Results 251 to 260 of about 10,440,305 (287)

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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Structure–function relationships of A-, F- and V-ATPases

Journal of Experimental Biology, 2001
SUMMARYIon-translocating ATPases, such as the F1Fo-, V1Vo- and archaeal A1Ao enzymes, are essential cellular energy converters which transduce the chemical energy of ATP hydrolysis into transmembrane ionic electrochemical potential differences. Based on subunit composition and primary structures of the subunits, these types of ATPases are related ...
G, Grüber, H, Wieczorek, W R, Harvey, V, Müller   +3 more
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The V-ATPase inhibitor archazolid

2014
Fighting metastasis is a major challenge in cancer therapy and novel therapeutic targets and drugs are highly appreciated. Resistance of invasive cells to anoikis, a particular type of apoptosis induced by loss of cell-extracellular matrix (ECM) contact, is a major prerequisite for their metastatic spread. Inducing anoikis in metastatic cancer cells is
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V-ATPases

2013
J. Capecci, M. Forgac
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