| Year |
Citation |
Score |
| 2022 |
Pennauer M, Buczak K, Prescianotto-Baschong C, Spiess M. Shared and specific functions of Arfs 1-5 at the Golgi revealed by systematic knockouts. The Journal of Cell Biology. 221. PMID 34749397 DOI: 10.1083/jcb.202106100 |
0.302 |
|
| 2021 |
Janoschke M, Zimmermann M, Brunauer A, Humbel R, Junne T, Spiess M. 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. PMID 34373330 DOI: 10.1073/pnas.2102675118 |
0.416 |
|
| 2021 |
Jung SJ, Eun Hani Kim J, Junne T, Spiess M, Kim H. Cotranslational targeting and posttranslational translocation can cooperate in Spc3 topogenesis. Journal of Molecular Biology. 167109. PMID 34153287 DOI: 10.1016/j.jmb.2021.167109 |
0.38 |
|
| 2020 |
Spiess M, Beuret N, Prescianotto Baschong C, Rutishauser J. Amyloid-like aggregation of provasopressin. Vitamins and Hormones. 113: 55-77. PMID 32138954 DOI: 10.1016/Bs.Vh.2019.08.014 |
0.354 |
|
| 2019 |
Spiess M, Friberg M, Beuret N, Prescianotto-Baschong C, Rutishauser J. Role of protein aggregation and degradation in autosomal dominant neurohypophyseal diabetes insipidus. Molecular and Cellular Endocrinology. 501: 110653. PMID 31785344 DOI: 10.1016/J.Mce.2019.110653 |
0.359 |
|
| 2019 |
Spiess M, Junne T, Janoschke M. Membrane Protein Integration and Topogenesis at the ER. The Protein Journal. PMID 30927129 DOI: 10.1007/S10930-019-09827-6 |
0.543 |
|
| 2019 |
Buser DP, Spiess M. Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells. Journal of Visualized Experiments : Jove. PMID 30855580 DOI: 10.3791/59111 |
0.389 |
|
| 2018 |
Buser DP, Schleicher KD, Prescianotto-Baschong C, Spiess M. 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. PMID 29915061 DOI: 10.1073/Pnas.1801865115 |
0.384 |
|
| 2017 |
Shi G, Somlo D, Kim GH, Prescianotto-Baschong C, Sun S, Beuret N, Long Q, Rutishauser J, Arvan P, Spiess M, Qi L. ER-associated degradation is required for vasopressin prohormone processing and systemic water homeostasis. The Journal of Clinical Investigation. PMID 28920920 DOI: 10.1172/Jci94771 |
0.376 |
|
| 2017 |
Estoppey D, Lee CM, Janoschke M, Lee BH, Wan KF, Dong H, Mathys P, Filipuzzi I, Schuhmann T, Riedl R, Aust T, Galuba O, McAllister G, Russ C, Spiess M, et al. The Natural Product Cavinafungin Selectively Interferes with Zika and Dengue Virus Replication by Inhibition of the Host Signal Peptidase. Cell Reports. 19: 451-460. PMID 28423309 DOI: 10.1016/J.Celrep.2017.03.071 |
0.374 |
|
| 2017 |
Zimmermann M, Janoschke M, Spiess M. Bip Binding Affects Integration of Transmembrane Domains Biophysical Journal. 112: 500a. DOI: 10.1016/J.Bpj.2016.11.2707 |
0.46 |
|
| 2016 |
Junne T, Spiess M. Integration of transmembrane domains is regulated by their downstream sequences. Journal of Cell Science. PMID 27909247 DOI: 10.1242/Jcs.194472 |
0.459 |
|
| 2016 |
Kälin S, Buser DP, Spiess M. A fresh look at the function of Rabaptin5 on endosomes. Small Gtpases. 7: 34-7. PMID 26940354 DOI: 10.1080/21541248.2016.1140616 |
0.417 |
|
| 2015 |
Kälin S, Hirschmann DT, Buser DP, Spiess M. Rabaptin5 is recruited to endosomes by Rab4 and Rabex5 to regulate endosome maturation. Journal of Cell Science. PMID 26430212 DOI: 10.1242/Jcs.174664 |
0.476 |
|
| 2015 |
Mihov D, Spiess M. Glycosaminoglycans: Sorting determinants in intracellular protein traffic. The International Journal of Biochemistry & Cell Biology. 68: 87-91. PMID 26327396 DOI: 10.1016/J.Biocel.2015.08.019 |
