Quantitative proteomics reveals CLR interactome in primary human cells by Manolis, D, Hasan, S, Maraveyas, A, O'Brien, DP, Kessler, BM, Kramer, H, Nikitenko, LL

Targeting the ubiquitylation and ISGylation machinery for the treatment of COVID-19 by Vere, G, Alam, MR, Farrar, S, Kealy, R, Kessler, BM, O’Brien, DP, Pinto-Fernández, A

Perceptions of a Buruli ulcer controlled human infection model: How, who, and why? by Muhi, S, Schmidt, S, Marshall, JL, O’Brien, DP, Johnson, PDR, McCarthy, JS, Jamrozik, E, Osowicki, J, Stinear, TP

Deubiquitinases in muscle physiology and disorders by Olie, CS, O'Brien, DP, Jones, HBL, Liang, Z, Damianou, A, Sur-Erdem, I, Pinto-Fernández, A, Raz, V, Kessler, BM

Structural premise of selective deubiquitinase USP30 inhibition by small-molecule benzosulfonamides by O'Brien, DP, Jones, HBL, Guenther, F, Murphy, EJ, England, KS, Anderson, M, Brennan, P, Davis, JB, Pinto-Fernandez, A, Turnbull, AP, Kessler, BM

Integrative omics reveals subtle molecular perturbations following ischemic conditioning in a porcine kidney transplant model by O’Brien, DP, Thorne, AM, Huang, H, Pappalardo, E, Yao, X, Thyrrestrup, PS, Ravlo, K, Secher, N, Norregaard, R, Ploeg, RJ, Jespersen, B, Kessler, BM

Structural premise of selective deubiquitinase USP30 inhibition by small-molecule benzosulfonamides by O’Brien, DP, Jones, HBL, Guenther, F, Murphy, EJ, England, KS, Vendrell, I, Anderson, M, Brennan, PE, Davis, JB, Pinto-Fernández, A, Turnbull, AP, Kessler, BM

Identification of high-performing antibodies for the reliable detection of Tau proteoforms by Western blotting and immunohistochemistry by Ellis, MJ, Lekka, C, Holden, KL, Tulmin, H, Seedat, F, O'Brien, DP, Dhayal, S, Zeissler, M-L, Knudsen, JG, Kessler, BM, Morgan, NG, Todd, JA, Richardson, SJ, Stefana, MI

Structural dynamics of the ubiquitin specific protease UPS30 in complex with a cyanopyrrolidine-containing covalent inhibitor by O’Brien, DP, Jones, HBL, Shi, Y, Guenther, F, Vendrell, I, Viner, R, Brennan, PE, Mead, E, Zarganes-Tzitzikas, T, Davis, JB, Pinto-Fernández, A, England, KS, Murphy, EJ, Turnbull, AP, Kessler, BM

USP16 is an ISG15 cross-reactive deubiquitinase targeting a subset of metabolic pathway-related proteins by Gan, J, Pinto-Fernandez, A, Flierman, D, Akkermans, JJLL, O'Brien, DP, Greenwood, H, Scott, HC, Neefjes, J, Fritz, G, Knobeloch, K-P, van Dam, H, Kessler, BM, Ovaa, H, Geurink, PP, Sapmaz, A

A high-affinity calmodulin-binding site in the CyaA toxin translocation domain is essential for invasion of eukaryotic cells by Voegele, A, Sadi, M, O'Brien, DP, Gehan, P, Raoux-Barbot, D, Davi, M, Hoos, S, Brûlé, S, Raynal, B, Weber, P, Mechaly, A, Haouz, A, Rodriguez, N, Vachette, P, Durand, D, Brier, S, Ladant, D, Chenal, A

Tau depletion in human neurons mitigates Aβ-driven toxicity by Ng, B, Vowles, J, Bertherat, F, Abey, A, Kilfeather, P, Beccano-Kelly, D, Stefana, MI, O’Brien, DP, Bengoa-Vergniory, N, Carling, PJ, Todd, JA, Caffrey, TM, Connor-Robson, N, Cowley, SA, Wade-Martins, R

USP16 is an ISG15 cross-reactive deubiquitinase that targets pro-ISG15 and ISGylated proteins involved in metabolism by Gan, J, Pinto-Fernández, A, Flierman, D, Akkermans, JJLL, O'Brien, DP, Greenwood, H, Scott, HC, Fritz, G, Knobeloch, K-P, Neefjes, J, van Dam, H, Ovaa, H, Ploegh, HL, Kessler, BM, Geurink, PP, Sapmaz, A

Tau filaments are tethered within brain extracellular vesicles in Alzheimer’s disease by Fowler, SL, Behr, TS, Turkes, E, Cauhy, PM, Foiani, MS, Schaler, A, Crowley, G, Bez, S, Ficulle, E, Tsefou, E, O'Brien, DP, Fischer, R, Geary, B, Gaur, P, Miller, C, D'Acunzo, P, Levy, E, Duff, KE, Ryskeldi-Falcon, B

Tau filaments are tethered within brain extracellular vesicles in Alzheimer’s disease by Fowler, SL, Behr, TS, Turkes, E, O’Brien, DP, Cauhy, PM, Rawlinson, I, Edmonds, M, Foiani, MS, Schaler, A, Crowley, G, Bez, S, Ficulle, E, Tsefou, E, Fischer, R, Geary, B, Gaur, P, Miller, C, D’Acunzo, P, Levy, E, Duff, KE, Ryskeldi-Falcon, B

A systems-based approach to uterine fibroids identifies differential splicing associated with abnormal uterine bleeding by Wang, CY, Philpott, M, O’Brien, DP, Ndungu, A, Malzahn, J, Maritati, M, Mehta, N, Gamble, V, Martinez-Burgo, B, Bonham, S, Fischer, R, Garbutt, K, Becker, CM, Manek, S, Harris, AL, Sacher, F, Obendorf, M, Schmidt, N, Mueller, J, Zollner, T, Zondervan, KT, Kessler, BM, Oppermann, U, Cribbs, AP