About: The influence of assembly conditions on effeiciency and morphology of in vitro assembled capsid-like particles formed from CA-NC of Mason-Pfirzer money virus

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: The influence of assembly conditions on effeiciency and morphology of in vitro assembled capsid-like particles formed from CA-NC of Mason-Pfirzer money virus Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	polyprotein Gag (cs) Domains within structural polyprotein Gag of all retroviruses initiate and direct assembly of the immature viral particles. Gag forms capsid-like particles in bacteria, mammalian cells and in vitro. Several studies have shown that Gag and its deletion mutants, e.g. capsid-nucleocapsid fusion protein (CA-NC) or CA assemble in vitro into spherical, conical or tubular particles. Morphology of formed particles depends on virus type and assembly conditions. CA itself can assemble in vitro into tubular or conical structures resembling a mature core. NC facilitates Gag interactions and it is crucial for specific incorporation of genomic RNA. In previous study we have shown that Mason-Pfizer monkey virus deletion construct consisting of CA and NC fusion protein that lacks the N-terminal proline (Pro-)CA-NC assembles into spherical particles when expressed in E. coli in contrast with tubular structures formed from CA-NC under the same conditions. To evaluate the effect of nucleic acids on the assembly of immat Domains within structural polyprotein Gag of all retroviruses initiate and direct assembly of the immature viral particles. Gag forms capsid-like particles in bacteria, mammalian cells and in vitro. Several studies have shown that Gag and its deletion mutants, e.g. capsid-nucleocapsid fusion protein (CA-NC) or CA assemble in vitro into spherical, conical or tubular particles. Morphology of formed particles depends on virus type and assembly conditions. CA itself can assemble in vitro into tubular or conical structures resembling a mature core. NC facilitates Gag interactions and it is crucial for specific incorporation of genomic RNA. In previous study we have shown that Mason-Pfizer monkey virus deletion construct consisting of CA and NC fusion protein that lacks the N-terminal proline (Pro-)CA-NC assembles into spherical particles when expressed in E. coli in contrast with tubular structures formed from CA-NC under the same conditions. To evaluate the effect of nucleic acids on the assembly of immat (en)
Title	The influence of assembly conditions on effeiciency and morphology of in vitro assembled capsid-like particles formed from CA-NC of Mason-Pfirzer money virus The influence of assembly conditions on effeiciency and morphology of in vitro assembled capsid-like particles formed from CA-NC of Mason-Pfirzer money virus (en) Vliv podmínek assembly na morfologii částic tvořených z CA-NC proteinu MPMV (cs)
skos:prefLabel	The influence of assembly conditions on effeiciency and morphology of in vitro assembled capsid-like particles formed from CA-NC of Mason-Pfirzer money virus The influence of assembly conditions on effeiciency and morphology of in vitro assembled capsid-like particles formed from CA-NC of Mason-Pfirzer money virus (en) Vliv podmínek assembly na morfologii částic tvořených z CA-NC proteinu MPMV (cs)
skos:notation	RIV/60461373:22330/04:00012908!RIV/2005/MSM/223305/N
http://linked.open.../vavai/riv/strany	254
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(LN00A079)
http://linked.open...vai/riv/dodaniDat	2005
http://linked.open...aciTvurceVysledku	Suchanová, Šárka Rumlová, Michaela Ulbrich, Pavel Ruml, Tomáš
http://linked.open.../riv/druhVysledku	D - Článek ve sborníku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Vysoká škola chemicko-technologická v Praze / Fakulta potravinářské a biochemické technologie
http://linked.open...dnocenehoVysledku	567808
http://linked.open...ai/riv/idVysledku	RIV/60461373:22330/04:00012908
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	capsid assembly (en)
http://linked.open.../riv/klicoveSlovo	capsid assembly
http://linked.open...ontrolniKodProRIV	[4082FF7748F4]
http://linked.open...v/mistoKonaniAkce	Vermont
http://linked.open...i/riv/mistoVydani	Vermont
http://linked.open...i/riv/nazevZdroje	Virus Assembly Conference
http://linked.open...in/vavai/riv/obor	EE
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Center of Integrated Genomics
http://linked.open...UplatneniVysledku	2004
http://linked.open...iv/tvurceVysledku	Ruml, Tomáš Rumlová, Michaela Ulbrich, Pavel Haubová, Šárka Hunter, Eric
http://linked.open...vavai/riv/typAkce	WRD - Světová
http://linked.open.../riv/zahajeniAkce	2004-01-01 (xsd:date)
number of pages	1 (xsd:int)
http://purl.org/ne...btex#hasPublisher	Vermont Academy
http://localhost/t...ganizacniJednotka	22330

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 84 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software