Results 241 to 250 of about 33,437,851 (274)

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

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

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

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

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

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 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, Xiaomin, Song, Ling, Li, Nan, Song, Yongzhang, Luo   +8 more
openaire   +2 more sources

Voltage-dependent anion-selective channel 1 (VDAC1)—a mitochondrial protein, rediscovered as a novel enzyme in the plasma membrane

The International Journal of Biochemistry & Cell Biology, 2005
The eukaryotic porin or voltage-dependent anion-selective channel (VDAC1) is a pore-forming protein discovered twenty five years ago in the mitochondrial outer membrane. Its gene in eukaryotes is known, but its tertiary structure has never been solved.
A. LAWEN, J. D. LY, D. J. R. LANE, K. ZARSHLER, MESSINA, Angela Anna, DE PINTO, Vito Nicola   +5 more
openaire   +2 more sources

Endosomes: another extra-mitochondrial location of type-1 porin/voltage-dependent anion-selective channels (VDAC)

Pfl�gers Archiv European Journal of Physiology, 1998
Endocytotic vesicles (EV) isolated from rat renal cortex were subjected to SDS-polyacrylamide gel electrophoresis and Western blotting. A monoclonal antibody against human type-1 porin (31 kDa) detected a strong band of 31 kDa. The same antibody has been used as the primary antibody in indirect immunocytochemistry. Light microscopy of cryostat sections
Reymann, S., Haase, W., Krick, W., Burckhardt, G., Thinnes, F.   +4 more
openaire   +3 more sources