Staff profile

Ph.D. Technical University of Darmstadt, Darmstadt, Germany, 1996. Postdoctoral Fellow, Howard Hughes Medical Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, USA, 1997 - 2004.

• Molecular Biology
• Unfolded Protein Response
• Yeast Genetics

Authored book

• Molecular chaperones of the endoplasmic reticulum
  
  Schröder, M. (2010). Molecular chaperones of the endoplasmic reticulum. NOVA Science Publishers.
• Identifikation limitierter Schritte der Antithrombin III Produktion in genamplifizierten CHO-Zellen
  
  Schröder, M. (1997). Identifikation limitierter Schritte der Antithrombin III Produktion in genamplifizierten CHO-Zellen. Shaker.

Chapter in book

• Molecular chaperones of the endoplasmic reticulum
  
  Schröder, M. (2009). Molecular chaperones of the endoplasmic reticulum. In P. Durante & L. Colucci (Eds.), Handbook of Molecular Chaperones: Roles, Structures and Mechanisms (pp. 1-78). NOVA Science Publishers.
• Unfolded protein response
  
  Schröder, M. (2008). Unfolded protein response. In J. Weil, D. Blumel, S. Malmoli, & J. Netting (Eds.), Yearbook of Science and Technology (pp. 356-360). McGraw-Hill.
• Allgemeine Methoden
  
  Frech, M., Mikosch, T., Schröder, M., & Stassen, M. (2007). Allgemeine Methoden. In M. Jansohn (Ed.), Gentechnische Methoden: eine Sammlung von Arbeitsanleitungen für das molekularbiologische Labor (pp. 1-35). Elsevier.
• Isolierung von RNA
  
  Schröder, M. (2007). Isolierung von RNA. In M. Jansohn (Ed.), Gentechnische Methoden (pp. 131-154). Elsevier.
• The cellular response to protein unfolding stress
  
  Schröder, M. (2007). The cellular response to protein unfolding stress. In G. Robson, P. van West, & G. Gadd (Eds.), BMS Symposium Series, Exploitation of Fungi (pp. 117-139). Cambridge University Press.
• The unfolded protein response
  
  Strudwick, N., & Schröder, M. (2007). The unfolded protein response. In M. Al-Rubeai & M. Fussenegger (Eds.), Cell Engineering Vol 5: Systems Biology (pp. 69-157). Springer Netherlands.
• Allgemeine Methoden
  
  Frech, M., Mikosch, T., Schröder, M., & Stassen, M. (2002). Allgemeine Methoden. In G. Schrimpf & A. Aigner (Eds.), Gentechnische Methoden: eine Sammlung von Arbeitsanleitungen für das molekularbiologische Labor (pp. 1-37). Spektrum Akademischer Verlag.
• Isolierung von RNA
  
  Schröder, M. (2002). Isolierung von RNA. In G. Schrimpf (Ed.), Gentechnische Methoden (3rd ed., pp. 129-145). Spektrum Academischer Verlag.
• Isolierung von RNA
  
  Schröder, M. (1999). Isolierung von RNA. In H. Gassen & G. Schrimpf (Eds.), Genrechnische Methoden (2nd ed., pp. 225-242). Spektrum Akademischer Verlag.
• Metabolism of confluent vascular endothelial cell cultures
  
  Schrimpf, G., Schröder, M., Weitnauer, E., & Friedl, P. (1995). Metabolism of confluent vascular endothelial cell cultures. In E. Beuvery, J. Griffiths, & W. Zeijlemaker (Eds.), Animal Cell Technology: Developments towards the 21st century (pp. 1127-1131). Kluwer Academic Publishers.

