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Transcriptional regulation of the N ε ‐fructoselysine metabolism in Escherichia coli by global and substrate‐specific cues

von Armansperg, B., Koller, F., Gericke, N., Hellwig, M., Jagtap, P. K. A., Heermann, R., Hennig, J., Henle, T., & Lassak, J. (2020) · Molecular Microbiology · doi:10.1111/mmi.14608 · Cited by 17

Bacteria in the ageing gut: did the taming of fire promote a long human lifespan?

Danchin, A. (2018) · Environmental Microbiology · doi:10.1111/1462-2920.14255 · Cited by 16

Integrated Use of Biochemical, Native Mass Spectrometry, Computational, and Genome-Editing Methods to Elucidate the Mechanism of a deglycase

Sengupta, A., Wu, J., Seffernick, J. T., Sabag-Daigle, A., Thomsen, N., Chen, T., Capua, A. D., Bell, C. E., Ahmer, B. M. M., Lindert, S., et al. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.08.017 · Cited by 16

Maillard Reactions in Hyperthermophilic Archaea: Implications for Better Understanding of Non-Enzymatic Glycation in Biology

Szwergold, B. S. (2013) · Rejuvenation Research · doi:10.1089/rej.2012.1401 · Cited by 15

Growth and transcriptional response of Salmonella Typhimurium LT2 to glucose–lysine-based Maillard reaction products generated under low water activity conditions

Chalova, V. I., Hernández‐Hernández, O., Muthaiyan, A., Sirsat, S. A., Natesan, S., Sanz, M. L., Moreno, F. J., O’Bryan, C. A., Crandall, P. G., & Ricke, S. C. (2011) · Food Research International · doi:10.1016/j.foodres.2011.06.044 · Cited by 16

Advancing the Development of Glycated Protein Biosensing Technology

Kameya, M., Sakaguchi‐Mikami, A., Ferri, S. R., Tsugawa, W., & Sode, K. (2015) · Journal of Diabetes Science and Technology · doi:10.1177/1932296814565784 · Cited by 14

Identification of protein-ribulosamine-5-phosphatase as human low-molecular-mass protein tyrosine phosphatase-A

Fortpied, J., Gemayel, R., Vertommen, D., & SCHAFTINGEN, E. V. (2007) · Biochemical Journal · doi:10.1042/bj20061485 · Cited by 13

Nitrogen assimilation by E. coli in the mammalian intestine

Doranga, S., & Conway, T. (2024) · mBio · doi:10.1128/mbio.00025-24 · Cited by 14

Aging: Drugs to Eliminate Methylglyoxal, a Reactive Glucose Metabolite, and Advanced Glycation Endproducts

Dhar, I., & Desai, K. M. (2012) · InTech eBooks · doi:10.5772/34337 · Cited by 14

Mutation accumulation and horizontal gene transfer inEscherichia colicolonizing the gut of old mice

Barreto, H. C., Frazão, N., Sousa, A., Konrad, A., & Gordo, I. (2020) · Communicative & Integrative Biology · doi:10.1080/19420889.2020.1783059 · Cited by 12

Neoformed Compounds from the Maillard Reaction in Infant Formulas: A New Risk Factor for Allergy?

Baskara, B., Niquet‐Léridon, C., Anton, P. M., & Delayre‐Orthez, C. (2017) · EMJ Allergy & Immunology · doi:10.33590/emjallergyimmunol/10312063 · Cited by 12

Evolved extracellular polymeric substances act as a frontline shield against antibiotic tolerance and resistance in Escherichia coli

Yu, J., Kaw, H. Y., Yang, Q., Fan, C., Ma, X., Zhu, L., & Wang, W. (2026) · Nature Water · doi:10.1038/s44221-025-00564-y · Cited by 10

Differences in gut microbial fructoselysine degradation activity between breast-fed and formula-fed infants

van Dongen, K. C. W., Ioannou, A., Wesseling, S., Beekmann, K., & Belzer, C. (2022) · FEMS Microbiology Ecology · doi:10.1093/femsec/fiac145 · Cited by 10

Non-canonical food sources: bacterial metabolism of Maillard reaction products and its regulation

Lassak, J., Aveta, E. F., Vougioukas, P., & Hellwig, M. (2023) · Current Opinion in Microbiology · doi:10.1016/j.mib.2023.102393 · Cited by 9

Bacterial Adaptation to Stress Induced by Glyoxal/Methylglyoxal and Advanced Glycation End Products

Kuczyńska‐Wiśnik, D., Stojowska‐Swędrzyńska, K., & Laskowska, E. (2025) · Microorganisms · doi:10.3390/microorganisms13122778 · Cited by 9

Expression levels of transcription factors in Escherichia coli: growth phase- and growth condition-dependent variation of 90 regulators from six families

Yamamoto, K., Watanabe, H., & Ishihama, A. (2014) · Microbiology · doi:10.1099/mic.0.079889-0 · Cited by 9

Identification of glucoselysine-6-phosphate deglycase, an enzyme involved in the metabolism of the fructation product glucoselysine

Wiame, E., Lamosa, P., Santos, H., & SCHAFTINGEN, E. V. (2005) · Biochemical Journal · doi:10.1042/bj20051183 · Cited by 37

Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the unusual Amadori compound psicoselysine in Escherichia coli

Wiame, E., & SCHAFTINGEN, E. V. (2004) · Biochemical Journal · doi:10.1042/bj20031527 · Cited by 28

Étude structurale de la fructoselysine 6-kinase d’Escherichia coli : reconnaissance de substrats et mécanisme enzymatique

Arthus-Cartier, G. (2009) · doi:10.71781/30142

New pathways for the metabolism of fructosamines and other glycation products in bacteria

Wiame, E. (2005) · Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B))

The metabolism of 1‐(ϵ‐N‐Lysyl)‐1‐deoxy‐ D ‐fructose by Escherichia coli

Griffiths, D. R., & Pridham, J. B. (1980) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.2740311113 · Cited by 7