Refine
Year of publication
- 2006 (840) (remove)
Document Type
- Article (581)
- Doctoral Thesis (82)
- Monograph/Edited Volume (54)
- Conference Proceeding (32)
- Postprint (26)
- Preprint (24)
- Review (18)
- Other (17)
- Master's Thesis (3)
- Working Paper (2)
Language
- English (840) (remove)
Keywords
- climate change (4)
- polyelectrolyte (4)
- Fluoreszenz-Resonanz-Energie-Transfer (3)
- Immunoassay (3)
- Nanopartikel (3)
- Nichtlineare Dynamik (3)
- Optimality Theory (3)
- Polyelektrolyt (3)
- metabolite profiling (3)
- metabolomics (3)
Institute
- Institut für Physik und Astronomie (159)
- Institut für Biochemie und Biologie (128)
- Institut für Chemie (81)
- Institut für Geowissenschaften (73)
- Institut für Mathematik (71)
- Institut für Informatik und Computational Science (55)
- Department Linguistik (46)
- Extern (37)
- Department Psychologie (36)
- Institut für Anglistik und Amerikanistik (34)
Reversible assembly of the V0V1 holoenzyme from V-0 and V-1 subcomplexes is a widely used mechanism for regulation of vacuolar-type H+-ATPases (V-ATPases) in animal cells. in the blowfly (Calliphora vicina) salivary gland, V- ATPase is located in the apical membrane of the secretory cells and energizes the secretion of a KCl-rich saliva in response to the hormone serotonin. We have examined whether the CAMP pathway, known to be activated by serotonin, controls V-ATPase assembly and activity. Fluorescence measurements of pH changes at the luminal surface of isolated glands demonstrate that CAMP, Sp-adenosine-3',5'-cyclic monophosphorothioate, or forskolin, similar to serotonin, cause V-ATPase-dependent luminal acidification. In addition, V-ATPase-dependent ATP hydrolysis increases upon treatment with these agents. Immunofluorescence microscopy and pelleting assays have demonstrated further that V, components become translocated from the cytoplasm to the apical membrane and V-ATPase holoenzymes are assembled at the apical membrane during conditions that increase intracellular cAMP. Because these actions occur without a change in cytosolic Ca2+, our findings suggest that the cAMP pathway mediates the reversible assembly and activation of V-ATPase molecules at the apical membrane upon hormonal stimulus
Calpain 1-gamma filamin interaction in muscle cells :a possible in situ regulation by PKC-alpha
(2006)
Calpain 1-gamma filamin interaction in muscle cells : a possible in situ regulation by PKC-alpha
(2006)
Calpain 1-gamma filamin interaction in muscle cells : a possible in situ regulation by PKC-alpha
(2006)
Calpains are a family of calcium-dependant cysteine-proteases involved in cytoskeleton remodelling and muscle differentiation. In a recent study, we observed the presence of calpain I in the muscle contractile apparatus and specifically in the N1- and N2-fines. This calpain isoform was found to be involved in the degradation of muscle fibres via proteolysis of key proteins in Z-disk and costameric junctions. The goal of this study was to determine whether gamma-filamin - a specific muscle isoform of the filamin family - is a calpain, I substrate and to characterise this interaction. gamma-Filamin is a major muscle architectural protein located in the Z-fine and under the sarcolemmal membrane. This protein is a component of the chain binding the sarcolemma to the sarcomeric structure. In this study, we found that gamma-filamin formed a stable complex in vitro and in cells with calpain I in the absence of calcium stimulation. We also located the binding domains in the C-terminus of gamma-filamin with a cleavage site between serine 2626 and serine 2627 in the hinge 2 region. The catalytic (80 kDa) and regulatory (28 kDa) subunits of calpain I are both involved in high affinity binding at gamma-filamin. Moreover, we showed that phosphorylation of the filamin C- terminus domain by PKC alpha protected gamma-filamin against proteolysis by calpain I in COS cells. Stimulation of PKC activity in myotubes, prevented gamma-filamin proteolysis by calpain and resulted in an increase in myotube adhesion.
Business process management
(2006)
A new precursor route for the preparation of bulk oxides and thin films of bismuth vanadates is proposed. The method involves the thermal treatment under air and mild conditions of hybrid organic-inorganic precursors, made from a zwitterionic salt-free polymer matrix and selected inorganic species. Monoclinic BiVO4 was obtained in the form of bulk oxide by calcination of the powdered homogeneous hybrid materials at 600 degrees C, from precursors containing Bi and V in stoichiometric amounts. In the same way, thermodiffractometry studies performed on a hybrid material exhibiting a Bi/ V molar ratio of 2 revealed that the ionic conductor gamma-Bi4V2O11 phase can be stabilized under very soft thermal conditions (300 degrees C). Additionally, thin films of yellow monoclinic BiVO4 were for the first time fabricated, by thermal treatment of the same hybrid polymeric precursors deposited on quartz substrates by spin coating, using a layer- by-layer technique. The presence of the target phase at the surface of the plates was confirmed by X-ray diffraction as well as UV-vis measurements
We give a new view on building content clusters from page pair models. We measure the heuristic importance within every two pages by computing the distance of their accessed positions in usage sessions. We also compare our page pair models with the classical pair models used in information theories and natural language processing, and give different evaluation methods to build the reasonable content communities. And we finally interpret the advantages and disadvantages of our models from detailed experiment results