W. (Winfried) Roseboom
Faculty of Science
Swammerdam Institute for Life Sciences
Visiting address
- Science Park 904
- Room number: C2.267
Postal address
- Postbus 1212
1000 BE Amsterdam
Contact details
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Profiel Winfried Roseboom
SILS Mass Spectrometry of Biomacromolecules
I work as research Technician in the Mass Spectrometry Group of the Swammerdam Institute of Life Sciences (SILS).
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Publications
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), [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), [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), [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, [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), [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, [103987]. 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), [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), [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), [1700169 ]. 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, [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. 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. W., & 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
2007
- Kasper, P. T., Back, J. W., Vitale, M. R., Hartog, A. F., Roseboom, W., de Koning, L. J., ... 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., ... 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., ... 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. [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]
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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Ancillary activities
- No ancillary activities
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), [13614].