Institut de Biologie StructuraleGrenoble / France

Contacts relatifs à cet article / WEISSENHORN Winfried


2017 :

97. Gray, E.R., Brookes, J.C., Caillat, C., Turbé, V., Webb, B.L.J., Granger, L.A., Miller, B.S., McCoy, L.E., El Khattabi, M., Verrips, C.T., Weiss, R.A., Duffy, D.M., Weissenhorn, W. and McKendry, R.A. (2017) Unravelling the Molecular Basis of High Affinity Nanobodies against HIV p24 : In Vitro Functional, Structural, and in Silico Insights. ACS Infect Dis. 14 ;3(7):479-491.
96. Cerutti, N., Loredo-Varela, J.L., Caillat, C. and Weissenhorn, W. (2017) Anti-gp41 membrane proximal external region antibodies and the art of using the membrane for neutralization. Curr Opin HIV AIDS 12(3):250-256.
95. Saletti, D, Radzimanowski, J., Effantin, G., Midtvedt, D., Mangenot, S, Weissenhorn, W*, Bassereau, P.* and Bally, M.* (2017) The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model. Sci Rep. 7:40801.

  1. 2016 :

94. Effantin, G., Estrozi, L., Ashman, N., Renesto, P., Stanke, N., Lindemann, D., Schoehn, G., and Weissenhorn, W. (2016) Cryo-electron microscopy Structure of the native Prototype Foamy Virus Glycoprotein and virus Architecture. PLoS Pathogens 12(7):e1005721

2015 :

93. C. Caillat, P. Macheboeuf, Y. Wu, A.A. McCarthy, E. Boeri-Erba, G. Effantin, H.G. Gottlinger, W. Weissenhorn and P. Renesto (2015) Asymmetric ring structure of Vps4 required for ESCRT-III disassembly. Nat Commun 6:8781.
92. Lopez J, Bittame A, Massera C, Vasseur V, Effantin G, Valat A, Buaillon C, Allart S, Fox BA, Rommereim LM, Bzik DJ, Schoehn G, Weissenhorn W, Dubremetz JF, Gagnon J, Mercier C, Cesbron-Delauw MF, Blanchard N. (2015) Intravacuolar Membranes Regulate CD8 T Cell Recognition of Membrane-Bound Toxoplasma gondii Protective Antigen. Cell Rep. 15 ;13(10):2273-86.
91. M.G. Bego, É. A. Côt, N. Aschman, J. Mercier, W. Weissenhorn and E. A. Cohen (2015) Human Immunodeficiency Virus Accessory Protein Vpu Inhibits the Antiviral Response of Plasmacytoid Dendritic Cells for Innate Immune Evasion. PLoS Pathogen, 11(7):e1005024.
90. Bittame A, Effantin G, Pètre G, Ruffiot P, Travier L, Schoehn G, Weissenhorn W, Cesbron-Delauw MF, Gagnon J, Mercier C. (2015) Toxoplasma gondii : Biochemical and biophysical characterization of recombinant soluble dense granule proteins GRA2 and GRA6. Biochem Biophys Res Commun 459(1):107-12.

2014 :

89. M.V. Petoukhov, W. Weissenhorn and D.I Svergun (2014) Endophilin-A1 BAR domain interaction with arachidonyl CoA Front. Mol. Biosci. doi : 10.3389/fmolb. 2014.00020
88. M.V. Hamann, E. Müllers, J. Reh, N. Stanke, G. Effantin, W. Weissenhorn and D. Lindemann (2014) The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation. Retrovirology. 2014 Oct 8,11(1):87.
87. J. Radzimanowski, G. Effantin and W. Weissenhorn (2014) Conformational plasticity of the Ebola virus matrix protein VP40. Protein Sci. 2014 Nov ;23(11),1519-27.
86. R. P.J. Lai, M. Hock, J. Radzimanowski, P. Tonks, D. Lutje Hulsik, G. Effantin, D. J. Seilly, H. Dreja, A. Kliche, R. Wagner, S. W. Barnett, N. Tumba, L. Morris, C. C. LaBranche, D. C. Montefiori, M. S. Seaman, J. L. Heeney and W. Weissenhorn (2014) A fusion intermediate gp41 immunogen elicits neutralizing antibodies to HIV-1. J Biol Chem 289(43):29912-26.
85. W. Weissenhorn and M.-O. Fauvarque (2014) A small switch has a large effect on autophagy. Structure, 22(1),1-2.

