Вы искали: replikona (Хорватский - Английский)

genotip replikona
genotype replicons

srednja vrijednost iz višestrukih pokusa istog laboratorijskog replikona.
mean value from multiple experiments of same laboratory replicon.

podaci iz kimeričkih replikona ns5a koji nose aminokiseline ns5a 9-184.
data from a chimeric ns5a replicon carrying ns5a amino acids 9-184.

tablica 5: djelovanje ledipasvira i sofosbuvira protiv kimeričkih replikona
table 5: activity of ledipasvir and sofosbuvir against chimeric replicons

Čini se da je gubitak rnk replikona proces prvog reda u odnosu na vrijeme liječenja.
loss of replicon rna appears to be first-order with respect to time of treatment.

liječenje pri ic90 tijekom 72 sata rezultiralo je padom rnk replikona od 1–log10.
treatment at ic90 for 72 hours resulted in a 1-log10 drop in replicon rna.

tablica 4: djelovanje sofosbuvira i velpatasvira protiv replikona pune duljine ili kimeričkih laboratorijskih replikona
table 4: activity of sofosbuvir and velpatasvir against full-length or chimeric laboratory replicons

prisutnost 50%-tnog ljudskog seruma smanjila je aktivnost simeprevira protiv replikona za 2,4 puta.
the presence of 50% human serum reduced simeprevir replicon activity by 2.4-fold.

kod replikona genotipa 1b, pojedinačne supstitucije l31f i y93h u proteinu ns5a smanjile su antivirusnu aktivnost elbasvira 17 puta.
in genotype 1b replicons, single ns5a substitutions l31f and y93h reduced elbasvir antiviral activity by 17-fold.

podaci iz raznih sojeva replikona ns5a pune duljine ili kimeričkih replikona ns5a koji nose gene ns5a pune duljine koji sadrže polimorfizme l31 ili m31.
data from various strains of full length ns5a replicons or chimeric ns5a replicons carrying full-length ns5a genes that contain l31 or m31 polymorphisms.

kod replikona genotipa 4, pojedinačne supstitucije l30s, m31v i y93h u proteinu ns5a smanjile su antivirusnu aktivnost elbasvira od 3 do 23 puta.
in genotype 4 replicons, single ns5a substitutions l30s, m31v, and y93h reduced elbasvir antiviral activity by 3- to 23-fold.

kod replikona genotipa 4, pojedinačne supstitucije d168a/v u proteinu ns3 smanjile su antivirusnu aktivnost grazoprevira od 110 do 320 puta.
in genotype 4 replicons, single ns3 substitutions d168a/v reduced grazoprevir antiviral activity by 110- to 320-fold.

ritonavir nije imao izravan antivirusni učinak na replikaciju subgenomskih replikona hcv-a niti je njegova prisutnost utjecala na antivirusnu aktivnost paritaprevira in vitro.
ritonavir did not exhibit a direct antiviral effect on the replication of hcv subgenomic replicons, and the presence of ritonavir did not affect the in vitro antiviral activity of paritaprevir.

dodatno, rezistencija na simeprevir bila je procijenjena u testovima replikona hcv-a genotipa 1a i 1b koristeći ciljane mutante i kimerne replikone koji su nosili ns3 sekvence derivirane iz kliničkih izolata.
additionally, resistance to simeprevir was evaluated in hcv genotype 1a and 1b replicon assays using site-directed mutants and chimeric replicons carrying ns3 sequences derived from clinical isolates.

u sustavu replikona razvijenom na staničnoj kulturi, supstitucije koje su uzrokovale rezistenciju genotipova 1-4 na daklatazvir primijećene su u regiji od 100 aminokiselina na n-kraju proteina ns5a.
substitutions conferring daclatasvir resistance in genotypes 1-4 were observed in the n-terminal 100 amino acid region of ns5a in a cell-based replicon system.

in vitro odabir replikona hcv-a sa smanjenom osjetljivošću na velpatasvir proveden je u staničnoj kulturi za više genotipova uključujući 1a, 1b, 2a, 3a, 4a, 5a i 6a.
in vitro selection of hcv replicons with reduced susceptibility to velpatasvir was performed in cell culture for multiple genotypes including 1a, 1b, 2a, 3a, 4a, 5a and 6a.

aktivnost boceprevira protiv replikona hcv genotipa 1a bila je smanjena (2 do 6 puta) zbog sljedećih aminokiselinskih supstitucija u domeni ns3 proteaze: v36a/l/m, q41r, t54a/s, v55a, r155k i v158i.
the activity of boceprevir against the hcv genotype 1a replicon was reduced (2- to 6-fold) by the following amino acid substitutions in the ns3 protease domain: v36a/l/m, q41r, t54a/s, v55a, r155k and v158i.