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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F04%3A00012789%21RIV%2F2005%2FMSM%2F223305%2FN
rdf:type
skos:Concept n19:Vysledek
dcterms:description
The role of retroviral proteases is well known. These aspartic proteases are active as homodimers and cleave Gag polyprotein precursors during particle release. M-PMV assembles immature particles in the cytoplasm and activation of the protease within the immature particles is delayed until viral budding. Gene encoding M-PMV PR is located at the 3' end of the pro ORF. The first active form of the protease is a 17 kDa protein, containing about 50 amino acids C-terminal domain which is characteristic only for betaretroviruses. Other structural elements and the overall structure of M-PMC PR are similar to other retroviral proteases1. The 17 kDa PR undergoes an autocatalytic processing from the C-terminus yielding 13 and 12 kDa proteases2. Here we have investigated the role of C-terminal domain of PR for the maturation of M-PMV. Sequences encoding the C-terminal domain of PR were deleted in the M-PMV genome and the processing of Gag polyproteins, the RT activity, and viral infectivity were analysed. T funkce proteasových domén MPMV The role of retroviral proteases is well known. These aspartic proteases are active as homodimers and cleave Gag polyprotein precursors during particle release. M-PMV assembles immature particles in the cytoplasm and activation of the protease within the immature particles is delayed until viral budding. Gene encoding M-PMV PR is located at the 3' end of the pro ORF. The first active form of the protease is a 17 kDa protein, containing about 50 amino acids C-terminal domain which is characteristic only for betaretroviruses. Other structural elements and the overall structure of M-PMC PR are similar to other retroviral proteases1. The 17 kDa PR undergoes an autocatalytic processing from the C-terminus yielding 13 and 12 kDa proteases2. Here we have investigated the role of C-terminal domain of PR for the maturation of M-PMV. Sequences encoding the C-terminal domain of PR were deleted in the M-PMV genome and the processing of Gag polyproteins, the RT activity, and viral infectivity were analysed. T
dcterms:title
FUNCTIONS OF PROTEASE DOMAINS IN M-PMV funkce proteasových domén MPMV FUNCTIONS OF PROTEASE DOMAINS IN M-PMV
skos:prefLabel
funkce proteasových domén MPMV FUNCTIONS OF PROTEASE DOMAINS IN M-PMV FUNCTIONS OF PROTEASE DOMAINS IN M-PMV
skos:notation
RIV/60461373:22330/04:00012789!RIV/2005/MSM/223305/N
n4:strany
42
n4:aktivita
n15:P
n4:aktivity
P(LN00A079)
n4:dodaniDat
n9:2005
n4:domaciTvurceVysledku
n10:9372040 n10:6998798
n4:druhVysledku
n8:D
n4:duvernostUdaju
n21:S
n4:entitaPredkladatele
n16:predkladatel
n4:idSjednocenehoVysledku
565008
n4:idVysledku
RIV/60461373:22330/04:00012789
n4:jazykVysledku
n13:eng
n4:klicovaSlova
protease;G-patch
n4:klicoveSlovo
n7:G-patch n7:protease
n4:kontrolniKodProRIV
[23F01726930C]
n4:mistoKonaniAkce
Praha
n4:mistoVydani
Praha
n4:nazevZdroje
The retrovirus assembly meeting
n4:obor
n11:EE
n4:pocetDomacichTvurcuVysledku
2
n4:pocetTvurcuVysledku
4
n4:projekt
n14:LN00A079
n4:rokUplatneniVysledku
n9:2004
n4:tvurceVysledku
Bauerová, Helena Hunter, Eric Pichová, Iva Ruml, Tomáš
n4:typAkce
n12:WRD
n4:zahajeniAkce
2004-01-01+01:00
s:numberOfPages
1
n18:hasPublisher
JPM Tisk s. r. o.
n17:isbn
80-86313-13-1
n5:organizacniJednotka
22330