2013 :

84. W. Weissenhorn, E. Poudevigne, G. Effantin and P. Bassereau (2013) How to get out : ssRNA enveloped viruses and membrane fission. Current Opin Virol. 3, 159-167.
83. D. Lutje Hulsik, Y. Y. Liu, N. M. Strokappe, S. Battella, M. El Khattabi, L.E. McCoy, C. Sabin, A. Hinz, M. Hock, P. Macheboeuf, A.M.J.J. Bonvin, J.P.M. Langedijk, D. Davis, A. Forsman-Quigley, M. M.I. Aasa-Chapman, M. S. Seaman, A. Ramos, P. Poignard, A. Favier, J.-P. Simorre, R. A. Weiss, C. T. Verrips, W. Weissenhorn* and L. Rutten* (2013) A gp41 MPER-specific llama VHH requires a hydrophobic CDR3 for neutralization but not for antigen recognition. PLoS Pathogens, 9 (3) e1003202 (*corresponding authors).
82. G. Effantin, R. Hamasaki, T. Kawasaki,M. Bacia, C. Moriscot, W. Weissenhorn, T. Yamada and G. Schoehn (2013) Cryo-electron microscopy three-dimensional structure of the jumbo phage phiRSL1 infecting the phytopathogen Ralstonia solanacearum. Structure 21(2), 298-305.
81. G. Effantin, A. Dordor, V. Sandrin, N. Martinelli, W.I. Sundquist, G. Schoehn and W. Weissenhorn (2013) ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. Cell Microbiol., 15(2), 213-26.

2012 :

80. W. Weissenhorn, N. Miguet, N. Ashman, P. Renesto, Y. Usami, and H.G. Göttlinger (2012) Structural basis for tetherin function. Curr HIV Res. 10(4), 298-306.
79. N. Aschman, W. Weissenhorn and P. Renesto (2012) La tetherine, dernière amarre du VIH/ Tetherin, last link to HIV. Virologie, 16, 32-42.
78. N. Martinelli,, B. Hartlieb, C. Sabin, A. Dordor, Y. Usami, H. Göttlinger and W. Weissenhorn (2012) CC2D1A is a regulator of ESCRT-III CHMP4B. J. Mol. Biol., 419(1-2), 75-88.

2011 :

77. O. Reynard, K. Nemirov, A. Page, M. Mateo, H. Raoul, W. Weissenhorn, V. E. Volchkov (2011) Conserved Proline-Rich Region of Ebola Virus Matrix Protein VP40 Is Essential for Plasma Membrane Targeting and Virus-Like Particle Release. J Infect Dis. 204, S884-S891.
76. G. Bodon, R. Chassefeyre, K. Pernet-Gallay, N. Martinelli, G. Effantin, D. Lutje Hulsik, A. Belly, Y. Goldberg, C. Chatellard-Causse, B. Blot, G. Schoehn, W. Weissenhorn and R. Sadoul (2011) ESCRT-III CHMP2B polymerizes into helical structures deforming the plasma membrane. J. Boil. Chem. 286(46), 40276-86.
75. A. Dordor, E. Poudevigne, H. Göttlinger and W. Weissenhorn (2011) Essential and supporting host cell factors for HIV-1 budding. Future Microbiol. 6 (10), 1159-1170
74. J. Solomons, C. Sabin, E. Poudevigne, Y. Usami, D. Lutje-Hulsik, P. Macheboeuf, B. Hartlieb, H. Gottlinger and W. Weissenhorn (2011) Structural basis of ESCRT-III CHMP3 recruitment of AMSH. Structure, 19(8), 1149-59.
73. C. Moriscot, S. Gribaldo, J.-M. Jault, M. Krupovic, J. Arnaud, M. Jamin, G. Schoehn, P.Forterre, W. Weissenhorn and P. Renesto (2011) Crenarchaeal CdvA forms double-helical filaments containing DNA and interacts with ESCRT-III-like CdvB. PLoS ONE, 6(7):e21921.
72. W. Weissenhorn and H.G. Gottlinger (2011) Essential Ingredients for HIV-1 Budding. Cell Host & Microbe 9(3), 172-4.
71. S. Peel, P. Macheboeuf, N. Martinelli and W. Weissenhorn (2011) Divergent pathways lead to ESCRT-III catalyzed membrane fission. Trends in Biochemical Sciences, 36(4), 199-210.