Journal Article

• The Unfolded Protein Response: An Overview
  
  Read, A., & Schröder, M. (2021). The Unfolded Protein Response: An Overview. Biology, 10(5), Article 384. https://doi.org/10.3390/biology10050384
• Endoplasmic reticulum stress causes insulin resistance by inhibiting delivery of newly synthesised insulin receptors to the cell surface
  
  Brown, M., Dainty, S., Strudwick, N., Mihai, A. D., Watson, J. N., Dendooven, R., Paton, A. W., Paton, J. C., & Schröder, M. (2020). Endoplasmic reticulum stress causes insulin resistance by inhibiting delivery of newly synthesised insulin receptors to the cell surface. Molecular Biology of the Cell, 31(23), 2495-2629. https://doi.org/10.1091/mbc.e18-01-0013
• Bypass of activation loop phosphorylation by aspartate 836 in activation of the endoribonuclease activity of Ire1
  
  Armstrong, M., Sestak, S., Ali, A., Sagini, H., Brown, M., Baty, K., Treumann, A., & Schröder, M. (2017). Bypass of activation loop phosphorylation by aspartate 836 in activation of the endoribonuclease activity of Ire1. Molecular and Cellular Biology, 37(16), Article e00655-16. https://doi.org/10.1128/mcb.00655-16
• An initial phase of JNK activation inhibits cell death early in the endoplasmic reticulum stress response
  
  Brown, M., Strudwick, N., Suwara, M., Sutcliffe, L., Mihai, A., Ali, A., Watson, J., & Schröder, M. (2016). An initial phase of JNK activation inhibits cell death early in the endoplasmic reticulum stress response. Journal of Cell Science, 129(12), 2317-2328. https://doi.org/10.1242/jcs.179127
• Glucose starvation and hypoxia, but not the saturated fatty acid palmitic acid or cholesterol, activate the unfolded protein response in 3T3-F442A and 3T3-L1 adipocytes
  
  Mihai, A., & Schröder, M. (2015). Glucose starvation and hypoxia, but not the saturated fatty acid palmitic acid or cholesterol, activate the unfolded protein response in 3T3-F442A and 3T3-L1 adipocytes. Adipocyte, 4(3), 188-202. https://doi.org/10.4161/21623945.2014.989728
• 5’-Deoxy-5’-hydrazinylguanosine as an initiator of T7 RNA polymerase-catalyzed transcriptions for the preparation of labeling-ready RNAs
  
  Skipsey, M., Hack, G., Hooper, T., Shankey, M., Conway, L., Schröder, M., & Hodgson, D. (2013). 5’-Deoxy-5’-hydrazinylguanosine as an initiator of T7 RNA polymerase-catalyzed transcriptions for the preparation of labeling-ready RNAs. Nucleosides, Nucleotides and Nucleic Acids, 32(12), 670-681. https://doi.org/10.1080/15257770.2013.851393
• Measuring signaling by the unfolded protein response.
  
  Cox, D., Srudwick, N., Ali, A., Paton, A., Paton, J., & Schröder, M. (2011). Measuring signaling by the unfolded protein response. Methods in Enzymology, 491, 261-292. https://doi.org/10.1016/b978-0-12-385928-0.00015-8
• Chemical approaches twoards unraveling kinase-mediated signaling pathways
  
  Hodgson, D., & Schröder, M. (2011). Chemical approaches twoards unraveling kinase-mediated signaling pathways. Chemical Society Reviews, 40(3), 1211-1223.
• Ime1 and Ime2 are required for pseudohyphal growth of Saccharomyces cerevisiae on Nonfermentable Carbon Sources.
  
  Strudwick, N., Brown, M., Parmar, V., & Schröder, M. (2010). Ime1 and Ime2 are required for pseudohyphal growth of Saccharomyces cerevisiae on Nonfermentable Carbon Sources. Molecular and Cellular Biology, 30(23), 5514-5530. https://doi.org/10.1128/mcb.00390-10
• Consequences of stress in the secretory pathway: the ER stress response and its role in the metabolic syndrome.
  
