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Itskanov, Samuel and Wang, Laurie and Junne, Tina and Sherriff, Rumi and Xiao, Li and Blanchard, Nicolas and Shi, Wei Q. and Forsyth, Craig and Hoepfner, Dominic and Spiess, Martin and Park, Eunyong. (2023) A common mechanism of Sec61 translocon inhibition by small molecules. Nature Chemical Biology.

Pennauer, Mirjam and Buczak, Katarzyna and Prescianotto-Baschong, Cristina and Spiess, Martin. (2022) Shared and specific functions of Arfs 1-5 at the Golgi revealed by systematic knockouts. Journal of Cell Biology, 221 (1). e202106100.

Reck, Jennifer and Beuret, Nicole and Demirci, Erhan and Prescianotto-Baschong, Cristina and Spiess, Martin. (2022) Small disulfide loops in peptide hormones mediate self-aggregation and secretory granule sorting. Life science alliance, 5 (5). e202101279.

Millarte, Valentina and Spiess, Martin. (2022) RABEP1/Rabaptin5: a link between autophagy and early endosome homeostasis. Autophagy, 18. pp. 1-2.

Buser, Dominik P. and Bader, Gaétan and Spiess, Martin. (2022) Retrograde transport of CDMPR depends on several machineries as analyzed by sulfatable nanobodies. Life science alliance, 5 (7). e202101269.

Janoschke, Marco and Zimmermann, Mirjam and Brunauer, Anna and Humbel, Raffael and Junne, Tina and Spiess, Martin. (2021) Efficient integration of transmembrane domains depends on the folding properties of the upstream sequences. Proceedings of the National Academy of Sciences of the United States of America, 118 (33). e2102675118.

Jung, Sung-Jun and Kim, Ji Eun Hani and Junne, Tina and Spiess, Martin and Kim, Hyun. (2021) Cotranslational Targeting and Posttranslational Translocation can Cooperate in Spc3 Topogenesis. Journal of Molecular Biology, 433 (18). p. 167109.

Millarte, Valentina and Schlienger, Simon and Kälin, Simone and Spiess, Martin. (2021) Rabaptin5 targets autophagy to damaged endosomes and Salmonella vacuoles via FIP200 and ATG16L1. EMBO Reports. e53429.

Spiess, Martin and Beuret, Nicole and Rutishauser, Jonas. (2020) Genetic forms of neurohypophyseal diabetes insipidus. Best Practice and Research Clinical Endocrinology and Metabolism, 34 (5). p. 101432.

Spiess, Martin and Beuret, Nicole and Prescianotto Baschong, Cristina and Rutishauser, Jonas. (2020) Amyloid-like aggregation of provasopressin. Vitamins and hormones, 113. pp. 55-77.

Spiess, Martin and Friberg, Michael and Beuret, Nicole and Prescianotto-Baschong, Cristina and Rutishauser, Jonas. (2020) Role of protein aggregation and degradation in autosomal dominant neurohypophyseal diabetes insipidus. Molecular and cellular endocrinology, 501. p. 110653.

Buser, Dominik P. and Spiess, Martin. (2019) Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells. Journal of visualized experiments, 144. e59111.

Spiess, Martin and Junne, Tina and Janoschke, Marco. (2019) Membrane Protein Integration and Topogenesis at the ER. The Protein Journal, 38 (3). pp. 306-316.

Buser, Dominik P. and Ritz, Marie-Françoise and Moes, Suzette and Tostado, Cristobal and Frank, Stephan and Spiess, Martin and Mariani, Luigi and Jenö, Paul and Boulay, Jean-Louis and Hutter, Gregor. (2019) Quantitative proteomics reveals reduction of endocytic machinery components in gliomas. EBioMedicine, 46. pp. 36-41.

Rutishauser, Jonas and Beuret, Nicole and Prescianotto-Baschong, Cristina and Spiess, Martin. (2019) Hereditary Neurohypophyseal Diabetes Insipidus. In: Genetics of Endocrine Diseases and Syndromes. Cham, pp. 299-315.

