Results 31 to 40 of about 615,643 (389)
Dysregulation of Na+/K+ ATPase by amyloid in APP+PS1 transgenic mice [PDF]
, 2005 BACKGROUND: The pathology of Alzheimer's disease (AD) is comprised of extracellular amyloid plaques, intracellular tau tangles, dystrophic neurites and neurodegeneration. The mechanisms by which these various pathological features arise are under intense
Dickey, Chad A +5 more
core +3 more sources
Journal of Biological Chemistry, 2009 Mitochondrial F(1)-ATPase contains a hexamer of alternating alpha and beta subunits. The assembly of this structure requires two specialized chaperones, Atp11p and Atp12p, that bind transiently to beta and alpha. In the absence of Atp11p and Atp12p, the hexamer is not formed, and alpha and beta precipitate as large insoluble aggregates.
Anthony Ludlam +5 more
openaire +3 more sources
Regulation of vacuolar H+-ATPase activity by the Cdc42 effector Ste20 in Saccharomyces cerevisiae [PDF]
, 2012 In the budding yeast Saccharomyces cerevisiae, the Cdc42 effector Ste20 plays a crucial role in the regulation of filamentous growth, a response to nutrient limitation.
Höfken, T, Kane, PM, Li, SC, Lin, M
core +1 more source
Chemical aspect of the influence of cobalt ions on ATPase activity [PDF]
Journal of the Serbian Chemical Society, 2000 The influence of Co2+ ions on the activities of Na+/K+-ATPase and Mg2+-ATPase, enzymes from rat brain synaptic plasma membrane, was studied. The aim of this study was to investigate the inhibition of both ATPases activities by exposure to cobalt ions as ...
JOVAN VUCETIC +2 more
doaj +2 more sources
Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1 [PDF]
, 2002 Client protein activation by Hsp90 involves a plethora of cochaperones whose roles are poorly defined. A ubiquitous family of stress-regulated proteins have been identified (Aha1, activator of Hsp90 ATPase) that bind directly to Hsp90 and are required ...
Chadli +39 more
core +1 more source
All motors have to decide is what to do with the DNA that is given them
Biomolecular Concepts, 2014 DNA translocases are a diverse group of molecular motors responsible for a wide variety of cellular functions. The goal of this review is to identify common aspects in the mechanisms for how these enzymes couple the binding and hydrolysis of ATP to their
Briggs Koan, Fischer Christopher J.
doaj +1 more source
In the absence of ATPase activity, pre-RC formation is blocked prior to MCM2-7 hexamer dimerization [PDF]
, 2013 The origin recognition complex (ORC) of Saccharomyces cerevisiae binds origin DNA and cooperates with Cdc6 and Cdt1 to load the replicative helicase MCM2–7 onto DNA. Helicase loading involves two MCM2–7 hexamers that assemble into a double hexamer around
A. Fernandez-Cid +47 more
core +1 more source
Journal of Biological Chemistry, 2012 In this article, I reflect on research on two ATPases. The first is F(1)F(0)-ATPase, also known as ATP synthase. It is the terminal enzyme in oxidative phosphorylation and famous as a nanomotor. Early work on mitochondrial enzyme involved purification in large amount, followed by deduction of subunit composition and stoichiometry and determination of ...
openaire +2 more sources
Function-related positioning of the type II secretion ATPase of Xanthomonas campestris pv. campestris. [PDF]
PLoS ONE, 2013 Gram-negative bacteria use the type II secretion (T2S) system to secrete exoproteins for attacking animal or plant cells or to obtain nutrients from the environment. The system is unique in helping folded proteins traverse the outer membrane.
Yih-Lin Chen, Nien-Tai Hu
doaj +1 more source
Stabilisation of Na,K-ATPase structure by the cardiotonic steroid ouabain [PDF]
, 2013 Cardiotonic steroids such as ouabain bind with high affinity to the membrane-bound cation-transporting P-type Na,K-ATPase, leading to complete inhibition of the enzyme.
Abdul-Gader +30 more
core +1 more source