0.495 |
|
| 2015 |
Mihov D, Raja E, Spiess M. Chondroitin Sulfate Accelerates Trans-Golgi-to-Surface Transport of Proteoglycan Amyloid Precursor Protein. Traffic (Copenhagen, Denmark). 16: 853-70. PMID 25951880 DOI: 10.1111/Tra.12294 |
0.429 |
|
| 2015 |
Hirschmann DT, Kasper CA, Spiess M. Quantitative analysis of transferrin cycling by automated fluorescence microscopy. Methods in Molecular Biology (Clifton, N.J.). 1270: 365-78. PMID 25702129 DOI: 10.1007/978-1-4939-2309-0_25 |
0.31 |
|
| 2015 |
Huser S, Suri G, Crottet P, Spiess M. Recruitment of coat proteins to liposomes and peptidoliposomes. Methods in Molecular Biology (Clifton, N.J.). 1270: 91-106. PMID 25702111 DOI: 10.1007/978-1-4939-2309-0_7 |
0.475 |
|
| 2015 |
Junne T, Wong J, Studer C, Aust T, Bauer BW, Beibel M, Bhullar B, Bruccoleri R, Eichenberger J, Estoppey D, Hartmann N, Knapp B, Krastel P, Melin N, Oakeley EJ, ... ... Spiess M, et al. Decatransin, a new natural product inhibiting protein translocation at the Sec61/SecYEG translocon. Journal of Cell Science. 128: 1217-29. PMID 25616894 DOI: 10.1242/Jcs.165746 |
0.607 |
|
| 2014 |
Spiess M. Protein translocation: the Sec61/SecYEG translocon caught in the act. Current Biology : Cb. 24: R317-9. PMID 24735854 DOI: 10.1016/J.Cub.2014.02.051 |
0.429 |
|
| 2013 |
Demirci E, Junne T, Baday S, Bernèche S, Spiess M. Functional asymmetry within the Sec61p translocon. Proceedings of the National Academy of Sciences of the United States of America. 110: 18856-61. PMID 24191046 DOI: 10.1073/Pnas.1318432110 |
0.426 |
|
| 2013 |
Sommer N, Junne T, Kalies KU, Spiess M, Hartmann E. TRAP assists membrane protein topogenesis at the mammalian ER membrane. Biochimica Et Biophysica Acta. 1833: 3104-11. PMID 24013069 DOI: 10.1016/J.Bbamcr.2013.08.018 |
0.536 |
|
| 2013 |
Huser S, Suri G, Crottet P, Spiess M. Interaction of amphiphysins with AP-1 clathrin adaptors at the membrane. The Biochemical Journal. 450: 73-83. PMID 23190214 DOI: 10.1042/Bj20121373 |
0.432 |
|
| 2012 |
Kocik L, Junne T, Spiess M. Orientation of internal signal-anchor sequences at the Sec61 translocon. Journal of Molecular Biology. 424: 368-78. PMID 23084973 DOI: 10.1016/J.Jmb.2012.10.010 |
0.511 |
|
| 2010 |
Appenzeller-Herzog C, Riemer J, Zito E, Chin KT, Ron D, Spiess M, Ellgaard L. Disulphide production by Ero1α-PDI relay is rapid and effectively regulated. The Embo Journal. 29: 3318-29. PMID 20802462 DOI: 10.1038/Emboj.2010.203 |
0.335 |
|
| 2010 |
Junne T, Kocik L, Spiess M. The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration. Molecular Biology of the Cell. 21: 1662-70. PMID 20357000 DOI: 10.1091/Mbc.E10-01-0060 |
0.463 |
|
| 2009 |
Kobialka S, Beuret N, Ben-Tekaya H, Spiess M. Glycosaminoglycan chains affect exocytic and endocytic protein traffic. Traffic (Copenhagen, Denmark). 10: 1845-55. PMID 19912578 DOI: 10.1111/J.1600-0854.2009.00987.X |
0.462 |
|
| 2009 |
Birk J, Friberg MA, Prescianotto-Baschong C, Spiess M, Rutishauser J. Dominant pro-vasopressin mutants that cause diabetes insipidus form disulfide-linked fibrillar aggregates in the endoplasmic reticulum. Journal of Cell Science. 122: 3994-4002. PMID 19825939 DOI: 10.1242/Jcs.051136 |
0.335 |
|
| 2009 |