Buser, Dominik P. and Schleicher, Kai D. and Prescianotto-Baschong, Cristina and Spiess, Martin. (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, 115 (27). E6227-E6236.

Junne, Tina and Spiess, Martin. (2017) Integration of transmembrane domains is regulated by their downstream sequences. Journal of Cell Science, 130. pp. 372-381.

Beuret, Nicole and Hasler, Franziska and Prescianotto-Baschong, Cristina and Birk, Julia and Rutishauser, Jonas and Spiess, Martin. (2017) Amyloid-like aggregation of provasopressin in diabetes insipidus and secretory granule sorting. BMC Biology, 15 (1). p. 5.

Estoppey, David and Lee, Chia Min and Janoschke, Marco and Lee, Boon Heng and Wan, Kah Fei and Dong, Hongping and Mathys, Philippe and Filipuzzi, Ireos and Schuhmann, Tim and Riedl, Ralph and Aust, Thomas and Galuba, Olaf and McAllister, Gregory and Russ, Carsten and Spiess, Martin and Bouwmeester, Tewis and Bonamy, Ghislain M. C. and Hoepfner, Dominic. (2017) The Natural Product Cavinafungin Selectively Interferes with Zika and Dengue Virus Replication by Inhibition of the Host Signal Peptidase. Cell Reports , 19 (3). pp. 451-460.

Shi, Guojun and Somlo, Diane and Kim, Geun Hyang and Prescianotto-Baschong, Cristina and Sun, Shengyi and Beuret, Nicole and Long, Qiaoming and Rutishauser, Jonas and Arvan, Peter and Spiess, Martin and Qi, Ling. (2017) ER-associated degradation is required for vasopressin prohormone processing and systemic water homeostasis. Journal of Clinical Investigation, 127 (10). pp. 3897-3912.

Rutishauser, Jonas and Spiess, Martin and Kopp, Peter. (2016) Genetic forms of neurohypophyseal diabetes insipidus. Best practice and research clinical endocrinology and metabolism, 30 (2). pp. 249-262.

Kälin, Simone and Buser, Dominik P. and Spiess, Martin. (2016) A fresh look at the function of Rabaptin5 on endosomes. Small GTPases, 7 (1). pp. 34-37.

Kälin, Simone and Hirschmann, David T. and Buser, Dominik P. and Spiess, Martin. (2015) Rabaptin5 is recruited to endosomes by Rab4 and Rabex5 to regulate endosome maturation. Journal of Cell Science, 128 (22). pp. 4126-4137.

Ramming, Thomas and Okumura, Masaki and Kanemura, Shingo and Baday, Sefer and Birk, Julia and Moes, Suzette and Spiess, Martin and Jenö, Paul and Bernèche, Simon and Inaba, Kenji and Appenzeller-Herzog, Christian. (2015) A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1. Free radical biology & medicine, 83. pp. 361-372.

Hirschmann, David T. and Kasper, Christoph A. and Spiess, Martin. (2015) Quantitative analysis of transferrin cycling by automated fluorescence microscopy. Methods in Molecular Biology, Vol. 1270. pp. 365-378.

Junne, Tina and Wong, Joanne and Studer, Christian and Aust, Thomas and Bauer, Benedikt W. and Beibel, Martin and Bhullar, Bhupinder and Bruccoleri, Robert and Eichenberger, Jürg and Estoppey, David and Hartmann, Nicole and Knapp, Britta and Krastel, Philipp and Melin, Nicolas and Oakeley, Edward J. and Oberer, Lukas and Riedl, Ralph and Roma, Guglielmo and Schuierer, Sven and Petersen, Frank and Tallarico, John A. and Rapoport, Tom A. and Spiess, Martin and Hoepfner, Dominic. (2015) Decatransin, a novel natural product inhibiting protein translocation at the Sec61/SecY translocon. Journal of Cell Science, 128 (6). pp. 1217-1229.

