Swedish
Albanian
Arabic
Armenian
Azerbaijani
Belarusian
Bengali
Bosnian
Catalan
Czech
Danish
Deutsch
Dutch
English
Estonian
Finnish
Français
Greek
Haitian Creole
Hebrew
Hindi
Hungarian
Icelandic
Indonesian
Irish
Italian
Japanese
Korean
Latvian
Lithuanian
Macedonian
Mongolian
Norwegian
Persian
Polish
Portuguese
Romanian
Russian
Serbian
Slovak
Slovenian
Spanish
Swahili
Swedish
Turkish
Ukrainian
Vietnamese
Български
中文(简体)
中文(繁體)
Sida 1 från 36 resultat
Rubella virus nonstructural protein protease domains involved in trans- and cis-cleavage activities.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
Rubella virus (RV) genomic RNA contains two large open reading frames (ORFs): a 5'-proximal ORF encoding nonstructural proteins (NSPs) that function primarily in viral RNA replication and a 3'-proximal ORF encoding the viral structural proteins. Proteolytic processing of the RV NSP ORF translation
The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The substrate requirement for rubella virus protease trans-activity is unknown. Here, we analyzed the cleavability of RV P200-derived substrates varying in their N-terminal lengths (72-475 amino acids) from the cleavage site by the RV protease trans-activity. Only substrates with at least 309 amino
Characterization of the zinc binding activity of the rubella virus nonstructural protease.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The rubella virus (RUB) nonstructural (NS) protein (NSP) ORF encodes a protease that cleaves the NSP precursor (240 kDa) at a single site to produce two products. A cleavage site mutation was introduced into a RUB infectious cDNA clone and found to be lethal, demonstrating that cleavage of the NSP
Characterization of the rubella virus nonstructural protease domain and its cleavage site.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The region of the rubella virus nonstructural open reading frame that contains the papain-like cysteine protease domain and its cleavage site was expressed with a Sindbis virus vector. Cys-1151 has previously been shown to be required for the activity of the protease (L. D. Marr, C.-Y. Wang, and T.
A cysteine-rich metal-binding domain from rubella virus non-structural protein is essential for viral protease activity and virus replication.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The protease domain within the RUBV (rubella virus) NS (non-structural) replicase proteins functions in the self-cleavage of the polyprotein precursor into the two mature proteins which form the replication complex. This domain has previously been shown to require both zinc and calcium ions for
The rubella virus nonstructural protease requires divalent cations for activity and functions in trans.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The rubella virus (RUB) nonstructural (NS) protease is a papain-like cysteine protease (PCP) located in the NS-protein open reading frame (NSP-ORF) that cleaves the NSP-ORF translation product at a single site to produce two products, P150 (the N-terminal product) and P90 (the C-terminal product).
Protease and helicase domains are related to the temperature sensitivity of wild-type rubella viruses.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
Wild-type rubella viruses grow well at 39°C (non-temperature sensitivity: non-ts), while vaccine strains do not (temperature sensitivity: ts). Histidine at position 1042 of the p150 region of the KRT vaccine strain was found to be responsible for ts, while wild-type viruses had tyrosine at position
Identification of a Ca2+-binding domain in the rubella virus nonstructural protease.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The rubella virus (RUB) nonstructural protein (NS) open reading frame (ORF) encodes a polypeptide precursor that is proteolytically self cleaved into two replicase components involved in viral RNA replication. A putative EF-hand Ca(2+)-binding motif that was conserved across different genotypes of
Calcium-dependent association of calmodulin with the rubella virus nonstructural protease domain.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The rubella virus (RUBV) nonstructural (NS) protease domain, a Ca(2+)- and Zn(2+)-binding papain-like cysteine protease domain within the nonstructural replicase polyprotein precursor, is responsible for the self-cleavage of the precursor into two mature products, P150 and P90, that compose the
Rescue of rubella virus replication-defective mutants using vaccinia virus recombinant expressing rubella virus nonstructural proteins.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The genome of rubella virus (RV) is translated into a polyprotein precusor, p200, of the nonstructural proteins (NSPs). This is proteolytically processed by a viral-encoded protease into two mature products, p150 and p90. p150 contains sequence corresponding to the predicted methyltransferase and
Rubella virus-induced superinfection exclusion studied in cells with persisting replicons.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
For the first time, homologous superinfection exclusion was documented for rubella virus (RUB) by using Vero cells harbouring persisting RUB replicons. Infection with wild-type RUB was reduced by tenfold, whereas Sindbis virus infection was unaffected. Replication following infection with packaged
Mutational analysis of the arginine residues in the E2-E1 junction region on the proteolytic processing of the polyprotein precursor of rubella virus.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
Endoproteolytic cleavage of precursors is a key step in biosynthesis of functional proteins. The structural proteins of rubella virus are initially translated as a precursor polyprotein in the order NH2-C-E2-E1-COOH and are cleaved by host signal peptidase to yield three structural proteins. Between
Expression of the rubella virus nonstructural protein ORF and demonstration of proteolytic processing.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
To analyze the proteins produced from the rubella virus (RUB) nonstructural protein open reading frame (NSP-ORF), a DNA containing the RUB NSP-ORF was introduced into the expression vector pTM3 in which the sequences to be expressed are downstream from a T7 RNA polymerase promoter. In cells infected
Proteolytic processing of rubella virus nonstructural proteins.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
The genomic RNA of rubella virus contains two long open reading frames (ORF), a 5'-proximal ORF that codes for the nonstructural proteins and a 3'-proximal ORF that encodes the structural proteins. The cDNA encoding the nonstructural protein ORF of the wild-type M33 strain of rubella virus has been
Mapping of genetic determinants of rubella virus associated with growth in joint tissue.
Endast registrerade användare kan översätta artiklar
Logga in Bli medlem
Rubella virus (RV) strains vary in their abilities to replicate and persist in cell cultures derived from human joint tissue (synovial cells [SC]), and this arthrotropism appears to be linked to their association with joint symptoms in vivo. In order to map the genetic determinants of arthrotropism,
Den mest kompletta databasen med medicinska örter som stöds av vetenskapen
- Fungerar på 55 språk
- Växtbaserade botemedel som stöds av vetenskap
- Örter igenkänning av bild
- Interaktiv GPS-karta - märka örter på plats (kommer snart)
- Läs vetenskapliga publikationer relaterade till din sökning
- Sök efter medicinska örter efter deras effekter
- Organisera dina intressen och håll dig uppdaterad med nyheterna, kliniska prövningar och patent
Skriv ett symptom eller en sjukdom och läs om örter som kan hjälpa, skriv en ört och se sjukdomar och symtom den används mot.
* All information baseras på publicerad vetenskaplig forskning
