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Dr. J. (Joost) Snijder

Universitair docent 
Bètawetenschappen
Scheikunde
Biomolecular Sciences
Biomol.Mass Spectrometry & Proteom.
Biomol.Mass Spectrometry & Proteom.

Dr. J. (Joost) Snijder

Universitair docent
Biomol.Mass Spectrometry & Proteom.
j.snijder@uu.nl
Profiel Publicaties Onderwijs Contact
Profiel Publicaties Onderwijs Contact
Expertises
Onderzoeksthema's

Publicaties

2024

Wetenschappelijke publicaties

Beugelink, J. W., Sweep, E., Janssen, B. J. C., Snijder, J., & Pronker, M. F. (2024). Structural basis for recognition of the FLAG-tag by anti-FLAG M2. bioRxiv. https://doi.org/10.1101/2024.03.25.586599
https://dspace.library.uu.nl/bitstream/handle/1874/438010/2024.03.25.586599v2.full.pdf?sequence=1
Peng, W., Giesbers, K., Siborova, M., Beugelink, W., Pronker, M., Schulte, D., Hilkens, J., Janssen, B., Strijbis, K., & Snijder, J. (2024). Reverse-engineering the anti-MUC1 antibody 139H2 by mass spectrometry–based de novo sequencing. Life Science Alliance, 7(6), Article e202302366. https://doi.org/10.26508/lsa.202302366
https://dspace.library.uu.nl/bitstream/handle/1874/437699/e202302366.full.pdf?sequence=1
Kaiser, F. K., Hernandez, M. G., Krüger, N., Englund, E., Du, W., Mykytyn, A. Z., Raadsen, M. P., Lamers, M. M., Rodrigues Ianiski, F., Shamorkina, T. M., Snijder, J., Armando, F., Beythien, G., Ciurkiewicz, M., Schreiner, T., Gruber-Dujardin, E., Bleyer, M., Batura, O., Erffmeier, L., ... Osterhaus, A. D. M. E. (2024). Filamentous fungus-produced human monoclonal antibody provides protection against SARS-CoV-2 in hamster and non-human primate models. Nature Communications, 15(1), Article 2319. https://doi.org/10.1038/s41467-024-46443-0
https://dspace.library.uu.nl/bitstream/handle/1874/436997/s41467-024-46443-0.pdf?sequence=1
Chataigner, L. M. P., Thärichen, L., Beugelink, J. W., Granneman, J. C. M., Mokiem, N. J., Snijder, J., Förster, F., & Janssen, B. J. C. (2024). Contactin 2 homophilic adhesion structure and conformational plasticity. Structure, 32(1), 60-73.e5. https://doi.org/10.1016/j.str.2023.10.012
https://dspace.library.uu.nl/bitstream/handle/1874/437548/mmc2_1_.pdf?sequence=1
Bondt, A., Hoek, M., Dingess, K., Tamara, S., de Graaf, B., Peng, W., den Boer, M. A., Damen, M., Zwart, C., Barendregt, A., van Rijswijck, D. M. H., Schulte, D., Grobben, M., Tejjani, K., van Rijswijk, J., Völlmy, F., Snijder, J., Fortini, F., Papi, A., ... Heck, A. J. R. (2024). Into the dark serum proteome: personalized features of IgG1 and IgA1 repertoires in severe COVID-19 patients. Molecular and Cellular Proteomics, 23(1), 100690. Article 100690. https://doi.org/10.1016/j.mcpro.2023.100690
https://dspace.library.uu.nl/bitstream/handle/1874/434962/PIIS1535947623002013.pdf?sequence=1

