β2GPI and anti-β2GPI antibodies (selected publications)

1. Kumar S, Vaid D, Lonati P, Da Via A, Tonello M, Meroni PL, Pengo V, Pozzi N. Domain and residue mapping of autoantibodies to β2GPI reveals differences among antiphospholipid syndrome phenotypes. Blood. 2025; 146 (26): 3234–3245, doi: https://doi.org/10.1182/blood.2025029488. Commentary-> Urbanus R.T. Beyond Arg39: new insights into antiphospholipid antibodies. Blood (2025) 146 (26): 3141–3143. https://doi.org/10.1182/blood.2025031543
2. Kumar S, Pozzi N. Understanding the structure of β2-glycoprotein I: new insights and future paths for antiphospholipid syndrome. Blood Vessels, Thrombosis & Hemostasis. 2025, doi: 10.1016/j.bvth.2024.100041. eCollection 2025 May.
3. Hasdemir HS, Pozzi N, Tajkhorshid E. Atomistic characterization of β2-glycoprotein I domain V interaction with anionic membranes. J Thromb Haemost. 2024 Jul 22:S1538-7836(24)00427-6. doi: 10.1016/j.jtha.2024.07.010. PMID: 39047943.
4. Taylor A, Kumar S, Pozzi N. Forecasting the Future of Antiphospholipid Syndrome: Prospects and Challenges. Missouri Medicine. 2023 Sep-Oct;120(5):359-366.
5. Kumar S, Wulf J 2nd, Basore K, Pozzi N. Structural analyses of β2-glycoprotein I: is there a circular conformation? J Thromb Haemost. 2023 Aug 1:S1538-7836(23)00579-2. Commentary-> Lancellotti S, Sacco M., De Cristofaro R. Commentary on “Structural analyses of β2-glycoprotein I: is there a circular conformation?” J Thromb Haemost. 2023 Dec;21(12):3354-3356.
6. Kumar S*, Chinnaraj M*, Planer W, Zuo X, Macor P, Tedesco F, Pozzi N. An allosteric redox switch in domain V of β2-glycoprotein I controls membrane binding and anti-domain I autoantibody recognition. J Biol Chem. 2021 Aug;297(2):100890. (* equal contribution).
7. Ruben E*, Planer W*, Chinnaraj M, Chen Z, Zuo X, Pengo V, De Filippis V, Alluri RK, McCrae KR, Macor P, Tedesco F, Pozzi N. The J-elongated conformation of β2-glycoprotein I predominates in solution: implications for our understanding of antiphospholipid syndrome. J Biol Chem. 2020 Jul 31;295(31):10794 (* equal contribution).

Prothrombin and anti-prothrombin antibodies (selected publications)

1. Pengo V, Pozzi N. Lupus anticoagulant and antiprothrombin antibodies: embracing the future. J. Thromb Haemost. 2025, Jul;23(7):2262-2269. doi: 10.1016/j.jtha.2025.03.029. Epub 2025 Apr 6.
2. Pozzi N, Pontara E, Kumar S, Pengo V. Understanding the difference between type I and type II antiprothrombin antibodies and their effect on activated protein C resistance. J Thromb Haemost. 2024 Oct;22(10):2935-2938. doi: 10.1016/j.jtha.2024.07.005. PMID: 39029741
3. Kumar S, Summers B, Basore K, Pengo V, Flaumenhaft R, Pozzi N. Cryo-EM structure and functional basis of prothrombin recognition by a Type-I anti-prothrombin antiphospholipid antibody. Blood. 2024 Feb 16:blood.2023022942. doi: 10.1182/blood.202302294. Cover and Commentary-> Urbanus R.T. Prothrombin forced into an awkward position. Blood (2024) 143 (19): 1888–1890. https://doi.org/10.1182/blood.202402424.
4. Chinnaraj M, Pengo V, Pozzi N. A Novel ELISA Assay for the Detection of Anti-Prothrombin Antibodies in Antiphospholipid Syndrome Patients at High Risk of Thrombosis. Front Immunol. 2021 Sep 8;12:741589.
5. Chinnaraj M, Planer W, Pengo V, Pozzi N. Discovery and characterization of 2 novel subpopulations of aPS/PT antibodies in patients at high risk of thrombosis. Blood Adv. 2019 Jun 11;3(11):1738-1749.
6. Chinnaraj M, Planer W, Pozzi N. Structure of Coagulation Factor II: Molecular Mechanism of Thrombin Generation and Development of Next-Generation Anticoagulants. Front Med. 2018;5:281.
7. Chinnaraj M, Chen Z, Pelc LA, Grese Z, Bystranowska D, Di Cera E, Pozzi N. Structure of prothrombin in the closed form reveals new details on the mechanism of activation. Sci Rep. 2018 Feb 13;8(1):2945.
8. Pozzi N, Bystranowska D, Zuo X, Di Cera E. Structural Architecture of Prothrombin in Solution Revealed by Single Molecule Spectroscopy. J Biol Chem. 2016 Aug 26;291(35):18107-16.

Thiol-isomerases (selected publications)

1. Ponzar N, Pagotto A, Bandyopadhayay S., Meyers M.J., De Filippis V, Flaumenhaft R, Pozzi N. Molecular determinants of allosteric modulation of protein disulfide isomerase by small-molecule b’-ligands. Redox Biol. 2026 Jan 21:90:104044. doi: 10.1016/j.redox.2026.104044. PMID: 41610518
2. Ponzar N*, Chinnaraj M*, Pagotto A, De Filippis V, Flaumenhaft R, Pozzi N. Mechanistic basis of activation and inhibition of Protein Disulfide Isomerase by allosteric antithrombotic compounds. J Thromb Haemost. 2024 Oct 23:S1538-7836(24)00625-1. doi: 10.1016/j.jtha.2024.09.036. PMID: 39454880
3. Ponzar N, Pozzi N. Probing the conformational dynamics of thiol-isomerases using non-canonical amino acids and single-molecule FRET. Methods. 2023 Apr 15;214:8-17.
4. Yang M, Chiu J, Scartelli C, Ponzar N, Patel S, Patel A, Ferreira RB, Keyes RF, Carroll K, Pozzi N, Hogg PJ, Smith BC, Flaumenhaft R. Sulfenylation links oxidative stress to protein disulfide isomerase oxidase activity and thrombus formation. J. Thromb Haemost. 2023 Apr 8:S1538-7836(23)00268-4. Commentary-> Gaspar R.S., Laurindo F.R.M. Commentary on “Sulfenylation links oxidative stress to protein disulfide isomerase oxidase activity and thrombus formation.” J Thromb Haemost. 2023 Aug; 21(8):2054-2057
5. Chinnaraj M, Flaumenhaft R, Pozzi N. Reduction of protein disulfide isomerase results in open conformations and stimulates dynamic exchange between structural ensembles. J Biol Chem. 2022 Jun 30;298(8):102217.
6. Chinnaraj M, Barrios DA, Frieden C, Heyduk T, Flaumenhaft R, Pozzi N. Bioorthogonal Chemistry Enables Single-Molecule FRET Measurements of Catalytically Active Protein Disulfide Isomerase. Chembiochem. 2021 Jan 5;22(1):134-138