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Biosynthesis and function of the coronavirus spike protein.
Vennema H, Rottier PJ, Heijnen L, Godeke GJ, Horzinek MC, Spaan WJ. Vennema H, et al. Adv Exp Med Biol. 1990;276:9-19. doi: 10.1007/978-1-4684-5823-7_3. Adv Exp Med Biol. 1990. PMID: 2103106 No abstract available.
Assembly of the coronavirus envelope: homotypic interactions between the M proteins.
de Haan CA, Vennema H, Rottier PJ. de Haan CA, et al. Among authors: vennema h. J Virol. 2000 Jun;74(11):4967-78. doi: 10.1128/jvi.74.11.4967-4978.2000. J Virol. 2000. PMID: 10799570 Free PMC article.
Mutant M proteins which were not able to assemble into viruslike particles (VLPs) by themselves (C. A. M. de Haan, L. Kuo, P. S. Masters, H. Vennema, and P. J. M. Rottier, J. Virol. 72:6838-6850, 1998) were tested for the ability to associate with other M proteins a …
Mutant M proteins which were not able to assemble into viruslike particles (VLPs) by themselves (C. A. M. de Haan, L. Kuo, P. S. Masters, …
Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein.
de Haan CA, Smeets M, Vernooij F, Vennema H, Rottier PJ. de Haan CA, et al. Among authors: vennema h. J Virol. 1999 Sep;73(9):7441-52. doi: 10.1128/JVI.73.9.7441-7452.1999. J Virol. 1999. PMID: 10438834 Free PMC article.
Interestingly, changes in the amino-terminal and extreme carboxy-terminal domains of M, which did not disrupt the interaction with S, are known to be fatal to the ability of the protein to engage in virus particle formation (C. A. M. de Haan, L. Kuo, P. S. Masters, H. V
Interestingly, changes in the amino-terminal and extreme carboxy-terminal domains of M, which did not disrupt the interaction with S, are kn …
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