W. (Winfried) Roseboom
Faculteit der Natuurwetenschappen, Wiskunde en Informatica
Swammerdam Institute for Life Sciences
Bezoekadres
- Science Park 904
- Kamernummer: C2.267
Postadres
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Postbus 1212
1000 BE Amsterdam
Contactgegevens
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Profiel Winfried Roseboom
I work as research Technician in the Mass Spectrometry Group of the Swammerdam Institute of Life Sciences (SILS).
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Publicaties
2024
Huang, Y., Swarge, B. N., Roseboom, W., Bleeker, J. D., Brul, S., Setlow, P., & Kramer, G. (2024). Integrative Metabolomics and Proteomics Allow the Global Intracellular Characterization of Bacillus subtilis Cells and Spores. Journal of Proteome Research, 23(2), 596-608. https://doi.org/10.1021/acs.jproteome.3c00386 [details]- van Karnebeek, C. D. M., Tarailo-Graovac, M., Leen, R., Meinsma, R., Correard, S., Jansen-Meijer, J., Prykhozhij, S. V., Pena, I. A., Ban, K., Schock, S., Saxena, V., Pras-Raves, M. L., Drögemöller, B. I., Grootemaat, A. E., van der Wel, N. N., Dobritzsch, D., Roseboom, W., Schomakers, B. V., Jaspers, Y. R. J., ... van Kuilenburg, A. B. P. (2024). CIAO1 and MMS19 deficiency: a lethal neurodegenerative phenotype caused by cytosolic Fe-S cluster protein assembly disorders. Genetics in Medicine, 26(6), Article 101104. https://doi.org/10.1016/j.gim.2024.101104
2023
- Naalden, D., Dermauw, W., Ilias, A., Baggerman, G., Mastop, M., Silven, J., van Kleeff, P. J. M., Dangol, S., Gaertner, N. F., Roseboom, W., Kwaaitaal, M., Kramer, G., van der Burg, H., Vontas, J., Van Leeuwen, T., Kant, M., & Schuurink, R. (2023). Interaction of whitefly effector G4 with tomato proteins impacts whitefly performance. Molecular Plant-Microbe Interactions. Advance online publication. https://doi.org/10.1094/MPMI-04-23-0045-R
- Seekles, S. J., van den Brule, T., Punt, M., Dijksterhuis, J., Arentshorst, M., Ijadpanahsaravi, M., Roseboom, W., Meuken, G., Ongenae, V., Zwerus, J., Ohm, R. A., Kramer, G., Wösten, H. A. B., de Winde, J. H., & Ram, A. F. J. (2023). Compatible solutes determine the heat resistance of conidia. Fungal biology and biotechnology, 10, Article 21. https://doi.org/10.1186/s40694-023-00168-9
2022
- Gao, X., Swarge, B. N., Roseboom, W., Setlow, P., Brul, S., & Kramer, G. (2022). Time-Resolved Proteomics of Germinating Spores of Bacillus cereus. International Journal of Molecular Sciences, 23(21), Article 13614. https://doi.org/10.3390/ijms232113614 [details]
- Gao, X., Swarge, B. N., Roseboom, W., Wang, Y., Dekker, H. L., Setlow, P., Brul, S., & Kramer, G. (2022). Changes in the Spore Proteome of Bacillus cereus in Response to Introduction of Plasmids. Microorganisms, 10(9), Article 1695. https://doi.org/10.3390/microorganisms10091695 [details]
2021
- Gao, X., Swarge, B. N., Dekker, H. L., Roseboom, W., Brul, S., & Kramer, G. (2021). The membrane proteome of spores and vegetative cells of the food-borne pathogen Bacillus cereus. International Journal of Molecular Sciences, 22(22), Article 12475. https://doi.org/10.3390/ijms222212475 [details]
- Roeters, S. J., Golbek, T. W., Bregnhøj, M., Drace, T., Alamdari, S., Roseboom, W., Kramer, G., Šantl-Temkiv, T., Finster, K., Pfaendtner, J., Woutersen, S., Boesen, T., & Weidner, T. (2021). Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water. Nature Communications, 12, Article 1183. https://doi.org/10.1038/s41467-021-21349-3 [details]
- Tu, Z., Dekker, H. L., Roseboom, W., Swarge, B. N., Setlow, P., Brul, S., & Kramer, G. (2021). High resolution analysis of proteome dynamics during bacillus subtilis sporulation. International Journal of Molecular Sciences, 22(17), Article 9345. https://doi.org/10.3390/ijms22179345 [details]
