Results 31 to 40 of about 13,998 (216)

Erastin Disrupts Mitochondrial Permeability Transition Pore (mPTP) and Induces Apoptotic Death of Colorectal Cancer Cells. [PDF]

PLoS ONE, 2016
We here evaluated the potential anti-colorectal cancer activity by erastin, a voltage-dependent anion channel (VDAC)-binding compound. Our in vitro studies showed that erastin exerted potent cytotoxic effects against multiple human colorectal cancer cell
Haizhong Huo, Zhiyuan Zhou, Jian Qin, Wenyong Liu, Bing Wang, Yan Gu   +5 more
doaj   +1 more source

Strategies for maximizing ATP supply in the microsporidian Encephalitozoon cuniculi: direct binding of mitochondria to the parasitophorous vacuole and clustering of the mitochondrial porin VDAC [PDF]

, 2013
Microsporidia are obligate intracellular parasites with extremely reduced genomes and a dependence on host-derived ATP. The microsporidium Encephalitozoon cuniculi proliferates within a membranous vacuole and we investigated how the ATP supply is ...
Bhella, David, Hacker, Christian, Howell, Matthew, Lucocq, John   +3 more
core   +5 more sources

Cell-free electrophysiology of human VDACs incorporated into nanodiscs: An improved method

Biophysical Reports, 2021
Voltage-dependent anion-selective channel (VDAC) is one of the main proteins of the outer mitochondrial membrane of all eukaryotes, where it forms aqueous, voltage-sensitive, and ion-selective channels.
Stefano Conti Nibali, Maria Carmela Di Rosa, Oliver Rauh, Gerhard Thiel, Simona Reina, Vito De Pinto   +5 more
doaj   +1 more source

TSPO: kaleidoscopic 18-kDa amid biochemical pharmacology, control and targeting of mitochondria [PDF]

, 2016
The 18-kDa translocator protein (TSPO) localizes in the outer mitochondrial membrane (OMM) of cells and is readily up-regulated under various pathological conditions such as cancer, inflammation, mechanical lesions and neurological diseases. Able to bind
Aghazadeh, Aghazadeh, Alho, Amitani, Anholt, Anholt, Anholt, Anholt, Antkiewicz-Michaluk, Arbo, Banati, Banati, Bar-Ami, Barron, Basile, Batarseh, Batarseh, Batarseh, Batarseh, Batra, Beinlich, Benavides, Bernassau, Besman, Bird, Bitran, Bose, Boujrad, Boujrad, Braestrup, Bribes, Bribes, Brunette, Cagnin, Campanella, Campioli, Casellas, Chauveau, Chen, Chen, Cho, Clark, Colasanti, Corcia, Costa, Costa, Costa, Cuhlmann, Daugherty, De Souza, Decaudin, Decker, Delavoie, Delerive, Doperalski, Enders, Epstein, Fafalios, Fan, Fan, Fan, Fur, Fur, Galiegue, Gastaldello, Gatliff, Gatliff, Gavish, Gavish, Gazouli, Gehlert, Gerhard, Gervois, Giatti, Giatzakis, Giatzakis, Golani, Gonzalez-Polo, Guillon, Gulyas, Guo, Guo, Gut, Hardwick, Hardwick, Hauet, Hauet, Jamin, Jaremko, Jaremko, Jemma Gatliff, Joo, Joseph-Liauzun, Karlstetter, Kita, Kondo, Konigsrainer, Korkhov, Kreisl, Kruczek, Kumar, Lacapere, Lacapere, Lavisse, Li, Li, Li, Li, Li, Li, Libby, Liu, Liu, Maia, Maury, Mazurika, McEnery, Miao, Michelangelo Campanella, Midzak, Midzak, Miettinen, Miller, Mills, Mizrahi, Morohaku, Murail, Nagler, Obame, Oberto, Olson, Ostuni, Ouchi, Owen, Owen, Owen, Papadopoulos, Papadopoulos, Papadopoulos, Papadopoulos, Papadopoulos, Papadopoulos, Papadopoulos, Paradis, Pastorino, Pelechano, Petrescu, Poynter, Raghavan, Rey, Romeo, Rone, Rosenberg, Rosenberg, Rosenberg, Rupprecht, Rupprecht, Scarf, Schaller, Selvaraj, Shoukrun, Sileikyte, Soustiel, Sutter, Tang, Taylor, Teboul, Thompson, Trincavelli, Tu, Tu, Tu, Vanhee, Varrone, Vega, Verma, Wang, Wang, Wei, Whalin, Xiao, Yang, Yang, Yasuno, Yeliseev, Yoder, Zhang, Zhang, Zhao, Zhou   +189 more
core   +2 more sources

Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase

Nature Communications, 2023
Mitochondria are double-membrane-bounded organelles that depend critically on phospholipids supplied by the endoplasmic reticulum. These lipids must cross the outer membrane to support mitochondrial function, but how they do this is unclear.
Helene Jahn, Ladislav Bartoš, Grace I. Dearden, Jeremy S. Dittman, Joost C. M. Holthuis, Robert Vácha, Anant K. Menon   +6 more
doaj   +1 more source

The Mitochondrial Ca(2+) Uniporter: Structure, Function, and Pharmacology. [PDF]