  Schröder, M., & Sutcliffe, L. (2010). Consequences of stress in the secretory pathway: the ER stress response and its role in the metabolic syndrome. Methods in Molecular Biology., 648, 43-62. https://doi.org/10.1007/978-1-60761-756-3_3
• Endoplasmic reticulum stress responses
  
  Schröder, M. (2008). Endoplasmic reticulum stress responses. Cellular and Molecular Life Sciences, 65(6), 862-894. https://doi.org/10.1007/s00018-007-7383-5
• Engineering of chaperone systems and of the unfolded protein response
  
  Khan, S., & Schröder, M. (2008). Engineering of chaperone systems and of the unfolded protein response. Cytotechnology, 57(3), 207-231. https://doi.org/10.1007/s10616-008-9157-9
• Engineering eukaryotic protein factories
  
  Schröder, M. (2008). Engineering eukaryotic protein factories. Biotechnology Letters, 30(2), 187-196. https://doi.org/10.1007/s10529-007-9524-1
• Recent advances in understanding the unfolded protein response
  
  Schröder, M., & Kohno, K. (2007). Recent advances in understanding the unfolded protein response. Antioxidants and Redox Signaling, 9(12), 2241-2244. https://doi.org/10.1089/ars.2007.1877
• The unfolded protein response
  
  Schröder, M. (2006). The unfolded protein response. Molecular Biotechnology, 34(2), 279-290.
• Divergent roles for IRE1α and PERK in the unfolded protein response
  
  Schröder, M., & Kaufman, R. (2006). Divergent roles for IRE1α and PERK in the unfolded protein response. Current Molecular Medicine, 6(1), 5-36.
• ER stress signalling by regulated splicing: IRE1/HAC1/XBP1
  
  Back, S., Schröder, M., Lee, K., Zhang, K., & Kaufman, R. (2005). ER stress signalling by regulated splicing: IRE1/HAC1/XBP1. Methods, 35(4), 395-416. https://doi.org/10.1016/j.ymeth.2005.03.001
• The mammalian unfolded protein response
  
  Schröder, M., & Kaufman, R. (2005). The mammalian unfolded protein response. Annual Review of Biochemistry, 74, 739-789.
• ER stress and the unfolded protein response
  
  Schröder, M., & Kaufman, R. (2005). ER stress and the unfolded protein response. Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis, 569(1-2), 29-63. https://doi.org/10.1016/j.mrfmmm.2004.06.056
• The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase
  
  Schröder, M., Clark, R., Liu, C., & Kaufman, R. (2004). The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase. EMBO Journal, 23(11), 2281-2292. https://doi.org/10.1038/sj.emboj.7600233
• Serum- and protein-free media formulations for the Chinese hamster ovary cell line DUKXB11
  
  Schröder, M., Matischak, K., & Friedl, P. (2004). Serum- and protein-free media formulations for the Chinese hamster ovary cell line DUKXB11. Journal of Biotechnology, 108(3), 279-292. https://doi.org/10.1016/j.jbiotec.2003.12.005
• GermOnline, a cross-species knowledgebase on germ cell differentiation
  
  Wiederkehr, C., Basavaraj, R., Sarrauste de Menthiere, C., Hermida, L., Koch, R., Schlecht, U., Amon, A., Brachat, S., Breitenbach, M., Briza, P., Caburet, S., Cherry, M., Davis, R., Deutschbauer, A., Dickinson, H., Dumitrescu, T., Fellous, M., Goldman, A., Grootegoed, J., … Primig, M. (2004). GermOnline, a cross-species knowledgebase on germ cell differentiation. Nucleic Acids Research, 32(Database issue), D560-D567. https://doi.org/10.1093/nar/gkh055
• IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast
  
  Schröder, M., Clark, R., & Kaufman, R. (2003). IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast. Molecular Microbiology, 49(3), 591-606. https://doi.org/10.1046/j.1365-2958.2003.03585.x
• The unfolded protein response in nutrient sensing and differentiation
  
