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The V-ATPase as drug target

, 2018
Huss, M., Bender, Tobias, Grond, S., von Zezschwitz, Paultheo, Kunze, Brigitte, Sasse, Florenz, Menche, D., Wieczorek, H.   +7 more
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V-ATPases as Drug Targets

Journal of Bioenergetics and Biomembranes, 2005
V-ATPases are large, complex enzymes responsible for acidification of many internal compartments in eukaryotic cells. They also occur on plasma membranes of specialized cells, where they acidify the surrounding milieu. Numerous physiological processes depend on the activity of V-ATPases, and V-ATPases are implicated as a contributing factor in multiple
Emma Jean, Bowman, Barry J, Bowman
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V-ATPases in phagocytic cells

Journal of Experimental Biology, 1992
ABSTRACT V-ATPases in phagocytic cells are known to mediate the acidification of most intracellular organelles. Proton-pump-mediated acidification of these organellar compartments is vital to numerous cell processes, including receptor recycling, protein processing and sorting and microbial degradation.
S, Grinstein, A, Nanda, G, Lukacs, O, Rotstein   +3 more
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Structure of V-ATPase from citrus fruit

Structure, 2022
AbstractVacuolar-type ATPases (V-ATPases) are rotary proton pumps involved in numerous essential cellular processes in all eukaryotes. Difficulty in obtaining preparations of purified V-ATPase from plants in sufficient quantities for structural analysis has hindered determining the 3D structure of the plant V-ATPase.
Yong Zi Tan, Kristine A. Keon, Rana Abdelaziz, Peter Imming, Waltraud Schulze, Karin Schumacher, John L Rubinstein   +6 more
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Biochemistry of the renal V-ATPase

Journal of Experimental Biology, 1992
ABSTRACT In most eukaryotic cells, vacuolar H+-ATPases (V-ATPases) are present primarily or exclusively in intracellular membrane compartments, functioning in the acidification of the endocytic and secretory vacuolar apparatus necessary for constitutive cell function. V-ATPases also participate in renal hydrogen ion secretion in both the
S L, Gluck, R D, Nelson, B S, Lee, Z Q, Wang, X L, Guo, J Y, Fu, K, Zhang   +6 more
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Physiology of V-ATPases

Journal of Experimental Biology, 1992
ABSTRACT Protons migrate much faster than other ions through water, ice and water-lined membrane channels because they participate in hydrogen bonding and H+H2O exchange. Similarly, hydrogen bonding enables protons with amino, carbonyl, phosphoryl and sulfonyl residues to influence critically the charge, conformation and stability of ...
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Evolution and isoforms of V-ATPase subunits

Journal of Experimental Biology, 1992
ABSTRACT The structure of V- and F-ATPases/ATP synthases is remarkably conserved throughout evolution. Sequence analyses show that the V- and F-ATPases evolved from the same enzyme that was already present in the last common ancestor of all known extant life forms.
J P, Gogarten, T, Starke, H, Kibak, J, Fishman, L, Taiz   +4 more
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V-ATPases of the plasma membrane

Journal of Experimental Biology, 1992
ABSTRACT V-ATPases reside in high densities on the plasma membrane in specialized types of insect and vertebrate cells. They provide unique biochemical and electrophysiological properties that allow them to function in energizing the plasma membrane in insects, and in cellular acid excretion in vertebrates.
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The V-ATPase: small cargo, large effects

Current Opinion in Plant Biology, 2010
About 30 years ago seminal reports of anion-sensitive proton-pumping activity associated with microsomal membranes initiated research on the plant vacuolar-type H(+)-ATPase (V-ATPase, VHA). Since, it has been firmly established that these complex molecular machines are essential for what can be defined as cellular logistics.
Karin, Schumacher, Melanie, Krebs
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