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Spiess, Martin; Beuret, Nicole; Rutishauser, Jonas (2020). Genetic forms of neurohypophyseal diabetes insipidus. Best practice & research. Clinical endocrinology & metabolism, 101432.

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

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


Rutishauser, Jonas; Beuret, Nicole; Prescianotto-Baschong, Cristina; Spiess, Martin (2019). Hereditary Neurohypophyseal Diabetes Insipidus. Experientia supplementum (2012), 111, 299-315.

Buser, Dominik P.; Ritz, Marie-Françoise; Moes, Suzette; Tostado, Cristobal; Frank, Stephan; Spiess, Martin; Mariani, Luigi; Jenö, Paul; Boulay, Jean-Louis; Hutter, Gregor (2019). Quantitative proteomics reveals reduction of endocytic machinery components in gliomas. EBioMedicine, 46, 32-41.

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

Buser, Dominik P.; 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 (144), e59111.


Buser, Dominik P.; Schleicher, Kai D.; Prescianotto-Baschong, Cristina; 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.


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

Estoppey, David; Lee, Chia Min; Janoschke, Marco; Lee, Boon Heng; Wan, Kah Fei; Dong, Hongping; Mathys, Philippe; Filipuzzi, Ireos; Schuhmann, Tim; Riedl, Ralph; Aust, Thomas; Galuba, Olaf; McAllister, Gregory; Russ, Carsten; Spiess, Martin; Bouwmeester, Tewis; Bonamy, Ghislain M. C.; 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), 451-460.

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

Junne, Tina; Spiess, Martin (2017). Integration of transmembrane domains is regulated by their downstream sequences. Journal of Cell Science, 130 (2), 372-381.


Rutishauser, Jonas; Spiess, Martin; Kopp, Peter (2016). Genetic forms of neurohypophyseal diabetes insipidus. Best practice and research clinical endocrinology and metabolism, 30 (2), 249-62.

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


Kälin, Simone; Hirschmann, David T.; Buser, Dominik P.; Spiess, Martin (2015). Rabaptin5 is recruited to endosomes by Rab4 and Rabex5 to regulate endosome maturation. Journal of Cell Science, 128 (22), 4126-37.

Mihov, Deyan; Raja, Eva; Spiess, Martin (2015). Chondroitin Sulfate Accelerates Trans-Golgi-to-Surface Transport of Proteoglycan Amyloid Precursor Protein. Traffic, 16 (8), 853-70.

Hirschmann, David T.; Kasper, Christoph A.; Spiess, Martin (2015). Quantitative analysis of transferrin cycling by automated fluorescence microscopy. Methods in Molecular Biology, 1270, 365-78.

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

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

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

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


Spiess, Martin (2014). Protein Translocation : The Sec61/SecYEG Translocon Caught in the Act. Current biology, 24 (8), R317-9.


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

Sommer, Nicole; Junne, Tina; Kalies, Kai-Uwe; Spiess, Martin; Hartmann, Enno (2013). TRAP assists membrane protein topogenesis at the mammalian ER membrane. Biochimica et biophysica acta, 1833 (12), 3104-11.

Seuring, C.; Nespovitaya, N.; Rutishauser, J.; Spiess, M.; Riek, R.: Hormone amyloids in sickness and in health, in: Otzen, DE(Ed.). (2013). Amyloid fibrils and prefibrillar aggregates : molecular and biological properties, Weinheim, Germany: Wiley-VCH Verlag, S.395-410.

Demirci, Erhan; Junne, Tina; Baday, Sefer; Bernèche, Simon; Spiess, Martin (2013). Functional asymmetry within the Sec61p translocon. Proceedings of the National Academy of Sciences of the United States of America, 110 (47), 18856-61.


Kocik, Lucyna; Junne, Tina; Spiess, Martin (2012). Orientation of Internal Signal-Anchor Sequences at the Sec61 Translocon. Journal of molecular biology, 424 (5), 368-78.


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

Junne, T.; Kocik, L.; Spiess, M. (2010). The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration. Molecular Biology of the Cell, 21 (10), 1662-1670.


