BartonE.S., ConnollyJ.L., ForrestJ.C., ChappellJ.D., DermodyT.S.2001a. Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem, 276:2200–2211.
2.
BartonE.S., ForrestJ.C., ConnollyJ.L., ChappellJ.D., LiuY., SchnellF.J., NusratA., ParkosC.A., DermodyT.S.2001b. Junction adhesion molecule is a receptor for reovirus. Cell, 104:441–451.
3.
BrownM.T., CooperJ.A.1996. Regulation, substrates and functions of src. Biochim Biophys Acta, 1287:121–149.
4.
CampbellJ.A., ShellingP., WetzelJ.D., JohnsonE.M., WilsonG.A.R., ForrestJ.C., Aurrand-LionsM., ImhofB., StehleT., DermodyT.S.2005. Junctional adhesion molecule-A serves as a receptor for prototype and field-isolate strains of mammalian reovirus. J. Virol, 79:7967–7978.
ChandranK., FarsettaD.L., NibertM.L.2002. Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein μ1 mediates membrane disruption. J Virol, 76:9920–9933.
7.
ChandranK., ParkerJ.S., EhrlichM., KirchhausenT., NibertM.L.2003. The delta region of outer-capsid protein micro 1 undergoes conformational change and release from reovirus particles during cell entry. J Virol, 77:13361–13375.
8.
ChandranK., SullivanN.J., FelborU., WhelanS.P., CunninghamJ.M.2005. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science, 308:1643–1645.
9.
CooperJ.A., GouldK.L., CartwrightC.A., HunterT.1986. Tyr527 is phosphorylated in pp60c-src: implications for regulation. Science, 231:1431–1434.
10.
CoteM., MisasiJ., RenT., BruchezA., LeeK., FiloneC.M., HensleyL., LiQ., OryD., ChandranK., CunninghamJ.2011. Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature, 477:344–348.
11.
CoyneC.B., BergelsonJ.M.2006. Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell, 124:119–131.
12.
DanthiP., CoffeyC.M., ParkerJ.S., AbelT.W., DermodyT.S.2008. Independent regulation of reovirus membrane penetration and apoptosis by the μ1 φ domain. PLoS Pathog, 4:e1000248.
13.
DanthiP., HansbergerM.W., CampbellJ.A., ForrestJ.C., DermodyT.S.2006. JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis. J Virol, 80:1261–1270.
DiederichS., SauerheringL., WeisM., AltmeppenH., SchaschkeN., ReinheckelT., ErbarS., MaisnerA.2012. Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment. J Virol, 86:3736–3745.
16.
DoyleJ.D., DanthiP., KendallE.A., OomsL.S., WetzelJ.D., DermodyT.S.2012. Molecular determinants of proteolytic disassembly of the reovirus outer capsid. J Biol Chem, 287:8029–8038.
17.
EbertD.H., DeussingJ., PetersC., DermodyT.S.2002. Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J Biol Chem, 277:24609–24617.
18.
EhrlichM., BollW., Van OijenA., HariharanR., ChandranK., NibertM.L., KirchhausenT.2004. Endocytosis by random initiation and stabilization of clathrin-coated pits. Cell, 118:591–605.
19.
ForrestJ.C., CampbellJ.A., SchellingP., StehleT., DermodyT.S.2003. Structure-function analysis of reovirus binding to junctional adhesion molecule 1. Implications for the mechanism of reovirus attachment. J Biol Chem, 278:48434–48444.
20.
GoldenJ.W., BaheJ.A., LucasW.T., NibertM.L., SchiffL.A.2004. Cathepsin S supports acid-independent infection by some reoviruses. J Biol Chem, 279:8547–8557.
21.
GuhaS., PadhH.2008. Cathepsins: fundamental effectors of endolysosomal proteolysis. Indian J Biochem Biophys, 45:75–90.
22.
HuangI.C., BoschB.J., LiF., LiW., LeeK.H., GhiranS., VasilievaN., DermodyT.S., HarrisonS.C., DormitzerP.R., FarzanM., RottierP.J., ChoeH.2006. SARS coronavirus, but not human coronavirus NL63, utilizes cathepsin L to infect ACE2-expressing cells. J Biol Chem, 281:3198–3203.
MoserM., LegateK.R., ZentR., FasslerR.2009. The tail of integrins, talin, and kindlins. Science, 324:895–899.
32.
NanboA., ImaiM., WatanabeS., NodaT., TakahashiK., NeumannG., HalfmannP., KawaokaY.2010. Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner. PLoS Pathog, 6:e1001121.
33.
NibertM.L., OdegardA.L., AgostoM.A., ChandranK., SchiffL.A.2005. Putative autocleavage of reovirus μ1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization. J Mol Biol, 345:461–474.
34.
OdegardA.L., ChandranK., ZhangX., ParkerJ.S., BakerT.S., NibertM.L.2004. Putative autocleavage of outer capsid protein μ1, allowing release of myristoylated peptide μ1N during particle uncoating, is critical for cell entry by reovirus. J Virol, 78:8732–8745.
35.
OuattaraL.A., BarinF., BarthezM.A., BonnaudB., RoingeardP., GoudeauA., CastelnauP., VernetG., Paranhos-BaccalaG., Komurian-PradelF.2011. Novel human reovirus isolated from children with acute necrotizing encephalopathy. Emerg Infect Dis, 17:1436–1444.
36.
PagerC.T., CraftW.W.Jr., PatchJ., DutchR.E.2006. A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology, 346:251–257.
37.
PagerC.T., DutchR.E.2005. Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J Virol, 79:12714–12720.
ParsonsJ.T., WeberM.J.1989. Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr Top Microbiol Immunol, 147:79–127.
SeversonE.A., ParkosC.A.2009. Structural determinants of Junctional Adhesion Molecule A (JAM-A) function and mechanisms of intracellular signaling. Curr Opin Cell Biol, 21:701–707.
42.
SimmonsG., GosaliaD.N., RennekampA.J., ReevesJ.D., DiamondS.L., BatesP.2005. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc Natl Acad Sci U S A, 102:11876–11881.