2023

Wetenschappelijke publicaties

Peng, W., Giesbers, K. C. A. P., Šiborová, M., Beugelink, J. W., Pronker, M. F., Schulte, D., Hilkens, J., Janssen, B. J. C., Strijbis, K., & Snijder, J. (2023). Reverse engineering the anti-MUC1 hybridoma antibody 139H2 by mass spectrometry-based de novo sequencing. bioRxiv. https://doi.org/10.1101/2023.07.05.547778
https://dspace.library.uu.nl/bitstream/handle/1874/436026/2023.07.05.547778v1.full.pdf?sequence=1
Pronker, M. F., Creutznacher, R., Drulyte, I., Hulswit, R. J. G., Li, Z., van Kuppeveld, F. J. M., Snijder, J., Lang, Y., Bosch, B.-J., Boons, G.-J., Frank, M., de Groot, R. J., & Hurdiss, D. L. (2023). Sialoglycan binding triggers spike opening in a human coronavirus. Nature, 624(7990), 201-206. https://doi.org/10.1038/s41586-023-06599-z
https://dspace.library.uu.nl/bitstream/handle/1874/434377/s41586-023-06599-z.pdf?sequence=1
Yin, V., Devine, P. W. A., Saunders, J. C., Barendregt, A., Cusdin, F., Ristani, A., Hines, A., Shepherd, S., Dembek, M., Dobson, C. L., Snijder, J., Bond, N. J., & Heck, A. J. R. (2023). Stochastic assembly of biomacromolecular complexes: impact and implications on charge interpretation in native mass spectrometry. Chemical Science, 14(35), 9316-9327. https://doi.org/10.1039/d3sc03228k
https://dspace.library.uu.nl/bitstream/handle/1874/434369/d3sc03228k.pdf?sequence=1
Thijssen, V., Hurdiss, D. L., Debski-Antoniak, O. J., Spence, M. A., Franck, C., Norman, A., Aggarwal, A., Mokiem, N. J., Dongen, D. A. A. V., Vermeir, S. W., Liu, M., Li, W., Chatziandreou, M., Donselaar, T., Du, W., Drulyte, I., Bosch, B.-J., Snijder, J., Turville, S., ... Jongkees, S. A. K. (2023). A broad-spectrum macrocyclic peptide inhibitor of the SARS-CoV-2 spike protein. (pp. 1-27). bioRxiv. https://doi.org/10.1101/2022.11.11.516114
Peng, W., den Boer, M. A., Tamara, S., Mokiem, N. J., van der Lans, S. P. A., Bondt, A., Schulte, D., Haas, P.-J., Minnema, M. C., Rooijakkers, S. H. M., van Zuilen, A. D., Heck, A. J. R., & Snijder, J. (2023). Direct Mass Spectrometry-Based Detection and Antibody Sequencing of Monoclonal Gammopathy of Undetermined Significance from Patient Serum: A Case Study. Journal of Proteome Research, 22(9), 3022-3028. https://doi.org/10.1021/acs.jproteome.3c00330
https://dspace.library.uu.nl/bitstream/handle/1874/434237/peng-et-al-2023-direct-mass-spectrometry-based-detection-and-antibody-sequencing-of-monoclonal-gammopathy-of.pdf?sequence=1
Spruit, C. M., Sweet, I. R., Maliepaard, J. C. L., Bestebroer, T., Lexmond, P., Qiu, B., Damen, M. J. A., Fouchier, R. A. M., Reiding, K. R., Snijder, J., Herfst, S., Boons, G.-J., & de Vries, R. P. (2023). Contemporary human H3N2 influenza a viruses require a low threshold of suitable glycan receptors for efficient infection. Glycobiology, 33(10), 784–800. https://doi.org/10.1093/glycob/cwad060
Thijssen, V., Hurdiss, D. L., Debski-Antoniak, O. J., Spence, M. A., Franck, C., Norman, A., Aggarwal, A., Mokiem, N. J., van Dongen, D. A. A., Vermeir, S. W., Liu, M., Li, W., Chatziandreou, M., Donselaar, T., Du, W., Drulyte, I., Bosch, B.-J., Snijder, J., Turville, S. G., ... Jongkees, S. A. K. (2023). A broad-spectrum macrocyclic peptide inhibitor of the SARS-CoV-2 spike protein. Proceedings of the National Academy of Sciences of the United States of America, 120(26), Article e2303292120. https://doi.org/10.1073/pnas.2303292120

