{"id":20,"date":"2015-06-23T08:36:58","date_gmt":"2015-06-23T08:36:58","guid":{"rendered":"http:\/\/springergroup.user.jacobs-university.de\/?page_id=20"},"modified":"2026-01-14T10:01:15","modified_gmt":"2026-01-14T10:01:15","slug":"20-2","status":"publish","type":"page","link":"https:\/\/pages.constructor.university\/springergroup\/20-2\/","title":{"rendered":"Publications"},"content":{"rendered":"\n

 A guided tour of our research with links to individual papers is on the Research<\/a> page.<\/p>\n\n\n\n

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Preprints<\/h3>\n\n\n\nNone currently\n\n\n\n

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Peer-Reviewed Papers<\/h3>\n\n\n\n
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Ankur Saikia, Yelyzaveta Makedon, Bianka Nagy, Sebastian Springer:
Empty MHC Class I Protein Production. <\/a>
In: Stratikos, E. (eds) Antigen Processing and Presentation. Methods in Molecular Biology<\/em>, vol 3007 (2026). Humana, New York, NY. doi: https:\/\/doi.org\/10.1007\/978-1-0716-5092-9_2 <\/a>\n

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Simone Goeppert, Sebastian Springer, and Martin Zacharias:
How conformational changes near the F pocket of MHC class I proteins mediate chaperone assisted peptide loading. <\/a>
Frontiers Immunol.<\/em> (2025). doi: https:\/\/doi.org\/10.3389\/fimmu.2025.1689803<\/a>\n<\/p>\n

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Fernando M. Ruggiero, Fran\u00e7ois-Xavier Mauvais, Ursula Wellbrock, Peter M. van Endert, Sebastian Springer:
Surface emergence and persistence of MHC class I free heavy chains. <\/a>
J.Biol.Chem<\/em> (2025). doi: https:\/\/doi.org\/10.1016\/j.jbc.2025.110799<\/a>\n<\/p>\n

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Jocky C. K. Kung, Alan K\u00e1dek, Knut K\u00f6lbel, Steffi Bandelow, Sadia Bari, Jens Buck, Carl Caleman, Jan Commandeur, Tomislav Damjanovi\u0107, Simon D\u00f6rner, Karim Fahmy, Lara Flacht, Johannes Heidemann, Khon Huynh, Janine-Denise Kopicki, Boris Krichel, Julia Lockhauserb\u00e4umer, Kristina Lorenzen, Yinfei Lu, Ronja Pogan, Jasmin Rehmann, Kira Schamoni-Kast, Lucas Schwob, Lutz Schweikhard, Sebastian Springer, Pamela H.W. Svensson, Florian Simke, Florian Trinter, Sven Toleikis, Thomas Kierspel, Charlotte Uetrecht:
X-ray Spectroscopy Meets Native Mass Spectrometry: Probing Gas-phase Protein Complexes. <\/a>
BioRxiv<\/em> (2025). doi: https:\/\/doi.org\/10.1039\/D5CP00604J<\/a>
Phys. Chem. Chem. Phys.<\/em> 27<\/b> (2025), 13234-13242.\n<\/p>\n

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Silva Z, Raba\u00e7a JA, Luz V, Louren\u00e7o RA, Salio M, Oliveira AC, Bule P, Springer S, Videira PA:
New insights into the immunomodulatory potential of sialic acid on monocyte-derived dendritic cells. <\/a>
Cancer Immunol. Immunother.<\/em> (2024). doi: https:\/\/doi.org\/10.1007\/s00262-024-03863-7<\/a>\n<\/p>\n

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Sebastian Springer and Martin Zacharias:
Peptide vaccines get an OS update. <\/a>
Nat. Chem. Biol.<\/em> (2024). doi: https:\/\/doi.org\/10.1038\/s41589-024-01608-2<\/a>\n<\/p>\n

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Katharina Hartman, Guido Steiner, Michel Siegel, Cary M Looney,\nTimothy P Hickling, Katharine Bray-French, Sebastian Springer, C\u00e9line\nMarban-Doran, Axel Ducret:
Expanding the MAPPs assay to accommodate MHC-II pan receptors for\nimproved predictability of potential T cell epitopes.<\/a>
Biology<\/em> (2023), 1265. doi: https:\/\/doi.org\/10.3390\/biology12091265y<\/a>\n<\/p>\n

