Two palmitylated cysteine residues of the severe acute respiratory syndrome coronavirus spike (S) protein are critical for S incorporation into virus-like particles, but not for M-S co-localization

Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity

(2011) Kazuya Shirato et al.   VIRUS RESEARCH

Enhanced cell fusion activity in porcine epidemic diarrhea virus adapted to suckling mice

(2010) Kazuya Shirato et al.   ARCHIVES OF VIROLOGY

Palmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell–cell fusion but not interaction with M protein

(2010) Corrin E. McBride et al.   VIROLOGY

Role of Spike Protein Endodomains in Regulating Coronavirus Entry

(2009) Ana Shulla et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A Single Tyrosine in the Severe Acute Respiratory Syndrome Coronavirus Membrane Protein Cytoplasmic Tail Is Important for Efficient Interaction with Spike Protein

(2009) C. E. McBride et al.   JOURNAL OF VIROLOGY

Protease-Mediated Entry via the Endosome of Human Coronavirus 229E

(2008) M. Kawase et al.   JOURNAL OF VIROLOGY

The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles

(2008) Y. L. Siu et al.   JOURNAL OF VIROLOGY