2022

Wetenschappelijke publicaties

Yin, V., Devine, P. W. A., Saunders, J. C., Hines, A., Shepherd, S., Dembek, M., Dobson, C. L., Snijder, J., Bond, N. J., & Heck, A. J. R. (2022). Spectral Interferences Impede the High-Resolution Mass Analysis of Recombinant Adeno-Associated Viruses. bioRxiv. https://doi.org/10.1101/2022.08.27.505551
Spruit, C. M., Sweet, I. R., Bestebroer, T., Lexmond, P., Qiu, B., Damen, M. J. A., Fouchier, R. A. M., Snijder, J., Herfst, S., Boons, G.-J., & Vries, R. P. D. (2022). Contemporary human H3N2 influenza A viruses require a low threshold of suitable glycan receptors for efficient infection. (pp. 1-48). bioRxiv. https://doi.org/10.1101/2022.11.16.516725
https://dspace.library.uu.nl/bitstream/handle/1874/426440/2022.11.16.516725v1.full.pdf?sequence=1
Schulte, D., Peng, W., & Snijder, J. (2022). Template-Based Assembly of Proteomic Short Reads For De Novo Antibody Sequencing and Repertoire Profiling: Analytical Chemistry. Industrial And Engineering Chemistry Analytical Edition, 94(29), 10391-10399. https://doi.org/10.1021/acs.analchem.2c01300
Pascha, M. N., Thijssen, V., Egido, J. E., Linthorst, M. W., van Lanen, J. H., van Dongen, D. A. A., Hopstaken, A. J. P., van Kuppeveld, F. J. M., Snijder, J., de Haan, C. A. M., & Jongkees, S. A. K. (2022). Inhibition of H1 and H5 Influenza A Virus Entry by Diverse Macrocyclic Peptides Targeting the Hemagglutinin Stem Region: ACS Chemical Biology. ACS Chemical Biology, 17(9), 2425-2436. https://doi.org/10.1021/acschembio.2c00040
Peng, W., Rayaprolu, V., Parvate, A. D., Pronker, M. F., Hui, S., Parekh, D., Shaffer, K., Yu, X., Saphire, E. O., & Snijder, J. (2022). Glycan shield of the ebolavirus envelope glycoprotein GP. Communications Biology, 5(1), 1-11. Article 785. https://doi.org/10.1038/s42003-022-03767-1
Wang, C., Hesketh, E. L., Shamorkina, T. M., Li, W., Franken, P. J., Drabek, D., van Haperen, R., Townend, S., van Kuppeveld, F. J. M., Grosveld, F., Ranson, N. A., Snijder, J., de Groot, R. J., Hurdiss, D. L., & Bosch, B.-J. (2022). Antigenic structure of the human coronavirus OC43 spike reveals exposed and occluded neutralizing epitopes. Nature Communications, 13(1), 1-15. Article 2921. https://doi.org/10.1038/s41467-022-30658-0
Wörner, T. P., Aizikov, K., Snijder, J., Fort, K. L., Makarov, A. A., & Heck, A. J. R. (2022). Frequency chasing of individual megadalton ions in an Orbitrap analyser improves precision of analysis in single-molecule mass spectrometry. Nature Chemistry, 14(5), 515-522. https://doi.org/10.1038/s41557-022-00897-1
Hurdiss, D. L., El Kazzi, P., Bauer, L., Papageorgiou, N., Ferron, F. P., Donselaar, T., Van Vliet, A. L. W., Shamorkina, T. M., Snijder, J., Canard, B., Decroly, E., Brancale, A., Zeev-Ben-Mordehai, T., Förster, F., Van Kuppeveld, F. J. M., & Coutard, B. (2022). Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes a ring-shaped hexameric complex. Science advances, 8(1), 1-12. Article abj7615. https://doi.org/10.1126/sciadv.abj7615
Wörner, T. P., Snijder, J., Friese, O., Powers, T., & Heck, A. J. R. (2022). Assessment of genome packaging in AAVs using Orbitrap-based charge-detection mass spectrometry. Molecular Therapy - Methods and Clinical Development, 24, 40-47. https://doi.org/10.1016/j.omtm.2021.11.013

