Publications

Spiess, M., Beuret, N., Prescianotto Baschong, C. and Rutishauser, J. (2020) “Amyloid-like aggregation of provasopressin”, Vitamins and hormones, 113, pp. 55–77. doi: 10.1016/bs.vh.2019.08.014.   
Spiess, M., Beuret, N. and Rutishauser, J. (2020) “Genetic forms of neurohypophyseal diabetes insipidus”, Best practice & research. Clinical endocrinology & metabolism, p. 101432. doi: 10.1016/j.beem.2020.101432.   
Spiess, M., Friberg, M., Beuret, N., Prescianotto-Baschong, C. and Rutishauser, J. (2020) “Role of protein aggregation and degradation in autosomal dominant neurohypophyseal diabetes insipidus”, Molecular and cellular endocrinology, 501, p. 110653. doi: 10.1016/j.mce.2019.110653.   
Rutishauser, J., Beuret, N., Prescianotto-Baschong, C. and Spiess, M. (2019) “Hereditary Neurohypophyseal Diabetes Insipidus”, in Igaz, P. and Patócs , A. (eds.) Genetics of Endocrine Diseases and Syndromes. Cham: Springer Nature Switzerland (Experientia Supplementum), pp. 299–315. doi: 10.1007/978-3-030-25905-1_14.   edoc | Open Access
Buser, D. P., Ritz, M.-F., Moes, S., Tostado, C., Frank, S., Spiess, M., Mariani, L., Jenö, P., Boulay, J.-L. and Hutter, G. (2019) “Quantitative proteomics reveals reduction of endocytic machinery components in gliomas”, EBioMedicine. Elsevier, 46, pp. 36–41. doi: 10.1016/j.ebiom.2019.07.039.   edoc | Open Access
Spiess, M., Junne, T. and Janoschke, M. (2019) “Membrane Protein Integration and Topogenesis at the ER”, The Protein Journal. Springer, 38(3), pp. 306–316. doi: 10.1007/s10930-019-09827-6.   edoc | Open Access
Buser, D. P. and Spiess, M. (2019) “Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells ”, Journal of visualized experiments. JoVE, 144, p. e59111. doi: 10.3791/59111.   edoc
Buser, D. P., Schleicher, K. D., Prescianotto-Baschong, C. and Spiess, M. (2018) “A versatile nanobody-based toolkit to analyze retrograde transport from the cell surface”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 115(27), pp. E6227-E6236. doi: 10.1073/pnas.1801865115.   edoc
Estoppey, D., Lee, C. M., Janoschke, M., Lee, B. H., Wan, K. F., Dong, H., Mathys, P., Filipuzzi, I., Schuhmann, T., Riedl, R., Aust, T., Galuba, O., McAllister, G., Russ, C., Spiess, M., Bouwmeester, T., Bonamy, G. M. C. and Hoepfner, D. (2017) “The Natural Product Cavinafungin Selectively Interferes with Zika and Dengue Virus Replication by Inhibition of the Host Signal Peptidase”, Cell Reports . Elsevier, 19(3), pp. 451–460. doi: 10.1016/j.celrep.2017.03.071.   edoc
Beuret, N., Hasler, F., Prescianotto-Baschong, C., Birk, J., Rutishauser, J. and Spiess, M. (2017) “Amyloid-like aggregation of provasopressin in diabetes insipidus and secretory granule sorting”, BMC Biology. BioMed Central, 15(1), p. 5. doi: 10.1186/s12915-017-0347-9.   edoc
Shi, G., Somlo, D., Kim, G. H., Prescianotto-Baschong, C., Sun, S., Beuret, N., Long, Q., Rutishauser, J., Arvan, P., Spiess, M. and Qi, L. (2017) “ER-associated degradation is required for vasopressin prohormone processing and systemic water homeostasis”, Journal of Clinical Investigation. American Society for Clinical Investigation, 127(10), pp. 3897–3912. doi: 10.1172/JCI94771.   edoc
Junne, T. and Spiess, M. (2017) “Integration of transmembrane domains is regulated by their downstream sequences”, Journal of Cell Science. Company of Biologists, 130, pp. 372–381. doi: 10.1242/jcs.194472.   edoc | Open Access