2010 :

70. C. Sabin, D. Corti, V. Buzon, M. S. Seaman, D. Lutje Hulsik, A. Hinz, F. Vanzetta, G. Agatic, C. Silacci, L. Mainetti, G. Scarlatti, F. Sallusto, R. Weiss, A. Lanzavecchia and W. Weissenhorn (2010) Crystal structure and size-dependent neutralization properties of HK20, a human antibody binding to the highly conserved heptad repeat 1 of gp41. PLoS Pathogens, 6(11), e1001195.
69. A. Hinz, D. Lutje Hulsik, A. Forsman, W. Koh, H. Belrhali, A. Gorlani, H. de Haard, R. A. Weiss, T. Verrips and W. Weissenhorn (2010) Crystal structure of the neutralizing llama VHH D7 and its mode of HIV-1 gp120 interaction. PLoS ONE, 5(5) e10482.
68. V. Buzon, G. Natrajan, D. Schibli, F. Campelo, M. M. Kozlov, and W. Weissenhorn (2010) Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathogens, 6(5) e1000880
67. A. Hinz, N.Miguet, G. Natrajan, Y. Usami, H. Yamanaka, P. Renesto, B. Hartlieb, A. A. McCarthy, J.-P. Simorre, H. Gottlinger and W. Weissenhorn (2010) Structural basis of HIV-1 tethering to membranes by the Bst2/tetherin ectodomain. Cell Host Microbe, 7, 314-323.
66. D. Corti, J.P.M. Langedijk, A. Hinz, M. S. Seaman, F. Vanzetta, B. M. Fernandez-Rodriguez, C. Silacci, D. Pinna, D. Jarrossay, S.Balla-Jhagjhoorsingh, B.Willems, M. J. Zekveld, H. Dreja, E. O’Sullivan, C. Pade, C. Orkin, S. A. Jeffs, D. C. Montefiori, D. Davis, W. Weissenhorn, Á. McKnight, J. L. Heeney, F. Sallusto, Q. J. Sattentau, R. A. Weiss and A. Lanzavecchia (2010) Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS ONE 5(1) : e8805.
65. M. Hock, I. Kraus, G. Schoehn, M. Jamin, C. Andrei-Selmer, W. Garten and W. Weissenhorn (2010) RNA induced polymerization of the Borna disease virus nucleoprotein. Virology, 397, 64-72.

2009 :

64. G. Fabrikant, S. Lata, J. D. Riches, J.A. Briggs, W. Weissenhorn and M.M. Kozlov (2009) Computational model of membrane fission catalyzed by ESCRT-III. PLoS Comput Biol 5(11), e1000575.
63. A. Hinz, G. Schoehn, H. Quendler, D. Lutje Hulsik,G. Stiegler, H. Katinger, D. M. Seaman, Montefiori and W. Weissenhorn (2009) Characterization of a trimeric MPER containing HIV-1 gp41 antigen. Virology, 390(2), 221-7.
62. R. Pires, B. Hartlieb, L. Signor, G. Schoehn, S. Lata, M. Roessle, C. Moriscot, S. Popov, A. Hinz, M. Jamin, V. Boyer, R. Sadoul, E. Forest, D. I. Svergun, H. G. Göttlinger and W. Weissenhorn (2009) A crescent shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure 17, 843-856.
61. Usami Y, Popov S, Popova E, Inoue M, Weissenhorn W., G Göttlinger H. (2009) The ESCRT pathway and HIV-1 budding. Biochem Soc Trans. 37, 181-184.
60. Lata S, Schoehn G, Solomons J, Pires R, Göttlinger HG, Weissenhorn W. (2009) Structure and function of ESCRT-III. Biochem Soc Trans. 37, 156-160.