2021

Wetenschappelijke publicaties

Olmedillas, E., Mann, C. J., Peng, W., Wang, Y.-T., Avalos, R. D., Bedinger, D., Valentine, K., Shafee, N., Schendel, S. L., Yuan, M., Lang, G., Rouet, R., Christ, D., Jiang, W., Wilson, I. A., Germann, T., Shresta, S., Snijder, J., & Saphire, E. O. (2021). Structure-based design of a highly stable, covalently-linked SARS-CoV-2 spike trimer with improved structural properties and immunogenicity. (pp. 1-51). bioRxiv. https://doi.org/10.1101/2021.05.06.441046
Almendral, J. M., Asokan, A., Berns, K. I., Chapman, M., Chatterjee, S., Chiorini, J., Flotte, T., Gao, G., Grimm, D., Hauswirth, W., Heilbronn, R., Kleinschmidt, J., Kotin, R., Lisowski, L., Logan, G., Alexander, I., Long, J., Lyumkis, D., Nathwani, A., ... Wilson, J. (2021). TRIBUTE TO MAVIS AGBANDJE-MCKENNA A Beautiful Mind and the Heart of an Explorer. Human Gene Therapy, 32(7-8), 321-326. https://doi.org/10.1089/hum.2021.29158.mam
Dudas, G., Hong, S. L., Potter, B. I., Calvignac-Spencer, S., Niatou-Singa, F. S., Tombolomako, T. B., Fuh-Neba, T., Vickos, U., Ulrich, M., Leendertz, F. H., Khan, K., Huber, C., Watts, A., Olendraitė, I., Snijder, J., Wijnant, K. N., Bonvin, A. M. J. J., Martres, P., Behillil, S., ... Baele, G. (2021). Emergence and spread of SARS-CoV-2 lineage B.1.620 with variant of concern-like mutations and deletions. Nature Communications, 12(1), 1-12. Article 5769. https://doi.org/10.1038/s41467-021-26055-8
Bondt, A., Hoek, M., Tamara, S., de Graaf, B., Peng, W., Schulte, D., van Rijswijck, D. M. H., den Boer, M. A., Greisch, J.-F., Varkila, M. R. J., Snijder, J., Cremer, O. L., Bonten, M. J. M., & Heck, A. J. R. (2021). Human plasma IgG1 repertoires are simple, unique, and dynamic. Cell Systems, 12(12), 1131-1143.e5. https://doi.org/10.1016/j.cels.2021.08.008
Peng, W., Pronker, M. F., & Snijder, J. (2021). Mass Spectrometry-Based De Novo Sequencing of Monoclonal Antibodies Using Multiple Proteases and a Dual Fragmentation Scheme. Journal of Proteome Research, 20(7), 3559-3566. https://doi.org/10.1021/acs.jproteome.1c00169
Wörner, T. P., Bennett, A., Habka, S., Snijder, J., Friese, O., Powers, T., Agbandje-McKenna, M., & Heck, A. J. R. (2021). Adeno-associated virus capsid assembly is divergent and stochastic. Nature Communications, 12(1), 1-9. Article 1642. https://doi.org/10.1038/s41467-021-21935-5
Bouwman, K., Tomris, I., Turner, H. L., van der Woude, R., Shamorkina, T., Bosman, G., Rockx, B., Herfst, S., Snijder, J., Haagmans, B. L., Ward, A. B., Boons, G.-J., & de Vries, R. (2021). Multimerization- and glycosylation-dependent receptor binding of SARS-CoV-2 spike proteins. PLoS Pathogens, 17(2), Article e1009282. https://doi.org/10.1371/journal.ppat.1009282
Wörner, T. P., Shamorkina, T. M., Snijder, J., & Heck, A. J. R. (2021). Mass Spectrometry-Based Structural Virology. Analytical Chemistry, 93(1), 620-640. https://doi.org/10.1021/acs.analchem.0c04339