- de Jong, L., Roseboom, W., & Kramer, G. (2021). A composite filter for low FDR of protein-protein interactions detected by in vivo cross-linking. Journal of Proteomics, 230, Article 103987. Advance online publication. https://doi.org/10.1016/j.jprot.2020.103987 [details]
- de Jong, L., Roseboom, W., & Kramer, G. (2021). Towards low false discovery rate estimation for protein-protein interactions detected by chemical cross-linking. Biochimica et Biophysica Acta. Proteins and Proteomics, 1869(7), Article 140655. https://doi.org/10.1016/j.bbapap.2021.140655 [details]
2018
- Roseboom, W., Nazir, M. G., Meiresonne, N. Y., Mohammadi, T., Verheul, J., Buncherd, H., Bonvin, A. M. J. J., de Koning, L. J., de Koster, C. G., de Jong, L., & den Blaauwen, T. (2018). Mapping the Contact Sites of the Escherichia coli Division-Initiating Proteins FtsZ and ZapA by BAMG Cross-Linking and Site-Directed Mutagenesis. International Journal of Molecular Sciences, 19(10), Article 2928. https://doi.org/10.3390/ijms19102928 [details]
- Swarge, B. N., Roseboom, W., Zheng, L., Abhyankar, W. R., Brul, S., de Koster, C. G., & de Koning, L. J. (2018). "One‐Pot" Sample Processing Method for Proteome‐Wide Analysis of Microbial Cells and Spores. Proteomics Clinical Applications, 12(5), Article 1700169 . Advance online publication. https://doi.org/10.1002/prca.201700169 [details]
2017
- de Jong, L., de Koning, E. A., Roseboom, W., Buncherd, H., Wanner, M. J., Dapic, I., Jansen, P. J., van Maarseveen, J. H., Corthals, G. L., Lewis, P. J., Hamoen, L. W., & de Koster, C. G. (2017). In-Culture Cross-Linking of Bacterial Cells Reveals Large-Scale Dynamic Protein-Protein Interactions at the Peptide Level. Journal of Proteome Research, 16(7), 2457-2471. https://doi.org/10.1021/acs.jproteome.7b00068 [details]
2016
- Buncherd, H., Roseboom, W., Chokchaichamnankit, D., Sawangareetrakul, P., Phongdara, A., Srisomsap, C., de Jong, L., & Svasti, J. (2016). β-Elimination coupled with strong cation-exchange chromatography for phosphopeptide analysis. Rapid Communications in Mass Spectrometry, 30(14), 1695-1704. https://doi.org/10.1002/rcm.7606 [details]
- Zheng, L., Abhyankar, W., Ouwerling, N., Dekker, H. L., van Veen, H., van der Wel, N. N., Roseboom, W., de Koning, L. J., Brul, S., & de Koster, C. G. (2016). Bacillus subtilis Spore Inner Membrane Proteome. Journal of Proteome Research, 15(2), 585-594. https://doi.org/10.1021/acs.jproteome.5b00976 [details]
2015
- Borirak, O., Rolfe, M. D., de Koning, L. J., Hoefsloot, H. C. J., Bekker, M., Dekker, H. L., Roseboom, W., Green, J., de Koster, C. G., & Hellingwerf, K. J. (2015). Time-series analysis of the transcriptome and proteome of Escherichia coli upon glucose repression. Biochimica et Biophysica Acta. Proteins and Proteomics, 1854(10, Part A), 1269-1279. https://doi.org/10.1016/j.bbapap.2015.05.017 [details]
- Borirak, O., de Koning, L. J., van der Woude, A. D., Hoefsloot, H. C. J., Dekker, H. L., Roseboom, W., de Koster, C. G., & Hellingwerf, K. J. (2015). Quantitative proteomics analysis of an ethanol- and a lactate-producing mutant strain of Synechocystis sp. PCC6803. Biotechnology for Biofuels, 8, Article 111. https://doi.org/10.1186/s13068-015-0294-z [details]
- Glas, M., van den Berg van Saparoea, H. B., McLaughlin, S. H., Roseboom, W., Liu, F., Koningstein, G. M., Fish, A., den Blaauwen, T., Heck, A. J. R., de Jong, L., Bitter, W., de Esch, I. J. P., & Luirink, J. (2015). The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL form a Trimeric Complex with Sub-micromolar Affinity. The Journal of Biological Chemistry, 290(35), 21498-21509. Advance online publication. https://doi.org/10.1074/jbc.M115.654756 [details]
2012
- Buncherd, H., Nessen, M. A., Nouse, N., Stelder, S. K., Roseboom, W., Dekker, H. L., Arents, J. C., Smeenk, L. E., Wanner, M. J., van Maarseveen, J. H., Yang, X., Lewis, P. J., de Koning, L. J., de Koster, C. G., & de Jong, L. (2012). Selective enrichment and identification of cross-linked peptides to study 3-D structures of protein complexes by mass spectrometry. Journal of Proteomics, 75(7), 2205-2215. https://doi.org/10.1016/j.jprot.2012.01.025 [details]
