Results 251 to 260 of about 91,154 (289)

Role of voltage-dependent anion channel 1 in neurodegeneration: Mechanisms, implications, and therapeutic potential.

Neural Regeneration Research
Voltage-dependent anion channel 1 is an integral outer membrane protein of the mitochondria that governs apoptosis, enables metabolite exchange, and influences mitochondrial activity.
A. Parikh, Anas Cholavaram, Ajith Kumar Chitti Babu, K. Deepankumar, M. Vijayan   +4 more
semanticscholar   +2 more sources

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Mapping the N-Terminal Hexokinase-I Binding Site onto Voltage-Dependent Anion Channel-1 To Block Peripheral Nerve Demyelination.

Journal of Medicinal Chemistry, 2022
The voltage-dependent anion channel (VDAC), the most abundant protein on the outer mitochondrial membrane, is implicated in ATP, ion and metabolite exchange with cell compartments. In particular, the VDAC participates in cytoplasmic and mitochondrial Ca2+
Benoît Gautier, Mélanie Forêt Jacquard, Sophie Guelfi, Scarlette Abbou, E. González, J. Berthelot, H. Boukhaddaoui, A. Lebrun, B. Legrand, N. Tricaud, N. Inguimbert   +10 more
semanticscholar   +1 more source

Voltage‐dependent anion channel 1 is involved in endostatin‐induced endothelial cell apoptosis

The FASEB Journal, 2008
ABSTRACT Endostatin (ES) was reported to stimulate apoptosis in endothelial cells, but the exact mechanism remains controversial. In the present study, we elucidate the mechanism of ES‐induced endothelial cell apoptosis.
Shaopeng Yuan, Yan Fu, Xiaofeng Wang, Hubing Shi, Yujie Huang, Xiaoming Song, Ling Li, Nan Song, Yongzhang Luo   +8 more
semanticscholar   +3 more sources

Localization of the voltage-dependent anion channel-1 Ca2+-binding sites

Cell Calcium, 2007
Photoreactive azido ruthenium (AzRu) has been recently shown to specifically interact with Ca(2+)-binding proteins and to strongly inhibit their Ca(2+)-dependent activities. Upon UV irradiation, AzRu can bind covalently to such proteins. In this study, AzRu was used to localize and characterize Ca(2+)-binding sites in the voltage-dependent anion ...
Adrian, Israelson, Salah, Abu-Hamad, Hilal, Zaid, Edna, Nahon, Varda, Shoshan-Barmatz   +4 more
openaire   +2 more sources

Structural Analysis of Murine Voltage Dependent Anion Channel (VDAC) 1

The FASEB Journal, 2006
VDAC is a mammalian integral protein expressed in the outer mitochondrial membrane. It has a bi‐functional role in mitochondrial biology: under physiological conditions, it transports nucleotides and small molecules across the outer membrane and
Rachna Ujwal, Peipei Ping, Jun Zhang, Gabriel Mercado, Thomas M. Vondriska, H. Ronald Kaback, Jeff Abramson   +6 more
openaire   +1 more source

Mapping of the Human Voltage-Dependent Anion Channel Isoforms 1 and 2 Reconsidered

Biochemical and Biophysical Research Communications, 1999
Eukaryotic porins or VDACs (Voltage-Dependent Anion-selective Channels) are integral membrane proteins forming large hydrophilic pores. Three functioning genes for VDAC isoforms have been detected in mouse and the corresponding cDNAs are known also in humans.
MESSINA, Angela Anna, OLIVA M., ROSATO C., HUIZING M, RUITENBEEK W., VAN DEN HEUVEL L. P., FORTE M., ROCCHI M., DE PINTO, Vito Nicola   +8 more
openaire   +4 more sources

Mapping the ruthenium red-binding site of the voltage-dependent anion channel-1

Cell Calcium, 2008
We have previously shown that ruthenium red (RuR) binds to the voltage-dependent anion channel (VDAC) in the outer mitochondrial membrane, decreasing channel conductance and protecting against apoptotic cell death. In this report, we define the murine and yeast VDAC1 amino acid residues involved in the interaction with RuR.
Adrian, Israelson, Hilal, Zaid, Salah, Abu-Hamad, Edna, Nahon, Varda, Shoshan-Barmatz   +4 more
openaire   +2 more sources

Bioreductive activation of quinone antitumor drugs by mitochondrial voltage-dependent anion channel 1

Anatomical Science International, 2008
The authors recently demonstrated that the mitochondrial voltage-dependent anion channel 1 (VDAC1) is involved in the sensitivity of cancer cells to furanonaphthoquinone (FNQ). The aim of the present study was to investigate whether mitochondrial VDAC1 reduces quinone antitumor drugs.
Eriko, Simamura, Hiroki, Shimada, Yasuhito, Ishigaki, Toshihisa, Hatta, Nobuaki, Higashi, Kei-Ichi, Hirai   +5 more
openaire   +2 more sources

Voltage-dependent anion channel 1 mediates mitochondrial fission and glucose metabolic reprogramming in response to ionizing radiation.

Science of the Total Environment
The ionizing radiation (IR) represents a formidable challenge as an environmental factor to mitochondria, leading to disrupt cellular energy metabolism and posing health risks.
Ying Xie, Xiaochang Liu, Dafei Xie, Wen Zhang, Hongling Zhao, H. Guan, Pingkun Zhou   +6 more
semanticscholar   +1 more source

Presence of a voltage-dependent anion channel 1 in the rat postsynaptic density fraction

NeuroReport, 1999
Little is known about the molecular organization and functions of the postsynaptic density (PSD), a cytoskeletal specialization on the postsynaptic membrane. In an attempt to elucidate the protein composition of PSD, we have sequenced a 35 kDa protein of the rat forebrain PSD fraction.
JUNG IL MOON, YONG WOOK JUNG, BOK HYUN KO, DE PINTO, Vito Nicola, INGNYOL JIN, IL SOO MOON   +5 more
openaire   +2 more sources