Stettler H, Beuret N, Prescianotto-Baschong C, Fayard B, Taupenot L, Spiess M. 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: 81-91. PMID 18973469 DOI: 10.1042/Bj20071382 |
0.395 |
|
| 2008 |
Suri G, Spiess M, Crottet P. Recruitment of coat proteins to peptidoliposomes. Methods in Molecular Biology (Clifton, N.J.). 457: 227-39. PMID 19066031 DOI: 10.1007/978-1-59745-261-8_17 |
0.484 |
|
| 2007 |
Junne T, Schwede T, Goder V, Spiess M. Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology. The Journal of Biological Chemistry. 282: 33201-9. PMID 17893139 DOI: 10.1074/Jbc.M707219200 |
0.772 |
|
| 2006 |
Junne T, Schwede T, Goder V, Spiess M. 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: 4063-8. PMID 16822836 DOI: 10.1091/Mbc.E06-03-0200 |
0.769 |
|
| 2005 |
Pagano A, Spiess M. Reconstitution of Rab4-dependent vesicle formation in vitro. Methods in Enzymology. 403: 81-92. PMID 16473579 DOI: 10.1016/S0076-6879(05)03008-9 |
0.418 |
|
| 2005 |
Meyer DM, Crottet P, Maco B, Degtyar E, Cassel D, Spiess M. Oligomerization and dissociation of AP-1 adaptors are regulated by cargo signals and by ArfGAP1-induced GTP hydrolysis. Molecular Biology of the Cell. 16: 4745-54. PMID 16093346 DOI: 10.1091/Mbc.E05-06-0568 |
0.445 |
|
| 2005 |
Stettler H, Suri G, Spiess M. Proprotein convertase PC3 is not a transmembrane protein. Biochemistry. 44: 5339-45. PMID 15807527 DOI: 10.1021/Bi047430C |
0.488 |
|
| 2005 |
Higy M, Gander S, Spiess M. Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum. Biochemistry. 44: 2039-47. PMID 15697229 DOI: 10.1021/Bi047976Z |
0.554 |
|
| 2004 |
Higy M, Junne T, Spiess M. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry. 43: 12716-22. PMID 15461443 DOI: 10.1021/Bi048368M |
0.597 |
|
| 2004 |
Pagano A, Crottet P, Prescianotto-Baschong C, Spiess M. 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: 4990-5000. PMID 15331762 DOI: 10.1091/Mbc.E04-04-0355 |
0.446 |
|
| 2004 |
Friberg MA, Spiess M, Rutishauser J. Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome. The Journal of Biological Chemistry. 279: 19441-7. PMID 14996841 DOI: 10.1074/Jbc.M310249200 |
0.399 |
|
| 2004 |
Beuret N, Stettler H, Renold A, Rutishauser J, Spiess M. Expression of regulated secretory proteins is sufficient to generate granule-like structures in constitutively secreting cells. The Journal of Biological Chemistry. 279: 20242-9. PMID 14996840 DOI: 10.1074/Jbc.M310613200 |
0.376 |
|
| 2004 |
Goder V, Junne T, Spiess M. Sec61p contributes to signal sequence orientation according to the positive-inside rule. Molecular Biology of the Cell. 15: 1470-8. PMID 14668483 DOI: 10.1091/Mbc.E03-08-0599 |
0.766 |
|
| 2003 |
Goder V, Spiess M. Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. The Embo Journal. 22: 3645-53. PMID 12853479 DOI: 10.1093/Emboj/Cdg361 |
0.755 |
|
| 2002 |
Crottet P, Meyer DM, Rohrer J, Spiess M. 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: 3672-82. PMID 12388765 DOI: 10.1091/Mbc.E02-05-0309 |
0.488 |
|
| 2002 |
Rutishauser J, Spiess M. Endoplasmic reticulum storage diseases. Swiss Medical Weekly. 132: 211-22. PMID 12087487 DOI: 10.4414/Smw.2002.09861 |
0.394 |
|
| 2002 |
Vogel LK, Sahkri S, Sjostrom H, Noren O, Spiess M. Secretion of antithrombin is converted from nonpolarized to apical by exchanging its amino terminus for that of apically secreted family members. The Journal of Biological Chemistry. 277: 13883-8. PMID 11839735 DOI: 10.1074/Jbc.M107997200 |