Huser, Sonja and Suri, Gregor and Crottet, Pascal and Spiess, Martin. (2015) Recruitment of coat proteins to liposomes and peptidoliposomes. Methods in Molecular Biology, Vol. 1270. pp. 91-106.

Mihov, Deyan and Raja, Eva and Spiess, Martin. (2015) Chondroitin Sulfate Accelerates Trans-Golgi-to-Surface Transport of Proteoglycan Amyloid Precursor Protein. Traffic, Vol. 16, H. 8. pp. 853-870.

Deyan Mihov, and Martin Spiess, . (2015) Glycosaminoglycans: sorting determinants in intracellular protein traffic. The international journal of biochemistry & cell biology, Vol. 68. pp. 87-91.

Spiess, Martin. (2014) Protein Translocation : The Sec61/SecYEG Translocon Caught in the Act. Current biology, Vol. 24, H. 8 , R317-319.

Huser, Sonja and Suri, Gregor and Crottet, Pascal and Spiess, Martin. (2013) Interaction of amphiphysins with AP-1 clathrin adaptors at the membrane. Biochemical journal, Vol. 450, Pt. 1. pp. 73-83.

Seuring, C. and Nespovitaya, N. and Rutishauser, J. and 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, pp. 395-410.

Sommer, Nicole and Junne, Tina and Kalies, Kai-Uwe and Spiess, Martin and Hartmann, Enno. (2013) TRAP assists membrane protein topogenesis at the mammalian ER membrane. Biochimica et biophysica acta, Vol. 1833, H. 12. pp. 3104-3111.

Demirci, Erhan and Junne, Tina and Baday, Sefer and Bernèche, Simon and Spiess, Martin. (2013) Functional asymmetry within the Sec61p translocon. Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, H. 47. pp. 18856-18861.

Kocik, Lucyna and Junne, Tina and Spiess, Martin. (2012) Orientation of Internal Signal-Anchor Sequences at the Sec61 Translocon. Journal of molecular biology, Vol. 424, H. 5. pp. 368-378.

Junne, T. and 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, 21 (10). pp. 1662-1670.

Appenzeller-Herzog, Christian and Riemer, Jan and Zito, Ester and Chin, King-Tung and Ron, David and Spiess, Martin and Ellgaard, Lars. (2010) Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated. The EMBO journal, Vol. 29, H. 19. pp. 3318-3329.

Birk, J. and Friberg, M. A. and Prescianotto-Baschong, C. and 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, Vol. 122, H. 21. pp. 3994-4002.

Stettler, H. and Beuret, N. and Prescianotto-Baschong, C. and Fayard, B. and 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, Vol. 418, Pt. 1. pp. 81-91.

Kobialka, S. and Beuret, N. and Ben-Tekaya, H. and Spiess, M.. (2009) Glycosaminoglycan chains affect exocytic and endocytic protein traffic. Traffic, Vol. 10, H. 12. pp. 1845-1855.

Suri, Gregor and Spiess, Martin and Crottet, Pascal. (2008) Recruitment of coat proteins to peptidoliposomes. Methods in Molecular Biology, 457. pp. 227-239.

Junne, T. and Schwede, T. and Goder, V. and Spiess, M.. (2007) Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology. Journal of biological chemistry, Vol. 282, H. 45. pp. 33201-33209.

Junne, T. and Schwede, T. and 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, 17 (9). pp. 4063-4068.

Meyer, D. M. and Crottet, P. and Maco, B. and Degtyar, E. and 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, 16 (10). pp. 4745-4754.

Stettler, H. and Suri, G. and Spiess, M.. (2005) Proprotein convertase PC3 is not a transmembrane protein. Biochemistry, Vol. 44, H. 14. pp. 5339-5345.

Higy, M. and Gander, S. and Spiess, M.. (2005) Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum. Biochemistry, Vol. 44, H. 6. pp. 2039-2047.