Rutishauser, J., Spiess, M. and Kopp, P. (2016) “Genetic forms of neurohypophyseal diabetes insipidus”, Best practice and research clinical endocrinology and metabolism. Elsevier, 30(2), pp. 249–262. doi: 10.1016/j.beem.2016.02.008.   edoc
Kälin, S., Buser, D. P. and Spiess, M. (2016) “A fresh look at the function of Rabaptin5 on endosomes”, Small GTPases. Taylor & Francis, 7(1), pp. 34–37. doi: 10.1080/21541248.2016.1140616.   edoc
Kälin, S., Hirschmann, D. T., Buser, D. P. and Spiess, M. (2015) “Rabaptin5 is recruited to endosomes by Rab4 and Rabex5 to regulate endosome maturation”, Journal of Cell Science. Company of Biologists, 128(22), pp. 4126–4137. doi: 10.1242/jcs.174664.   edoc | Open Access
Ramming, T., Okumura, M., Kanemura, S., Baday, S., Birk, J., Moes, S., Spiess, M., Jenö, P., Bernèche, S., Inaba, K. and Appenzeller-Herzog, C. (2015) “A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1”, Free radical biology & medicine. Pergamon Press , 83, pp. 361–372. doi: 10.1016/j.freeradbiomed.2015.02.011.   edoc
Deyan Mihov and Martin Spiess (2015) “Glycosaminoglycans: sorting determinants in intracellular protein traffic”, The international journal of biochemistry & cell biology. Elsevier, Vol. 68, pp. 87–91. doi: 10.1016/j.biocel.2015.08.019.   edoc
Mihov, D., Raja, E. and Spiess, M. (2015) “Chondroitin Sulfate Accelerates Trans-Golgi-to-Surface Transport of Proteoglycan Amyloid Precursor Protein”, Traffic. Blackwell, Vol. 16, H. 8, pp. 853–870. doi: 10.1111/tra.12294.   edoc
Junne, T., Wong, J., Studer, C., Aust, T., Bauer, B. W., Beibel, M., Bhullar, B., Bruccoleri, R., Eichenberger, J., Estoppey, D., Hartmann, N., Knapp, B., Krastel, P., Melin, N., Oakeley, E. J., Oberer, L., Riedl, R., Roma, G., Schuierer, S., Petersen, F., Tallarico, J. A., Rapoport, T. A., Spiess, M. and Hoepfner, D. (2015) “Decatransin, a novel natural product inhibiting protein translocation at the Sec61/SecY translocon”, Journal of Cell Science. Company of Biologists, 128(6), pp. 1217–1229. doi: 10.1242/jcs.165746.   edoc | Open Access
Huser, S., Suri, G., Crottet, P. and Spiess, M. (2015) “Recruitment of coat proteins to liposomes and peptidoliposomes”, Methods in Molecular Biology. Humana Press, Vol. 1270, pp. 91–106. doi: 10.1007/978-1-4939-2309-0_7.   edoc
Hirschmann, D. T., Kasper, C. A. and Spiess, M. (2015) “Quantitative analysis of transferrin cycling by automated fluorescence microscopy”, Methods in Molecular Biology. Humana Press, Vol. 1270, pp. 365–378. doi: 10.1007/978-1-4939-2309-0_25.   edoc
Spiess, M. (2014) “Protein Translocation : The Sec61/SecYEG Translocon Caught in the Act”, Current biology. Cell Press, Vol. 24, H. 8 , R317-319. doi: 10.1016/j.cub.2014.02.051.   edoc
Demirci, E., Junne, T., Baday, S., Bernèche, S. and Spiess, M. (2013) “Functional asymmetry within the Sec61p translocon”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, Vol. 110, H. 47, pp. 18856–18861. doi: 10.1073/pnas.1318432110.   edoc
Sommer, N., Junne, T., Kalies, K.-U., Spiess, M. and Hartmann, E. (2013) “TRAP assists membrane protein topogenesis at the mammalian ER membrane”, Biochimica et biophysica acta. Elsevier, Vol. 1833, H. 12, pp. 3104–3111. doi: 10.1016/j.bbamcr.2013.08.018.   edoc
