Analysis of Mason-Pfizer monkey virus gag domains required for capsid assembly in bacteria: role of the N-terminal proline residue of CA in directing particle shape.

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F00%3A57000264" target="_blank" >RIV/61388963:_____/00:57000264 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Analysis of Mason-Pfizer monkey virus gag domains required for capsid assembly in bacteria: role of the N-terminal proline residue of CA in directing particle shape.

Original language description

The domains necessary for the assembly of the Gag polyprotein precursor of Mason-Pfizer monkey virus were analysed. The results shown that CA and NC domains are absolutely necessary for the assembly. Furthermore, it was shown that N-terminal proline of CA plays a key role in directing particle shape, since the expression of a CANC protein lacking this proline results in the assembly of spherical particles in place of the sheets assembled by the CANC protein.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2000

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Virology

ISSN

0022-538X

e-ISSN

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Volume of the periodical

74

Issue of the periodical within the volume

18

Country of publishing house

US - UNITED STATES

Number of pages

8

Pages from-to

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UT code for WoS article

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EID of the result in the Scopus database

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