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Publications

Check out Google Scholar for a complete list of Dr Calabrese's publications and access to all articles.

If you are unable to access the full text of an article, please contact Dr Calabrese.

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2024

  • K. L. Fenn, J. E. Horne, J. A. Crossley, N. Bohringer, R. J. Horne, T. F. Schaberle, A. N. Calabrese, S. E. Radford, N. A. Ranson, Outer membrane protein assembly orchestrated by BAM-SurA complexes, Nature Commun, 2024, 15, 7612

  •  B. Schiffrin, J. A. Crossley, M. Walko, J. M. Machin, G. N. Khan, I. W. Manfield, A. J. Wilson, D. J. Brockwell, T. Fessl, A. N. Calabrese, S. E. Radford, A. Zhurvaleva, Dual client binding sites in the ATP-independent chaperone SurA, Nature Commun, 2024, 15, 8071

  •  C. M. Jones, A. Rohwedder, K. M. Suen, S. Zahed Mohajerani, A. N. Calabrese, S. Knipp, M. T. Bedford, J. E. Ladbury, Affinity purification mass spectrometry characterization of the interactome of receptor tyrosine kinase proline rich motifs in cancer, Heliyon, 2024, 10, e35480

  •  B. Schiffrin, A. N. Calabrese, Chaperones in concert: Orchestrating co-translational protein folding in the cell (article Preview), Mol Cell, 2024, 84, 2403

  •  R.-G. Xu, C. Tiede, A. N. Calabrese, L. T. Cheah, T. L. Adams, J. S. Gauer, M. S. Hindle, B. A. Webb, D. M. Yates, A. Slater, C. Duval, K. M. Naseem, A. B. Herr, D. C. Tomlinson, S. P. Watson, R. A. S. Ariëns, Affimer reagents as tool molecules to modulate platelet GPVI-ligand interactions and specifically bind GPVI dimer, Blood Advances, 2024, 8, 3917

  •  J. Santos, J. Cuellar, I. Pallarès, E. J Byrd, A. Lends, F. Moro, M. B. Abdul-Shukkoor, J. Pujols, L. Velasco-Carneros, F. Sobott, D. E. Otzen, A. N. Calabrese, A. Muga, J. Skov Pedersen, A. Loquet, J. M. Valpuesta, S. E. Radford and S. Ventura, A targetable N-terminal motif orchestrates α-Synuclein oligomer to fibril conversion, under revision at J Am Chem Soc, 2024, 146, 12702

  •  V. Krishnamoorthy, M. Foglizzo, R. L. Dilley, A. Wu, P. Dutta, L. J. Campbell, O. Degtjarik, L. J. Musgrove, A. N. Calabrese, E. Zeqiraj, R. A. Greenberg, The SPATA5-SPATA5L1 unfoldase complex directs replisome proteostasis to ensure genome integrity, Cell, 2024, 187, 2250

  •  L. Makhlouf, J. J. Peter, H. M. Magnussen, R. Thakur, D. Millrine, T. C. Minshull, G. Harrison, J. Varghese, F. Lamoliatte, M. Foglizzo, T. Macartney, A. N. Calabrese, E. Zeqiraj, Y. Kulathu, The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons, Nature, 2024, 627, 437

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2023

  • M. Dulchavsky, R. Mitra, K. Wu, J. Li, K. Boer, X. Liu, Z. Zhang, C. Vasquez, C. T. Clark, K. Funckes, K. Shankar, S. Bon-net-Zahedi, M. Siddiq, Y. Sepulveda, R. Suhandynata, J. D. Momper, A. N. Calabrese, O. George, F. Stull, J. C.A. Bardwell, Directed evolution unlocks oxygen reactivity for a nicotine degrading flavoenzyme, Nat Chem Biol, 2023, 19, 1405

  • H. Britt, R. Beveridge, A.N. Calabrese, A special issue of Essays in Biochemistry, on structural mass spectrometry, Essays in Biochemistry, 2023, 67, 147

  • F. Paoletti, S. Covaceuszach, A. Cassett, A.N. Calabrese, P. Konarev, J. Grdadolnik, D. Lamba and S. G. Grdadolnika, Conformational switching in Intrinsically Unstructured Proteins by Small Endogenous Ligands: decreased local proNGF flexibility upon ATP binding, Protein Sci, 2023, 32, e4563

