Karsten C, Buettner F, Cajic S, Nehlmeier I, Roshani B, Klippert A
PLoS Pathog. 2024; 20(5):e1012190.
PMID: 38805549
PMC: 11161069.
DOI: 10.1371/journal.ppat.1012190.
Compans R, Kemp M
Curr Top Membr Transp. 2020; 11:233-277.
PMID: 32287477
PMC: 7146817.
DOI: 10.1016/S0070-2161(08)60750-9.
Seegers S, Frasier C, Greene S, Nesmelova I, Grdzelishvili V
J Virol. 2019; 94(3).
PMID: 31694943
PMC: 7000975.
DOI: 10.1128/JVI.01643-19.
Ortega V, Stone J, Contreras E, Iorio R, Aguilar H
Glycobiology. 2018; 29(1):2-21.
PMID: 29878112
PMC: 6291800.
DOI: 10.1093/glycob/cwy053.
Hundt J, Li Z, Liu Q
World J Gastroenterol. 2014; 19(47):8929-39.
PMID: 24379618
PMC: 3870546.
DOI: 10.3748/wjg.v19.i47.8929.
Role of N-linked glycans in the functions of hepatitis C virus envelope proteins incorporated into infectious virions.
Helle F, Vieyres G, Elkrief L, Popescu C, Wychowski C, Descamps V
J Virol. 2010; 84(22):11905-15.
PMID: 20844034
PMC: 2977866.
DOI: 10.1128/JVI.01548-10.
Correlation of glycosylation forms with position in amino acid sequence.
Pollack L, Atkinson P
J Cell Biol. 1983; 97(2):293-300.
PMID: 6350314
PMC: 2112528.
DOI: 10.1083/jcb.97.2.293.
Acylation of viral spike glycoproteins: a feature of enveloped RNA viruses.
Schmidt M
Virology. 1982; 116(1):327-38.
PMID: 6278712
PMC: 7131792.
DOI: 10.1016/0042-6822(82)90424-x.
Separation of cyanogen bromide-cleaved peptides of the vesicular stomatitis virus glycoprotein and analysis of their carbohydrate content.
Kingsford L, Emerson S, Kelley J
J Virol. 1980; 36(2):309-16.
PMID: 6253657
PMC: 353647.
DOI: 10.1128/JVI.36.2.309-316.1980.
Polylactosaminoglycan modification of a small integral membrane glycoprotein, influenza B virus NB.
Williams M, Lamb R
Mol Cell Biol. 1988; 8(3):1186-96.
PMID: 3367907
PMC: 363263.
DOI: 10.1128/mcb.8.3.1186-1196.1988.
Domains of virus glycoproteins.
SCHLESINGER M, Schlesinger S
Adv Virus Res. 1987; 33:1-44.
PMID: 3296693
PMC: 7131334.
DOI: 10.1016/s0065-3527(08)60315-2.
Expression of the Saccharomyces cerevisiae glycoprotein invertase in mouse fibroblasts: glycosylation, secretion, and enzymatic activity.
Bergh M, Cepko C, Wolf D, Robbins P
Proc Natl Acad Sci U S A. 1987; 84(11):3570-4.
PMID: 3295866
PMC: 304916.
DOI: 10.1073/pnas.84.11.3570.
Determination of the orientation of an integral membrane protein and sites of glycosylation by oligonucleotide-directed mutagenesis: influenza B virus NB glycoprotein lacks a cleavable signal sequence and has an extracellular NH2-terminal region.
Williams M, Lamb R
Mol Cell Biol. 1986; 6(12):4317-28.
PMID: 3025652
PMC: 367213.
DOI: 10.1128/mcb.6.12.4317-4328.1986.
A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface.
Machamer C, Florkiewicz R, Rose J
Mol Cell Biol. 1985; 5(11):3074-83.
PMID: 3018499
PMC: 369121.
DOI: 10.1128/mcb.5.11.3074-3083.1985.
Hazelhurst-vesicular-stomatitis-virus G and Sindbis-virus E1 glycoproteins undergo similar host-cell-dependent variation in oligosaccharide processing.
Davidson S, Hunt L
Biochem J. 1985; 229(1):47-55.
PMID: 2994631
PMC: 1145148.
DOI: 10.1042/bj2290047.
An enzymatic assay reveals that proteins destined for the apical or basolateral domains of an epithelial cell line share the same late Golgi compartments.
Fuller S, Bravo R, Simons K
EMBO J. 1985; 4(2):297-307.
PMID: 2990898
PMC: 554186.
DOI: 10.1002/j.1460-2075.1985.tb03629.x.
Intracellular transport of herpes simplex virus gD occurs more rapidly in uninfected cells than in infected cells.
Johnson D, SMILEY J
J Virol. 1985; 54(3):682-9.
PMID: 2987522
PMC: 254852.
DOI: 10.1128/JVI.54.3.682-689.1985.
Preliminary characterization of a Chinese hamster ovary cell glycosylation mutant isolated by screening for low intracellular lysosomal enzyme activity.
Hall C, ROBBINS A, Krag S
Mol Cell Biochem. 1986; 72(1-2):35-45.
PMID: 2950312
DOI: 10.1007/BF00230634.
Isolation and characterization of mouse FM3A cell mutants which are devoid of Newcastle disease virus receptors.
Hara T, Hattori S, Kawakita M
J Virol. 1989; 63(1):182-8.
PMID: 2535724
PMC: 247671.
DOI: 10.1128/JVI.63.1.182-188.1989.
Characterization and significance of delayed processing of the feline leukemia virus FeLV-FAIDS envelope glycoprotein.
Poss M, Quackenbush S, Mullins J, Hoover E
J Virol. 1990; 64(9):4338-45.
PMID: 2166820
PMC: 247901.
DOI: 10.1128/JVI.64.9.4338-4345.1990.