S
Serge Lissitzky
Researcher at French Institute of Health and Medical Research
Publications - 155
Citations - 5457
Serge Lissitzky is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Thyroglobulin & Thyroid. The author has an hindex of 40, co-authored 155 publications receiving 5424 citations. Previous affiliations of Serge Lissitzky include Centre national de la recherche scientifique & University of Liège.
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Purification of the human thyroid peroxidase and its identification as the microsomal antigen involved in autoimmune thyroid diseases
TL;DR: It has been demonstrated that sera with anti‐microsomal autoantibodies from patients presenting Graves' or Hashimoto's thyroiditis diseases were able to bind to purified TPO and to inhibit in a dose‐dependent manner the mAb binding to purifiedTPO, suggesting that TPO is the thyroid antigen termed to date the microsomal antigen.
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Purification of animal neurotoxins. Isolation and characterization of eleven neurotoxins from the venoms of the scorpions Androctonus australis hector, Buthus occitanus tunetanus and Leiurus quinquestriatus quinquestriatus.
TL;DR: Using the same method of purification of small molecular weight proteins worked out to obtain pure scorpion neurotoxins, four neurotoxin have been isolated from the venom of the cobra Naja haje, suggesting that each venom originating from a different sub-species has a taxonomical counterpart.
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Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA
Yves Malthièry,Serge Lissitzky +1 more
TL;DR: The mRNA encoding human thyroglobulin has been cloned and sequenced and shows an interesting homology with the acetylcholinesterase of Torpedo californica.
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The amino acid sequence of neurotoxin I of Androctonus australis hector.
TL;DR: The complete amino acid sequence of neurotoxin II of the North African scorpion Androctonus australis Hector has been determined and the complete amino acids sequence of the protein has been inferred.
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Purification and properties of the insect toxin from the venom of the scorpion Androctonus australis Hector
TL;DR: The purification of a protein toxic to insects from the venom of the scorpion Androctonus australis Hector has been performed by recycling Sephadex G-50 gel filtration and equilibrium chromatography on DEAE-SephadeX A-50 and Amberlite CG-50.