Results 261 to 270 of about 156,998 (303)

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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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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Structure and Regulation of the V-ATPases

Journal of Bioenergetics and Biomembranes, 2005
The V-ATPases are ATP-dependent proton pumps present in both intracellular compartments and the plasma membrane. They function in such processes as membrane traffic, protein degradation, renal acidification, bone resorption and tumor metastasis. The V-ATPases are composed of a peripheral V(1) domain responsible for ATP hydrolysis and an integral V(0 ...
Takao, Inoue, Yanru, Wang, Kevin, Jefferies, Jie, Qi, Ayana, Hinton, Michael, Forgac   +5 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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V-ATPase: a potential pH sensor

Nature Cell Biology, 2006
An interaction between V-ATPase, a multi-subunit complex responsible for endosome acidification, and ARNO, the GDP/GTP exchange factor for ARF1 and ARF6, indicates that V-ATPase is the long-sought pH-sensor that regulates trafficking in the endocytic pathway.
Chiara Recchi, Philippe Chavrier
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V-ATPase functions in normal and disease processes

Pflügers Archiv - European Journal of Physiology, 2007
Eukaryotic cells have evolved a family of ATP-dependent proton pumps known as the vacuolar (H(+))-ATPases (or V-ATPases) to regulate the pH of intracellular compartments, the extracellular space, and the cytoplasm. V-ATPases present within intracellular compartments are important for such normal cellular processes as receptor-mediated endocytosis and ...
Ayana, Hinton, Sarah, Bond, Michael, Forgac   +2 more
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