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2022

  • M.J. Burke, J.N.F. Scott, T.C. Minshull, Z. Gao, I. Manfield, P.G. Stockley, A.N. Calabrese, J. Boyes, A bovine antibody possessing an ultralong complementarity-determining region CDRH3 targets a highly conserved epitope in sarbecovirus spike proteins, J. Biol. Chem., 2022, 298, 102624

  • B.J. Lane, B. Wang, Y. Ma, A.N. Calabrese, H. El Mkami, C. Pliotas, HDX-guided EPR spectroscopy to interrogate membrane protein conformational dynamics, STAR Protocols, 2022, 3, 101562

  • K. Wu, T.C. Minshull, S.E. Radford, A.N. Calabrese, J.C.A. Bardwell, Trigger factor both holds and folds its clients, Nat. Commun., 2022, 13, 4126

  • B. Schiffrin, J. Machin, T.K. Karamanos, A.E. Ashcroft, D.J. Brockwell, S.E. Radford, A.N. Calabrese, Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding, Commun. Biol., 2022, 5, 560

  • B. Wang, B. J. Lane, C. Kapsalis, J. Ault, F. Sobott, H. El Mkami, A. N. Calabrese, A. C. Kalli, C. Pliotas, Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state, Structure, 2022, 30, 608-622​

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2021

  • J. P. K. Bravo, K. Bartnik, L. Venditti, J. Acker, E. H. Gail, A. Colyer, C. Davidovich, D. C. Lamb, R. Tuma, A. N. Calabrese, A. Borodavka, Structural basis of rotavirus RNA chaperone displacement and RNA annealing, Proc Natl Acad Sci, 2021, 118, e2100198118, https://doi.org/10.1073/pnas.2100198118

  • P. White, S. F. Haysom, M.G. Iadanza, A. J. Higgins, J. M. Machin, J. M. Whitehouse, J. E. Horne, B. Schiffrin, C. Carpenter-Platt, A. N. Calabrese, K. M. Storek, S. T. Rutherford, D. J. Brockwell, N. A. Ranson, S. E. Radford, The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding, Nat. Commun, 2021, 12, 4174

  • R. Beveridge, A. N. Calabrese, Structural proteomics methods to interrogate the conformation and dynamics of intrinsically disordered proteins, Frontiers in Chemistry, 2021, https://doi.org/10.3389/fchem.2021.603639

 

​​​2020​

  • M. G. Iadanza, B. Schiffrin, P. White, M. A. Watson, J. E. Horne, A. J. Higgins, A. N. Calabrese, D. J. Brockwell, R. Tuma,  A. C. Kalli, S. E. Radford, N. A. Ranson, Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs, Commun. Biol., 2020, 3, 766

  • J. H. Tomlinson, A. P. Kalverda, A. N. Calabrese, Fusidic acid resistance through changes in the dynamics of the drug target, Proc Natl Acad Sci, 2020, 117, 25523-25531

  •  B. Schiffrin, S. E. Radford, D. J. Brockwell, A N. Calabrese, PyXlinkViewer: a flexible tool for visualisation of protein chemical crosslinking data within the PyMOL molecular graphics system, Protein Science, 2020, 29, 1851-1857

  •  R. Rodríguez-Alonso, J. Létoquart, V. S. Nguyen, G. Louis, A. N. Calabrese, S. E. Radford, S.-Y. Cho, H. Remaut, J.-F. Collet, Structural insight into the formation of lipoprotein-β-barrel complexes by the β-barrel assembly machinery, Nat. Chem Biol., 2020, 16, 1019-1025

  •  A.N. Calabrese, B. Schiffrin, M. Watson, M. Walko, J.R. Humes, T.K. Karamanos, J.E. Horne, P. White, A.C. Kalli, R. Tuma, A.E. Ashcroft, D.J. Brockwell, S.E. Radford, Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients, Nat. Commun., 2020, 11, 2155

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2011-2019​

  • T.K. Karamanos, M.P. Jackson, A.N. Calabrese, S.C. Goodchild, E.E. Cawood, G.S. Thompson, A.P. Kalverda, E.W. Hewitt, S.E. Radford, Structural mapping of oligomeric intermediates in an amyloid assembly pathway, eLife, 2019, 8:e46574