0.38 |
|
| 2001 |
Goder V, Spiess M. Topogenesis of membrane proteins: determinants and dynamics. Febs Letters. 504: 87-93. PMID 11532438 DOI: 10.1016/S0014-5793(01)02712-0 |
0.783 |
|
| 2000 |
Goder V, Crottet P, Spiess M. In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation. The Embo Journal. 19: 6704-12. PMID 11118205 DOI: 10.1093/Emboj/19.24.6704 |
0.756 |
|
| 2000 |
Laird V, Spiess M. A novel assay to demonstrate an intersection of the exocytic and endocytic pathways at early endosomes. Experimental Cell Research. 260: 340-5. PMID 11035929 DOI: 10.1006/Excr.2000.5006 |
0.403 |
|
| 2000 |
Meier M, Bider MD, Malashkevich VN, Spiess M, Burkhard P. Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. Journal of Molecular Biology. 300: 857-65. PMID 10891274 DOI: 10.1006/Jmbi.2000.3853 |
0.394 |
|
| 2000 |
Rösch K, Naeher D, Laird V, Goder V, Spiess M. The topogenic contribution of uncharged amino acids on signal sequence orientation in the endoplasmic reticulum. The Journal of Biological Chemistry. 275: 14916-22. PMID 10747915 DOI: 10.1074/Jbc.M000456200 |
0.769 |
|
| 2000 |
Renold A, Cescato R, Beuret N, Vogel LK, Wahlberg JM, Brown JL, Fiedler K, Spiess M. Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface. The Journal of Biological Chemistry. 275: 9290-5. PMID 10734069 DOI: 10.1074/Jbc.275.13.9290 |
0.539 |
|
| 2000 |
Cescato R, Dumermuth E, Spiess M, Paganetti PA. Increased generation of alternatively cleaved beta-amyloid peptides in cells expressing mutants of the amyloid precursor protein defective in endocytosis. Journal of Neurochemistry. 74: 1131-9. PMID 10693945 DOI: 10.1046/J.1471-4159.2000.741131.X |
0.329 |
|
| 1999 |
Goder V, Bieri C, Spiess M. Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon. The Journal of Cell Biology. 147: 257-66. PMID 10525533 DOI: 10.1083/Jcb.147.2.257 |
0.787 |
|
| 1999 |
Heilker R, Spiess M, Crottet P. Recognition of sorting signals by clathrin adaptors. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 21: 558-67. PMID 10472183 DOI: 10.1002/(Sici)1521-1878(199907)21:7<558::Aid-Bies4>3.0.Co;2-R |
0.464 |
|
| 1999 |
Beuret N, Rutishauser J, Bider MD, Spiess M. Mechanism of endoplasmic reticulum retention of mutant vasopressin precursor caused by a signal peptide truncation associated with diabetes insipidus. The Journal of Biological Chemistry. 274: 18965-72. PMID 10383395 DOI: 10.1074/Jbc.274.27.18965 |
0.451 |
|
| 1998 |
Eusebio A, Friedberg T, Spiess M. The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane. Experimental Cell Research. 241: 181-5. PMID 9633526 DOI: 10.1006/Excr.1998.4042 |
0.583 |
|
| 1998 |
Spiess M, Beuret N. PCR-directed in vitro mutagenesis using a 'temporary' restriction site Technical Tips Online. 3: 51-53. DOI: 10.1016/S1366-2120(08)70097-7 |
0.326 |
|
| 1997 |
Wahlberg JM, Spiess M. Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain. The Journal of Cell Biology. 137: 555-62. PMID 9151664 DOI: 10.1083/Jcb.137.3.555 |
0.592 |
|
| 1996 |
Bider MD, Wahlberg JM, Kammerer RA, Spiess M. The oligomerization domain of the asialoglycoprotein receptor preferentially forms 2:2 heterotetramers in vitro. The Journal of Biological Chemistry. 271: 31996-2001. PMID 8943247 DOI: 10.1074/Jbc.271.50.31996 |