2020

Wetenschappelijke publicaties

Wörner, T. P., Snijder, J., Bennett, A., Agbandje-McKenna, M., Makarov, A. A., & Heck, A. J. R. (2020). Resolving heterogeneous macromolecular assemblies by Orbitrap-based single-particle charge detection mass spectrometry. Nature Methods, 17(4), 395-398. https://doi.org/10.1038/s41592-020-0770-7
Hurdiss, D. L., Drulyte, I., Lang, Y., Shamorkina, T. M., Pronker, M. F., van Kuppeveld, F. J. M., Snijder, J., & de Groot, R. J. (2020). Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans. Nature Communications, 11(1), 1-10. Article 4646. https://doi.org/10.1038/s41467-020-18440-6
Snijder, J., & Axmann, I. M. (2020). The Kai-protein clock-keeping track of Cyanobacteria's daily life. Sub-Cellular Biochemistry, 93, 359-391. https://doi.org/10.1007/978-3-030-28151-9_12

2019

Wetenschappelijke publicaties

Walls, A. C., Tortorici, M. A., Xiong, X., Snijder, J., Frenz, B., Bosch, B.-J., DiMaio, F., Corti, D., Rey, F. A., & Veesler, D. (2019). Structural Studies of Coronavirus Fusion Proteins. Microscopy and Microanalysis, 25(S2), 1300-1301. https://doi.org/10.1017/s1431927619007232
Dang, H. V., Chan, Y. P., Park, Y. J., Snijder, J., Da Silva, S. C., Vu, B., Yan, L., Feng, Y. R., Rockx, B., Geisbert, T. W., Mire, C. E., Broder, C. C., & Veesler, D. (2019). An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections. Nature Structural and Molecular Biology, 26(10), 980-987. https://doi.org/10.1038/s41594-019-0308-9
Masson, G. R., Burke, J. E., Ahn, N. G., Anand, G. S., Borchers, C., Brier, S., Bou-Assaf, G. M., Engen, J. R., Englander, S. W., Faber, J., Garlish, R., Griffin, P. R., Gross, M. L., Guttman, M., Hamuro, Y., Heck, A. J. R., Houde, D., Iacob, R. E., Jørgensen, T. J. D., ... Rand, K. D. (2019). Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments. Nature Methods, 16(7), 595-602. https://doi.org/10.1038/s41592-019-0459-y
Marcandalli, J., Fiala, B., Ols, S., Perotti, M., de van der Schueren, W., Snijder, J., Hodge, E., Benhaim, M., Ravichandran, R., Carter, L., Sheffler, W., Brunner, L., Lawrenz, M., Dubois, P., Lanzavecchia, A., Sallusto, F., Lee, K. K., Veesler, D., Correnti, C. E., ... King, N. P. (2019). Induction of Potent Neutralizing Antibody Responses by a Designed Protein Nanoparticle Vaccine for Respiratory Syncytial Virus. Cell, 176(6), 1420-1431. https://doi.org/10.1016/j.cell.2019.01.046
Walls, A. C., Xiong, X., Park, Y. J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., Zambon, M., Rey, F. A., Corti, D., & Veesler, D. (2019). Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion. Cell, 176(5), 1026-1039. https://doi.org/10.1016/j.cell.2018.12.028