  • K. Shen, M. Gamerdinger, R. Chan, K. Gense, E. M. Martin, N. Sachs, P. D. Knight, R. Schömer, A. N. Calabrese, K. L. Stewart, L. Leiendecker, A. Baghel, S. E. Radford, J. Frydman, E. Deuerling, Dual role of ribosome-binding domain of NAC as a potent suppressor of protein aggregation and aging-related proteinopathies, Mol. Cell, 2019, 74, 729-741

  •  J. R. Humes, B. Schiffrin, A. N. Calabrese, A. J. Higgins, D. R. Westhead, D. J. Brockwell, S. E. Radford, The Role of SurA PPIase Domains in Preventing Aggregation of the Outer Membrane Proteins tOmpA and OmpT, J. Mol. Biol., 2019, 431, 1267-1283

  • J. E. Horne*, M. Walko*, A. N. Calabrese*, M. A. Levenstein, D. J. Brockwell, N. Kapur, A. J. Wilson, S. E. Radford, Rapid mapping of protein interactions using tag-transfer photocrosslinkers, Angew. Chem. Int. Ed., 2018, 57, 16688-16692

  • J. P. K. Bravo, A. Borodavka, A. Barth, A. N. Calabrese, P. Mojzes, J. J. B. Cockburn, D. C. Lamb, R. Tuma, Stability of local secondary structure determines selectivity of viral RNA chaperones, Nucleic Acids Res., 2018, 46, 7924-7937

  • A. N. Calabrese*, S. E. Radford, Mass spectrometry-enabled structural biology of membrane proteins, Methods, 2018, 147, 187-205

  • L. L. Martin, C. Kubeil, S. Piantavigna, T. Tikkoo, N. P. Gray, T. John, A. N. Calabrese, Y. Liu, Y. Hong, M. A. Hossain, N. Patil, B. Abel, R. Hoffmann, J. H. Bowie, J. A. Carver, Amyloid Aggregation and Membrane Activity of the Antimicrobial Peptide Uperin 3.5, Peptide Sci., 2018, 110:e24052

  • B. Schiffrin, A. N. Calabrese, A. J. Higgins, J. R. Humes, A. E. Ashcroft, A. C. Kalli, D. J. Brockwell, S. E. Radford, Effects of periplasmic chaperones and membrane thickness on in vitro BamA-catalysed outer membrane protein folding, J. Mol. Biol., 2017, 429, 3776-3792

  • A. N. Calabrese, S. M. Jackson, L. N. Jones, F. Heinkel, O. Beckstein, J. Gsponer, D. Sharples, M. Sans, M. Kokkinidou, A. R. Pearson, S. E. Radford, A. E. Ashcroft, P. J. F. Henderson, Topological dissection of the membrane transport protein Mhp1 derived from cysteine accessibility and mass spectrometry, Anal. Chem., 2017, 89, 8844–8852

  • P. W. A. Devine, H. C. Fisher, A. N. Calabrese, F. Whelan, D. R. Higazi, J. R. Potts, D. C. Lowe, S. E. Radford, A. E. Ashcroft, Investigating the structural compaction of biomolecules upon transition to the gas-phase using ESI-TWIMS-MS, J. Am. Soc. Mass Spectrom., 2017, 28, 1855-1862

  • T. G. Watkinson, A. N. Calabrese, J. R. Ault, S. E. Radford, A. E. Ashcroft, FPOP-LC-MS/MS suggests differences in interaction sites of amphipols and detergents with outer membrane proteins, J. Am. Soc. Mass Spectrom., 2017, 28, 50-55

  • M. G. Iadanza, A. J. Higgins, B. Schiffrin, A. N. Calabrese, D. J. Brockwell, A. E. Ashcroft, S. E. Radford, N. A. Ranson, Lateral opening of the intact β-barrel assembly machinery captured by cryo-EM, Nat. Commun., 2016, 7:12865, doi: 10.1038/ncomms12865

  • B. Schiffrin*, A.N. Calabrese*, P. Devine, S. A Harris, A. E. Ashcroft, D. J. Brockwell, S.  E. Radford, Skp is a multivalent chaperone of outer membrane proteins, Nat. Struct. Mol. Biol., 2016, 23, 786–793

