Aliper E, Efremov R
Int J Mol Sci. 2023; 24(22).
PMID: 38003610
PMC: 10671605.
DOI: 10.3390/ijms242216421.
S Mesquita F, Abrami L, Sergeeva O, Turelli P, Qing E, Kunz B
Dev Cell. 2021; 56(20):2790-2807.e8.
PMID: 34599882
PMC: 8486083.
DOI: 10.1016/j.devcel.2021.09.016.
Duverge A, Negroni M
Viruses. 2020; 12(11).
PMID: 33207797
PMC: 7697029.
DOI: 10.3390/v12111311.
Ramsey J, Mukhopadhyay S
Viruses. 2017; 9(8).
PMID: 28820485
PMC: 5580485.
DOI: 10.3390/v9080228.
Ramsey J, Renzi E, Arnold R, Trinidad J, Mukhopadhyay S
J Virol. 2016; 91(3).
PMID: 27852864
PMC: 5244351.
DOI: 10.1128/JVI.02000-16.
Molecular pathogenesis of H5 highly pathogenic avian influenza: the role of the haemagglutinin cleavage site motif.
Luczo J, Stambas J, Durr P, Michalski W, Bingham J
Rev Med Virol. 2015; 25(6):406-30.
PMID: 26467906
PMC: 5057330.
DOI: 10.1002/rmv.1846.
Dynamic palmitoylation and the role of DHHC proteins in T cell activation and anergy.
Ladygina N, Martin B, Altman A
Adv Immunol. 2011; 109:1-44.
PMID: 21569911
PMC: 5464999.
DOI: 10.1016/B978-0-12-387664-5.00001-7.
A structural and functional perspective of alphavirus replication and assembly.
Jose J, Snyder J, Kuhn R
Future Microbiol. 2009; 4(7):837-56.
PMID: 19722838
PMC: 2762864.
DOI: 10.2217/fmb.09.59.
Spike protein assembly into the coronavirion: exploring the limits of its sequence requirements.
Bosch B, de Haan C, Smits S, Rottier P
Virology. 2005; 334(2):306-18.
PMID: 15780881
PMC: 7111810.
DOI: 10.1016/j.virol.2005.02.001.
The influenza virus ion channel and maturation cofactor M2 is a cholesterol-binding protein.
Schroeder C, Heider H, Moncke-Buchner E, Lin T
Eur Biophys J. 2004; 34(1):52-66.
PMID: 15221235
DOI: 10.1007/s00249-004-0424-1.
Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication.
Law L, Everitt J, Beatch M, Holmes C, Hobman T
J Virol. 2003; 77(3):1764-71.
PMID: 12525610
PMC: 140988.
DOI: 10.1128/jvi.77.3.1764-1771.2003.
Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein.
Chang K, Sheng Y, Gombold J
Virology. 2000; 269(1):212-24.
PMID: 10725213
PMC: 7131280.
DOI: 10.1006/viro.2000.0219.
Adaptive mutations in Sindbis virus E2 and Ross River virus E1 that allow efficient budding of chimeric viruses.
Kim K, Strauss E, Strauss J
J Virol. 2000; 74(6):2663-70.
PMID: 10684281
PMC: 111755.
DOI: 10.1128/jvi.74.6.2663-2670.2000.
The function of the spike protein of mouse hepatitis virus strain A59 can be studied on virus-like particles: cleavage is not required for infectivity.
BOS E, Luytjes W, Spaan W
J Virol. 1997; 71(12):9427-33.
PMID: 9371603
PMC: 230247.
DOI: 10.1128/JVI.71.12.9427-9433.1997.
The molecular biology of coronaviruses.
Lai M, Cavanagh D
Adv Virus Res. 1997; 48:1-100.
PMID: 9233431
PMC: 7130985.
Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins.
Veit M, Reverey H, Schmidt M
Biochem J. 1996; 318 ( Pt 1):163-72.
PMID: 8761467
PMC: 1217603.
DOI: 10.1042/bj3180163.
Palmitoylation of Semliki Forest virus glycoproteins in insect cells (C6/36) occurs in an early compartment and is coupled to the cleavage of the precursor p62.
Scharer C, Naim H, KOBLET H
Arch Virol. 1993; 132(3-4):237-54.
PMID: 8379849
DOI: 10.1007/BF01309536.
The alphaviruses: gene expression, replication, and evolution.
Strauss J, Strauss E
Microbiol Rev. 1994; 58(3):491-562.
PMID: 7968923
PMC: 372977.
DOI: 10.1128/mr.58.3.491-562.1994.
Coronavirus glycoprotein E1, a new type of viral glycoprotein.
Niemann H, Klenk H
J Mol Biol. 1981; 153(4):993-1010.
PMID: 7343686
PMC: 7130891.
DOI: 10.1016/0022-2836(81)90463-0.
Identification of acyl donors and acceptor proteins for fatty acid acylation in BHK cells infected with Semliki Forest virus.
Berger M, Schmidt M
EMBO J. 1984; 3(4):713-9.
PMID: 6723626
PMC: 557416.
DOI: 10.1002/j.1460-2075.1984.tb01874.x.