2018

Wetenschappelijke publicaties

Borst, A. J., Weidle, C. E., Gray, M. D., Frenz, B., Snijder, J., Joyce, M. G., Georgiev, I. S., Stewart-Jones, G. B. E., Kwong, P. D., McGuire, A. T., Dimaio, F., Stamatatos, L., Pancera, M., & Veesler, D. (2018). Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer and a glycosylated HIV-1 gp120 core. eLife, 7, Article e37688. https://doi.org/10.7554/eLife.37688
Snijder, J., Ortego, M. S., Weidle, C., Stuart, A. B., Gray, M. D., McElrath, M. J., Pancera, M., Veesler, D., & McGuire, A. T. (2018). An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus. Immunity, 48(4), 799-811. https://doi.org/10.1016/j.immuni.2018.03.026
Sigmund, F., Massner, C., Erdmann, P., Stelzl, A., Rolbieski, H., Desai, M., Bricault, S., Wörner, T. P., Snijder, J., Geerlof, A., Fuchs, H., Hrabĕ de Angelis, M., Heck, A. J. R., Jasanoff, A., Ntziachristos, V., Plitzko, J., & Westmeyer, G. G. (2018). Bacterial encapsulins as orthogonal compartments for mammalian cell engineering. Nature Communications, 9(1), Article 1990. https://doi.org/10.1038/s41467-018-04227-3
Xiong, X., Tortorici, M. A., Snijder, J., Yoshioka, C., Walls, A. C., Li, W., McGuire, A. T., Rey, F. A., Bosch, B.-J., & Veesler, D. (2018). Glycan shield and fusion activation of a deltacoronavirus spike glycoprotein fine-tuned for enteric infections. Journal of Virology, 92(4), Article e06128-17. https://doi.org/10.1128/JVI.01628-17

2017

Wetenschappelijke publicaties

Snijder, J., Borst, A. J., Dosey, A., Walls, A. C., Burrell, A., Reddy, V. S., Kollman, J. M., & Veesler, D. (2017). Vitrification after multiple rounds of sample application and blotting improves particle density on cryo-electron microscopy grids. Journal of Structural Biology, 198(1), 38-42. https://doi.org/10.1016/j.jsb.2017.02.008
Walls, A. C., Tortorici, M. A., Snijder, J., Xiong, X., Bosch, B.-J., Rey, F. A., & Veesler, D. (2017). Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proceedings of the National Academy of Sciences of the United States of America, 114(42), 11157-11162. https://doi.org/10.1073/pnas.1708727114
Rodenburg, R. N. P., Snijder, J., van de Waterbeemd, M., Schouten, A., Granneman, J., Heck, A. J. R., & Gros, P. (2017). Stochastic palmitoylation of accessible cysteines in membrane proteins revealed by native mass spectrometry. Nature Communications, 8(1), Article 1280. https://doi.org/10.1038/s41467-017-01461-z
Snijder, J., Radtke, K., Anderson, F., Scholtes, L., Corradini, E., Baines, J., Heck, A. J. R., Wuite, G. J. L., Sodeik, B., & Roos, W. H. (2017). The vertex specific proteins pUL17 and pUL25 mechanically reinforce Herpes Simplex Virus capsids. Journal of Virology, 91(10). https://doi.org/10.1128/JVI.00123-17
van de Waterbeemd, M., Llauró, A., Snijder, J., Valbuena, A., Rodríguez-Huete, A., Fuertes, M. A., de Pablo, P. J., Mateu, M. G., & Heck, A. J. R. (2017). Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS. Biophysical Journal, 112(6), 1157-1165. https://doi.org/10.1016/j.bpj.2017.02.003
Snijder, J., Schuller, J. M., Wiegard, A., Lössl, P., Schmelling, N., Axmann, I. M., Plitzko, J. M., Förster, F., & Heck, A. J. R. (2017). Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state. Science, 355(6330), 1181-1184. https://doi.org/10.1126/science.aag3218
https://dspace.library.uu.nl/bitstream/handle/1874/348439/1181.full.pdf?sequence=1

