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September 1, 1999VirologyOpen Access

Second Site Mutations in the N-Terminus of the Major Capsid Protein (VP5) Overcome a Block at the Maturation Cleavage Site of the Capsid Scaffold Proteins of Herpes Simplex Virus Type 1

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PDPrashant DesaiJohns Hopkins UniversitySPStanley PersonSidney Kimmel Comprehensive Cancer Center

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Desai et al. (1999) studied this question.

synapsesocial.com/papers/6ab77e43ed6a4447fcebc4b5https://doi.org/10.1006/viro.1999.9877
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein1996 · 79 citations
  2. 2The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold1995 · 60 citations
  3. 3Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins1994 · 182 citations
  4. 4Mutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA1993 · 136 citations
  5. 5Transcriptional and genetic analyses of the herpes simplex virus type 1 genome: coordinates 0.29 to 0.451984 · 159 citations