Pagano, Adriana and Spiess, Martin. (2005) Reconstitution of Rab4-dependent vesicle formation in vitro. Methods in enzymology, vol. 403. pp. 81-92.

Pagano, A. and Crottet, P. and 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, 15 (11). pp. 4990-5000.

Higy, M. and Junne, T. and Spiess, M.. (2004) Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry, Vol. 43, H. 40. pp. 12716-12722.

Beuret, N. and Stettler, H. and Renold, A. and 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, Vol. 279, H. 19. pp. 20242-20249.

Friberg, M. A. and Spiess, M. and Rutishauser, J.. (2004) Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome. Journal of Biological Chemistry, Vol. 279, H. 19. pp. 19441-19447.

Goder, V. and Junne, T. and Spiess, M.. (2004) Sec61p contributes to signal sequence orientation according to the positive-inside rule. Molecular Biology of the Cell, 15 (3). pp. 1470-1478.

Goder, V. and Spiess, M.. (2003) Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. The EMBO journal, Vol. 22, H. 14. pp. 3645-3653.

Rutishauser, J. and Spiess, M.. (2002) Endoplasmic reticulum storage diseases. Swiss Medical Weekly, Vol. 132, H. 17/18. pp. 211-222.

Vogel, L. K. and Sahkri, S. and Sjostrom, H. and 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, Vol. 277 , no. 16. pp. 13883-13888.

Crottet, P. and Meyer, D. M. and 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, 13 (10). pp. 3672-3682.

Dumermuth, E. and Beuret, N. and Spiess, M. and Crottet, P.. (2002) Ubiquitous 9-O-acetylation of sialoglycoproteins restricted to the Golgi complex. Journal of biological chemistry, Vol. 277 , no. 21. pp. 18687-18693.

Goder, V. and Spiess, M.. (2001) Topogenesis of membrane proteins : determinants and dynamics. FEBS letters, Vol. 504, H. 3. pp. 87-93.

Meier, M. and Bider, M. D. and Malashkevich, V. N. and 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, Vol. 300, H. 4. pp. 857-865.

Goder, V. and Crottet, P. and Spiess, M.. (2000) In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation. The EMBO journal, Vol. 19, H. 24. pp. 6704-6712.

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, Vol. 260, H. 2. pp. 340-345.

Cescato, R. and Dumermuth, E. and 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, Vol. 74, H. 3. pp. 1131-1139.

Rosch, K. and Naeher, D. and Laird, V. and 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, Vol. 275 , no. 20. pp. 14916-14922.

Renold, A. and Cescato, R. and Beuret, N. and Vogel, L. K. and Wahlberg, J. M. and Brown, J. L. and 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, Vol. 275 , no. 13. pp. 9290-9295.

Laird, V.. (2000) Endocytosis meets exocytosis. In: Protein, lipid and membrane traffic. Amsterdam, p. 211.

Spiess, M.. (1999) Structure and function of the hepatic lectin. Biovalley Newsletter, Vol. 2, H. 2. p. 10.

Heilker, R. and Spiess, M. and Crottet, P.. (1999) Recognition of sorting signals by clathrin adaptors. Bioessays, Vol. 21, H. 7. pp. 558-567.

Goder, V. and 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, Vol. 147, H. 2. pp. 257-266.

Beuret, N. and Rutishauser, J. and 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, Vol. 274, H. 27. pp. 18965-18972.

Goder, V. and Spiess, M.. (1999) Topogenesis. In: Encyclopedia of molecular biology, Vol. 4. New York, pp. 2561-2567.

Bider, M. D. and Spiess, M.. (1998) Ligand-induced endocytosis of the asialoglycoprotein receptor : evidence for heterogeneity in subunit oligomerization. FEBS letters, Vol. 434, H. 1/2. pp. 37-41.

Eusebio, A. and Friedberg, T. and Spiess, M.. (1998) The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane. Experimental cell research, Vol. 241, H. 1. pp. 181-185.