  Kaufman, R., Scheuner, D., Schröder, M., Shen, X., Lee, K., Liu, C., & Arnold, S. (2002). The unfolded protein response in nutrient sensing and differentiation. Nature Reviews Molecular Cell Biology, 3(6), 411-421. https://doi.org/10.1038/nrm829
• Induction of protein aggregation in an early secretory compartment by elevation of expression level
  
  Schröder, M., Schäfer, R., & Friedl, P. (2002). Induction of protein aggregation in an early secretory compartment by elevation of expression level. Biotechnology and Bioengineering, 78(2), 131-140. https://doi.org/10.1002/bit.10206
• The unfolded protein response represses nitrogen-starvation induced developmental differentiation in yeast
  
  Schröder, M., Chang, J., & Kaufman, R. (2000). The unfolded protein response represses nitrogen-starvation induced developmental differentiation in yeast. Genes and Development, 14(23), 2962-2975.
• Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
  
  Liu, C., Schröder, M., & Kaufman, R. (2000). Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. Journal of Biological Chemistry, 275(32), 24881-24885.
• Quantitative analysis of transcription and translation in gene amplified Chinese hamster ovary cells on the basis of a kinetic model
  
  Schröder, M., Körner, C., & Friedl, P. (1999). Quantitative analysis of transcription and translation in gene amplified Chinese hamster ovary cells on the basis of a kinetic model. Cytotechnology, 29(2), 93-102. https://doi.org/10.1023/a%3A1008077603328
• Enzymatic determination of D-glucose in cell culture media using glucose oxidase, horseradish peroxidase and 3,3 ',5,5 '- tetramethylbenzidine
  
  Schröder, M., & Friedl, P. (1997). Enzymatic determination of D-glucose in cell culture media using glucose oxidase, horseradish peroxidase and 3,3 ’,5,5 ’- tetramethylbenzidine. The Genetic Engineer and Biotechnologist, 17(4), 157-163.
• A protein-free solution as replacement for serum in trypsinization protocols for anchorage-dependent cells
  
  Schröder, M., & Friedl, P. (1997). A protein-free solution as replacement for serum in trypsinization protocols for anchorage-dependent cells. Methods in Cell Science, 19(2), 137-147. https://doi.org/10.1023/a%3A1009792705772
• Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of the recombinant protein
  
  Schröder, M., & Friedl, P. (1997). Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of the recombinant protein. Biotechnology and Bioengineering, 53(6), 547-559. https://doi.org/10.1002/%28sici%291097-0290%2819970320%2953%3A6%3C547%3A%3Aaid-bit2%3E3.0.co%3B2-m
• Spectrophotometric determination of iodixanol in subcellular fractions of mammalian cells
  
  Schröder, M., Schäfer, R., & Friedl, P. (1997). Spectrophotometric determination of iodixanol in subcellular fractions of mammalian cells. Analytical Biochemistry, 244(1), 174-176. https://doi.org/10.1006/abio.1996.9861
• Indirect sandwich ELISA for human antithrombin III employing the interaction between D-biotin and streptavidin
  
  Schröder, M., Kaiser, D., Schäfer, R., & Friedl, P. (1996). Indirect sandwich ELISA for human antithrombin III employing the interaction between D-biotin and streptavidin. The Genetic Engineer and Biotechnologist, 16(4), 211-225.
• Metabolic rates of vascular endothelial cells in vitro
  
  Schrimpf, G., Schröder, M., Weitnauer, E., & Friedl, P. (1994). Metabolic rates of vascular endothelial cells in vitro. Cytotechnology, 16(1), 43-50. https://doi.org/10.1007/bf00761778
• Ire1
  
  Schröder, M., & Kaufman, R. (n.d.). Ire1. The AFCS-Nature Molecule Pages. Advance online publication. https://doi.org/10.1038/mp.a003134.01