Results 221 to 230 of about 147,751 (260)

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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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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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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The V-ATPase as a Target for Antifungal Drugs

Current Protein & Peptide Science, 2012
The ubiquitous and essential V-ATPase is a worthy chemotherapeutic target in the escalating battle against invasive fungal infections. Pathogenic fungi require optimum V-ATPase function for secretion of virulence factors, induction of stress response pathways, hyphal morphology and homeostasis of pH and other cations in order to successfully survive ...
Yongqiang, Zhang, Rajini, Rao
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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 in insect epithelia

Journal of Experimental Biology, 2017
![Figure][1] Mike O'Donnell discusses the impact of two classic papers, published by Helmut Wieczorek in Journal of Biological Chemistry in 1989 and 1991, which report the discovery of the the insect midgut V-ATPase.
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Evolution of structure and function of V-ATPases

Journal of Bioenergetics and Biomembranes, 1992
Proton pumping ATPases/ATPsynthases are found in all groups of present-day organisms. The structure of V- and F-type ATPases/ATP synthases is very conserved throughout evolution. Sequence analysis shows that the V- and F-type ATPases evolved from the same enzyme already present in the last common ancestor of all known extant life forms.
H, Kibak, L, Taiz, T, Starke, P, Bernasconi, J P, Gogarten   +4 more
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Structure and Assembly of the Yeast V-ATPase

Journal of Bioenergetics and Biomembranes, 2003
The yeast V-ATPase belongs to a family of V-type ATPases present in all eucaryotic organisms. In Saccharomyces cerevisiae the V-ATPase is localized to the membrane of the vacuole as well as the Golgi complex and endosomes. The V-ATPase brings about the acidification of these organelles by the transport of protons coupled to the hydrolysis of ATP.
Laurie A, Graham, Andrew R, Flannery, Tom H, Stevens   +2 more
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V-ATPases in Insects

1995
Insects are one of the most successful classes of organism in the world. Their small size, impermeable exocuticle and short generation times have allowed them to adapt to exploit a huge range of ecological niches, many of which place them in conflict with humans.
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