FEBS Letters · 1985 · 33 citations · 16 references
Life SciencesMolecular BiologyMolecular GeneticsMolecular VirologyProtein TranslationVirologyDna Virus BiologyViral InfectionsViral Protein ProcessingViral Rna BiologyVirus StructureAmino AcidsCdna SynthesisCloningHydrophobic FeaturesOpen Reading Frame LengthViral Envelope GlycoproteinsViral Envelope ProteinsViral Glycoproteins
We cloned a full-length complementary DNA for the hemagglutinin-neuraminidase (HN) mRNA of Sendai virus (HVJ) using a synthetic 27-mer as a probe. Nucleotide sequence analysis showed that there is a long open reading frame on the mRNA that encodes a protein of 575 amino acids. The deduced amino acid sequence indicated that only one hydrophobic region sufficiently long to anchor the protein in the membrane and located near the N-terminus (amino acids 35-60). It is suggested that HN protein is oriented with its N-terminus inside the membrane.
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Studies on transformation of Escherichia coli with plasmids
Douglas Hanahan · Journal of Molecular Biology · 1983 · 11.3K citations
Intracellular protein topogenesis
Günter Blobel · Proceedings of the National Academy of Sciences · 1980 · 1.4K citations · Full text