Dini Chillet

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A monoclonal antibody (GT335) directed against polyglutamylated tubulin was obtained by immunization with a synthetic peptide which mimics the structure of the polyglutamylated site of alpha-tubulin. This peptide corresponds to the C-terminal sequence Glu441-Gly448 and was chemically modified by the addition of two glutamyl units at Glu445. The specificity(More)
Polyglutamylation, a posttranslational modification which consists of the sequential addition of one to six glutamyl units in the carboxy-terminal domain of both tubulin subunits, is a major event in neurons. Its structure has been investigated by using monoreactive polyclonal antibodies directed against distinct glutamylation motifs, ie alpha- and(More)
Anatomic tissue atlases of the brain are widely used within the medical world and are important for identifying tissue and structural aberrations and inconsistencies within an individual. Unfortunately, there are many procedures and diseases that require examination of the brain’s vascular system, which is not easily identifiable in anatomic atlases. We(More)
We have developed a method for forming vascular atlases using vascular distance maps and a novel vascular model-to-image registration method. Our atlas formation process begins with MR or CT angiogram data from a set of subjects. We extract blood vessels from those data using our tubular object segmentation method. One subject’s vascular network model is(More)
The production and identification of a monoclonal antibody, 111 B52 C2, raised against fragments obtained after limited proteolysis of purified tubulin is described. The recognized epitope is located on the aminoterminal domain of the alpha-tubulin subunit and differs from the antigenic sites reacting with the presently existing panel of available(More)
Tubulin from the central nervous system of the Quail (Coturnix coturnix japonica) was analysed by two-dimensional gel electrophoresis. Either in soluble extracts or in tubulin enriched fractions, tubulin of forebrain, cerebellum and spinal cord is resolved into 3 components alpha, beta' and beta, characterized by their electrophoretic coordinates (alpha: pI(More)
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