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J.J.W. Kuiper, J. Prinz, E. Stratikos, P. Kusnierczyk , A. Arakawa, S. Springer, D. Mintoff, I. Padjen, R. Shumnalieva, S. Vural, I. Koetter, M. van de Sande, A. Boyvat, J.H. de Boer, N. G. Bertsias, N. de Vries, C. Krieckaert, I. Leal, N. Vidovic, I. Tutkun, H. el Khaldi Ahanach, F. Costantino, S. Glatigny, D. Mrazovac Zimak, F. Loetscher, F. Kerstens, M. Bakula, E. Viera Sousa, P. Boehm, K. Bosman, T.J. Kenna, S.J. Powis, M. Breban, A. G\u00fcl, J. Bowes, R. Lories, G. Wolbink, D. McGonagle, F. Turkstra, EULAR studygroup MHC-I-opathies:
EULAR study group on \u201cMHC-I-opathy\u201d: Crossing borders and disciplines to find evidence for a unifying concept.<\/a>
Annals of the Rheumatic Diseases<\/em> 82<\/b> (2023), 887. doi: https:\/\/doi.org\/10.1136\/ard-2022-222852<\/a>\n<\/p>\n

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Ankur Saikia, Andries Hadeler, Pranathi Prasad, Martin Zacharias, and Sebastian Springer:
Fast peptide exchange on MHC class I molecules by acidic stabilization of a peptide-empty intermediate. <\/a>
Protein Sci.<\/em> (2022). doi: https:\/\/doi.org\/10.1002\/pro.4478<\/a>\n<\/p>\n

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Andries Hadeler, Ankur Saikia, Martin Zacharias, and Sebastian Springer:
Rapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptide.<\/a>
Curr. Res. Immunol.<\/em> 3<\/b> (2022), 167. doi: https:\/\/doi.org\/10.1016\/j.crimmu.2022.08.002<\/a>\n
Video abstract on YouTube<\/a><\/b>\n<\/p>\n

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Lucy C. Walters, Daniel Rozbesky, Karl Harlos, Max Quastel, Hong Sun, Sebastian Springer, Robert P Rambo, Fiyaz Mohammed, E Yvonne Jones, Andrew J McMichael, Geraldine M. Gillespie:
Primary and secondary functions of HLA-E are determined by stability and conformation of the peptide-bound complexes.<\/a>
Cell Reports<\/em> 39<\/b> (2022), 110959. doi: https:\/\/doi.org\/10.1016\/j.celrep.2022.110959<\/a>\n<\/p>\n

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Janine-Denise Kopicki, Ankur Saikia, Stephan Niebling, Christian G\u00fcnther, Maria M. Garcia-Alai, Sebastian Springer*, Charlotte Uetrecht*:
Opening opportunities for K<\/em>d<\/sub> determination and screening of MHC peptide complexes.<\/a>
Communications Biology<\/em> 5<\/b>, 488 (2022). doi: https:\/\/doi.org\/10.1038\/s42003-022-03366-0<\/a>\n<\/p>\n

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Fernando M. Ruggiero and Sebastian Springer:
Homotypic and heterotypic in cis<\/em> associations of MHC class I molecules at the cell surface. <\/a>Review.
Curr. Res. Immunol. <\/em>3<\/b> (2022), 85-99. https:\/\/doi.org\/10.1016\/j.crimmu.2022.05.001<\/a>\n<\/p>\n

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Cindy Dirscherl, Sara Loechte, Zeynep Hein, Janine-Denise Kopicki, Antonia Regina Harders, Noemi Linden, Andreas Karner, Johannes Preiner,Julian Weghuber, Maria Garcia-Alai, Charlotte Uetrecht, Martin Zacharias, Jakob Piehler, Peter Lanzerstorfer, and Sebastian Springer:
Dissociation of \u03b22<\/sub>m from MHC Class I Triggers Formation of Noncovalent, Transient Heavy Chain Dimers.<\/a>
J. Cell Sci.<\/em> (2022), 135 (9): jcs259489.\nhttps:\/\/doi.org\/10.1242\/jcs.259498<\/a>
\nAlso on BioRxiv<\/a>.<\/p>\n

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Corinna A Kulicke, Erica De Zan, Zeynep Hein, Claudia Gonzalez-Lopez, Swapnil Ghanwat, Natacha Veerapen, Gurdyal Besra, Paul Klenerman, John C Christianson, Sebastian Springer, Sebastian Nijman, Vincenzo Cerundolo, and Mariolina Salio:
The P5-ATPase ATP13A1 modulates MR1-mediated antigen presentation.<\/a>
J. Biol. Chem.<\/em> (2021). doi: https:\/\/doi.org\/10.1016\/j.jbc.2021.101542<\/a><\/p>\n

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Alina Popa and Sebastian Springer:
Tailored nanoparticles as vaccine components.<\/a> Review.
Appl.Sci.<\/em> 11 <\/b>(2021), 11898. doi: https:\/\/doi.org\/10.3390\/app112411898<\/a><\/p>\n

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Maria Qatato, Vaishnavi Venugopalan, Alaa Al-Hashimi, Maren Rehders, Aaron D. Valentine, Zeynep Hein, Uillred Dallto, Sebastian Springer, and Klaudia Brix:
Trace amine-associated receptor 1 trafficking to cilia of thyroid epithelial cells.<\/a>
Cells<\/em> 10 <\/b>(2021), 1518. doi: https:\/\/doi.org\/10.3390\/cells10061518<\/a><\/p>\n