Seuring, C., Nespovitaya, N., Rutishauser, J., Spiess, M. and Riek, R. (2013) “Hormone amyloids in sickness and in health”, in Amyloid fibrils and prefibrillar aggregates : molecular and biological properties. Weinheim, Germany: Wiley-VCH Verlag, pp. 395–410.   edoc
Huser, S., Suri, G., Crottet, P. and Spiess, M. (2013) “Interaction of amphiphysins with AP-1 clathrin adaptors at the membrane”, Biochemical journal. Portland Press, Vol. 450, Pt. 1, pp. 73–83. doi: 10.1042/BJ20121373.   edoc
Kocik, L., Junne, T. and Spiess, M. (2012) “Orientation of Internal Signal-Anchor Sequences at the Sec61 Translocon”, Journal of molecular biology. Elsevier, Vol. 424, H. 5, pp. 368–378. doi: 10.1016/j.jmb.2012.10.010.   edoc
Appenzeller-Herzog, C., Riemer, J., Zito, E., Chin, K.-T., Ron, D., Spiess, M. and Ellgaard, L. (2010) “Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated”, The EMBO journal. Nature Publishing Group, Vol. 29, H. 19, pp. 3318–3329. doi: 10.1038/emboj.2010.203.   edoc | Open Access
Junne, T., Kocik, L. and Spiess, M. (2010) “The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration”, Molecular Biology of the Cell. American Society for Cell Biology, 21(10), pp. 1662–1670. doi: 10.1091/mbc.E10-01-0060.   edoc | Open Access
Kobialka, S., Beuret, N., Ben-Tekaya, H. and Spiess, M. (2009) “Glycosaminoglycan chains affect exocytic and endocytic protein traffic”, Traffic. Blackwell, Vol. 10, H. 12, pp. 1845–1855.   edoc
Stettler, H., Beuret, N., Prescianotto-Baschong, C., Fayard, B., Taupenot, L. and Spiess, M. (2009) “Determinants for chromogranin A sorting into the regulated secretory pathway are also sufficient to generate granule-like structures in non-endocrine cells”, The Biochemical Journal. Portland Press, Vol. 418, Pt. 1, pp. 81–91.   edoc
Birk, J., Friberg, M. A., Prescianotto-Baschong, C., Spiess, M. and Rutishauser, J. (2009) “Dominant pro-vasopressin mutants that cause diabetes insipidus form disulfide-linked fibrillar aggregates in the endoplasmic reticulum”, Journal of cell science. Company of Biologists, Vol. 122, H. 21, pp. 3994–4002.   edoc
Suri, G., Spiess, M. and Crottet, P. (2008) “Recruitment of coat proteins to peptidoliposomes”, Methods in Molecular Biology. Humana Press, 457, pp. 227–239.   edoc
Junne, T., Schwede, T., Goder, V. and Spiess, M. (2007) “Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 282, H. 45, pp. 33201–33209. doi: 10.1074/jbc.M707219200.   edoc
Junne, T., Schwede, T., Goder, V. and Spiess, M. (2006) “The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability”, Molecular Biology of the Cell. American Society for Cell Biology, 17(9), pp. 4063–4068. doi: 10.1091/mbc.E06-03-0200.   edoc | Open Access
Pagano, A. and Spiess, M. (2005) “Reconstitution of Rab4-dependent vesicle formation in vitro”, Methods in enzymology, vol. 403, pp. 81–92.   edoc
Higy, M., Gander, S. and Spiess, M. (2005) “Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum”, Biochemistry. American Chemical Society, Vol. 44, H. 6, pp. 2039–2047.   edoc
Stettler, H., Suri, G. and Spiess, M. (2005) “Proprotein convertase PC3 is not a transmembrane protein”, Biochemistry. American Chemical Society, Vol. 44, H. 14, pp. 5339–5345.   edoc
Meyer, D. M., Crottet, P., Maco, B., Degtyar, E., Cassel, D. and Spiess, M. (2005) “Oligomerization and dissociation of AP-1 adaptors are regulated by cargo signals and by ArfGAP1-induced GTP hydrolysis”, Molecular Biology of the Cell. American Society for Cell Biology, 16(10), pp. 4745–4754. doi: 10.1091/mbc.E05-06-0568.   edoc | Open Access
