Results 11 to 20 of about 56,880 (294)

Conductance hysteresis in the voltage-dependent anion channel [PDF]

European Biophysics Journal, 2015
Hysteresis in the conductance of voltage-sensitive ion channels is observed when the transmembrane voltage is periodically varied with time. Although this phenomenon has been used in studies of gating of the voltage-dependent anion channel, VDAC, from the outer mitochondrial membrane for nearly four decades, full hysteresis curves have never been ...
Rappaport, Shay M., Teijido Hermida, Óscar, Hoogerheide, David P., Rostovtseva, Tatiana K., Berezhkovskii, Alexander M., Bezrukov, Sergey M.   +5 more
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Functional dynamics in the voltage-dependent anion channel [PDF]

Proceedings of the National Academy of Sciences, 2010
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 solution NMR spectroscopy, Gaussian network model analysis, and molecular dynamics simulation.
Villinger, S., Briones, R., Giller, K., Zachariae, Ulrich, Lange, A., De Groot, B.L., Griesinger, C., Becker, S., Zweckstetter, M.   +8 more
openaire   +5 more sources

Structure of the human voltage-dependent anion channel [PDF]

Proceedings of the National Academy of Sciences, 2008
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 mitochondrially induced apoptosis.
Bayrhuber, M., Meins, T., Habeck, M., Becker , S., Giller, K., Villinger , S., Vonrhein, C., Griesinger, C., Zweckstetter, M., Zeth, K.   +9 more
openaire   +7 more sources

Functional Characterization of VDACs in Grape and Its Putative Role in Response to Pathogen Stress

Frontiers in Plant Science, 2021
Voltage-dependent anion channels (VDACs) are the most abundant proteins in the mitochondrial outer membranes of all eukaryotic cells. They participate in mitochondrial energy metabolism, mitochondria-mediated apoptosis, and cell growth and reproduction ...
Tengfei Xu, Xiaowei Wang, Hui Ma, Li Su, Wenyuan Wang, Jiangfei Meng, Yan Xu   +6 more
doaj   +1 more source

Structure, gating and interactions of the voltage-dependent anion channel [PDF]

European Biophysics Journal, 2021
AbstractThe voltage-dependent anion channel (VDAC) is one of the most highly abundant proteins found in the outer mitochondrial membrane, and was one of the earliest discovered. Here we review progress in understanding VDAC function with a focus on its structure, discussing various models proposed for voltage gating as well as potential drug targets to
Najbauer, Eszter E., Becker, Stefan, Giller, Karin, Zweckstetter, Markus, Lange, Adam, Steinem, Claudia, de Groot, Bert L., Griesinger, Christian, Andreas, Loren B., Najbauer, Eszter E.; Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, Becker, Stefan; Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, Giller, Karin; Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, Zweckstetter, Markus; Department of Neurology, University Medical Center Göttingen, University of Göttingen, Göttingen, Germany, Lange, Adam; Institut Für Biologie, Humboldt-Universität Zu Berlin, Berlin, Germany, Steinem, Claudia; Max-Planck Institute for Dynamics and Self-Organization, Göttingen, Germany, de Groot, Bert L.; Department of Theoretical and Computational Biophysics, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany, Griesinger, Christian; Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, Andreas, Loren B.; Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany   +17 more
openaire   +5 more sources

The Physiopathologic Roles of Calcium Signaling in Podocytes

Frontiers in Bioscience-Landmark, 2023
Calcium (Ca2+) plays a critical role in podocyte function. The Ca2+-sensitive receptors on the cell surface can sense changes in Ca2+ concentration, and Ca2+ flow into podocytes, after activation of Ca2+ channels (such as transient receptor potential ...
Yu-Chi Tu, Hua-Pan Shu, Lu-Lu Sun, Qian-Qian Liao, Li Feng, Ming Ren, Li-Jun Yao   +6 more
doaj   +1 more source

Neuronal and astroglial correlates underlying spatiotemporal Intrinsic Optical Signal in the rat hippocampal slice [PDF]

, 2013
Widely used for mapping afferent activated brain areas in vivo, the label-free intrinsic optical signal (IOS) is mainly ascribed to blood volume changes subsequent to glial glutamate uptake.
Héja, László, Kardos, Julianna, Nyitrai, Gabriella, Pál, Ildikó   +3 more
core   +6 more sources

A 3D model of the voltage‐dependent anion channel (VDAC) [PDF]

FEBS Letters, 2002
Eukaryotic porins are a group of membrane proteins whose best known role is to form an aqueous pore channel in the mitochondrial outer membrane. As opposed to the bacterial porins (a large family of protein whose 3D structure has been determined by X‐ray diffraction), the structure of eukaryotic porins (also termed VDACs, voltage‐dependent anion ...
Casadio, Rita, Jacoboni, Irene, Messina, Angela, De Pinto, Vito   +3 more
openaire   +4 more sources

Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century

Frontiers in Physiology, 2021
Eukaryotic porin, also known as Voltage-Dependent Anion Channel (VDAC), is the most frequent protein in the outer membrane of mitochondria that are responsible for cellular respiration.
Roland Benz
doaj   +1 more source

AtALMT12 represents an R-type anion channel required for stomatal movement in Arabidopsis guard cells [PDF]

, 2010
Stomatal pores formed by a pair of guard cells in the leaf epidermis control gas exchange and transpirational water loss. Stomatal closure is mediated by the release of potassium and anions from guard cells. Anion efflux from guard cells involves slow (S-
Al-Rasheid, K A S, Endler, A, Geiger, D, Hedrich, R, Imes, D, Marten, I, Martinoia, E, Meyer, S, Mumm, P, Weder, B   +9 more
core   +1 more source