Kobialka, Szymon; Beuret, Nicole; Ben-Tekaya, Houchaima; Spiess, Martin (2009). Glycosaminoglycan chains affect exocytic and endocytic protein traffic. Traffic, 10 (12), 1845-55.

Birk, Julia; Friberg, Michael A; Prescianotto-Baschong, Cristina; Spiess, Martin; Rutishauser, Jonas (2009). Dominant pro-vasopressin mutants that cause diabetes insipidus form disulfide-linked fibrillar aggregates in the endoplasmic reticulum. Journal of cell science, 122 (Pt21), 3994-4002.

Stettler, Hansruedi; Beuret, Nicole; Prescianotto-Baschong, Cristina; Fayard, Bérengère; Taupenot, Laurent; Spiess, Martin (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, 418 (1), 81-91.


Suri, Gregor; Spiess, Martin; Crottet, Pascal (2008). Recruitment of coat proteins to peptidoliposomes. Methods in Molecular Biology, 457, 227-39.


Junne, Tina; Schwede, Torsten; Goder, Veit; Spiess, Martin (2007). Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology. Journal of biological chemistry, 282 (45), 33201-9.


Junne, T.; Schwede, T.; Goder, V.; 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), 4063-4068.


Higy, Marie; Gander, Stefan; Spiess, Martin (2005). Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum. Biochemistry, 44 (6), 2039-47.

Stettler, Hansruedi; Suri, Gregor; Spiess, Martin (2005). Proprotein convertase PC3 is not a transmembrane protein. Biochemistry, 44 (14), 5339-45.

Meyer, D. M.; Crottet, P.; Maco, B.; Degtyar, E.; Cassel, D.; 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), 4745-54.

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


Goder, V.; Junne, T.; Spiess, M. (2004). Sec61p contributes to signal sequence orientation according to the positive-inside rule. Molecular Biology of the Cell, 15 (3), 1470-8.

Friberg, Michael A; Spiess, Martin; Rutishauser, Jonas (2004). Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome. Journal of Biological Chemistry, 279 (19), 19441-7.

Beuret, Nicole; Stettler, Hansruedi; Renold, Anja; Rutishauser, Jonas; Spiess, Martin (2004). Expression of regulated secretory proteins is sufficient to generate granule-like structures in constitutively secreting cells. Journal of Biological Chemistry, 279 (19), 20242-9.

Higy, Marie; Junne, Tina; Spiess, Martin (2004). Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry, 43 (40), 12716-22.

Pagano, A.; Crottet, P.; Prescianotto-Baschong, C.; 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), 4990-5000.


Goder, Veit; Spiess, Martin (2003). Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. The EMBO journal, 22 (14), 3645-53.


Dumermuth, Eric; Beuret, Nicole; Spiess, Martin; Crottet, Pascal (2002). Ubiquitous 9-O-acetylation of sialoglycoproteins restricted to the Golgi complex. Journal of biological chemistry, 277 (21), 18687-93.

Crottet, P.; Meyer, D. M.; Rohrer, J.; 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), 3672-3682.

Vogel, Lotte K; Sahkri, Sia; Sjostrom, Hans; Noren, Ove; Spiess, Martin (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, 277 (16), 13883-8.

Rutishauser, Jonas; Spiess, Martin (2002). Endoplasmic reticulum storage diseases. Swiss Medical Weekly, 132 (17-18), 211-22.


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


Renold, A; Cescato, R; Beuret, N; Vogel, L K; Wahlberg, J M; Brown, J L; Fiedler, K; Spiess, M (2000). Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface. Journal of biological chemistry, 275 (13), 9290-5.

Rösch, K; Naeher, D; Laird, V; Goder, V; Spiess, M (2000). The topogenic contribution of uncharged amino acids on signal sequence orientation in the endoplasmic reticulum. Journal of biological chemistry, 275 (20), 14916-22.

Laird, V; Spiess, M (2000). A novel assay to demonstrate an intersection of the exocytic and endocytic pathways at early endosomes. Experimental cell research, 260 (2), 340-5.

Goder, V; Crottet, P; Spiess, M (2000). In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation. The EMBO journal, 19 (24), 6704-12.

Meier, M; Bider, M D; Malashkevich, V N; Spiess, M; Burkhard, P (2000). Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. Journal of molecular biology, 300 (4), 857-65.