Beuret, N., Stettler, H., Renold, A., Rutishauser, J. and Spiess, M. (2004) “Expression of regulated secretory proteins is sufficient to generate granule-like structures in constitutively secreting cells”, Journal of Biological Chemistry. American Society of Biological Chemists, Vol. 279, H. 19, pp. 20242–20249.   edoc
Higy, M., Junne, T. and Spiess, M. (2004) “Topogenesis of membrane proteins at the endoplasmic reticulum”, Biochemistry. American Chemical Society, Vol. 43, H. 40, pp. 12716–12722.   edoc
Goder, V., Junne, T. and Spiess, M. (2004) “Sec61p contributes to signal sequence orientation according to the positive-inside rule”, Molecular Biology of the Cell. American Society for Cell Biology, 15(3), pp. 1470–1478. doi: 10.1091/mbc.E03-08-0599.   edoc | Open Access
Friberg, M. A., Spiess, M. and Rutishauser, J. (2004) “Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome”, Journal of Biological Chemistry. American Society of Biological Chemists, Vol. 279, H. 19, pp. 19441–19447.   edoc
Pagano, A., Crottet, P., Prescianotto-Baschong, C. and Spiess, M. (2004) “In vitro formation of recycling vesicles from endosomes requires adaptor protein-1/clathrin and is regulated by rab4 and the connector rabaptin-5”, Molecular Biology of the Cell. American Society for Cell Biology, 15(11), pp. 4990–5000. doi: 10.1091/mbc.E04-04-0355.   edoc | Open Access
Goder, V. and Spiess, M. (2003) “Molecular mechanism of signal sequence orientation in the endoplasmic reticulum”, The EMBO journal. Nature Publishing Group, Vol. 22, H. 14, pp. 3645–3653.   edoc
Vogel, L. K., Sahkri, S., Sjostrom, H., Noren, O. and Spiess, M. (2002) “Secretion of antithrombin is converted from nonpolarized to apical by exchanging its amino terminus for that of apically secreted family members”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 277 , no. 16, pp. 13883–13888.   edoc
Crottet, P., Meyer, D. M., Rohrer, J. and Spiess, M. (2002) “ARF1.GTP, tyrosine-based signals, and phosphatidylinositol 4,5-bisphosphate constitute a minimal machinery to recruit the AP-1 clathrin adaptor to membranes”, Molecular Biology of the Cell. American Society for Cell Biology, 13(10), pp. 3672–3682. doi: 10.1091/mbc.E02-05-0309.   edoc | Open Access
Rutishauser, J. and Spiess, M. (2002) “Endoplasmic reticulum storage diseases”, Swiss Medical Weekly. EMH, Vol. 132, H. 17/18, pp. 211–222.   edoc
Dumermuth, E., Beuret, N., Spiess, M. and Crottet, P. (2002) “Ubiquitous 9-O-acetylation of sialoglycoproteins restricted to the Golgi complex”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 277 , no. 21, pp. 18687–18693.   edoc
Goder, V. and Spiess, M. (2001) “Topogenesis of membrane proteins : determinants and dynamics”, FEBS letters. Elsevier Science, Vol. 504, H. 3, pp. 87–93.   edoc
Laird, V. (2000) “Endocytosis meets exocytosis”, in Protein, lipid and membrane traffic. Amsterdam: IOS Press, p. 211.   edoc
Renold, A., Cescato, R., Beuret, N., Vogel, L. K., Wahlberg, J. M., Brown, J. L., Fiedler, K. and Spiess, M. (2000) “Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 275 , no. 13, pp. 9290–9295.   edoc