Spiess, M. and Beuret, N.. (1998) PCR-directed in vitro mutagenesis using a "temporary" restriction site. Technical Tips Online, 1998, T01388.

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, Vol. 137, H. 3. pp. 555-562.

Cescato, R. and Spiess, M.. (1996) The signals for endocytosis and polarized sorting of the hepatic asialoglycoprotein receptor. Zeitschrift für Gastroenterologie, Vol. 34, Suppl. 3. pp. 89-91.

Bider, M. D. and Wahlberg, J. M. and 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, Vol. 271, H. 50. pp. 31996-32001.

Heilker, R. and Manning-Krieg, U. and 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.

Fuhrer, C. and Spiess, M.. (1996) The asialoglycoprotein receptor. In: Biomembranes. Vol. 4, Endocytosis and exocytosis. Greenwich, Conn., pp. 175-199.

Spiess, M.. (1995) Heads or tails - what determines the orientation of proteins in the membrane. FEBS letters, Vol. 369, H. 1. pp. 76-79.

Leitinger, B. and 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, Vol. 92, H. 22. pp. 10109-10113.

Wahlberg, J. M. and Geffen, I. and Reymond, F. and 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, Vol. 130, H. 2. pp. 285-297.

Denzer, A. J. and 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, Vol. 14, H. 24. pp. 6311-6317.

Bider, M. D. and Cescato, R. and 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, Vol. 230, H. 1. pp. 207-212.

Becker, S. and Spiess, M. and Klenk, H. D.. (1995) The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus. Journal of general virology, Vol. 76. pp. 393-399.

Dihanich, M. and Spiess, M.. (1994) A novel serine proteinase-like sequence from human brain. Biochimica et biophysica acta, Vol. 1218, H. 2. pp. 225-228.

Leitinger, B. and 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, Vol. 269. pp. 8115-8121.

Fuhrer, C. and Geffen, I. and Huggel, K. and Spiess, M.. (1994) The two subunits of the asialoglycoprotein receptor contain different sorting information. Journal of biological chemistry, Vol. 269, H. 5. pp. 3277-3282.

Geffen, I. and Fuhrer, C. and Leitinger, B. and Weiss, M. and Huggel, K. and Griffiths, G. and Spiess, M.. (1993) Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor. Journal of biological chemistry, Vol. 268, H. 28. pp. 20772-20777.

Vogel, L. K. and Spiess, M. and Sjostrom, H. and Noren, O.. (1992) Evidence for an apical sorting signal on the ectodomain of human aminopeptidase N. Journal of biological chemistry, Vol. 267, H. 4. pp. 2794-2797.

Geffen, I. and Spiess, M.. (1992) Phorbol Ester-Induced redistribution of the ASGP receptor is independent of receptor phosphorylation. FEBS letters, Vol. 305, H. 3. pp. 209-212.

Geffen, I. and Spiess, M.. (1992) The asialoglycoprotein receptor. International review of cytology, Vol. 137b. pp. 181-219.

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, Vol. 10, H. 12. pp. 3735-3742.

Fuhrer, C. and 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, Vol. 114, H. 3. pp. 423-432.

Geffen, I. and 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, Vol. 88, H. 19. pp. 8425-8429.

Wessels, H. P. and Beltzer, J. P. and Spiess, M.. (1991) Analysis of protein topology in the endoplasmic reticulum. Methods in cell biology, vol. 34. pp. 287-302.

Spiess, M.. (1990) The asialoglycoprotein receptor : a model for endocytic transport receptors. Biochemistry, Vol. 29, H. 43. pp. 10009-10018.

Wessels, H. P. and Hansen, G. H. and Fuhrer, C. and Look, A. T. and Sjostrom, H. and Noren, O. and Spiess, Martin. (1990) Aminopeptidase N is directly sorted to the apical domain in MDCK cells. Journal of Cell Biology, 111 (6). pp. 2923-2930.