2008 :

59. Lata S, Schoehn G, Jain A, Pires R, Piehler J, Gottlinger HG, Weissenhorn W. (2008) Helical structures of ESCRT-III are disassembled by VPS4. Science 321, 1354-1357.
58. Stange A, Lüftenegger D, Reh J, Weissenhorn W. and Lindemann D. (2008) Subviral particle release determinants of prototype foamy virus. J Virol. 82, 9858-9869.
57. Lata S, Roessle M, Solomons J, Jamin M, Gottlinger HG, Svergun DI, Weissenhorn W. (2008) Structural basis for autoinhibition of ESCRT-III CHMP3. J Mol Biol. 378, 818-827.

2007 :

56. A. Wagner, G. Stiegler, K. Vorauer-Uhl, H. Katinger, H. Quendler, A. Hinz and W. Weissenhorn (2007) One step membrane incorporation of viral antigens as a vaccine candidate against HIV. J. Liposome Res. 17(3-4):139-54.
55. A., Albertini, G. Schoehn, W. Weissenhorn and R. W. Ruigrok (2007) Structural aspects of rabies virus replication. Cell Mol. Life Sci. 65(2), 282-94
54. W. Weissenhorn and H. Gottlinger (2007) ESCRT-I Part II : Forming the real ESCRT-I complex. Cell Host & Microbe 2, 1-2.
53. W. Weissenhorn, A. Hinz and Y. Gaudin (2007) Virus membrane fusion. FEBS Lett. 581(11):2150-5.
52. B. Hartlieb, T. Muziol, W. Weissenhorn* and S. Becker* (2007) Crystal structure of the C-terminal domain of Ebola virus VP30 reveals a role in transcription and nucleocapsid assembly. Proc. Natl. Acad. Sci. USA, 104(2), 624-9 (*corresponding authors).
51. T. Saiyed, I. Paarmann, B. Schmitt, S. Haeger, M. Sola, G. Schmalzing, W. Weissenhorn and H. Betz (2007) Molecular basis of gephyrin clustering at inhibitory synapses : Role of G- and E-domain interactions. J. Biol. Chem. 282(8), 5625-32.
50. A. V. Albertini, C. R. Clapier, A. K. Wernimont, G. Schoehn, W. Weissenhorn and R. W. H. Ruigrok (2007) Isolation and crystallization of a unique size category of recombinant Rabies virus Nucleoprotein–RNA rings. J. Struct. Biol. 158(1), 129-33.

2006 :

49. A. Albertini, A. Wernimont, T. Muziol, R. B. G. Ravelli, C. R. Clapier, G. Schoehn, W. Weissenhorn* and R.W. Ruigrok (2006) Crystal structure of the rabies virus nucleoprotein reveals complete RNA sequestering. Science, 313, 360-363. (*corresponding author)
48. E. Molina-Pineda, H. Belrahli, A. Piefer, I. Akula, P. Bates and W. Weissenhorn (2006) The crystal structure of ESCRT-I Vps28 reveals a conserved surface required for ESCRT-III Vps20 recruitment. Traffic, 7, 1007-1016.
47. T. Muziol, E. Pineda-Molina, G. Schoehn, R. Ravelli, A. Zamborlini, Y. Usami, H. Göttlinger, and W. Weissenhorn (2006) Structural basis for budding by the ESCRT-III factor CHMP3. Dev. Cell, 10, 821-830.
46. B. Hartlieb and W. Weissenhorn (2006) Filovirus assembly and budding. Virology, 344(1):64-70

Before 2006 :