Rosch, K., Naeher, D., Laird, V., Goder, V. and Spiess, M. (2000) “The topogenic contribution of uncharged amino acids on signal sequence orientation in the endoplasmic reticulum”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 275 , no. 20, pp. 14916–14922.   edoc
Laird, V. and Spiess, M. (2000) “A novel assay to demonstrate an intersection of the exocytic and endocytic pathways at early endosomes”, Experimental cell research. Elsevier, Vol. 260, H. 2, pp. 340–345.   edoc
Goder, V., Crottet, P. and Spiess, M. (2000) “In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation”, The EMBO journal. Nature Publishing Group, Vol. 19, H. 24, pp. 6704–6712.   edoc
Cescato, R., Dumermuth, E., Spiess, M. and Paganetti, P. A. (2000) “Increased generation of alternatively cleaved beta-amyloid peptides in cells expressing mutants of the amyloid precursor protein defective in endocytosis”, Journal of neurochemistry. Wiley-Blackwell, Vol. 74, H. 3, pp. 1131–1139.   edoc
Meier, M., Bider, M. D., Malashkevich, V. N., Spiess, M. and Burkhard, P. (2000) “Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor”, Journal of molecular biology. Elsevier, Vol. 300, H. 4, pp. 857–865.   edoc
Goder, V. and Spiess, M. (1999) “Topogenesis”, in Encyclopedia of molecular biology. New York: John Wiley (Wiley biotechnology encyclopedias), pp. 2561–2567.   edoc
Goder, V., Bieri, C. and Spiess, M. (1999) “Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon”, The Journal of cell biology. Rockefeller University Press, Vol. 147, H. 2, pp. 257–266. doi: 10.1083/jcb.147.2.257.   edoc | Open Access
Spiess, M. (1999) “Structure and function of the hepatic lectin”, Biovalley Newsletter. BioValley, Vol. 2, H. 2, p. 10.   edoc
Heilker, R., Spiess, M. and Crottet, P. (1999) “Recognition of sorting signals by clathrin adaptors”, Bioessays. The Company of Biologists, Vol. 21, H. 7, pp. 558–567.   edoc
Beuret, N., Rutishauser, J., Bider, M. D. and Spiess, M. (1999) “Mechanism of endoplasmic reticulum retention of mutant vasopressin precursor caused by a signal peptide truncation associated with diabetes insipidus”, Journal of Biological Chemistry. American Society of Biological Chemists, Vol. 274, H. 27, pp. 18965–18972.   edoc
Spiess, M. and Beuret, N. (1998) “PCR-directed in vitro mutagenesis using a ‘temporary’ restriction site”, Technical Tips Online. Elsevier, 1998, T01388.   edoc
Bider, M. D. and Spiess, M. (1998) “Ligand-induced endocytosis of the asialoglycoprotein receptor : evidence for heterogeneity in subunit oligomerization”, FEBS letters. Elsevier Science, Vol. 434, H. 1/2, pp. 37–41.   edoc
Eusebio, A., Friedberg, T. and Spiess, M. (1998) “The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane”, Experimental cell research. Elsevier, Vol. 241, H. 1, pp. 181–185.   edoc
Wahlberg, J. M. and Spiess, M. (1997) “Multiple determinants direct the orientation of signal-anchor proteins : the topogenic role of the hydrophobic signal domain”, The Journal of cell biology. Rockefeller University Press, Vol. 137, H. 3, pp. 555–562. doi: 10.1083/jcb.137.3.555.   edoc | Open Access
Fuhrer, C. and Spiess, M. (1996) “The asialoglycoprotein receptor”, in Biomembranes. Vol. 4, Endocytosis and exocytosis. Greenwich, Conn.: Jai Press, pp. 175–199.   edoc
Heilker, R., Manning-Krieg, U., Zuber, J. F. and Spiess, M. (1996) “In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting”, The EMBO journal, Vol. 15, H. 11, pp. 2893–2899.   edoc