0.328 |
|
| 1996 |
Heilker R, Manning-Krieg U, Zuber JF, Spiess M. In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. The Embo Journal. 15: 2893-9. PMID 8654387 DOI: 10.1002/J.1460-2075.1996.Tb00650.X |
0.499 |
|
| 1995 |
Denzer AJ, Nabholz CE, Spiess M. 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: 6311-7. PMID 8557050 DOI: 10.1002/J.1460-2075.1995.Tb00321.X |
0.517 |
|
| 1995 |
Spiess M. Heads or tails--what determines the orientation of proteins in the membrane. Febs Letters. 369: 76-9. PMID 7641889 DOI: 10.1016/0014-5793(95)00551-J |
0.605 |
|
| 1995 |
Wahlberg JM, Geffen I, Reymond F, Simmen T, Spiess M. 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: 285-97. PMID 7615632 DOI: 10.1083/Jcb.130.2.285 |
0.513 |
|
| 1995 |
Leitinger B, Hille-Rehfeld A, Spiess M. 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: 10109-13. PMID 7479735 DOI: 10.1073/Pnas.92.22.10109 |
0.431 |
|
| 1994 |
Leitinger B, Brown JL, Spiess M. Tagging secretory and membrane proteins with a tyrosine sulfation site. Tyrosine sulfation precedes galactosylation and sialylation in COS-7 cells. The Journal of Biological Chemistry. 269: 8115-21. PMID 8132536 |
0.35 |
|
| 1994 |
Fuhrer C, Geffen I, Huggel K, Spiess M. The two subunits of the asialoglycoprotein receptor contain different sorting information. The Journal of Biological Chemistry. 269: 3277-82. PMID 8106365 DOI: 10.5167/Uzh-136 |
0.345 |
|
| 1993 |
Geffen I, Fuhrer C, Leitinger B, Weiss M, Huggel K, Griffiths G, Spiess M. Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor. The Journal of Biological Chemistry. 268: 20772-7. PMID 8407903 DOI: 10.5167/Uzh-147 |
0.511 |
|
| 1992 |
Vogel LK, Spiess M, Sjöström H, Norén O. Evidence for an apical sorting signal on the ectodomain of human aminopeptidase N. The Journal of Biological Chemistry. 267: 2794-7. PMID 1346396 |
0.389 |
|
| 1992 |
Geffen I, Spiess M. Phorbol ester-induced redistribution of the ASGP receptor is independent of receptor phosphorylation. Febs Letters. 305: 209-12. PMID 1299617 DOI: 10.1016/0014-5793(92)80669-8 |
0.337 |
|
| 1991 |
Beltzer JP, Fiedler K, Fuhrer C, Geffen I, Handschin C, Wessels HP, Spiess M. Charged residues are major determinants of the transmembrane orientation of a signal-anchor sequence. The Journal of Biological Chemistry. 266: 973-8. PMID 1985975 |
0.503 |
|
| 1991 |
Wessels HP, Beltzer JP, Spiess M. Analysis of protein topology in the endoplasmic reticulum. Methods in Cell Biology. 34: 287-302. PMID 1943805 DOI: 10.1016/B978-0-12-683755-1.50008-9 |
0.392 |
|
| 1991 |
Beltzer JP, Spiess M. In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles. The Embo Journal. 10: 3735-42. PMID 1935897 DOI: 10.1002/J.1460-2075.1991.Tb04942.X |
0.434 |
|
| 1991 |
Geffen I, Fuhrer C, Spiess M. 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: 8425-9. PMID 1924301 DOI: 10.1073/Pnas.88.19.8425 |
0.388 |
|
| 1991 |
Fuhrer C, Geffen I, Spiess M. 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: 423-31. PMID 1907285 DOI: 10.1083/Jcb.114.3.423 |
0.415 |
|
| 1990 |
Wessels HP, Hansen GH, Fuhrer C, Look AT, Sjöström H, Norén O, Spiess M. Aminopeptidase N is directly sorted to the apical domain in MDCK cells. The Journal of Cell Biology. 111: 2923-30. PMID 1980123 DOI: 10.1083/Jcb.111.6.2923 |
0.49 |
|