45. W. Weissenhorn (2005) Crystal structure of endophilin A1. J. Mol. Biol. 351(3), 653-61.
44. T. L. Nguyen, G. Schoehn, W. Weissenhorn, A. R. Hermone, J. C. Burnett, R. G. Panchal, C. McGrath, D. W. Zaharevitz, M. J. Aman, Gussio, R., and S. Bavari (2005) An all atom model of the pore-like structure of hexameric VP40 from Ebola : Structural insight into the monomer-hexamer transition. J. Struct. Biol. 151(1), 30-40.
43. D. J. Schibli and W. Weissenhorn (2005) Class I and class II viral fusion protein structures reveal similar principles in membrane fusion. Mol. Membr. Biol. 21, 361-371.
42. O. Lenz, M. T. Dittmar, A. Wagner, B. Ferko, K. Vorauer-Uhl, G. Stiegler and W. Weissenhorn (2005) Trimeric membrane anchored gp41 inhibits HIV membrane fusion. J. Biol. Chem. 280(6), 4095-101.
41. T. Hoenen, V. Volchkov, L. Kolesnikova, E. Mittler, J. Timmins, M. Ottmann, O. Reynard, S. Becker and W. Weissenhorn (2005) VP40 octamers are essential for Ebola virus replication. J. Virol. 79(3), 1898-905.
40. A. K. Wernimont and W. Weissenhorn (2004) Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II. BMC Struct. Biol 4 (1), 10.
39. M. Sola, V.N. Bavro, J. Timmins, S. T. Franz, Ricard-Blum, G. Schoehn, R. H.W. Ruigrok, G. A. O’Sullivan, T. Saiyed, B. Schmitt, H. Betz, and W. Weissenhorn (2004) Structural basis of dynamic glycine receptor clustering by gephyrin EMBO J, 23(13):2510-9.
38. J. Timmins, R.H.W. Ruigrok, and W. Weissenhorn (2004) Structural studies on the Ebola virus matrix protein VP40 indicate that matrix proteins of enveloped RNA viruses are analogues but not homologues. FEMS Microbiol.Lett.15 ;233(2), 179-86.
37. A. Bracher and W. Weissenhorn (2004) Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus. BMC Struct. Biol. 4(1), 6.
36. R., Eichler, T., Strecker, L., Kolesnikova, J. ter Meulen, W., Weissenhorn, S.,Becker, H.-D.,Klenk, W., Garten and O., Lenz (2004) Lassa virus Z protein is the driving force for virus-like particle release. Virus Res., 100(2), 249-55.
35. G., Schoehn, A.M. Di Guilmi, D. Lemaire, I. Attree, W. Weissenhorn, and A. Dessen (2003). Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas. EMBO J. 22(19), 4957-4967.
34. T. Strecker, R.Eichler, J. ter Meulen, W. Weissenhorn, H.-D. Klenk, W. Garten and O. Lenz (2003) Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles. J. Virol. 77(19), 10700-10705.
33. J. Timmins, G., Schoehn, C. Kohlhaas, H.-D. Klenk, R.W.H., Ruigrok and W. Weissenhorn (2003) Oligomerization and polymerization of the filovirus matrix protein VP40. Virology, 312, 359-368.
32. F. X. Gomis-Rüth, A. Dessen, J. Timmins, A. Bracher, L. Kolesnikowa, S. Becker, H.-D. Klenk, and W. Weissenhorn (2003) The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties. Structure (Cambridge), 11, 423-433.
31. J. Timmins, G. Schoehn, S. Ricard-Blum, S. Scianimanico, T. Vernet, R.W.H. Ruigrok and W. Weissenhorn (2003) Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4. J. Mol. Biol. 326, 493-502.
30. A. Bracher and W. Weissenhorn (2002) Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p. EMBO J. 21, 6144-6124.
29. A. Bracher, J. Kadlec, H. Betz and W. Weissenhorn (2002) X-ray structure of a neuronal complexin/SNARE complex from squid. J. Biol. Chem. 277, 26517-26523.
28. V. N. Bavro, M. Sola, A. Bracher, M. Kneussel, H. Betz, and W. Weissenhorn (2002) Crystal structure of the GABAA receptor associated protein, GABARAP. EMBO Rep. 3, 183-189.
27. M. Sola, M. Kneussel, I. Heck, H. Betz and W. Weissenhorn (2001) X-Ray crystal structure of the trimeric N-terminal domain of gephyrin. J. Biol. Chem., 276, 25294-25301.
26. N. J. Mantis, P. A. Kozlowski, D. W. Mielcarz, W. Weissenhorn and M. R. Neutra. (2001) Immunization of mice with recombinant gp41 in a systemic prime/mucosal boost protocol induces HIV-1-specific serum IgG and secretory IgA antibodies. Vaccine, 19, 3990-4001.
25. J. Timmins, S. Scianimanico, G. Schoehn, and W. Weissenhorn (2001) Vesicular release of Ebola virus matrix protein VP40. Virology, 283, 1-6.
24. F. Baudin, I. Petit, W. Weissenhorn and R. W. H. Ruigrok. (2001) In vitro dissection of the membrane binding and RNP binding activities of influenza virus M1 protein. Virology, 281, 102-108.
23. A. Bracher and W. Weissenhorn (2001) Crystal structures of neuronal squid Sec1 implicate inter-domain hinge movement in the release of t-SNAREs. J. Mol. Biol., 306, 7-13.
22. S. Scianimanico, G. Schoehn, J. Timmins, R. H. W. Ruigrok, H.-D. Klenk, and W. Weissenhorn (2000) Membrane association induces a conformational change in the Ebola virus matrix protein. EMBO J., 19, 6732-6741.