Geffen, I. and Wessels, H. P. and Roth, J. and 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, Vol. 8, H. 10. pp. 2855-2862.

Beltzer, J. P. and Wessels, H. P. and Spiess, M.. (1989) Signal peptidase can cleave inside a polytopic membrane protein. FEBS letters, Vol. 253, H. 1/2. pp. 93-98.

Spiess, M. and Handschin, C. and Baker, K. P.. (1989) Stop-transfer activity of hydrophobic sequences depends on the translation system. Journal of biological chemistry, Vol. 264. pp. 19117-19124.

Wessels, H. P. and Spiess, M.. (1988) Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell, Vol. 55, H. 1. pp. 61-70.

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, Vol. 263. pp. 16886-16891.

Olsen, J. and Cowell, G. M. and Konigshofer, E. and Danielsen, E. M. and Moller, J. and Laustsen, L. and Hansen, O. C. and Welinder, K. G. and Engberg, J. and Hunziker, W. and Spiess, Martin and Sjostrom, H. and Noren, O.. (1988) Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. FEBS Letters, 238 (2). pp. 307-314.

Hu, C. B. and 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, Vol. 896, H. 2,. pp. 275-286.

Spiess, M. and Hunziker, W. and Lodish, H. F. and Semenza, G.. (1987) Molecular cell biology of brush border hydrolases : sucrase-isomaltase and gamma-glutamyl transpeptidase. In: Mammalian Ectoenzymes. Amsterdam, pp. 87-110.

Barsukov, L. I. and Bergelson, L. D. and Spiess, M. and Hauser, H. and Semenza, G.. (1986) Phospholipid topology and flip-flop in intestinal brush-border membrane. Biochimica et biophysica acta, Vol. 862, H. 1. pp. 87-99.

Hunziker, W. and Spiess, M. and 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, Vol. 46, H. 2. pp. 227-234.

Spiess, M. and Lodish, H. F.. (1986) An internal signal sequence : the asialoglycoprotein receptor membrane anchor. Cell, Vol. 44, H. 1. pp. 177-185.

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, Vol. 82. pp. 6465-6469.

Spiess, M. and 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, Vol. 260. pp. 1979-1982.

Brunner, J. and Spiess, M. and Aggeler, R. and Huber, P. and Semenza, G.. (1983) Hydrophobic labeling of a single leaflet of the human erythrocyte membrane. Biochemistry, Vol. 22, H. 16. pp. 3812-3820.

Hauser, H. and Gains, N. and Semenza, G. and Spiess, M.. (1982) Orientation and motion of spin-labels in rabbit small intestinal brush border vesicle membranes. Biochemistry, Vol. 21, H. 22. pp. 5621-5628.

Spiess, M. and 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, Vol. 257. pp. 2370-2377.

Barsukov, L. I. and 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.

Sjostrom, H. and Noren, O. and Christiansen, L. A. and Wacker, H. and Spiess, Martin and Biglermeier, B. and 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, 148 (2). pp. 321-325.

Trueb, B. and Grobli, B. and Spiess, Martin and Odermatt, B. F. and Winterhalter, K. H.. (1982) Basement membrane (type IV) collagen is a heteropolymer. Journal of Biological Chemistry, 257 (9). pp. 5239-5245.

Spiess, M. and Hauser, H. and Rosenbusch, J. P. and Semenza, G.. (1981) Hydrodynamic properties of phospholipid vesicles and of sucrase isomaltase-phospholipid vesicles. Journal of biological chemistry, Vol. 256, H. 17. pp. 8977-8982.

Hauser, H. and Guyer, W. and Spiess, M. and 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, Vol. 137. pp. 265-282.

Trüeb, B. and Odermatt, B. F. and Sahu, A. P. and Spiess, Martin and Rüttner, J. R. and Winterhalter, K. H.. (1980) Type IV collagen is a heteropolymer with the formula C2D. Kidney & Blood Pressure Research, 3 (1-6). pp. 23-29.