Intrinsic differences in the mechanisms of Tie2 binding to angiopoietins exploited by directed evolution to create an Ang2-selective ligand trap.

Bate, Neil; Lodge, James; Brindle, Nicholas P J

Bate, Neil; Lodge, James; Brindle, Nicholas P J.

Affiliation

Bate N; Department of Molecular & Cell Biology, and Department of Cardiovascular Sciences, University of Leicester, Leicester, United Kingdom.
Lodge J; Department of Molecular & Cell Biology, and Department of Cardiovascular Sciences, University of Leicester, Leicester, United Kingdom.
Brindle NPJ; Department of Molecular & Cell Biology, and Department of Cardiovascular Sciences, University of Leicester, Leicester, United Kingdom. Electronic address: npjb1@le.ac.uk.

J Biol Chem ; 297(2): 100888, 2021 08.

Article in En | MEDLINE | ID: mdl-34153320

Subject(s)

Angiopoietin-1/metabolism; Angiopoietin-2/metabolism; Directed Molecular Evolution/methods; Receptor, TIE-2/metabolism; Angiopoietin-1/chemistry; Angiopoietin-2/chemistry; Cells, Cultured; Humans; Ligands; Neovascularization, Physiologic; Protein Binding; Receptor, TIE-2/chemistry; Signal Transduction

Key words

Tie2; angiogenesis; angiopoietin; cardiovascular; directed evolution; endothelial cell; receptor

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Directed Molecular Evolution / Receptor, TIE-2 / Angiopoietin-1 / Angiopoietin-2 Limits: Humans Language: En Journal: J Biol Chem Year: 2021 Document type: Article Affiliation country: United kingdom Country of publication: United States

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