Domain Organization of Vaccinia Virus Helicase-Primase D5.
about
Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline.Online ion-exchange chromatography for small-angle X-ray scattering.An in vitro fluorescence based study of initiation of RNA synthesis by influenza B polymerase.The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.The French Armed Forces Virology Unit: A Chronological Record of Ongoing Research on Orthopoxvirus.Global ubiquitination analysis reveals extensive modification and proteasomal degradation of cowpox virus proteins, but preservation of viral cores.
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P2860
Domain Organization of Vaccinia Virus Helicase-Primase D5.
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年學術文章
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2016年學術文章
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2016年學術文章
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name
Domain Organization of Vaccinia Virus Helicase-Primase D5.
@en
type
label
Domain Organization of Vaccinia Virus Helicase-Primase D5.
@en
prefLabel
Domain Organization of Vaccinia Virus Helicase-Primase D5.
@en
P2093
P2860
P50
P356
P1433
P1476
Domain Organization of Vaccinia Virus Helicase-Primase D5.
@en
P2093
Adam Round
Frédéric Iseni
Gregory Effantin
Stefan Reich
P2860
P304
P356
10.1128/JVI.00044-16
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P577
2016-02-24T00:00:00Z