| 1989 |
Wessels HP, Geffen I, Spiess M. A hepatocyte-specific basolateral membrane protein is targeted to the same domain when expressed in Madin-Darby canine kidney cells. The Journal of Biological Chemistry. 264: 17-20. PMID 2909512 |
0.42 |
|
| 1989 |
Spiess M, Handschin C, Baker KP. Stop-transfer activity of hydrophobic sequences depends on the translation system. The Journal of Biological Chemistry. 264: 19117-24. PMID 2808416 |
0.461 |
|
| 1989 |
Geffen I, Wessels HP, Roth J, Shia MA, Spiess M. Endocytosis and recycling of subunit H1 of the asialoglycoprotein receptor is independent of oligomerization with H2. The Embo Journal. 8: 2855-61. PMID 2684632 DOI: 10.1002/J.1460-2075.1989.Tb08433.X |
0.345 |
|
| 1989 |
Beltzer JP, Wessels HP, Spiess M. Signal peptidase can cleave inside a polytopic membrane protein. Febs Letters. 253: 93-8. PMID 2668036 DOI: 10.1016/0014-5793(89)80937-8 |
0.597 |
|
| 1988 |
Schmid SR, Spiess M. Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence. The Journal of Biological Chemistry. 263: 16886-91. PMID 3053698 |
0.498 |
|
| 1988 |
Wessels HP, Spiess M. Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell. 55: 61-70. PMID 2844410 DOI: 10.1016/0092-8674(88)90009-8 |
0.593 |
|
| 1987 |
Spiess M, Handschin C. Deletion analysis of the internal signal-anchor domain of the human asialoglycoprotein receptor H1. The Embo Journal. 6: 2683-91. PMID 3678203 DOI: 10.1002/J.1460-2075.1987.Tb02560.X |
0.575 |
|
| 1987 |
Hu CB, Spiess M, Semenza G. 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: 275-86. PMID 3099840 DOI: 10.1016/0005-2736(87)90188-X |
0.389 |
|
| 1986 |
Barsukov LI, Bergelson LD, Spiess M, Hauser H, Semenza G. Phospholipid topology and flip-flop in intestinal brush-border membrane Bba - Biomembranes. 862: 87-99. PMID 3768371 DOI: 10.1016/0005-2736(86)90472-4 |
0.43 |
|
| 1986 |
Hunziker W, Spiess M, Semenza G, Lodish HF. The sucrase-isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein Cell. 46: 227-234. PMID 3755079 DOI: 10.1016/0092-8674(86)90739-7 |
0.47 |
|
| 1986 |
Spiess M, Lodish HF. An internal signal sequence: The asialoglycoprotein receptor membrane anchor Cell. 44: 177-185. PMID 3753585 DOI: 10.1016/0092-8674(86)90496-4 |
0.502 |
|
| 1985 |
Spiess M, Lodish HF. 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: 6465-6469. PMID 3863106 DOI: 10.1073/Pnas.82.19.6465 |
0.329 |
|
| 1985 |
Spiess M, Schwartz AL, Lodish HF. Sequence of human asialoglycoprotein receptor cDNA. An internal signal sequence for membrane insertion Journal of Biological Chemistry. 260: 1979-1982. PMID 2982798 |
0.376 |
|
| 1983 |
Brunner J, Spiess M, Aggeler R, Huber P, Semenza G. Hydrophobic labeling of a single leaflet of the human erythrocyte membrane Biochemistry. 22: 3812-3820. PMID 6688533 DOI: 10.1021/Bi00285A016 |
0.382 |
|
| 1982 |
Sjöström H, Norén O, Christiansen LA, Wacker H, Spiess M, Bigler-Meier B, Rickli EE, Semenza G. 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: 321-325. PMID 7152027 DOI: 10.1016/0014-5793(82)80833-8 |
0.456 |
|
| 1982 |
Hauser H, Gains N, Semenza G, Spiess M. Orientation and motion of spin-labels in rabbit small intestinal brush border vesicle membranes Biochemistry. 21: 5621-5628. PMID 6293550 DOI: 10.1021/Bi00265A036 |
0.373 |
|
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