Cescato, R. and Spiess, M. (1996) “The signals for endocytosis and polarized sorting of the hepatic asialoglycoprotein receptor”, Zeitschrift für Gastroenterologie. Delta Verl, Vol. 34, Suppl. 3, pp. 89–91.   edoc
Bider, M. D., Wahlberg, J. M., Kammerer, R. A. and Spiess, M. (1996) “The oligomerization domain of the asialoglycoprotein receptor preferentially forms 2:2 heterotetramers in vitro”, Journal of Biological Chemistry. American Society of Biological Chemists, Vol. 271, H. 50, pp. 31996–32001.   edoc
Becker, S., Spiess, M. and Klenk, H. D. (1995) “The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus”, Journal of general virology. Cambridge University Press, Vol. 76, pp. 393–399.   edoc
Bider, M. D., Cescato, R., Jeno, P. and Spiess, M. (1995) “High-affinity ligand binding to subunit H1 of the asialoglycoprotein receptor in the absence of subunit H2”, European journal of biochemistry. Blackwell, Vol. 230, H. 1, pp. 207–212.   edoc
Denzer, A. J., Nabholz, C. E. and Spiess, M. (1995) “Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain”, The EMBO journal. Nature Publishing Group, Vol. 14, H. 24, pp. 6311–6317.   edoc
Leitinger, B., Hille-Rehfeld, A. and Spiess, M. (1995) “Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, Vol. 92, H. 22, pp. 10109–10113.   edoc
Spiess, M. (1995) “Heads or tails - what determines the orientation of proteins in the membrane”, FEBS letters. Elsevier Science, Vol. 369, H. 1, pp. 76–79.   edoc
Wahlberg, J. M., Geffen, I., Reymond, F., Simmen, T. and Spiess, M. (1995) “trans-Golgi retention of a plasma membrane protein : mutations in the cytoplasmic domain of the asialoglycoprotein receptor subunit h1 result in trans-Golgi retention”, The Journal of cell biology. Rockefeller University Press, Vol. 130, H. 2, pp. 285–297. doi: 10.1083/jcb.130.2.285.   edoc | Open Access
Fuhrer, C., Geffen, I., Huggel, K. and Spiess, M. (1994) “The two subunits of the asialoglycoprotein receptor contain different sorting information”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 269, H. 5, pp. 3277–3282.   edoc
Leitinger, B., Brown, J. L. and Spiess, M. (1994) “Tagging secretory and membrane proteins with a tyrosine sulfation site : Tyrosine sulfation precedes galactosylation and sialylation in COS-7 cells”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 269, pp. 8115–8121.   edoc
Dihanich, M. and Spiess, M. (1994) “A novel serine proteinase-like sequence from human brain”, Biochimica et biophysica acta. Elsevier, Vol. 1218, H. 2, pp. 225–228.   edoc
Geffen, I., Fuhrer, C., Leitinger, B., Weiss, M., Huggel, K., Griffiths, G. and Spiess, M. (1993) “Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 268, H. 28, pp. 20772–20777.   edoc
Geffen, I. and Spiess, M. (1992) “The asialoglycoprotein receptor”, International review of cytology. Academic Press, Vol. 137b, pp. 181–219.   edoc
Vogel, L. K., Spiess, M., Sjostrom, H. and Noren, O. (1992) “Evidence for an apical sorting signal on the ectodomain of human aminopeptidase N”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 267, H. 4, pp. 2794–2797.   edoc
Geffen, I. and Spiess, M. (1992) “Phorbol Ester-Induced redistribution of the ASGP receptor is independent of receptor phosphorylation”, FEBS letters. Elsevier Science, Vol. 305, H. 3, pp. 209–212.   edoc
