A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly
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Title
A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly
Authors
Keywords
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Journal
Science Advances
Volume 3, Issue 7, Pages e1700423
Publisher
American Association for the Advancement of Science (AAAS)
Online
2017-07-27
DOI
10.1126/sciadv.1700423
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Related references
Note: Only part of the references are listed.- Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation
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- Charge Detection Mass Spectrometry with Resolved Charge States
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- Peering Down the Barrel of a Bacteriophage Portal: The Genome Packaging and Release Valve in P22
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- Bacteriophage P22 capsid size determination: Roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus
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- Seeing the Portal in Herpes Simplex Virus Type 1 B Capsids
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- Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching
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- ‘Let the phage do the work’: Using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants
- (2010) Carolyn M. Teschke et al. VIROLOGY
- In vitro incorporation of the phage Phi29 connector complex
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- Determination of Stoichiometry and Conformational Changes in the First Step of the P22 Tail Assembly
- (2008) Kristina Lorenzen et al. JOURNAL OF MOLECULAR BIOLOGY
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