Membrane-containing virus particles exhibit the mechanics of a composite material for genome protection.

about

Membrane-containing virus particles exhibit the mechanics of a composite material for genome protection.

Item

http://www.wikidata.org/entity/Q54235355

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh

2018年學術文章

@zh-hant

name

Membrane-containing virus part ...... aterial for genome protection.

@en

Membrane-containing virus part ...... aterial for genome protection.

@en-gb

Membrane-containing virus part ...... aterial for genome protection.

@nl

type

Item

label

Membrane-containing virus part ...... aterial for genome protection.

@en

Membrane-containing virus part ...... aterial for genome protection.

@en-gb

Membrane-containing virus part ...... aterial for genome protection.

@nl

prefLabel

Membrane-containing virus part ...... aterial for genome protection.

@en

Membrane-containing virus part ...... aterial for genome protection.

@en-gb

Membrane-containing virus part ...... aterial for genome protection.

@nl

P1154

2-s2.0-85046103137

http://www.w3.org/2001/XMLSchema#string

P1433

Nanoscale

P1476

Membrane-containing virus part ...... aterial for genome protection.

@en

P2093

G A Schwartz

http://www.w3.org/2001/XMLSchema#string

P2860

Bacteriophage capsids: tough nanoshells with complex elastic properties

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

A structural model of the genome packaging process in a membrane-containing double stranded DNA virus

Fluctuating Nonlinear Spring Model of Mechanical Deformation of Biological Particles

Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions

Minor proteins, mobile arms and membrane-capsid interactions in the bacteriophage PRD1 capsid

The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions

Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks.

Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection

UCSF Chimera--a visualization system for exploratory research and analysis

P304

7769-7779

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1039/C8NR00196K

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

P5530

37632670

http://www.w3.org/2001/XMLSchema#string

P577

2018-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P6179

1103271558

http://www.w3.org/2001/XMLSchema#string

P698

29658555

http://www.w3.org/2001/XMLSchema#string

P932

5944389

http://www.w3.org/2001/XMLSchema#string

P953

129692/