نتایج جستجو برای: binding p type atpase

تعداد نتایج: 2782987  

2017
Johannes D. Clausen Lasse Kjellerup Karen O'Hanlon Cohrt John Bondo Hansen William Dalby-Brown Anne-Marie L. Winther

Compounds belonging to a carbazole series have been identified as potent fungal plasma membrane proton adenosine triphophatase (H+-ATPase) inhibitors with a broad spectrum of antifungal activity. The carbazole compounds inhibit the adenosine triphosphate (ATP) hydrolysis activity of the essential fungal H+-ATPase, thereby functionally inhibiting the extrusion of protons and extracellular acidif...

Journal: :Current Biology 2004
Alfred Lammens Alexandra Schele Karl-Peter Hopfner

Structural maintenance of chromosome (SMC) proteins play a central role in higher-order chromosome structure in all kingdoms of life. SMC proteins consist of a long coiled-coil domain that joins an ATP binding cassette (ABC) ATPase domain on one side and a dimerization domain on the other side. SMC proteins require ATP binding or hydrolysis to promote cohesion and condensation, which is suggest...

Journal: :The Journal of biological chemistry 1998
V N Podust N Tiwari R Ott E Fanning

Replication factor C (RF-C), a complex of five subunits, and several subassemblies of RF-C, representing intermediates along the proposed protein assembly pathway (Podust, V. N., and Fanning, E. (1997) J. Biol. Chem. 272, 6303-6310), were expressed in insect cells using baculoviruses encoding individual subunits (p140, p40, p38, p37, and p36). Purified proteins were analyzed for ATPase activity...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2004
Yoshinori Takahashi Masaki Edamatsu Yoko Y Toyoshima

Cytoplasmic dynein is a minus-end-directed microtubule motor involved in numerous essential processes within eukaryotic cells, such as nuclear segregation and trafficking of intracellular particles. The motor domain of the dynein heavy chain comprises six tandemly linked AAA (ATPase associated with diverse cellular activities) modules (AAA1-AAA6). The first four modules include nucleotide-bindi...

Journal: :American journal of physiology. Cell physiology 2002
Dawn A Lowe David D Thomas LaDora V Thompson

We tested the hypothesis that age-associated decline in muscle function is related to a change in myosin ATPase activity. Single, glycerinated semimembranosus fibers from young (8-12 mo) and aged (32-37 mo) Fischer 344 x Brown Norway male rats were analyzed simultaneously for force and myosin ATPase activity over a range of Ca2+ concentrations. Maximal force generation was ~20% lower in fibers ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1985
I Angel R L Hauger M D Luu B Giblin P Skolnick S M Paul

Preincubation of rat hypothalamic slices in glucose-free Krebs-Ringer buffer (37 degrees C) resulted in a time-dependent decrease in specific (+)-[3H]amphetamine binding in the crude synaptosomal fraction prepared from these slices. The addition of D-glucose resulted in a dose- and time-dependent stimulation of (+)-[3H]amphetamine binding, whereas incubation with L-glucose, 2-deoxy-D-glucose, o...

Journal: :The Journal of biological chemistry 2009
Xiaoyu Liu Takashi Daiho Kazuo Yamasaki Guoli Wang Stefania Danko Hiroshi Suzuki

Roles of hydrogen bonding interaction between Ser(186) of the actuator (A) domain and Glu(439) of nucleotide binding (N) domain seen in the structures of ADP-insensitive phosphorylated intermediate (E2P) of sarco(endo)plasmic reticulum Ca(2+)-ATPase were explored by their double alanine substitution S186A/E439A, swap substitution S186E/E439S, and each of these single substitutions. All the muta...

2013
Cui-Cui Liu Shan Sun Sen-Fang Sui

N-ethylmaleimide-sensitive factor (NSF) is a member of the type II AAA+ (ATPase associated with various cellular activities) family. It plays a critical role in intracellular membrane trafficking by disassembling soluble NSF attachment protein receptor (SNARE) complexes. Each NSF protomer consists of an N-terminal domain (N domain) followed by two AAA ATPase domains (D1 and D2) in tandem. The N...

Journal: :The Journal of biological chemistry 2011
Anne-Sophie Piette Rita Derua Etienne Waelkens Marc Boutry Geoffrey Duby

The plant plasma membrane H(+)-ATPase is regulated by an auto-inhibitory C-terminal domain that can be displaced by phosphorylation of the penultimate residue, a Thr, and the subsequent binding of 14-3-3 proteins. By mass spectrometric analysis of plasma membrane H(+)-ATPase isoform 2 (PMA2) isolated from Nicotiana tabacum plants and suspension cells, we identified a new phosphorylation site, T...

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