2016

Wetenschappelijke publicaties

Kononova, O., Snijder, J., Kholodov, Y., Marx, K. A., Wuite, G. J. L., Roos, W. H., & Barsegov, V. (2016). Fluctuating Nonlinear Spring Model of Mechanical Deformation of Biological Particles. PLoS Computational Biology, 12(1), Article e1004729. https://doi.org/10.1371/journal.pcbi.1004729
Pronker, M. F., Lemstra, S., Snijder, J., Heck, A. J. R., Thies - Weesie, D., Pasterkamp, R. J., & Janssen, B. J. C. (2016). Structural basis of myelin-associated glycoprotein adhesion and signalling. Nature Communications, 7, 1-13. Article 13584. https://doi.org/10.1038/ncomms13584
Walls, A. C., Tortorici, M. A., Frenz, B., Snijder, J., Li, W., Rey, F. A., DiMaio, F., Bosch, B.-J., & Veesler, D. (2016). Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy. Nature Structural and Molecular Biology, 23(10), 899-905. https://doi.org/10.1038/nsmb.3293
Snijder, J., Kononova, O., Barbu, I. M., Uetrecht, C., Rurup, W. F., Koay, M. S. T., Burnley, R. J., Cornelissen, J. J. L. M., Roos, W. H., Barsegov, V., Wuite, G. J. L., & Heck, A. J. R. (2016). Assembly and Mechanical Properties of the Cargo-Free and Cargo-Loaded Bacterial Nanocompartment Encapsulin. Biomacromolecules, 17(8), 2522–2529. https://doi.org/10.1021/acs.biomac.6b00469
https://dspace.library.uu.nl/bitstream/handle/1874/335944/Assembly.pdf?sequence=1
van de Waterbeemd, M., Snijder, J., Tsvetkova, I. B., Dragnea, B. G., Cornelissen, J. J., & Heck, A. J. R. (2016). Examining the Heterogeneous Genome Content of Multipartite Viruses BMV and CCMV by Native Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 27(6), 1000-1009. https://doi.org/10.1007/s13361-016-1348-6

2015

Wetenschappelijke publicaties

Snijder, J., Van De Waterbeemd, M., Glover, M. S., Shi, L., Clemmer, D. E., & Heck, A. J. R. (2015). Conformational landscape and pathway of disulfide bond reduction of human alpha defensin. Protein Science, 24(8), 1264-1271. https://doi.org/10.1002/pro.2694
https://dspace.library.uu.nl/bitstream/handle/1874/323081/conformational.pdf?sequence=1
Snijder, J. (2015). Extending the boundaries of native mass spectrometry to study virus structure and assembly. [Doctoral thesis 1 (Research UU / Graduation UU), Universiteit Utrecht]. Utrecht Universiry.
https://dspace.library.uu.nl/bitstream/handle/1874/319575/Snijder.pdf?sequence=1

