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Basic Characteristics of Mutations
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Mutation Site
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S170P |
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Mutation Site Sentence
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In particular, Melegari et al. reported that S162A leads to a profound encapsidation defect, S170P leads to a less profound decrease and S155A does not affect encapsidation. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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C |
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Standardized Encoding Gene
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C
|
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Genotype/Subtype
|
D |
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Viral Reference
|
V01460.1
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Functional Impact and Mechanisms
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Disease
|
-
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Immune
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- |
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Target Gene
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-
|
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
|
- |
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Location
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- |
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Literature Information
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|
PMID
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21358805
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Title
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Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically
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Author
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Lewellyn EB,Loeb DD
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Journal
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PloS one
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Journal Info
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2011 Feb 15;6(2):e17202
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Abstract
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The core protein of hepatitis B virus can be phosphorylated at serines 155, 162, and 170. The contribution of these serine residues to DNA synthesis was investigated. Core protein mutants were generated in which each serine was replaced with either alanine or aspartate. Aspartates can mimic constitutively phosphorylated serines while alanines can mimic constitutively dephosphorylated serines. The ability of these mutants to carry out each step of DNA synthesis was determined. Alanine substitutions decreased the efficiency of minus-strand DNA elongation, primer translocation, circularization, and plus-strand DNA elongation. Aspartate substitutions also reduced the efficiency of these steps, but the magnitude of the reduction was less. Our findings suggest that phosphorylated serines are required for multiple steps during DNA synthesis. It has been proposed that generation of mature DNA requires serine dephosphorylation. Our results suggest that completion of rcDNA synthesis requires phosphorylated serines.
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Sequence Data
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-
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