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Oded Livnah

Researcher at Hebrew University of Jerusalem

Publications -  91
Citations -  5077

Oded Livnah is an academic researcher from Hebrew University of Jerusalem. The author has contributed to research in topics: Avidin & Kinase. The author has an hindex of 36, co-authored 88 publications receiving 4817 citations. Previous affiliations of Oded Livnah include Scripps Research Institute & Life Sciences Institute.

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Three-dimensional structures of avidin and the avidin-biotin complex

TL;DR: The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its complex with biotin have been determined and the amino acid residues critical for stabilization of the tetrameric assembly and for the exceptionally tight binding of biotin are revealed.
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Functional Mimicry of a Protein Hormone by a Peptide Agonist: The EPO Receptor Complex at 2.8 Å

TL;DR: The crystal structure of a complex of this agonist peptide with the extracellular domain of EPO receptor reveals that a peptide dimer induces an almost perfect twofold dimerization of the receptor, and suggests the design of nonpeptidic small molecule mimetics for EPO and other cytokines may indeed be achievable.
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Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation.

TL;DR: This model for a preformed dimer on the cell surface provides insights into the organization, activation, and plasticity of recognition of hematopoietic cell surface receptors.
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Essentials of biorecognition: the (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction.

TL;DR: This review examines the versatile avidin-biotin complex as a model system for study of the biorecognition phenomenon with respect to protein-protein, protein-peptide,protein-ligand and protein-DNA interactions.
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An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation.

TL;DR: Comparison of the biological properties of agonist and antagonist EMPs with EPO suggests that the extracellular domain orientation is tightly coupled to the cytoplasmic signaling events and provides valuable new insights into the design of synthetic ligands for EPOR and other cytokine receptors.