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Detection of organohalide-respiring enzyme biomarkers at a bioaugmented TCE-contaminated field site
Heavner, G. L. W., Mansfeldt, C. B., Wilkins, M. J., Nicora, C. D., Debs, G. E., Edwards, E. A., & Richardson, R. E. (2019). Detection of organohalide-respiring enzyme biomarkers at a bioaugmented TCE-contaminated field site. Frontiers in Microbiology, 10, 1433 (12 pp.). https://doi.org/10.3389/fmicb.2019.01433
Biomarkers' responses to reductive dechlorination rates and oxygen stress in bioaugmentation culture KB-1<sup>TM</sup>
Heavner, G. L. W., Mansfeldt, C. B., Debs, G. E., Hellerstedt, S. T., Rowe, A. R., & Richardson, R. E. (2018). Biomarkers' responses to reductive dechlorination rates and oxygen stress in bioaugmentation culture KB-1TM. Microorganisms, 6(1), 13 (15 pp.). https://doi.org/10.3390/microorganisms6010013
Evolution of egg coats: linking molecular biology and ecology
Shu, L., Suter, M. J. F., & Räsänen, K. (2015). Evolution of egg coats: linking molecular biology and ecology. Molecular Ecology, 24(16), 4052-4073. https://doi.org/10.1111/mec.13283
Phenotypic plasticity influences the eco-evolutionary dynamics of a predator-prey system
Fischer, B. B., Kwiatkowski, M., Ackermann, M., Krismer, J., Roffler, S., Suter, M. J. F., … Matthews, B. (2014). Phenotypic plasticity influences the eco-evolutionary dynamics of a predator-prey system. Ecology, 95(11), 3080-3092. https://doi.org/10.1890/14-0116.1
Mass spectrometric target analysis and proteomics in environmental toxicology
Groh, K. J., & Suter, M. J. F. (2014). Mass spectrometric target analysis and proteomics in environmental toxicology. In J. Banoub (Ed.), NATO Science for Peace and Security Series A: Chemistry and Biology. Detection of chemical, biological, radiological and nuclear agents for the prevention of terrorism (pp. 149-167). https://doi.org/10.1007/978-94-017-9238-7_10
Mass spectrometry in environmental toxicology
Groh, K. J., & Suter, M. J. F. (2014). Mass spectrometry in environmental toxicology. Chimia, 68(3), 140-145. https://doi.org/10.2533/chimia.2014.140
Genetic and metabolic analysis of the carbofuran catabolic pathway in <I>Novosphingobium</I> sp. KN65.2
Nguyen, T. P. O., Helbling, D. E., Bers, K., Fida, T. T., Wattiez, R., Kohler, H. P. E., … De Mot, R. (2014). Genetic and metabolic analysis of the carbofuran catabolic pathway in Novosphingobium sp. KN65.2. Applied Microbiology and Biotechnology, 98(19), 8235-8252. https://doi.org/10.1007/s00253-014-5858-5
Sustainable syntrophic growth of <I>Dehalococcoides ethenogenes</I> strain 195 with <I>Desulfovibrio vulgaris</I> Hildenborough and <I>Methanobacterium congolense</I>: global transcriptomic and proteomic analyses
Men, Y., Feil, H., Verberkmoes, N. C., Shah, M. B., Johnson, D. R., Lee, P. K. H., … Alvarez-Cohen, L. (2012). Sustainable syntrophic growth of Dehalococcoides ethenogenes strain 195 with Desulfovibrio vulgaris Hildenborough and Methanobacterium congolense: global transcriptomic and proteomic analyses. ISME Journal, 6(2), 410-421. https://doi.org/10.1038/ismej.2011.111
Global proteomics analysis of testis and ovary in adult zebrafish (<I>Danio rerio</I>)
Groh, K. J., Nesatyy, V. J., Segner, H., Eggen, R. I. L., & Suter, M. J. F. (2011). Global proteomics analysis of testis and ovary in adult zebrafish (Danio rerio). Fish Physiology and Biochemistry, 37(3), 619-647. https://doi.org/10.1007/s10695-010-9464-x
On the acquisition of +1 charge states during high-throughput proteomics: implications on reproducibility, number and confidence of protein identifications
Nesatyy, V. J., Groh, K., Nestler, H., & Suter, M. J. F. (2009). On the acquisition of +1 charge states during high-throughput proteomics: implications on reproducibility, number and confidence of protein identifications. Journal of Proteomics, 72(5), 761-770. https://doi.org/10.1016/j.jprot.2009.03.003
Analysis of environmental stress response on the proteome level
Nesatyy, V. J., & Suter, M. J. F. (2008). Analysis of environmental stress response on the proteome level. Mass Spectrometry Reviews, 27(6), 556-574. https://doi.org/10.1002/mas.20177