, 2017
Mitochondrial Ca(2+) uptake is crucial for an array of cellular functions while an imbalance can elicit cell death. In this chapter, we briefly reviewed the various modes of mitochondrial Ca(2+) uptake and our current understanding of mitochondrial Ca(2+)
A Quintana, A Raffaello, A Rasola, A Tosatto, A Varadi, AA Rowland, AI Tarasov, AN Antony, AR Marks, B Chance, B Glancy, B Moreau, C Giorgi, C Petrungaro, CC Mendes, CD Lobaton, CV Logan, CV Nicchitta, D Chaudhuri, D Chaudhuri, D De Stefani, D Jiang, D Lewis-Smith, D Tomar, D Vecellio Reane, DA Cox, DD Hall, DG Nicholls, DJ Pagliarini, E Carafoli, E Carafoli, E Kovacs-Bogdan, E Murphy, E Noack, E Rapizzi, F Fieni, F Fieni, F Perocchi, FD Vasington, G Bathori, G Beutner, G Beutner, G Csordas, G Csordas, G Csordas, G Csordas, G Csordas, G Csordas, G Csordas, G Czirjak, G Giannini, G Hajnoczky, G Hajnoczky, G Huang, G Michels, G Munch, G Szabadkai, G Szalai, G Szanda, G Szanda, GA Rutter, GC Sparagna, GD Schellenberg, GL Becker, H Vais, HF Deluca, I Bogeski, I Drago, I Zimanyi, J Matesanz-Isabel, J Nakai, J O-Uchi, J O-Uchi, J O-Uchi, J Qiu, J Santo-Domingo, J Schwartz, JD Martell, JG McCormack, JL Harrington, JM Baughman, JQ Kwong, JS Marchant, JT Lanner, JW Putney Jr, K Mallilankaraman, K Mallilankaraman, K Oxenoid, KJ Kamer, KM Holmstrom, L Buntinas, L Hymel, L Mela, L Wang, LH Jeyakumar, LK Seidlmayer, LS Jouaville, M Boerries, M Crompton, M Crompton, M Giacomello, M Giacomello, M Hoth, M Hoth, M Montero, M Montero, M Murgia, M Patron, M Plovanich, M Salvi, M Sastrasinh, MA Matlib, MF Tsai, MK Park, ML Joiner, ML Joiner, ML Litsky, ML Olson, MR Alam, MR Duchen, N MacQuaide, NE Hoffman, NJ Dolman, P Bernardi, P Koncz, P Pinton, PJ Doonan, PS Brookes, R Amann, R Jakob, R Malli, R Malli, R Perez-Campo, R Rizzuto, R Rizzuto, R Rizzuto, R Rizzuto, RM Denton, RM Denton, RM Denton, RS Sohal, S Feng, S Fuente de la, S Grimm, S Marchi, S Shanmughapriya, S Xu, SA Thayer, SS Lam, SY Ryu, T Pozzan, T Rharass, T Yamamoto, TE Gunter, TE Gunter, TE Gunter, TS Luongo, V Hung, V Paupe, VK Sharma, W Tan, WL Ying, X Pan, X Quan, Y Kirichok, Y Lee, Y Sancak, Y Wu   +167 more
core   +2 more sources

TSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control [PDF]

, 2014
The 18-kDa TSPO (translocator protein) localizes on the outer mitochondrial membrane (OMM) and participates in cholesterol transport. Here, we report that TSPO inhibits mitochondrial autophagy downstream of the PINK1-PARK2 pathway, preventing essential ...
Anholt R, Daniel East, Decaudin D, Garnier M, Gatliff J, Hirsch JD, James Crosby, Jemma Gatliff, Krueger KE, Li H, Michelangelo Campanella, Miettinen H, Okatsu K, Ozawa K, Papadopoulos V, Peter Parker, Robert Harvey, Rosella Abeti, Seneviratne MS, Sileikyte J, Snyder SH, Tamse CT, William Craigen   +22 more
core   +3 more sources

The proapoptotic protein BNIP3 interacts with VDAC to induce mitochondrial release of endonuclease G. [PDF]

PLoS ONE, 2014
BNIP3 is a proapoptotic protein that induces cell death through a mitochondria-mediated pathway. We reported previously that mitochondrial localization of BNIP3 and translocation of EndoG from mitochondria to the nucleus are critical steps of the BNIP3 ...
Xiaosha Zhang, Xiuwu Bian, Jiming Kong
doaj   +1 more source

Mitochondrial Ion Channels in Cancer Transformation [PDF]

, 2015
Cancer transformation involves reprograming of mitochondrial function to avert cell death mechanisms, monopolize energy metabolism, accelerate mitotic proliferation, and promote metastasis. Mitochondrial ion channels have emerged as promising therapeutic
Kevin N. Damri, Laurent M. Dejean, Pablo M. Peixoto, Stephen M. Madamba   +3 more
core   +2 more sources

Characterizing ATP Permeation through the Voltage-Dependent Anion Channel VDAC [PDF]

Biophysical Journal, 2014
Voltage-dependent anion channels (VDAC) mediate the transfer of metabolites such as ATP, ADP, and NADH across the outer mitochondrial membrane of all eukaryotic cells. The open state is selective for anions, while the partially closed state is selective for cations. The x-ray crystal structure of VDAC from mouse (mVDAC1) (Ujwal et al.
Choudhary, Om P., Paz, Aviv, Adelman, Joshua, Colletier, Jacques-Philippe, Abramson, Jeff, Grabe, Michael   +5 more
openaire   +1 more source