21. A. Dessen, V. Volchkov, O. Dolnik, H.-D. Klenk and W. Weissenhorn (2000) Crystal structure of the matrix protein VP40 from Ebola virus. EMBO J., 19, 4228-4236.
20. Bracher, A. Perrakis, Dresbach, H. Betz, and W. Weissenhorn (2000) Crystal structure of neuronal Sec1 from squid sheds new light on the role of this protein in exocytosis. Structure Fold. Des., 8, 685-694.
19. R. W. H. Ruigrok, G. Schoen, A. Dessen, E. Forest, V. Volchkov, O. Dolnik, H.-D. Klenk, and W. Weissenhorn (2000) Structural characterization and membrane binding properties of the matrix protein VP40 of Ebola virus. J. Mol. Biol., 300, 103-112.
18. A. Dessen, E. Forest, V. Volchkov, O. Dolnik, H.-D. Klenk and W. Weissenhorn (2000) Crystallization and preliminary X-ray analysis of the matrix protein from Ebola virus. Acta Cryst. D56, 758-760.
17. A. Bracher, T. Dresbach, H. Betz and W. Weissenhorn (2000) Crystallization and preliminary X-ray analysis of squid neuronal Sec1. Acta Cryst. D56, 501-503.
16. G. Zhou, M. Ferrer, R. Chopra, T. M. Kapoor, T. Strassmeier, W. Weissenhorn, J. J. Skehel, D. Oprian, S. L. Schreiber, S. C. Harrison, and D. C. Wiley. (2000) The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core. Bioorg. Med. Chem., 8, 2219-2227.
15. M. Ferrer, T. Kapoor, T. Strassmeier, W. Weissenhorn, J. J. Skehel, D. Oprian, S. Schreiber, D. C. Wiley and S. C. Harrison. (1999) Selection of gp41-mediated cell entry inhibitors from biased combinatorial libraries of non-natural binding elements. Nature Struct. Biol., 10, 953-960.
14. W. Weissenhorn, A. Dessen, L. J.Calder, S. C. Harrison, J. J. Skehel, and D. C. Wiley (1999) Structural basis for membrane fusion by enveloped viruses. Mol. Membr. Biol. 16, 3-9.
13. W. Weissenhorn, A. Carfi, K.-H. Lee, J. J. Skehel, and D. C. Wiley (1998) Crystal structure of the Ebola Virus membrane fusion subunit, Gp2, from the envelope glycoprotein ectodomain. Mol Cell, 2, 605-616.
12. W. Weissenhorn, L. J. Calder, S. A. Wharton, J. J. Skehel and D. C. Wiley (1998) The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple stranded coiled coil. Proc. Nat. Acad. Sci. U.S.A, 95, 6032-6036.
11. W. Weissenhorn, A. Dessen, S. C. Harrison, J.J. Skehel and D. C. Wiley (1997) Atomic structure of an ectodomain from HIV-1 gp41. Nature 387, 426-430.
10. W. Weissenhorn, L. J. Calder, A. Dessen J. J. Skehel and D. C. Wiley (1997) Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in E. coli.. Proc. Nat. Acad. Sci.. U.S.A. 94, 6065-6069.
9. W. Weissenhorn, Y.-H. Chen, C. Reiter, C. Federle, E. H. Weiss G. Riethmüller and E. P. Rieber (1996) Structural diversity of monoclonal CD4 antibodies and their capacity to block the HIV gp120/CD4-interaction. Hybridoma 15, 117-124.
8. W. Weissenhorn, M. J. Eck, S. C. Harrison and D. C. Wiley (1996) Phosphorylated T cell receptor -chain and ZAP70 tandem SH2 domains form a 1:3 complex in vitro. Eur. J. Biochem. 238, 440-445.
7. W. Weissenhorn, S. A. Wharton, L. J. Calder, P. Earl, B. Moss, E. Aliprandis, J. J. Skehel and D. C. Wiley (1996) The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO J. 15, 1507-1514.
6. J. Chen, S. A. Wharton, W. Weissenhorn, L. J. Calder, F. M. Hughson, J. J. Skehel and D. C. Wiley (1995) The domain of the soluble membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc. Nat. Acad. Sci. U.S.A. 92, 12205-12209.
5. A. Braun, S. Kammerer, W. Weissenhorn, Weiss E. H. and H. Cleve (1994) Sequence of a putative human housekeeping gene (HK33) localized on chromosome 1. Gene, 146, 291-295
4. W. Weissenhorn, W. Scheuer, B. Kaluza, M. Schwirzke, C. Reiter, D. Flieger, H. Lenz, E. H. Weiss, E. P. Rieber, G. Riethmüller and U. H. Weidle (1992) Combinatorial functions of two chimeric antibodies directed to human CD4 and one directed to the alpha chain of the human interleukin-2 receptor. Gene, 121, 271-278.
3. W. Weissenhorn, Y. H. Chen, G. Riethmüller, E. P. Rieber and E. H.Weiss (1992) VH-related idiotopes detected by site-directed mutagenesis. J. Immunol. 149, 1237-124.
2. J. Zwirner, W. Weissenhorn, L. Karlson, A. Becker, E. P. Rieber, G. Riethmüller, E. H. Weiss, P. Peterson and G. Widera (1992) Expression of a functional chimeric immuno-globulin-MHC classII protein. J. Immunol. 148, 272-276.
1. W. Weissenhorn, E. H. Weiss, M. Schwirzke, B. Kaluza and U. H. Weidle (1991) Chimerization of antibodies by isolation of rearranged genomic variable regions by the polymerase chain reaction. Gene 106, 273-277.