Wessels, H. P., Beltzer, J. P. and Spiess, M. (1991) “Analysis of protein topology in the endoplasmic reticulum”, Methods in cell biology. Elsevier, vol. 34, pp. 287–302.   edoc
Fuhrer, C., Geffen, I. and Spiess, M. (1991) “Endocytosis of the ASGP receptor H1 is reduced by mutation of tyrosine-5 but still occurs via coated pits”, The Journal of cell biology. Rockefeller University Press, Vol. 114, H. 3, pp. 423–432. doi: 10.1083/jcb.114.3.423.   edoc | Open Access
Geffen, I., Fuhrer, C. and Spiess, M. (1991) “Endocytosis by the asialoglycoprotein receptor is independent of cytoplasmic serine residues”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, Vol. 88, H. 19, pp. 8425–8429.   edoc
Beltzer, J. P. and Spiess, M. (1991) “In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles”, The EMBO journal. Nature Publishing Group, Vol. 10, H. 12, pp. 3735–3742.   edoc
Wessels, H. P., Hansen, G. H., Fuhrer, C., Look, A. T., Sjostrom, H., Noren, O. and Spiess, M. (1990) “Aminopeptidase N is directly sorted to the apical domain in MDCK cells”, Journal of Cell Biology. Rockefeller University Press, 111(6), pp. 2923–2930. doi: 10.1083/jcb.111.6.2923.   edoc
Spiess, M. (1990) “The asialoglycoprotein receptor : a model for endocytic transport receptors”, Biochemistry. American Chemical Society, Vol. 29, H. 43, pp. 10009–10018.   edoc
Spiess, M., Handschin, C. and Baker, K. P. (1989) “Stop-transfer activity of hydrophobic sequences depends on the translation system”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 264, pp. 19117–19124.   edoc
Beltzer, J. P., Wessels, H. P. and Spiess, M. (1989) “Signal peptidase can cleave inside a polytopic membrane protein”, FEBS letters. Elsevier Science, Vol. 253, H. 1/2, pp. 93–98.   edoc
Geffen, I., Wessels, H. P., Roth, J., Shia, M. A. and Spiess, M. (1989) “Endocytosis and recycling of subunit H1 of the asialoglycoprotein receptor is independent of oligomerization with H2”, The EMBO journal. Nature Publishing Group, Vol. 8, H. 10, pp. 2855–2862.   edoc
Olsen, J., Cowell, G. M., Konigshofer, E., Danielsen, E. M., Moller, J., Laustsen, L., Hansen, O. C., Welinder, K. G., Engberg, J., Hunziker, W., Spiess, M., Sjostrom, H. and Noren, O. (1988) “Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA”, FEBS Letters. Wiley, 238(2), pp. 307–314. doi: 10.1016/0014-5793(88)80502-7.   edoc
Wessels, H. P. and Spiess, M. (1988) “Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence”, Cell. Cell Press, Vol. 55, H. 1, pp. 61–70.   edoc
Schmid, S. R. and Spiess, M. (1988) “Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 263, pp. 16886–16891.   edoc
Spiess, M., Hunziker, W., Lodish, H. F. and Semenza, G. (1987) “Molecular cell biology of brush border hydrolases : sucrase-isomaltase and gamma-glutamyl transpeptidase”, in Mammalian Ectoenzymes. Amsterdam: Elsevier Science Publishers B.V, pp. 87–110.   edoc
Hu, C. B., Spiess, M. and Semenza, G. (1987) “The mode of anchoring and precursor forms of sucrase-isomaltase and maltase-glucoamylase in chicken intestinal brush-border membrane Phylogenetic implications”, Biochimica et biophysica acta. Elsevier, Vol. 896, H. 2, pp. 275–286.   edoc
Hunziker, W., Spiess, M., Semenza, G. and Lodish, H. F. (1986) “The sucrase-isomaltase complex : primary structure, membrane- orientation, and evolution of a stalked, intrinsic brush border protein”, Cell. Cell Press, Vol. 46, H. 2, pp. 227–234.   edoc