Cescato, R; Dumermuth, E; Spiess, M; 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, 74 (3), 1131-9.

Laird, V.: Endocytosis meets exocytosis, in: Op den Kamp, J.A.F.(Ed.). (2000). Protein, lipid and membrane traffic, Amsterdam: IOS Press, S.211.


Beuret, N; Rutishauser, J; Bider, M D; 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, 274 (27), 18965-72.

Goder, V; Bieri, C; 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, 147 (2), 257-66.

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

Heilker, R; Spiess, M; Crottet, P (1999). Recognition of sorting signals by clathrin adaptors. Bioessays, 21 (7), 558-67.

Goder, V.; Spiess, M.: Topogenesis, in: Creighton, T.E.(Ed.). (1999). Encyclopedia of molecular biology, New York: John Wiley, Vol. 4, S.2561-2567.


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

Eusebio, A; Friedberg, T; Spiess, M (1998). The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane. Experimental cell research, 241 (1), 181-5.

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


Wahlberg, J M; 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, 137 (3), 555-62.


Heilker, R; Manning-Krieg, U; Zuber, J F; Spiess, M (1996). In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. The EMBO journal, 15 (11), 2893-9.

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

Bider, M.D.; Wahlberg, J.M.; Kammerer, R.A.; Spiess, M. (1996). The oligomerization domain of the asialoglycoprotein receptor preferentially forms 2:2 heterotetramers in vitro. Journal of Biological Chemistry, 271 (50), 31996-32001.

Fuhrer, C.; Spiess, M.: The asialoglycoprotein receptor, in: Lee, A.G.(Ed.). (1996). Biomembranes. Vol. 4, Endocytosis and exocytosis, Greenwich, Conn.: Jai Press, S.175-199.


Bider, M D; Cescato, R; Jenö, P; Spiess, M (1995). High-affinity ligand binding to subunit H1 of the asialoglycoprotein receptor in the absence of subunit H2. European journal of biochemistry, 230 (1), 207-12.

Leitinger, B; Hille-Rehfeld, A; 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, 92 (22), 10109-13.

Denzer, A J; Nabholz, C E; 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, 14 (24), 6311-7.

Wahlberg, J M; Geffen, I; Reymond, F; Simmen, T; 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, 130 (2), 285-97.

Spiess, M (1995). Heads or tails - what determines the orientation of proteins in the membrane. FEBS letters, 369 (1), 76-9.

Becker, S; Spiess, M; Klenk, H D (1995). The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus. Journal of general virology, 76 ( Pt 2), 393-9.


Leitinger, B; Brown, J L; 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, 269 (11), 8115-21.

Fuhrer, C; Geffen, I; Huggel, K; Spiess, M (1994). The two subunits of the asialoglycoprotein receptor contain different sorting information. Journal of biological chemistry, 269 (5), 3277-82.

Dihanich, M; Spiess, M (1994). A novel serine proteinase-like sequence from human brain. Biochimica et biophysica acta, 1218 (2), 225-8.


Geffen, I; Fuhrer, C; Leitinger, B; Weiss, M; Huggel, K; Griffiths, G; Spiess, M (1993). Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor. Journal of biological chemistry, 268 (28), 20772-7.


Vogel, L K; Spiess, M; Sjöström, H; Norén, O (1992). Evidence for an apical sorting signal on the ectodomain of human aminopeptidase N. Journal of biological chemistry, 267 (4), 2794-7.

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

Geffen, I; Spiess, M (1992). Phorbol Ester-Induced redistribution of the ASGP receptor is independent of receptor phosphorylation. FEBS letters, 305 (3), 209-12.


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

Geffen, I; Fuhrer, C; 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, 88 (19), 8425-9.

Fuhrer, C; Geffen, I; 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, 114 (3), 423-31.

Beltzer, J P; Spiess, M (1991). In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles. The EMBO journal, 10 (12), 3735-42.


Wessels, H. P.; Hansen, G. H.; Fuhrer, C.; Look, A. T.; Sjostrom, H.; Noren, O.; Spiess, Martin (1990). Aminopeptidase N is directly sorted to the apical domain in MDCK cells. Journal of Cell Biology, 111 (6Pt2), 2923-30.

