211 research outputs found
Ceccaldi P. F. — La criminalistique
No full textLévy Claude. Ceccaldi P. F. — La criminalistique. In: Population, 18ᵉ année, n°3, 1963. pp. 613-614
André Berthelot et F. Ceccaldi. Les cartes de la Corse, de Ptolémée au XIXe siècle
No full textChapot Victor. André Berthelot et F. Ceccaldi. Les cartes de la Corse, de Ptolémée au XIXe siècle. In: Journal des savants, Avril-juin 1942. pp. 93-94
André Berthelot et F. Ceccaldi. Les cartes de la Corse, de Ptolémée au XIXe siècle
No full textChapot Victor. André Berthelot et F. Ceccaldi. Les cartes de la Corse, de Ptolémée au XIXe siècle. In: Journal des savants, Avril-juin 1942. pp. 93-94
La restitution des documents altérés
No full textChevet G., Gauvert J., Vidament Y., Ceccaldi F. La restitution des documents altérés. In: La Gazette des archives, n°61, 1968. pp. 79-99
A. Berthelot et F. Ceccaldi, Les cartes de la Corse, de Ptolémée au XIXe siècle, 1939
No full textRadet Georges. A. Berthelot et F. Ceccaldi, Les cartes de la Corse, de Ptolémée au XIXe siècle, 1939. In: Revue des Études Anciennes. Tome 43, 1941, n°3-4. pp. 310-311
Rapid binding of synapsin I to F- and G-actin A study using fluorescence resonance energy transfer
No full textAbstractSynapsin I is a nerve terminal phosphoprotein which interacts with synaptic vesicles and actin in a phosphorylation-dependent manner. By using fluorescence resonance energy transfer between purified components labeled with fluorescent probes, we now show that the binding of synapsin I to actin is a rapid phenomenon. Binding of synapsin I to actin can also be demonstrated when synaptic vesicles are present in the medium and appears to be modulated by ionic strength and synapsin I phosphorylation
Effect of Synapsin I on Actin Polymerization: Possible Involvement in the Regulation of Neurotransmitter Release
No full textEffects of synaptic vesicles on actin polymerization
No full textAbstractWe have analyzed the effects of synaptic vesicles on actin polymerization by using a time-resolved spectrofluorometric assay. We have found that synaptic vesicles have complex effects on the kinetics of actin polymerization, which vary depending on whether the synaptic vesicle-specific phosphoprotein synapsin I is absent or present on their membrane. Synapsin I bound either to synaptic vesicles or to pure phospholipid vesicles exhibits phosphorylation-dependent actin-nucleating activity. Synaptic vesicles depleted of endogenous synapsin I decrease the rate and the final extent of actin polymerization, an effect which is not observed with pure phospholipid vesicles. Thus, the state of association of synapsin I with synaptic vesicles, which is modulated by its state of phosphorylation, may affect actin assembly and the physico-chemical characteristics of the synaptic vesicle microenvironment
Fluorescence approaches to the study of the actin-nucleating and bundling activities of synapsin I.
No full textEffects of synaptic vesicles on actin polymerization
No full textWe have analyzed the effects of synaptic vesicles on actin polymerization by using a time-resolved spectrofluorometric assay. We have found that synaptic vesicles have complex effects on the kinetics of actin polymerization, which vary depending on whether the synaptic vesicle-specific phosphoprotein synapsin I is absent or present on their membrane. Synapsin I bound either to synaptic vesicles or to pure phospholipid vesicles exhibits phosphorylation-dependent actin-nucleating activity. Synaptic vesicles depleted of endogenous synapsin I decrease the rate and the final extent of actin polymerization, an effect which is not observed with pure phospholipid vesicles. Thus, the state of association of synapsin I with synaptic vesicles, which is modulated by its state of phosphorylation, may affect actin assembly and the physico-chemical characteristics of the synaptic vesicle microenvironment
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