Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Saskia Villinger"'
Autor:
Markus Zweckstetter, Christian Griesinger, Christian Schmidt, Saskia Villinger, Stefan Becker, Łukasz Jaremko, Mariusz Jaremko
Publikováno v:
Angewandte Chemie. 128:10674-10678
15N-Spinrelaxationsraten konnen wichtige Informationen uber Fernstruktur und interne Bewegungen von Membranproteinen bereitstellen. Kombiniert mit einem verbesserten Berechnungsprotokoll offenbart die mittels Relaxationsraten abgeleitete Struktur des
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36e18eb08814fd69e3593548b08cfafc
https://doi.org/10.1002/ange.201602639
https://doi.org/10.1002/ange.201602639
Autor:
Markus Zweckstetter, Stefan Becker, Christian Griesinger, Saskia Villinger, Christian Schmidt, Mariusz Jaremko, Łukasz Jaremko
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie (International Ed. in English)
Angewandte Chemie / International edition 55(35), 10518-10521 (2016). doi:10.1002/anie.201602639
Angewandte Chemie (International Ed. in English)
Angewandte Chemie / International edition 55(35), 10518-10521 (2016). doi:10.1002/anie.201602639
15N spin‐relaxation rates are demonstrated to provide critical information about the long‐range structure and internal motions of membrane proteins. Combined with an improved calculation method, the relaxation‐rate‐derived structure of the 28
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84979b333b60e1bd35dc6b21ef9edd44
https://hdl.handle.net/11858/00-001M-0000-002B-34DA-C11858/00-001M-0000-002B-34DD-611858/00-001M-0000-002B-34DC-8
https://hdl.handle.net/11858/00-001M-0000-002B-34DA-C11858/00-001M-0000-002B-34DD-611858/00-001M-0000-002B-34DC-8
Autor:
Saskia Villinger, Stefan Becker, Thomas Meins, Markus Zweckstetter, Kornelius Zeth, Clemens Vonrhein, Michael Habeck, Christian Griesinger, Monika Bayrhuber, Karin Giller
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitoch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9b40a401d6368e7d70db825780e17e2
https://doi.org/10.1073/pnas.0808115105
https://doi.org/10.1073/pnas.0808115105
Autor:
Karin Giller, Markus Zweckstetter, Saskia Villinger, Daniel J. Müller, Stefan Becker, Stefania A. Mari, Lin Ge, Christian Griesinger
Publikováno v:
Structure
Structure 24(4), 585-594 (2016). doi:10.1016/j.str.2016.02.012
Structure 24(4), 585-594 (2016). doi:10.1016/j.str.2016.02.012
Summary The voltage-dependent anion channel (VDAC) regulates the flux of metabolites and ions across the outer mitochondrial membrane. Regulation of ion flow involves conformational transitions in VDAC, but the nature of these changes has not been re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28d8238d502ea2ff1d1115ea4f0f9672
https://pubmed.ncbi.nlm.nih.gov/27021164
https://pubmed.ncbi.nlm.nih.gov/27021164
Autor:
Adam Lange, Claudia Steinem, Markus Zweckstetter, Ingo Mey, Bert L. de Groot, Conrad Weichbrodt, Saskia Villinger, Rodolfo Briones, Stefan Becker, Licia Paltrinieri, Christian Griesinger, Karin Giller
Publikováno v:
Biophysical journal 111(6), 1223-1234 (2016). doi:10.1016/j.bpj.2016.08.007
Biophysical Journal
Biophysical Journal
The voltage-dependent anion channel 1 (VDAC-1) is an important protein of the outer mitochondrial membrane that transports energy metabolites and is involved in apoptosis. The available structures of VDAC proteins show a wide β -stranded barrel pore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26e7174414787a982cd64ff7cb1e4cce
https://pub.dzne.de/record/138791
https://pub.dzne.de/record/138791
Autor:
Christian Griesinger, Saskia Villinger, Monika Bayrhuber, Markus Zweckstetter, Adam Lange, Karin Giller, Stefan Becker
Publikováno v:
Journal of Biological Chemistry
The journal of biological chemistry 289(19), 13397-13406 (2014). doi:10.1074/jbc.M113.524173
The journal of biological chemistry 289(19), 13397-13406 (2014). doi:10.1074/jbc.M113.524173
Background: Human VDAC1 mediates and controls the transport of metabolites across the outer mitochondrial membrane. Results: The N-terminal helix of hVDAC1 is involved in binding to charged forms of ATP, UTP, and GTP with an important contribution fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::caa51f482edcefea7aaaf404d4734a37
https://pubmed.ncbi.nlm.nih.gov/24668813
https://pubmed.ncbi.nlm.nih.gov/24668813
Autor:
Markus Zweckstetter, Saskia Villinger, Ulrich Zachariae, Stefan Becker, Rodolfo Briones, Bert L. de Groot, Christian Griesinger, Adam Lange, Karin Giller
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
The voltage-dependent anion channel (VDAC), located in the outer mitochondrial membrane, acts as a gatekeeper for the entry and exit of mitochondrial metabolites. Here we reveal functional dynamics of isoform one of VDAC (VDAC1) by a combination of s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5f261c173d6288d3a40a674c814dc8b
https://hdl.handle.net/11858/00-001M-0000-0027-CA1F-511858/00-001M-0000-0011-5907-711858/00-001M-0000-002A-3862-F
https://hdl.handle.net/11858/00-001M-0000-0027-CA1F-511858/00-001M-0000-0011-5907-711858/00-001M-0000-002A-3862-F
Publikováno v:
Proteins. 78(16)
A large-scale comparison of essential dynamics (ED) modes from molecular dynamic simulations and normal modes from coarse-grained normal mode methods (CGNM) was performed on a dataset of 335 proteins. As CGNM methods, the elastic network model (ENM)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d20f65fc7f3f0c89ea614d86823b35cb
https://pubmed.ncbi.nlm.nih.gov/20848551
https://pubmed.ncbi.nlm.nih.gov/20848551
Autor:
Rodolfo Briones, Giller Karin, Christian Griesinger, Saskia Villinger, Markus Zweckstetter, Ulrich Zachariae, Vytautas Gapsys, Bert L. de Groot
Publikováno v:
Biophysical Journal. (3):147a
VDAC-1 (Voltage Dependent Anion Channel) is one of the main components of the outer mitochondrial membrane. It is responsible for the transport of ATP and other anions, and it is involved in apoptosis and cancer [1]. The X-ray and NMR structures [2-4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::061e0430edb7dbef68178e509a04ac1b