(Q27486629)

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Processing the nonstructural polyproteins of sindbis virus: nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans

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Processing the nonstructural polyproteins of sindbis virus: nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans (English)

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author name string

W R Hardy

1

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J H Strauss

2

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publication date

November 1989

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Journal of Virology

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63

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4653-64

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11

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Production of infectious RNA transcripts from Sindbis virus cDNA clones: mapping of lethal mutations, rescue of a temperature-sensitive marker, and in vitro mutagenesis to generate defined mutants

1 reference

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DNA sequence analysis with a modified bacteriophage T7 DNA polymerase

1 reference

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20 March 2017

Processing the nonstructural polyproteins of Sindbis virus: study of the kinetics in vivo by using monospecific antibodies

1 reference

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Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications

1 reference

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Mutagenesis of the in-frame opal termination codon preceding nsP4 of Sindbis virus: studies of translational readthrough and its effect on virus replication

1 reference

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20 March 2017

Mapping of RNA- temperature-sensitive mutants of Sindbis virus: complementation group F mutants have lesions in nsP4

1 reference

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57 Sequencing end-labeled DNA with base-specific chemical cleavages

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Sindbis virus proteins nsP1 and nsP2 contain homology to nonstructural proteins from several RNA plant viruses

1 reference

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29 September 2017

Viral proteinases

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Mapping of RNA- temperature-sensitive mutants of Sindbis virus: assignment of complementation groups A, B, and G to nonstructural proteins

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1 reference

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29 September 2017

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Primary structures of the core proteins of the alphaviruses Semliki Forest virus and Sindbis virus

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