  • A. N. Calabrese, Y. Liu, I. F. Musgrave, T. L. Pukala, L. L. Martin, J. A. Carver, J. H. Bowie, The amyloid fibril-forming properties of the amphibian antimicrobial peptide uperin 3.5, ChemBioChem, 2016, 17, 239-246

  • Y. Liu, T. Wang, A. N. Calabrese, J.A. Carver, S. F. Cummins, J. H. Bowie, The membrane-active amphibian peptide caerin 1.8 inhibits fibril formation of amyloid β1-42, Peptides, 2015, 73, 1-6

  • T. G. Watkinson, A. N. Calabrese, F. Giusti, M. Zoonens, S. E. Radford, A. E. Ashcroft, Systematic analysis of the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry, Int J. Mass Spectrom., 2015, 391, 54-61

  • A. N. Calabrese, J. R. Ault, S. E. Radford, A. E. Ashcroft, Using hydroxyl radical footprinting to explore the free energy landscape of protein folding, Methods, 2015, 89, 38-44

  • A. N. Calabrese, J. H. Bowie, T. L. Pukala, Structural analysis of calmodulin Binding by nNOS inhibitory amphibian peptides, Biochem., 2015, 54, 567-576

  • A. N. Calabrese, T. G. Watkinson, P. J. F. Henderson, S. E. Radford, A. E. Ashcroft, Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase, Anal. Chem., 2015, 87, 1118-1126

  • F. Giusti, J. Rieger, L. J. Catoire, S. Qian, A. N. Calabrese, T. G. Watkinson, M. Casiraghi, S. E. Radford, A. E. Ashcroft, J.-L. Popot, Synthesis, characterization and applications of a perdeuterated amphipol, J. Membrane Biol., 2014, 247, 909–924

  • Y. Liu, J. A. Carver, A. N. Calabrese, T. L. Pukala, Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation, BBA-Proteins Proteom., 2014, 1844, 1481–1485

  • A. N. Calabrese, T. L Pukala, Chemical cross-linking and mass spectrometry for the structural analysis of protein assemblies, Aust. J. Chem., 2013, 66, 749-759

  • J.M. Cottam, D.B. Scanlon, J. A. Karas, A.N. Calabrese, T.L. Pukala, B.E. Forbes, J.C. Wallace, A.D. Abell, Chemical synthesis of a fluorescent IGF-II analogue, Int. J. Pept. Res. Ther., 2013, 19, 61-69

  • A.N. Calabrese, T. Wang, J.H. Bowie, T.L. Pukala, Negative ion fragmentations of disulfide-containing cross-linking reagents are competitive with aspartic acid side chain induced cleavages, Rapid Commun. Mass Spectrom., 2013, 27, 238-248

  • A.N. Calabrese, K. Markulic, I.F. Musgrave, H. Guo, L. Zhang, J.H. Bowie, Structural and activity changes in three bioactive anuran peptides when Asp is replaced by isoAsp, Peptides, 2012, 38, 427-436

  • A.N. Calabrese, N.J. Good, T. Wang, J. He, J.H. Bowie, T.L. Pukala, A negative ion mass spectrometry approach to identify cross-linked peptides utilizing characteristic disulfide fragmentations, J. Am. Soc. Mass Spectrom., 2012, 23, 1364-1375

  • A.N. Calabrese, L.A. Speechley, T.L. Pukala, Characterisation of calmodulin structural transitions by Ion Mobility Mass Spectrometry, Aust. J. Chem., 2012, 65, 504-511

  • T. Wang, T.T.N. Tran, A.N. Calabrese, J.H. Bowie, Backbone fragmentations of [M–H]– anions from peptides. Reinvestigation of the mechanism of the beta prime cleavage, Rapid Commun. Mass Spectrom., 2012, 26, 1832-1840

  • T. Wang, H.J. Andreazza, T.L. Pukala, P.J. Sherman, A.N. Calabrese, J.H. Bowie, Histidine-containing host-defence skin peptides of anurans bind Cu2+.  An electrospray ionisation mass spectrometry and computational modelling study. Rapid Commun. Mass Spectrom., 2011, 12, 1209-1221

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