuning membrane protein mobility by confinement into nanodomains

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[2016/11/16] In cooperation with Prof. Peter Pohl (Institute of Biophysics, JKU), lead CBL researchers DI Andreas Karner and Dr. Johannes Preiner have developed a platform to study membrane proteins. ...  more of Tuning membrane protein mobility by confinement into nanodomains (Titel)

Linz Winter Workshop 2017

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3 to 6 February 2017 ...  more of Linz Winter Workshop 2017 (Titel)

Tiemann-Boege Awarded Pilgerstorferpreis

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[2016/07/07] Assoc. Prof. Dr. Irene Tiemann-Boege was awarded the Pilgerstorferpreis from the Medical Society of Upper Austria.

Heißl awarded ÖAW Doc Scholarship

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[2016/03/04] Angelika Heißl's 3-year DOC fellowship granted by the Austrian Acadamy of Sciences (ÖAW) started on the 1 January 2016. The title is: "Meiotic recombination as a potential driver of microsatellite evolution". ...  more of Heißl awarded ÖAW Doc Scholarship (Titel)

Cholesterol in the fight against allergies

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[2016/02/15] Cholesterol in the fight against allergies ...  more of Cholesterol in the fight against allergies (Titel)

Biophysics Researchers Discover New Immune Protein Structure

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[2016/02/05] Scientists at the JKU Institute for Biophysics (a working group under a. Univ. Prof. Christoph Romanin) have deciphered a key function in the “Orai1” immune protein. ...  more of Biophysics Researchers Discover New Immune Protein Structure (Titel)


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Rainer Schindl

Dr. Rainer Schindl

Dr. Rainer Schindl (Back to Team Overview)
PostDoc Ion Channels

Gruberstraße 40, Room 217
Phone: +43 732 2468 7611
Fax: +43 732 2468 7609
rainer.schindl(/\t)jku.at

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Calcium domain in Orai1 regulates NFAT dependent genes

FWF Project P28701 (2015 – 2018) € 348.411,00

This project was granted 2015 and examines a novel Ca2+ binding domain at the pore entrance of the Ca2+ channel Orai1. This important Ca2+ channel, triggering T cell activation and mast cells degranulation, contains a unique pore structure different to the pore-loop architecture of many other ion-selective channels. A combination of functional live cell experiments with molecular dynamics simulations will reveal the interplay of the extracellular calcium binding domain and the nearby selectivity filter. Particularly, I will investigate how the channel adjusts to environmental Ca2+ and maintains Ca2+ permeation in ubiquitous cell types. Furthermore, I will determine how Orai1 mediated Ca2+ micro-domains activate transcription factors, including the Nuclear Factor of Activated T-cells (NFAT).

Ion Channels and Immune Response toward a global understanding of immune cell physiology and for new therapeutic approaches

Member of COST Action: BM 1406 (2015 – 2019)

This COST Action network is a novel and exciting enterprise that involves internationally recognized scientists across 15 European countries. The specific aims are i) to develop a strong European workforce to understand the role of ion channels in immune cells, and how deregulation of their function can cause disease, ii) to identify new targets for therapeutic immuno-interventions through modulation of ion channels.

Transmembrane helix coupling regulates Orai channel gating

FWF Project P26067 (2014 – 2017) € 324.040,50

In this recent project I aim to determine the unique gating of Orai1 Ca2+ channel. The Orai channel is in a closed conformation at resting condition and requires STIM1 to open and permeate Ca2+. I have engineered an Orai mutant that is constitutively active, independent of STIM1 or a cellular activation cascade. In a biochemical cysteine scanning approach combined with side-directed mutagenesis as well as by electrophysiological measurements I will elucidate the intrinsic mechanism of channel gating and gating domains within the channel pore.

Intrinsic feedback regulations in Orai channels

FWF Project P22747 (2010 – 2013) € 245.217,-

The three Ca2+ channels, named Orai1-3 have an intrinsic feedback mechanism to allow transient Ca2+ influx and prevent the cell from apoptosis. Hence, they partially stop permeation within a time scale of 100ms, named fast Ca2+ dependent inactivation. The three human Orai channels differ in their inactivation. In this project I revealed structural domains within these channels that regulate the time dependent inactivation.

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