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Dr. D. (Dave) Speijer

Faculty of Science
Swammerdam Institute for Life Sciences

Visiting address
  • Science Park 904
Postal address
  • Postbus 1212
    1000 BE Amsterdam
Contact details
  • Publications

    2019

    2017

    • Huis In 't Veld, R. A. G., Kramer, G., van der Ende, A., Speijer, D., & Pannekoek, Y. (2017). The Hfq regulon of Neisseria meningitidis. FEBS OPEN BIO, 7(6), 777-788. https://doi.org/10.1002/2211-5463.12218
    • Pannekoek, Y., Huis In 't Veld, R. A. G., Schipper, K., Bovenkerk, S., Kramer, G., Brouwer, M. C., van de Beek, D., Speijer, D., & van der Ende, A. (2017). Neisseria meningitidis Uses Sibling Small Regulatory RNAs To Switch from Cataplerotic to Anaplerotic Metabolism. MBio, 8(2). https://doi.org/10.1128/mBio.02293-16
    • Pannekoek, Y., Huis In 't Veld, R., Schipper, K., Bovenkerk, S., Kramer, G., Speijer, D., & van der Ende, A. (2017). Regulation of Neisseria meningitidis cytochrome bc1 components by NrrF, a Fur-controlled small noncoding RNA. FEBS OPEN BIO, 7(9), 1302-1315. https://doi.org/10.1002/2211-5463.12266
    • van der Gulik, P. T. S., Hoff, W. D., & Speijer, D. (2017). In defence of the three-domains of life paradigm. BMC Evolutionary Biology, 17, [218]. https://doi.org/10.1186/s12862-017-1059-z [details]

    2016

    2015

    2014

    • Strang, A. C., Knetsch, M. L. W., Idu, M. M., Bisoendial, R. J., Kramer, G., Speijer, D., ... Rotmans, J. I. (2014). Superior in vivo compatibility of hydrophilic polymer coated prosthetic vascular grafts. Journal of Vascular Access, 15(2), 95-101. https://doi.org/10.5301/jva.5000166

    2013

    • Buhrman, H., van der Gulik, P. T. S., Klau, G. W., Schaffner, C., Speijer, D., & Stougie, L. (2013). A Realistic Model Under Which the Genetic Code is Optimal. Journal of molecular evolution, 77(4), 170-184. https://doi.org/10.1007/s00239-013-9571-2 [details]

    2012

    • Kramer, G., Moerland, P. D., Jeeninga, R. E., Vlietstra, W. J., Ringrose, J. H., Byrman, C., ... Speijer, D. (2012). Proteomic analysis of HIV-T cell interaction: an update. Frontiers in Microbiology, 3, 240. https://doi.org/10.3389/fmicb.2012.00240

    2011

    • Kwakman, P. H. S., Krijgsveld, J., de Boer, L., Nguyen, L. T., Boszhard, L., Vreede, J., ... Zaat, S. A. J. (2011). Native thrombocidin-1 and unfolded thrombocidin-1 exert antimicrobial activity via distinct structural elements. The Journal of Biological Chemistry, 286(50), 43506-43514. https://doi.org/10.1074/jbc.M111.248641 [details]

    2010

    • Hopman, C. T. P., Speijer, D., van den Ende, A., & Pannekoek, Y. (2010). Identification of a novel anti-sigmaE factor in Neisseria meningitidis. BMC Microbiology, 10(1), 164. https://doi.org/10.1186/1471-2180-10-164 [details]
    • 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

    2009

    • Boot, R. G., van Breemen, M. J., Wegdam, W., Sprenger, R. R., de Jong, S., Speijer, D., Hollak, C. E. M., van Dussen, L., Hoefsloot, H. C. J., Smilde, A. K., de Koster, C. G., Vissers, J. P. C., & Aerts, J. M. F. G. (2009). Gaucher disease: a model disorder for biomarker discovery. Expert Review of Proteomics, 6(4), 411-419. https://doi.org/10.1586/epr.09.54 [details]

    2008

    • Aerts, J. M., van Breemen, M. J., Bussink, A. P., Ghauharali, K., Sprenger, R., Boot, R. G., Groener, J. E., Hollak, C. E., Maas, M., Smit, S., Hoefsloot, H. C., Smilde, A. K., Vissers, J. P. C., de Jong, S., Speijer, D., & de Koster, C. G. (2008). Biomarkers for lysosomal storage disorders: Identification and application as exemplified by chitotriosidase in Gaucher disease. Acta Paediatrica, 97(s457), 7-14. https://doi.org/10.1111/j.1651-2227.2007.00641.x [details]
    • van den Bos, T., Speijer, D., Bank, R. A., Brömme, D., & Everts, V. (2008). Differences in matrix composition between calvaria and long bone in mice suggest differences in biomechanical properties and resorption: special emphasis on collagen. Bone, 43(3), 459-468. https://doi.org/10.1016/j.bone.2008.05.009 [details]

