Results 61 to 70 of about 808,587 (145)

‐translocating ATPases

, 1994
The Na+-translocating F1F0-ATPase of Acetobacterium woodii was examined by electron microscopy. After reconstitution into proteoliposomes, knobs typical for the F1 domain were visible on the outside of the membrane.
Jutta Reidlinger, Frank Mayer, Volker Müller   +2 more
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Substrates, regulation, cellular functions, and disease associations of P4-ATPases [PDF]

P4-ATPases, a subfamily of the P-type ATPase superfamily, play a crucial role in translocating membrane lipids from the exoplasmic/luminal leaflet to the cytoplasmic leaflet. This process generates and regulates transbilayer lipid asymmetry.
Shin, Hye-Won, Takatsu, Hiroyuki
core   +1 more source

A different conformation for EGC stator subcomplex in solution and in the assembled yeast V-ATPase: possible implications for regulatory disassembly

, 2008
Vacuolar ATPases (V-ATPases) are ATP-dependent proton pumps that maintain the acidity of cellular compartments. They are composed of a membrane-integrated proton-translocating V(0) and an extrinsic cytoplasmic catalytic domain V(1), joined by several ...
Venzke, David, Böttcher, Bettina, Batisse, C., Fethiere, J., Diepholz, Meikel, Rössle, Manfred, Svergun, D. I., Prinz, Simone, Florchinger, B., Roessle, M., Venzke, D., Bottcher, B., Svergun, Dmitri, Flörchinger, Beate, Prinz, S., Diepholz, M., Batisse, Claire, Féthière, James   +17 more
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Mitochondrial dysfunction redirects proton transport and energy homeostasis in Saccharomyces cerevisiae under variable pH and glucose conditions

Mitochondrial function is crucial for the regulation of energy metabolism, proton homeostasis, and stress adaptation in Saccharomyces cerevisiae . This study demonstrates the role of mitochondria in modulating cellular responses to varying extracellular ...
Guaragnella, Nicoletta, Trchounian, Karen, Shirvanyan, Anahit, Anikyan, Liana   +3 more
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No Longer Hidden Secrets of Proton Pumping: The Resolution Revolution Enlightens V-ATPases

, 2018
In this issue of Molecular Cell, Roh et al. (2018) present a high-resolution cryo-EM structure of the nanodisc-reconstituted yeast Vo proton channel that provides important new insights into subunit arrangements and the proton translocation pathway in V ...
Stephen P. Muench, Martin van der Laan, Muench, SP, van der Laan, M   +3 more
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Physiological increases in uncoupling protein 3 augment fatty acid oxidation and decrease reactive oxygen species production without uncoupling respiration in muscle cells

, 2005
Decreased uncoupling protein (UCP)3 is associated with insulin resistance in muscle of pre-diabetic and diabetic individuals, but the function of UCP3 remains unclear.
Gerrits, Martin F., Wheeler, Michael B., Harper, Mary-Ellen, MacLellan, J. Darcy, Gowing, Adrienne, Smith, Peter J.S.   +5 more
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ATP-dependent proton transport in human renal medulla

, 1986
An electrogenic proton-translocating ATPase (H+-ATPase) has been described in turtle urinary bladder and bovine and rat renal medulla. In the present study, a membrane fraction with ATP-dependent H+ transport activity was isolated from human renal ...
F. D. Diaz-Diaz, T. D. DuBose, E. F. LaBelle, D. C. Eaton   +3 more
core   +1 more source

Structure, function and regulation of A-ATPases

Proton translocating ATPases are central to biological energy conversion, one of the most fundamental biological processes on earth whose elucidation has already led to several Nobel prizes.

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The Protection of Polysaccharide from the Brown Seaweed Sargassum graminifolium against Ethylene Glycol-Induced Mitochondrial Damage

, 2013
The aim of the present study is to evaluate the protective effect of polysaccharide from the Brown Seaweed Sargassum graminifolium (SGP) on ethylene glycol-induced kidney damage and the mechanism of SGP-mediated protection.
Wen-Hui Wu, Ting Kong, Chao-Yan Zhang, Min-Bo Lan   +3 more
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Akzessorische Untereinheiten von Komplex I aus Yarrowia lipolytica [PDF]

, 2005
Mitochondial NADH:ubiquinone oxidoreductase (complex I) the largest multiprotein enzyme of the respiratory chain, catalyses the transfer of two electrons from NADH to ubiquinone, coupled to the translocation of four protons across the membrane.
Abdrakhmanova, Albina
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