Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ. Mol Cell Proteomics. 2021;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06. PMID: 33964423
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ. Mol Cell Proteomics. 2021;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06. PMID: 33964423
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ. Mol Cell Proteomics. 2021 May 06;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06. PMID: 33964423
Correction: α2-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester. Harwood SL, Nielsen NS, Jensen KT, Nielsen PK, Thøgersen IB, Enghild JJ. J Biol Chem. 2021 Jan-Jun;296:100208. doi: 10.1016/j.jbc.2020.100208. Epub 2021 Feb 10. PMID: 33837737