2010
- Kramer, G., Sprenger, R. R., Nessen, M. A., Roseboom, W., Speijer, D., de Jong, L., Teixeira de Mattos, M. J., Back, J., & de Koster, C. G. (2010). Proteome-wide alterations in Escherichia coli translation rates upon anaerobiosis. Molecular & Cellular Proteomics, 9(11), 2508-2516. https://doi.org/10.1074/mcp.M110.001826 [details]
2007
- Kasper, P. T., Back, J. W., Vitale, M. R., Hartog, A. F., Roseboom, W., de Koning, L. J., van Maarseveen, J. H., Muijsers, A. O., de Koster, C. G., & de Jong, L. (2007). An aptly positioned azido group in the spacer of a protein cross-linker for facile mapping of lysines in close proximity. ChemBioChem, 8(11), 1281-1292. https://doi.org/10.1002/cbic.200700150 [details]
- Long, M., Liu, J., Chen, Z., Bleijlevens, B., Roseboom, W., & Albracht, S. P. J. (2007). Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module. Journal of Biological Inorganic Chemistry, 12(1), 62-78. https://doi.org/10.1007/s00775-006-0162-1 [details]
2006
- Albracht, S. P. J., Roseboom, W., & Hatchikian, E. C. (2006). The active site of the [FeFe]-hydrogenase from D. desulfuricans. I: Light sensitivity and magnetic hyperfine interactions as observed by electron paramagnetic resonance. Journal of Biological Inorganic Chemistry, 11, 88-101. https://doi.org/10.1007/s00775-005-0039-8 [details]
- Roseboom, W., De Lacey, A. L., Fernandez, V. M., Hatchikian, E. C., & Albracht, S. P. J. (2006). The active site of the [FeFe]-hydrogenase from D. desulfuricans. II: Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy. Journal of Biological Inorganic Chemistry, 11, 102-118. https://doi.org/10.1007/s00775-005-0040-2 [details]
2005
- Roseboom, W., Blokesch, M., Böck, A., & Albracht, S. P. J. (2005). The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Letters, 579(2), 469-472. https://doi.org/10.1016/j.febslet.2004.12.013
- Volbeda, A., Martin, L., Cavazza, C., Matho, M., Faber, B. W., Roseboom, W., Albracht, S. P. J., Garcin, E., Rousset, M., & Fontecilla-Camps, J. C. (2005). Erratum: Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases (Journal of Biological Inorganic Chemistry (2005) 10 (239-249) DOI:10.1007/s00775-055-0632-x). Journal of Biological Inorganic Chemistry, 10(5), 591. https://doi.org/10.1007/s00775-005-0663-3
- Volbeda, A., Martin, L., Cavazza, C., Matho, M., Faber, B. W., Roseboom, W., Albracht, S. P. J., Garcin, E., Rousset, M., & Fontecilla-Camps, J. C. (2005). Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases. Journal of Biological Inorganic Chemistry, 10(3), 239-249. https://doi.org/10.1007/s00775-005-0632-x
2004
- Bleijlevens, B., van Broekhuizen, F. A., De Lacey, A. L., Roseboom, W., Fernandez, V. M., & Albracht, S. P. J. (2004). The activation of the [NiFe]-hydrogenase from Allochromatium vinosum. An infrared spectro-electrochemical study. Journal of Biological Inorganic Chemistry, 9, 743-752. https://doi.org/10.1007/s00775-004-0570-z [details]
- Lyon, E. J., Shima, S., Boecher, R., Thauer, R. K., Grevels, F-W., Bill, E., Roseboom, W., & Albracht, S. P. J. (2004). Carbon monoxide as an intrinsic ligand to iron in the active site of te iron-sulfur-cluster-free hydrogenase H(2)-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. Journal of the American Chemical Society, 126, 14239-14248. https://doi.org/10.1021/ja046818s [details]
2000
- Davidson, G., Choudhury, S. B., Gu, Z., Bose, K., Roseboom, W., Albracht, S. P. J., & Maroney, M. J. (2000). Structural examination of the nickel site in Chromatium vinosum hydrogenase: redox state oscillations and structural changes accompanying reductive activation and CO binding. Biochemistry, 39, 7468-7479. https://doi.org/10.1021/bi000300t [details]
