Global kinome profiling reveals DYRK1A as critical activator of the human mitochondrial import machinery

Autor: Corvin Walter, Adinarayana Marada, Tamara Suhm, Ralf Ernsberger, Vera Muders, Cansu Kücükköse, Pablo Sánchez-Martín, Zehan Hu, Abhishek Aich, Stefan Loroch, Fiorella Andrea Solari, Daniel Poveda-Huertes, Alexandra Schwierzok, Henrike Pommerening, Stanka Matic, Jan Brix, Albert Sickmann, Claudine Kraft, Jörn Dengjel, Sven Dennerlein, Tilman Brummer, F.-Nora Vögtle, Chris Meisinger

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)

Mitochondrial protein import is mediated by the translocase of the outer membrane (TOM), through which nearly all precursors traverse. Here, the authors perform global in vitro kinome profiling and by this identify that DYRK1A phosphorylates TOM70 an

Externí odkaz: https://doaj.org/article/ad335a0ad991411586d01fad9f3c40e2

Vibronic Dynamics of the Ultrafast all-trans to 13-cis Photoisomerization of Retinal in Channelrhodopsin-1

Autor: Christoph Schnedermann, Philipp Kukura, Joachim Heberle, Ramona Schlesinger, Vera Muders, D. Ehrenberg

Publikováno v: Europe PubMed Central

Channelrhodopsins are light-gated ion channels with extensive applications in optogenetics. Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) exhibits a red-shifted absorption spectrum as compared to Channelrhodopsin-2, which is highly benefici

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ada1021bc7e379aa43a34d10a5d4f71
https://doi.org/10.1021/jacs.5b12251

Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli

Autor: Thorsten Friedrich, Julia Walter, Thomas Pohl, Vera Muders, Stefan Steimle, Heiko Erhardt

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817:863-871

The proton-pumping NADH:ubiquinone oxidoreductase, respiratory complex I, couples the electron transfer from NADH to ubiquinone with the translocation of protons across the membrane. In Escherichia coli the complex is made up of 13 different subunits

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4da6d8243ebfd16f90344d908eab10c
https://doi.org/10.1016/j.bbabio.2011.10.008

The primary photoreaction of channelrhodopsin-1: wavelength dependent photoreactions induced by ground-state heterogeneity

Autor: Till Stensitzki, Karsten Heyne, Joachim Heberle, Ramona Schlesinger, Vera Muders

Publikováno v: Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences, Vol 2 (2015)

The primary photodynamics of channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) was investigated by VIS-pump supercontinuum probe experiments from femtoseconds to 100 picoseconds. In contrast to reported experiments on channelrhodopsin-2 from Ch

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6e3626487b52c8366d88277c2c538b6
http://europepmc.org/articles/PMC4510425

Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1

Autor: Joachim Heberle, Víctor A. Lórenz-Fonfría, Ramona Schlesinger, Vera Muders

Publikováno v: Lórenz Fonfría, Victor Armando Muders, V. Schlesinger, R. Heberle, J. 2014 Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1 Journal of Chemical Physics 14 141 22D507
RODERIC. Repositorio Institucional de la Universitat de Valéncia
instname
Europe PubMed Central

Water plays an essential role in the structure and function of proteins, particularly in the less understood class of membrane proteins. As the first of its kind, channelrhodopsin is a light-gated cation channel and paved the way for the new and vibr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::027c81ab943af704464671d37ff9cf1c
https://doi.org/10.1063/1.4895796