Spiess, M. and Lodish, H. F. (1986) “An internal signal sequence : the asialoglycoprotein receptor membrane anchor”, Cell. Cell Press, Vol. 44, H. 1, pp. 177–185.   edoc
Barsukov, L. I., Bergelson, L. D., Spiess, M., Hauser, H. and Semenza, G. (1986) “Phospholipid topology and flip-flop in intestinal brush-border membrane”, Biochimica et biophysica acta. Elsevier, Vol. 862, H. 1, pp. 87–99.   edoc
Spiess, M., Schwartz, A. L. and Lodish, H. F. (1985) “Sequence of human asialoglycoprotein receptor cDNA. An internal signal sequence for membrane insertion”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 260, pp. 1979–1982.   edoc
Spiess, M. and Lodish, H. F. (1985) “Sequence of a second human asialoglycoprotein receptor : conservation of two receptor genes during evolution”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, Vol. 82, pp. 6465–6469.   edoc
Brunner, J., Spiess, M., Aggeler, R., Huber, P. and Semenza, G. (1983) “Hydrophobic labeling of a single leaflet of the human erythrocyte membrane”, Biochemistry. American Chemical Society, Vol. 22, H. 16, pp. 3812–3820.   edoc
Trueb, B., Grobli, B., Spiess, M., Odermatt, B. F. and Winterhalter, K. H. (1982) “Basement membrane (type IV) collagen is a heteropolymer”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 257(9), pp. 5239–5245. Available at: http://www.jbc.org/content/257/9/5239.full.pdf.   edoc
Sjostrom, H., Noren, O., Christiansen, L. A., Wacker, H., Spiess, M., Biglermeier, B., Rickli, E. E. and Semenza, G. (1982) “N-Terminal sequences of pig intestinal sucrase-isomaltase and pro-sucrase--isomaltase. Implications for the biosynthesis and membrane insertion of pro-sucrase--isomaltase”, FEBS Letters. Wiley, 148(2), pp. 321–325. doi: 10.1016/0014-5793(82)80833-8.   edoc
Barsukov, L. I., Spiess, M. and Bergelson, L. D. (1982) “Transbilayer distribution of PC and PE in microvillous membrane vesicles from rabbit small intestine”, Doklady Akademii Nauk SSSR, Vol. 266, pp. 1014–1016.   edoc
Spiess, M., Brunner, J. and Semenza, G. (1982) “Hydrophobic labeling, isolation, and partial characterization of the NHâ‚‚-terminal membranous segment of sucrase-isomaltase complex”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 257, pp. 2370–2377.   edoc
Hauser, H., Gains, N., Semenza, G. and Spiess, M. (1982) “Orientation and motion of spin-labels in rabbit small intestinal brush border vesicle membranes”, Biochemistry. American Chemical Society, Vol. 21, H. 22, pp. 5621–5628.   edoc
Spiess, M., Hauser, H., Rosenbusch, J. P. and Semenza, G. (1981) “Hydrodynamic properties of phospholipid vesicles and of sucrase isomaltase-phospholipid vesicles”, Journal of biological chemistry. American Society of Biological Chemists, Vol. 256, H. 17, pp. 8977–8982.   edoc
Trüeb, B., Odermatt, B. F., Sahu, A. P., Spiess, M., Rüttner, J. R. and Winterhalter, K. H. (1980) “Type IV collagen is a heteropolymer with the formula C2D”, Kidney & Blood Pressure Research. Karger, 3(1-6), pp. 23–29. doi: 10.1159/000172737.   edoc
Hauser, H., Guyer, W., Spiess, M., Pascher, I. and Sundell, S. (1980) “The polar group conformation of a lysophosphatidyl choline analogue in solution : a high resolution nuclear magnetic resonance study”, Journal of molecular biology. Elsevier, Vol. 137, pp. 265–282.   edoc