Results 21 to 30 of about 72,259 (188)

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

Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions

Frontiers in Physiology, 2021
Mitochondrial porins, also known as voltage-dependent anion selective channels (VDACs), are pore-forming molecules of the outer mitochondrial membranes, involved in the regulation of metabolic flux between cytosol and mitochondria.
Maria Carmela Di Rosa, Francesca Guarino, Francesca Guarino, Stefano Conti Nibali, Andrea Magrì, Andrea Magrì, Vito De Pinto, Vito De Pinto   +7 more
doaj   +1 more source

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

A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings

Micromachines, 2020
Ion channel proteins play important roles in various cell functions, making them attractive drug targets. Artificial lipid bilayer recording is a technique used to measure the ion transport activities of channel proteins with high sensitivity and ...
Minako Hirano, Daiki Yamamoto, Mami Asakura, Tohru Hayakawa, Shintaro Mise, Akinobu Matsumoto, Toru Ide   +6 more
doaj   +1 more source

Voltage-Dependent Anion Channel-1, a Possible Ligand of Plasminogen Kringle 5. [PDF]

PLoS ONE, 2016
Kringle 5, the fifth fragment of plasminogen, is known to be important for inhibiting the proliferation and migration of vascular endothelial cell (VEC), while not having any effects on normal endothelial cells.
Yin-Ku Liang, Liu-Jiao Bian
doaj   +1 more source

Nucleotide Interactions of the Human Voltage-dependent Anion Channel [PDF]

Journal of Biological Chemistry, 2014
The voltage-dependent anion channel (VDAC) mediates and gates the flux of metabolites and ions across the outer mitochondrial membrane and is a key player in cellular metabolism and apoptosis. Here we characterized the binding of nucleotides to human VDAC1 (hVDAC1) on a single-residue level using NMR spectroscopy and site-directed mutagenesis.
Saskia Villinger, Karin Giller, Monika Bayrhuber, Adam Lange, Christian Griesinger, Stefan Becker, Markus Zweckstetter   +6 more
openaire   +4 more sources

Hydrogen sulphide regulates inward-rectifying K+ channels in conjunction with stomatal closure [PDF]

, 2015
Hydrogen sulphide (H2S) is the third biological gasotransmitter and, in animals, affects many physiological processes by modulating ion channels. H2S has been reported to protect plants from oxidative stress in diverse physiological responses. H2S closes
Blatt, Mike R., Garia-Mata, Carlos, Papanatsiou, Maria, Scuffi, Denisse   +3 more
core   +2 more sources

VDAC: Voltage Dependant Anion Channel

The FASEB Journal, 2011
VDAC (Voltage Dependent Anion Channel) is a channel protein located on the outer mitochondrial membrane. It regulates mitochondria functions and cell respiration through the exchange of molecules between the cytoplasm and the organelle, such as ADP, ATP, anions, cations, and other small, hydrophilic molecules.
Patrick Jordan, Alexander Borden, John Fuller, Christian Gummin, Joe Puchner, Judson Bro, Kevin Bustos, Keegan English, Andrew Keuler, Qateeb Khan, Daniel Kim, Hasaan Munim, Ryan Sung, Nicholas Zausch, Keith Klestinski, David Vogt, Mike Caballero, YiFan Zhou, Wai‐Meng Kwok   +18 more
openaire   +1 more source

Subcellular Localization of Human Voltage-dependent Anion Channel Isoforms [PDF]

Journal of Biological Chemistry, 1995
The voltage-dependent anion channel of the outer mitochondrial membrane, VDAC (also known as mitochondrial porin), is a small abundant protein which forms a voltage-gated pore when incorporated into planar lipid bilayers. This protein forms the primary pathway for movement of major metabolites through the outer membrane.
W H, Yu, W, Wolfgang, M, Forte
openaire   +2 more sources