Results 41 to 50 of about 22,016 (234)

The Role of Lipids in VDAC Oligomerization [PDF]

Biophysical Journal, 2012
Evidence has accumulated that the voltage-dependent anion channel (VDAC), located on the outer membrane of mitochondria, plays a central role in apoptosis. The involvement of VDAC oligomerization in apoptosis has been suggested in various studies.
Betaneli, Viktoria, Petrov, Eugene P., Schwille, Petra   +2 more
openaire   +2 more sources

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   +2 more sources

Evolution of Voltage-Dependent Anion Channel Function: From Molecular Sieve to Governator to Actuator of Ferroptosis

Frontiers in Oncology, 2017
The voltage-dependent anion channel (VDAC) is well known as the pathway for passive diffusion of anionic hydrophilic mitochondrial metabolites across the outer membrane, but a more complex functionality of the three isoforms of VDAC has emerged, as ...
John J. Lemasters, John J. Lemasters
doaj   +1 more source

Biophysical Effects Of Ion Concenteration On The Affinity Between Nanopore, OmpF Lumen and Passing Nucleotide [PDF]

, 2010
OmpF an outer-membrane porin channel of _E. Coli_ posses beta-barrel structure, whose conductivity and gating phenomena are affected by changes in pH, salt concentration and so on. The distribution of amino acids in OmpF induces a non homologous electric
Hamid Mobasheri, Saeid Hadi
core   +2 more sources

The intrinsically disordered N-terminus of the voltage-dependent anion channel.

PLoS Computational Biology, 2021
The voltage-dependent anion channel (VDAC) is a critical β-barrel membrane protein of the mitochondrial outer membrane, which regulates the transport of ions and ATP between mitochondria and the cytoplasm.
Jordane Preto, Isabelle Krimm
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

Voltage-dependent anion channel (VDAC) is involved in apoptosis of cell lines carrying the mitochondrial DNA mutation

BMC Medical Genetics, 2009
Background The mitochondrial voltage-dependent anion channel (VDAC) is increasingly implicated in the control of apoptosis. We have studied the effects the mitochondrial DNA (mtDNA) tRNAIle mutation on VDAC expression, localization, and apoptosis ...
Mohan Liu, Rui Chen, Lin Wang, Hua Xu, Zongbin Li, Yang Li, Lei Gao, Yuqi Liu, Yi Wen, Minxin Guan, Shiwen Wang   +10 more
doaj   +1 more source

Dual mechanism of ion permeation through VDAC revealed with inorganic phosphate ions and phosphate metabolites. [PDF]

PLoS ONE, 2015
In the exchange of metabolites and ions between the mitochondrion and the cytosol, the voltage-dependent anion channel (VDAC) is a key element, as it forms the major transport pathway for these compounds through the mitochondrial outer membrane. Numerous
Eva-Maria Krammer, Giang Thi Vu, Fabrice Homblé, Martine Prévost   +3 more
doaj   +1 more source

Decrypting strong and weak single-walled carbon nanotubes interactions with mitochondrial voltage-dependent anion channels using molecular docking and perturbation theory [PDF]

, 2017
[Abstract] The current molecular docking study provided the Free Energy of Binding (FEB) for the interaction (nanotoxicity) between VDAC mitochondrial channels of three species (VDAC1-Mus musculus, VDAC1-Homo sapiens, VDAC2-Danio rerio) with SWCNT-H ...
González-Durruthy, Michael, González-Díaz, Humberto, Machado, Karina S., Monserrat, José M., Munteanu, Cristian-Robert, Pazos, A., Seus, Vinicius, Werhli, Adriano V.   +7 more
core   +3 more sources

Role of mitochondrial raft-like microdomains in the regulation of cell apoptosis [PDF]

, 2015
Lipid rafts are envisaged as lateral assemblies of specific lipids and proteins that dissociate and associate rapidly and form functional clusters in cell membranes.
A Al-Saif, A Bertoni, A Cossarizza, A Ferri, A Israelson, A Raturi, A Valencia, A Valencia, AA Rowland, AE Rusinol, AL Nishimura, AL Wozniak, Alberto Ferri, AM Giammarioli, AO Hueber, B Kornmann, C Barbat, C Brooks, C Dall’Armi, C Frezza, C Gajate, C Garcia-Ruiz, C Garcia-Ruiz, C Martel, C Steinmann, C Vande Velde, CB Pickett, CD Austin, CH Chou, CL Schengrund, D Naon, D Scheel-Toellner, D Scheel-Toellner, DF Legler, DF Suen, DT Browman, E Bossy-Wetzel, E Lai, E Szegezdi, EM Lynes, EM Lynes, F Korobova, F Mollinedo, G Csordas, G Szabadkai, GC Shore, GM Cereghetti, H Grassmè, H Yano, I Annunziata, I Poggiolini, J Faitova, J Katz, J Stiban, JC Martinou, JC Wanson, JE Vance, JL Herrera, JR Friedman, JT Vollrath, K Banki, K Simons, K Simons, KF Ferri, KR Pitts, L Ciarlo, L Ciarlo, L Dupuis, L Scorrano, LA Lewis, M Cozzolino, M Cozzolino, M Degli Esposti, M Degli Esposti, M Fujimoto, M Hamasaki, M Hamasaki, M Karbowski, M Lutter, M Satoh, M Sorice, M Sorice, M Sorice, M Sorice, M Sorice, M Vey, Maria Grasso, Maurizio Sorice, ME Soriano, MG Martín, MM Young, MR Rippo, MT Dimanche-Boitre, N Myhill, N Naslavsky, N Zurgil, NT Watt, OM Brito de, OM Brito de, P Matarrese, P Matarrese, P Matarrese, P Pizzo, P Pizzo, P Pizzo, PA Parone, PJ Meier, R Rizzuto, R Rizzuto, R Sano, R Stoica, RG Burns, RM Siegel, Roberta Misasi, S Ayala-Peña, S Cipolat, S Eda, S Hoppins, S Montessuit, S Orrenius, S Ouasti, S Sonnino, SB Prusiner, SW Ahn, SY Gilady, T Garofalo, T Garofalo, T Gutierrez, T Hayashi, T Hayashi, T Hayashi, T Hayashi, T Kuwana, T Simmen, T Simmen, Tina Garofalo, UP Shirendeb, V Lallemand-Breitenbach, V Mattei, V Mattei, V Mattei, Valeria Manganelli, Vincenzo Mattei, W Hu, W Malorni, W Song, W Song, X Guo, Y Higuchi, Y Yoon, Y Zhang, YJ Lee, Z Sui, Z Wieslaw   +153 more
core   +1 more source