163,887 research outputs found
Olive J. Brose, Church and Parliament. The Reshaping of the Church of England, 1828-1860.
No full textCrouzet François. Olive J. Brose, Church and Parliament. The Reshaping of the Church of England, 1828-1860.. In: Annales. Economies, sociétés, civilisations. 17ᵉ année, N. 5, 1962. pp. 1010-1011
For better or for worse : Complexins regulate SNARE function and vesicle fusion
No full textIn contrast to constitutive secretion, SNARE-mediated synaptic vesicle fusion is controlled by multiple regulatory proteins, which determine the Ca(2+) sensitivity of the vesicle fusion process and the speed of excitation-secretion coupling. Complexins are among the best characterized SNARE regulators known to date. They operate by binding to trimeric SNARE complexes consisting of the vesicle protein synaptobrevin and the plasma membrane proteins syntaxin and SNAP-25. The question as to whether complexins facilitate or inhibit SNARE-mediated fusion processes is currently a matter of significant controversy. This is mainly because of the fact that biochemical experiments in vitro and studies on vertebrate complexins in vivo have yielded apparently contradictory results. In this review, I provide a summary of available data on the role of complexins in SNARE-mediated vesicle fusion and attempt to define a model of complexin function that incorporates evidence for both facilitatory and inhibitory roles of complexins in SNARE-mediated fusion
[Report to Chief J. E. Curry, by an unknown author #1]
No full textReport to Chief J. E. Curry, by an unknown author. The report contains a list of officers who gave depositions to the United States Attorney
[Report to Chief J. E. Curry, by an unknown author #2]
No full textReport to Chief J. E. Curry, by an unknown author. The report contains a list of officers who gave depositions to the United States Attorney
A chloride- and calcium-dependent glutamate-binding protein from rat brain. Identification as a ubiquitous constituent of the inner mitochondrial membrane
No full textWe have recently solubilized and enriched a chloride- and calcium-dependent glutamate-binding protein from rat brain (Brose, N., Halpain, S., Suchanek, C., and Jahn, R. (1989) J. Biol. Chem. 264, 9619-9625). The partially purified protein fraction, containing two major protein components of 51,000 Da and 105,000 Da, was used to generate a rabbit antiserum. This serum quantitatively precipitated the binding activity from membrane extracts. Small amounts of the antiserum inhibited glutamate binding when chloride was absent from the incubation medium. Three protein bands were labeled by the serum on immunoblots. From the affinity purified antibody fractions contained in the serum, only the antibodies directed against a 51,000-Da protein were able to immunoprecipitate the binding activity, indicating that this protein is an essential component of the binding site. A survey of a variety of rat tissues by immunoblot analysis revealed a ubiquitous distribution of the protein. After subcellular fractionation of liver and brain, the 51,000-Da protein copurified with mitochondrial markers. Furthermore, exclusive labeling of mitochondria was observed by light and electron microscopy immunocytochemistry. Subfractionation of purified liver mitochondria resulted in a selective association of the protein with inner mitochondrial membranes. Pharmacological characterization of glutamate binding to liver mitochondrial membranes revealed a pattern almost identical to that of the chloride- and calcium-dependent glutamate-binding site in rat brain
A chloride- and calcium-dependent glutamate-binding protein from rat brain. Identification as a ubiquitous constituent of the inner mitochondrial membrane
No full textWe have recently solubilized and enriched a chloride- and calcium-dependent glutamate-binding protein from rat brain (Brose, N., Halpain, S., Suchanek, C., and Jahn, R. (1989) J. Biol. Chem. 264, 9619-9625). The partially purified protein fraction, containing two major protein components of 51,000 Da and 105,000 Da, was used to generate a rabbit antiserum. This serum quantitatively precipitated the binding activity from membrane extracts. Small amounts of the antiserum inhibited glutamate binding when chloride was absent from the incubation medium. Three protein bands were labeled by the serum on immunoblots. From the affinity purified antibody fractions contained in the serum, only the antibodies directed against a 51,000-Da protein were able to immunoprecipitate the binding activity, indicating that this protein is an essential component of the binding site. A survey of a variety of rat tissues by immunoblot analysis revealed a ubiquitous distribution of the protein. After subcellular fractionation of liver and brain, the 51,000-Da protein copurified with mitochondrial markers. Furthermore, exclusive labeling of mitochondria was observed by light and electron microscopy immunocytochemistry. Subfractionation of purified liver mitochondria resulted in a selective association of the protein with inner mitochondrial membranes. Pharmacological characterization of glutamate binding to liver mitochondrial membranes revealed a pattern almost identical to that of the chloride- and calcium-dependent glutamate-binding site in rat brain
Eine gläserne Fabrik zur Produktion von Pkw-Fensterhebern - La nueva fabrica Brose SA
No full textS.269-283Im Neubau der Fensterheberfirma Brose wird die Idee des Fraktalen Unternehmens verwirklicht
Author response: Analysis of SUMO1-conjugation at synapses
No full textSUMO1-conjugation of proteins at neuronal synapses is considered to be a major post-translational regulatory process in nerve cell and synapse function, but the published evidence for SUMO1-conjugation at synapses is contradictory. We employed multiple genetic mouse models for stringently controlled biochemical and immunostaining analyses of synaptic SUMO1-conjugation. By using a knock-in reporter mouse line expressing tagged SUMO1, we could not detect SUMO1-conjugation of seven previously proposed synaptic SUMO1-targets in the brain. Further, immunostaining of cultured neurons from wild-type and SUMO1 knock-out mice showed that anti-SUMO1 immunolabelling at synapses is non-specific. Our findings indicate that SUMO1-conjugation of synaptic proteins does not occur or is extremely rare and hence not detectable using current methodology. Based on our data, we discuss a set of experimental strategies and minimal consensus criteria for the validation of SUMOylation that can be applied to any SUMOylation substrate and SUMO isoform.</jats:p
Murder on the mountain: author talk with Peter J. Wosh
No full textAuthor talk by Peter J. Wosh on May 5th, 2022, on his book, "Murder on the Mountain: crime, passion, and punishment in gilded age New Jersey.
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