- Happe, R. P., Roseboom, W., Egert, G., Friedrich, C. G., Massanz, C., Friedrich, B., & Albracht, S. P. J. (2000). Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha. FEBS Letters, 466, 259-263. https://doi.org/10.1016/S0014-5793(99)01799-8 [details]
1999
- Happe, R. P., Roseboom, W., & Albracht, S. P. J. (1999). Pre-steady-state kinetics of the reactions of [NiFe]-hydrogenase from Chromatium vinosum with H2 and CO. European Journal of Biochemistry, 259, 602-609. https://doi.org/10.1046/j.1432-1327.1999.00057.x [details]
- Pierik, A. J., Roseboom, W., Happe, R. P., Bagley, K. A., & Albracht, S. P. J. (1999). Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe}-hydrogenases. NiFe(CN)2CO, biology's way to activate H2. The Journal of Biological Chemistry, 274, 3331-3337. https://doi.org/10.1074/jbc.274.6.3331 [details]
1997
- Happe, R. P., Roseboom, W., Pierik, A. J., Albracht, S. P. J., & Bagley, K. A. (1997). Biological activation of hydrogen. Nature, (385), 126-126. [details]
1996
- Gu, Z., Dong, J., Allan, C. B., Choudhury, S. B., Franco, R., Moura, J. J. G., Moura, I., LeGall, J., Przybylia, A. E., Roseboom, W., Albracht, S. P. J., Axley, M. J., Scott, R. A., & Maroney, M. J. (1996). Structure of the Ni sites in hydrogenases by X-ray absorption spectroscopy. Species variation and effects of redox poise. Journal of the American Chemical Society, 118, 11155-11165. https://doi.org/10.1021/ja962429p [details]
1995
- Bagley, K. A., Duin, E. L., Roseboom, W., Albracht, S. P. J., & Woodruff, W. H. (1995). An infrared-detectable group senses changes in charge density on the nickel center in hydrogenase from Chromatium vinosum. Biochemistry, 34, 5527-5535. https://doi.org/10.1021/bi00016a026 [details]
2018
- Corthals, G., de Jong, L., de Koning, E. A., Roseboom, W., Buncherd, H., Wanner, M., Dapic, I., Jansen, P., van Maarseveen, J., Lewis, P., Hamoen, L., & de Koster, C. (2018). Identification of dynamic protein interactions from live cells. FEBS OPEN BIO, 8(S1), 17-18. Article S.32-5. https://doi.org/10.1002/2211-5463.12449 [details]
2014
- Buncherd, H., Roseboom, W., Ghavim, B., Du, W., de Koning, L. J., de Koster, C. G., & de Jong, L. (2014). Isolation of cross-linked peptides by diagonal strong cation exchange chromatography for protein complex topology studies by peptide fragment fingerprinting from large sequence databases. Journal of Chromatography A, 1348, 34-46. https://doi.org/10.1016/j.chroma.2014.04.083 [details]
- Buncherd, H., Roseboom, W., de Koning, L. J., de Koster, C. G., & de Jong, L. (2014). A gas phase cleavage reaction of cross-linked peptides for protein complex topology studies by peptide fragment fingerprinting from large sequence database. Journal of Proteomics, 108, 65-77. https://doi.org/10.1016/j.jprot.2014.05.003 [details]
2024
- Kramer, G., de Winde, J. H., Roseboom, W., Arentshorst, M., Ongenae, V. M. A., Meuken, G., Ijadpanahsaravi, M., Zwerus, J. & Ram, A. F. J. (2024). Additional file 9 of Compatible solutes determine the heat resistance of conidia. Figshare. https://doi.org/10.6084/m9.figshare.26639385.v1
- Kramer, G., de Winde, J. H., Ongenae, V. M. A., Arentshorst, M., Zwerus, J., Meuken, G., Ijadpanahsaravi, M., Roseboom, W. & Ram, A. F. J. (2024). Additional file 11 of Compatible solutes determine the heat resistance of conidia. Figshare. https://doi.org/10.6084/m9.figshare.26639391.v1
2022
- Gao, X., Swarge, B., Roseboom, W., Wang, Y., Dekker, H. L., Setlow, P., Brul, S. & Kramer, G. (2022). MassIVE MSV000090153 - Changes in the spore proteome of Bacillus cereus in response to introduction of plasmids.. MassIVE. https://doi.org/10.25345/c5pg1hs5v
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Huang, Y., Swarge, B. N., Roseboom, W., Bleeker, J. D., Brul, S., Setlow, P., & Kramer, G. (2024). Integrative Metabolomics and Proteomics Allow the Global Intracellular Characterization of Bacillus subtilis Cells and Spores. Journal of Proteome Research, 23(2), 596-608.