    2007

    • Bock, V. D., Speijer, D., Hiemstra, H., & van Maarseveen, J. H. (2007). 1,2,3-Triazoles as peptide bond isosteres: synthesis and biological evaluation of cyclotetrapeptide mimics. Organic & Biomolecular Chemistry, 5(6), 971-975. [details]
    • Houterman, P. M., Speijer, D., Dekker, H. L., de Koster, C. G., Cornelissen, B. J. C., & Rep, M. (2007). The mixed proteome of Fusarium oxysporum-infected tomato xylem vessels. Molecular Plant Pathology, 8, 215-221. https://doi.org/10.1111/j.1364-3703.2007.00384.x [details]

    2006

    • Rep, M., van der Does, H. C., Meijer, M., Houterman, P. M., Dekker, H. L., Speijer, D., de Koster, C. G., & Cornelissen, B. J. C. (2006). Secrets of xylem colonization- The xylem sap proteome of tomato infected with Fusarium oxysporum IS-MPM1. In C. Quinto, S. Lopes-Lara Sanchez, & O. Geiger (Eds.), Biology of Plant-Microbe Interactions. (pp. 597-601) [details]

    2004

    • Sprenger, R. R., Speijer, D., Back, J. W., de Koster, C. G., Pannekoek, H., & Horrevoets, A. J. G. (2004). Comparative proteomics of human endothelial cell caveolae and rafts using two-dimensional gel electrophoresis and mass spectrometry. Electrophoresis, 25(1), 156-172. https://doi.org/10.1002/elps.200305675 [details]

    2003

    • Blom, D., Speijer, D., Linthorst, G. E., Donker-Koopman, W. G., Strijland, A., & Aerts, J. M. F. G. (2003). Recombinant enzyme therapy for Fabry disease: absence of editing of human alpha-galactosidase A mRNA. American Journal of Human Genetics, 72, 23-31. https://doi.org/10.1086/345309 [details]

    2002

    • Meek, B., Back, J. W., Klaren, V. N. A., Speijer, D., & Peek, R. (2002). Conserved Regions of Protein Disulfide Isomerase are Targeted by Natural IgA Antibodies in Humans. International immunology, 14, 1291-1301. https://doi.org/10.1093/intimm/dxf091 [details]
    • Meek, B., Back, J. W., Klaren, V. N. A., Speijer, D., & Peek, R. (2002). Protein Disulfide Isomerase of Toxoplasma Gondii isTargeted by Mucosal IgA Antibodies in Humans. FEBS Letters, 522, 104-108. https://doi.org/10.1016/S0014-5793(02)02911-3 [details]
    • Rep, M., Dekker, H. L., Vossen, J. H., de Boer, A., Houterman, P. M., Speijer, D., Back, J. W., de Koster, C. G., & Cornelissen, B. J. C. (2002). Mass spectrometric identification of isoforms of PR proteins in xylem sap of fungus-infected tomato. Plant Physiology, 130, 904-917. https://doi.org/10.1104/pp.007427 [details]

    2001

    • Blom, D., van den Burg, J., Breek, C. K. D., Speijer, D., Muijsers, A. O., & Benne, R. (2001). Cloning aid characterization of two guide RNA-binding proteins from mitochondria of Crithidia fasciculata: gBP27, a novel protein, and gBP29, the orthologue of Trypanosoma brucei gBP21. Nucleic Acids Research, 29, 2950-2962. https://doi.org/10.1093/nar/29.14.2950 [details]
    • Blom, D., van den Burg, J., Breek, C. K. D., Speijer, D., Muijsers, A. O., & Benne, R. (2001). Cloning and characterization of two guide RNA-binding proteins from mitochondria of Crithidia fasciculat gBP27, a novel protein, and gBP29, the orthologue of Trypanosoma brucei gBP21. Nucleic Acids Research, 29(14), 2950-2962. https://doi.org/10.1093/nar/29.14.2950 [details]

    2000

    • Spelbrink, J. N., Toivonen, J. M., Hakkaart, G. A. J., Kurkela, J. M., Cooper, H. M., Lehtinen, S. K., ... Jacobs, H. T. (2000). In vivo functional analysis of the human mitochondrial DNA polymerase POLG expressed in cultured human cells. The Journal of Biological Chemistry, 275(32), 24815-24828. [details]

    1996

    • Speijer, D., Muijsers, A. O., Dekker, H. L., Beek, C. K. D., Albracht, S. P. J., & Benne, R. (1996). Purification and characterization of cytochrome c oxidase from the insect trypanosomatid Crithidia fasciculata. Molecular and biochemical parasitology, 78, 47-59. https://doi.org/10.1016/S0166-6851(96)02603-5 [details]

    2019

    • van der Gulik, P. T. S. (2019). Considerations in evolutionary biochemistry. Amsterdam: Institute for Logic, Language and Computation. [details]
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  • Ancillary activities
    No ancillary activities