2014

Wetenschappelijke publicaties

Luque, D., De La Escosura, A., Snijder, J., Brasch, M., Burnley, R. J., Koay, M. S. T., Carrascosa, J. L., Wuite, G. J. L., Roos, W. H., Heck, A. J. R., Cornelissen, J. J. L. M., Torres, T., & Castón, J. R. (2014). Self-assembly and characterization of small and monodisperse dye nanospheres in a protein cage. Chemical Science, 5(2), 575-581. https://doi.org/10.1039/c3sc52276h
Veesler, D., Khayat, R., Krishnamurthy, S., Snijder, J., Huang, R. K., Heck, A. J. R., Anand, G. S., & Johnson, J. E. (2014). Architecture of a dsDNA viral capsid in complex with its maturation protease. Structure, 22(2), 230-7. https://doi.org/10.1016/j.str.2013.11.007
Snijder, J., Burnley, R. J., Wiegard, A., Melquiond, A. S. J., Bonvin, A. M. J. J., Axmann, I. M., & Heck, A. J. R. (2014). Insight into cyanobacterial circadian timing from structural details of the KaiB-KaiC interaction. Proceedings of the National Academy of Sciences of the United States of America, 111(4), 1379-84. https://doi.org/10.1073/pnas.1314326111
Rurup, W. F., Snijder, J., Koay, M. S. T., Heck, A. J. R., & Cornelissen, J. J. L. M. (2014). Self-sorting of foreign proteins in a bacterial nanocompartment. Journal of the American Chemical Society, 136(10), 3828-32. https://doi.org/10.1021/ja410891c
Benevento, M., Di Palma, S., Snijder, J., Moyer, C. L., Reddy, V. S., Nemerow, G. R., & Heck, A. J. R. (2014). Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics. Journal of Biological Chemistry, 289(16), 11421-30. https://doi.org/10.1074/jbc.M113.537498
Snijder, J., Benevento, M., Moyer, C. L., Reddy, V., Nemerow, G. R., & Heck, A. J. R. (2014). The cleaved N-terminus of pVI binds peripentonal hexons in mature adenovirus. Journal of Molecular Biology, 426(9), 1971-9. https://doi.org/10.1016/j.jmb.2014.02.022
Lössl, P., Snijder, J., & Heck, A. J. R. (2014). Boundaries of mass resolution in native mass spectrometry. Journal of the American Society for Mass Spectrometry, 25(6), 906-17. https://doi.org/10.1007/s13361-014-0874-3
Snijder, J., van de Waterbeemd, M., Damoc, E., Denisov, E., Grinfeld, D., Bennett, A., Agbandje-McKenna, M., Makarov, A., & Heck, A. J. R. (2014). Defining the stoichiometry and cargo load of viral and bacterial nanoparticles by Orbitrap mass spectrometry. Journal of the American Chemical Society, 136(20), 7295-9. https://doi.org/10.1021/ja502616y
Snijder, J., & Heck, A. J. R. (2014). Analytical approaches for size and mass analysis of large protein assemblies. Annual review of analytical chemistry (Palo Alto, Calif.), 7, 43-64. https://doi.org/10.1146/annurev-anchem-071213-020015

2013

Wetenschappelijke publicaties

Kononova, O., Snijder, J., Brasch, M., Cornelissen, J., Dima, R. I., Marx, K. A., Wuite, G. J. L., Roos, W. H., & Barsegov, V. (2013). Structural transitions and energy landscape for cowpea chlorotic mottle virus capsid mechanics from nanomanipulation in vitro and in silico. Biophysical Journal, 105(8), 1893-1903. https://doi.org/10.1016/j.bpj.2013.08.032
Snijder, J., Reddy, V. S., May, E. R., Roos, W. H., Nemerow, G. R., & Wuite, G. J. L. (2013). Integrin and defensin modulate the mechanical properties of adenovirus. Journal of Virology, 87(5), 2756-2766. https://doi.org/10.1128/JVI.02516-12
Snijder, J., Rose, R. J., Veesler, D., Johnson, J. A., & Heck, A. J. R. (2013). Studying 18 MDa Virus Assemblies with Native Mass Spectrometry. Angewandte Chemie-International Edition, 52(14), 4020-4023. https://doi.org/10.1002/anie.201210197
Snijder, J., Uetrecht, C., Rose, R. J., Sanchez-Eugenia, R., Marti, G. A., Agirre, J., Guérin, D. M. A., Wuite, G. J. L., Heck, A. J. R., & Roos, W. H. (2013). Probing the biophysical interplay between a viral genome and its capsid. Nature Chemistry, 5, 502-509. https://doi.org/10.1038/nchem.1627

2012

Wetenschappelijke publicaties

Snijder, J., Ivanovska, I. L., Baclayon, M., Roos, W. H., & Wuite, G. J. L. (2012). Probing the impact of loading rate on the mechanical properties of viral nanoparticles. Micron, 43(12), 1343-1350. https://doi.org/10.1016/j.micron.2012.04.011

2011

Wetenschappelijke publicaties

Snijder, J., Rose, R. J., Raijmakers, R., & Heck, A. J. R. (2011). Site-specific methionine oxidation in calmodulin affects structural integrity and interaction with Ca2+/calmodulin-dependent protein kinase II. Journal of Structural Biology, 174(1), 187-195.

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