Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles (Q27660228)

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English	Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles	scientific article

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instance of

scholarly article

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title

Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles (English)

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main subject

cell biology

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Rous sarcoma virus

object named as

Rous Sarcoma Virus

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based on heuristic

inferred from title

author

Richard Kingston

series ordinal

3

object named as

Richard L Kingston

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author name string

Jae-Kyung Hyun

series ordinal

1

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Mazdak Radjainia

series ordinal

2

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Alok K Mitra

series ordinal

4

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language of work or name

English

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publication date

14 May 2010

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published in

Journal of Biological Chemistry

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volume

285

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issue

20

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page(s)

15056-64

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cites work

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Structure and self-association of the Rous sarcoma virus capsid protein

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Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses

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Adding the Third Dimension to Virus Life Cycles: Three-Dimensional Reconstruction of Icosahedral Viruses from Cryo-Electron Micrographs

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Characterization of the in vitro HIV-1 capsid assembly pathway

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29 September 2017

Visualization of a missing link in retrovirus capsid assembly

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Irregular and Semi-Regular Polyhedral Models for Rous Sarcoma Virus Cores.

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The structural biology of HIV assembly

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Critical role of conserved hydrophobic residues within the major homology region in mature retroviral capsid assembly.

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RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesis.

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Mutational analysis of the N-terminal domain of Moloney murine leukemia virus capsid protein

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Identifiers

DOI

10.1074/JBC.M110.108209

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Fatcat ID

release_2xigxli7mvb7hdns3vlfxpjhqu

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PMC publication ID

2865289

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PubMed publication ID

20228062

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ResearchGate publication ID

41943581

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