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Ankur Saikia and Sebastian Springer\u200b:
Peptide-MHC I complex stability measured by nanoscale differential scanning fluorimetry reveals molecular mechanism of thermal denaturation.<\/a>
Molecular Immunology<\/em> 136<\/b> (2021), p. 73-81. doi:10.1016\/j.molimm.2021.04.028<\/a><\/p>\n

See also: <\/div>\n
Sebastian Springer:
Reply to “Identification of thermodynamic quantities of the stability of peptide-MHC I complex using nanoscale differential scanning fluorimetry” by Jakob Harris and Jonghoon Kang.<\/a>
Molecular Immunology <\/em>(2021)
doi: https:\/\/doi.org\/10.1016\/j.molimm.2021.12.002<\/a><\/div>\n
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Stephan Niebling, Osvaldo Burastero\u200b, J\u00e9r\u00f4me B\u00fcrgi\u200b, Christian G\u00fcnther\u200b, Lucas A. Defelipe\u200b, Simon Sander\u200b, Ellen Gattkowski\u200b, Raghavendra Anjanappa\u200b, Matthias Wilmanns\u200b, Sebastian Springer\u200b, Henning Tidow\u200b, and Mar\u00eda Garc\u00eda-Alai\u200b:
FoldAffinity: Binding affinities from nDSF experiments.<\/a>
Scientific Reports<\/em> 5<\/b>, 9572 (2021). doi:10.1038\/s41598-021-88985-z<\/p>\n

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Natalia Lis, Zeynep Hein, Swapnil Subhash Ghanwat, Venkat Raman Ramnarayan, Benedict John Chambers, and Sebastian Springer:
The MCMV immunoevasin gp40\/m152 inhibits NKG2D receptor RAE-1\u03b3 by intracellular retention and cell surface masking.<\/a>
Journal of Cell Science<\/em> 134<\/b> (2021); doi: doi:10.1242\/jcs.257428<\/a>
Preprint at BioRxiv: doi:10.1101\/2020.11.17.386763<\/a><\/p>\n

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Nouria Jantz-Naeem and Sebastian Springer:
Venus Flytrap or Pas de Trois? The dynamics of MHC class I molecules<\/a>
Current Opinion in Immunology<\/em> 70<\/b> (2021), p. 82-9; doi:10.1016\/j.coi.2021.04.004<\/p>\n

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Alaa Al-Hashimi, Vaishnavi Venugopalan, Maren Rehders, Naphannop Sereesongsaeng, Zeynep Hein, Sebastian Springer, Ekkehard Weber, Dagmar F\u00fchrer, Matthew S. Bogyo, Christopher J. Scott, Roberta E. Burden, and Klaudia Brix:
Procathepsin V Is Secreted in a TSH Regulated Manner from Human Thyroid Epithelial Cells and Is Accessible to an Activity-Based Probe.<\/a>
International Journal of Molecular Sciences<\/em> 21<\/b> (2020), p. 9140; doi:10.3390\/ijms21239140<\/p>\n

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Alaa Al-Hashimi, Vaishnavi Venugopalan, Naphannop Sereesongsaeng, Sofia Tedelind, Alexandra M. Pinzaru, Zeynep Hein, Sebastian Springer, Ekkehard Weber, Dagmar F\u00fchrer, Christopher J. Scott, Roberta E. Burden, and Klaudia Brix:
Significance of nuclear cathepsin V in normal thyroid epithelial and carcinoma cells.<\/a>
BBA – Molecular Cell Research<\/em> 1867<\/b> (2020), p.118846; doi:10.1016\/j.bbamcr.2020.118846<\/p>\n

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Z\u00e9lia Silva, Tiago Ferro, Danielle Almeida, Helena Soares, Jos\u00e9 Alexandre Ferreira, Fanny M Deschepper, Paul J Hensbergen, Martina Pirro, Sandra J van Vliet, Sebastian Springer, and Paula A. Videira:
MHC Class I Stability is Modulated by Cell Surface Sialylation in Human Dendritic Cells.<\/a>
Pharmaceutics<\/em> 12<\/b> (2020), p.249; doi:10.3390\/pharmaceutics12030249<\/p>\n

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Raghavendra Anjanappa, Maria Garcia-Alai, Janine-Denise Kopicki, Julia Lockhauserb\u00e4umer, Mohamed Aboelmagd, Janina Hinrichs, Ioana Maria Nemtanu, Charlotte Uetrecht, Martin Zacharias, Sebastian Springer*, and Rob Meijers*:
Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection.<\/a>
Nature Communications<\/em> 11<\/b>, 1314 (2020). doi:10.1038\/s41467-020-14862-4<\/p>\n