Protein chainmail variants in dsDNA viruses. - Wikidata - awgldk - TriplyDB

Protein chainmail variants in dsDNA viruses.

Protein chainmail variants in dsDNA viruses.

http://www.wikidata.org/entity/Q46000096

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Atomic structure of the human cytomegalovirus capsid with its securing tegument layer of pp150.

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P2860

Protein chainmail variants in dsDNA viruses.

http://www.wikidata.org/entity/Q46000096

description

2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年學術文章

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2015年學術文章

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2015年學術文章

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name

Protein chainmail variants in dsDNA viruses.

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Protein chainmail variants in dsDNA viruses.

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type

label

Protein chainmail variants in dsDNA viruses.

@en

Protein chainmail variants in dsDNA viruses.

@nl

prefLabel

Protein chainmail variants in dsDNA viruses.

@en

Protein chainmail variants in dsDNA viruses.

@nl

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BIOPHY.2015.2.200

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AIMS biophysics

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Protein chainmail variants in dsDNA viruses.

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Z Hong Zhou

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Sequence permutations in the molecular evolution of DNA methyltransferases

Common ancestry of herpesviruses and tailed DNA bacteriophages.

Novel fold and capsid-binding properties of the lambda-phage display platform protein gpD

The crystal structure of a virus-like particle from the hyperthermophilic archaeon Pyrococcus furiosus provides insight into the evolution of viruses

Structural basis of enzyme encapsulation into a bacterial nanocompartment

P22 Coat Protein Structures Reveal a Novel Mechanism for Capsid Maturation: Stability without Auxiliary Proteins or Chemical Crosslinks

Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus

Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling

A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 Å resolution

Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling

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200-218

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scholarly article

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10.3934/BIOPHY.2015.2.200

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