Spiess, M (1990). The asialoglycoprotein receptor : a model for endocytic transport receptors. Biochemistry, 29 (43), 10009-18.


Spiess, M; Handschin, C; Baker, K P (1989). Stop-transfer activity of hydrophobic sequences depends on the translation system. Journal of biological chemistry, 264 (32), 19117-24.

Geffen, I; Wessels, H P; Roth, J; Shia, M A; Spiess, M (1989). Endocytosis and recycling of subunit H1 of the asialoglycoprotein receptor is independent of oligomerization with H2. The EMBO journal, 8 (10), 2855-61.

Beltzer, J P; Wessels, H P; Spiess, M (1989). Signal peptidase can cleave inside a polytopic membrane protein. FEBS letters, 253 (1-2), 93-8.


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, Martin; Sjostrom, H.; Noren, O. (1988). Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. FEBS Letters, 238 (2), 307-14.

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

Schmid, S R; Spiess, M (1988). Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence. Journal of biological chemistry, 263 (32), 16886-91.


Hu, C B; Spiess, M; 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, 896 (2), 275-86.

Spiess, M.; Hunziker, W.; Lodish, H. F.; Semenza, G.: Molecular cell biology of brush border hydrolases : sucrase-isomaltase and gamma-glutamyl transpeptidase, in: Kenny, A.J.; Turner, A.J.(Ed.). (1987). Mammalian Ectoenzymes, Amsterdam: Elsevier Science Publishers B.V., S.87-110.


Spiess, M; Lodish, H F (1986). An internal signal sequence : the asialoglycoprotein receptor membrane anchor. Cell, 44 (1), 177-85.

Hunziker, W; Spiess, M; Semenza, G; Lodish, H F (1986). The sucrase-isomaltase complex : primary structure, membrane- orientation, and evolution of a stalked, intrinsic brush border protein. Cell, 46 (2), 227-34.

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


Spiess, M; Schwartz, A L; Lodish, H F (1985). Sequence of human asialoglycoprotein receptor cDNA. An internal signal sequence for membrane insertion. Journal of biological chemistry, 260 (4), 1979-82.

Spiess, M; 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, 82 (19), 6465-9.


Brunner, J; Spiess, M; Aggeler, R; Huber, P; Semenza, G (1983). Hydrophobic labeling of a single leaflet of the human erythrocyte membrane. Biochemistry, 22 (16), 3812-20.


Trueb, B.; Grobli, B.; Spiess, Martin; Odermatt, B. F.; Winterhalter, K. H. (1982). Basement membrane (type IV) collagen is a heteropolymer. Journal of Biological Chemistry, 257 (9), 5239-45.

Spiess, M.; Brunner, J.; Semenza, G. (1982). Hydrophobic labeling, isolation, and partial characterization of the NHâ''-terminal membranous segment of sucrase-isomaltase complex. Journal of biological chemistry, 257, 2370-2377.

Sjostrom, H.; Noren, O.; Christiansen, L. A.; Wacker, H.; Spiess, Martin; Biglermeier, B.; Rickli, E. E.; 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), 321-5.

Hauser, H; Gains, N; Semenza, G; Spiess, M (1982). Orientation and motion of spin-labels in rabbit small intestinal brush border vesicle membranes. Biochemistry, 21 (22), 5621-8.

Barsukov, L.I.; Spiess, M.; Bergelson, L.D. (1982). Transbilayer distribution of PC and PE in microvillous membrane vesicles from rabbit small intestine. Doklady Akademii Nauk SSSR, 266, 1014-1016.


Spiess, M; Hauser, H; Rosenbusch, J P; Semenza, G (1981). Hydrodynamic properties of phospholipid vesicles and of sucrase isomaltase-phospholipid vesicles. Journal of biological chemistry, 256 (17), 8977-82.


Trüeb, B.; Odermatt, B. F.; Sahu, A. P.; Spiess, Martin; Rüttner, J. R.; Winterhalter, K. H. (1980). Type IV collagen is a heteropolymer with the formula C2D. Kidney & Blood Pressure Research, 3 (1-6), 23-9.

Hauser, H.; Guyer, W.; Spiess, M.; Pascher, I.; 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, 137, 265-282.

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