Text books and online tools

6. Kozlov M.M., Weissenhorn W., Bassereau P. From Molecules to Living Organisms : An Interplay Between Biology and Physics, Chapter 10 : Membrane Remodeling : Theoretical principles, structures of protein scaffolds and forces involved. Editors : E. Pebay-Peyroula, H. Nury, F. Parcy, R. W. Ruigrok, C. Ziegler, L. F. Cugliandolo. Oxford University Press 2016, pages 287-351 ; ISBN 978-0-19-875295-0.
5. Hock M and Weissenhorn W. (2014) Membrane fusion, Reference Module in Biomedical Sciences. 27-Oct-14 doi : 10.1016/B978-0-12-801238-3.04814-5.
4. W. Weissenhorn and H. G. Göttlinger. Chapter 7 : Assembly and release. In : Kurth, R ; Bannert, N (editors) (2010). Retroviruses : Molecular Biology, Genomics and Pathogenesis. Caister Academic Press ISBN 978-1-904455-55-4.
3. A. Hinz and W. Weissenhorn (2008) Membrane fusion. In : Enzyclopedia of Virology 5 vols (B.W.J Mahy and M.H.V van Regenmortel, editors) pp 292-301, Oxford Elsevier
2. W. Weissenhorn (2004) Structure of viral proteins. In : Ebola and Marburg Viruses : Molecular and Cellular Biology. Editors, H.-D. Klenk and H. Feldmann. Horizon Scientific Press. ISBN : 0-9545232-3-7.
1. W. Weissenhorn (2002) Structure and function of viral glycoproteins in membrane fusion. In Structure-Function Relationships of Human Pathogenic Viruses. Editors A. Holzenburg and E. Bogner. Kluwer Academic/Plenum Publishers ISBN 0-306-46768-2. Pages 25-54.

Conference proceedings

2. R. W. H. Ruigrok, F. Baudin, I. Petit, and W. Weissenhorn (2001) Role of influenza virus M1 protein in the viral budding process. Elseviers International Congress Series No.1219, pages 397-404.
1. H.-D. Klenk, H. Feldmann, V. E. Volchkov, V. A. Volchkova and W. Weissenhorn (2001) Structure and function of the proteins of Marburg and Ebola viruses. SGM symposium 60 : New challenges to health : the threat of virus infection. Editors G. L. Smith, W. L. Irving, J. W. McCauley, D. J. Rowlands. Cambridge University Press. ISBN 0521 806143. pages 233 -245