Items where Author is "Spiess, M."

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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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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

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

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.

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

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.

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.

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.

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.

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.

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.

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

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.

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.

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.

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.

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.

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.

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.

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.

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

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.

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.

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.

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.

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

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.. (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.

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.

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.

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.

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.