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| Description
| - Mason-Pfizer monkey virus (M-PMV) capsids that have assembled in the cytoplasm must be transported to and associate with the plasma membrane prior to being enveloped by a lipid bilayer during viral release. Structural studies have identified a positive-charge density on the membrane-proximal surface of the matrix (MA) protein component of the Gag polyprotein. To investigate if basic amino acids in MA play a role in intracellular transport and capsid-membrane interactions, mutants were constructed in which lysine and arginine residues (R10, K16, K20, R22, K25, K27, K33, and K39) potentially exposed on the capsid surface were replaced singly and in pairs by alanine. A majority of the charge substitution mutants were released less efficiently than the wild type. Electron microscopy of mutant Gag-expressing cells revealed four distinct phenotypes: K16A and K20A immature capsids accumulated on and budded into intracellular vesicles; R10A, K27A, and R22A capsid transport was arrested at the cellula
- Mason-Pfizer monkey virus (M-PMV) capsids that have assembled in the cytoplasm must be transported to and associate with the plasma membrane prior to being enveloped by a lipid bilayer during viral release. Structural studies have identified a positive-charge density on the membrane-proximal surface of the matrix (MA) protein component of the Gag polyprotein. To investigate if basic amino acids in MA play a role in intracellular transport and capsid-membrane interactions, mutants were constructed in which lysine and arginine residues (R10, K16, K20, R22, K25, K27, K33, and K39) potentially exposed on the capsid surface were replaced singly and in pairs by alanine. A majority of the charge substitution mutants were released less efficiently than the wild type. Electron microscopy of mutant Gag-expressing cells revealed four distinct phenotypes: K16A and K20A immature capsids accumulated on and budded into intracellular vesicles; R10A, K27A, and R22A capsid transport was arrested at the cellula (en)
- Kapsidy Mason-Pfizerova opičího viru (M-PMV), které byly složeny v cytoplasmě musí být transportovány k a asociovány s plasmatickou membránou buňky před získáním fosfolipidového obalu během uvolňování. Strukturní studie identifikovali pozitivní náboj na povrchu matrixové domény polyproteinu Gag v blízkosti membrány. Pro zjištění role bazických aminokyselin v intracelulárním transportu a interakci virové kapsidy s membránou byly zkonstruovány mutanty, ve kterých byly lysiny a argininy (R10, K16, K20, R22, K25, K27, K33 a K39)vyskytující se potencionálně na povrchu molekuly nahrazeny po jednom nebo v párch alaninem. Většina mutantů se změněným nábojem byly uvolňovány méně účinně než divoký typ viru. Elektronmikroskopické snímky buněk exprimujících polyprotein Gag se zmíněnými mutacemi vykazovali čtyri různé fenotypy: K16A a K20A nezralé kapsidy se hromadily na a pučely do intracelulárních váčků; R10A, K27A, a R22A transport kapsid byl zastaven na buněčných aktinových vláknech, zatímco nezralé kapsidy K (cs)
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| Title
| - Basic Residues in the Mason-Pfizer Monkey Virus Gag Matrix Domain Regulate Intracellular Trafficking and Capsid-Membrane Interactions
- Basic Residues in the Mason-Pfizer Monkey Virus Gag Matrix Domain Regulate Intracellular Trafficking and Capsid-Membrane Interactions (en)
- Bazické aminokyseliny matrixové domény polyproteinu Gag Mason-Pfizerova opičího viru regulují intracelulární transport a interakci virové kapsidy s cytoplasmatickou membránou (cs)
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| skos:prefLabel
| - Basic Residues in the Mason-Pfizer Monkey Virus Gag Matrix Domain Regulate Intracellular Trafficking and Capsid-Membrane Interactions
- Basic Residues in the Mason-Pfizer Monkey Virus Gag Matrix Domain Regulate Intracellular Trafficking and Capsid-Membrane Interactions (en)
- Bazické aminokyseliny matrixové domény polyproteinu Gag Mason-Pfizerova opičího viru regulují intracelulární transport a interakci virové kapsidy s cytoplasmatickou membránou (cs)
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| skos:notation
| - RIV/60461373:22330/07:00019200!RIV08-MSM-22330___
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/60461373:22330/07:00019200
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - Mason-Pfizer monkey virus; matrix; basic residues; intracellular trafficking; Capsid-Membrane Interactions (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| |
| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
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| http://linked.open...UplatneniVysledku
| |
| http://linked.open...iv/tvurceVysledku
| - Diehl, William
- Haubová, Šárka
- Hunter, Eric
- Stansell, Elizabeth
- Apkarian, Robert
- Tytler, Ewan
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| http://linked.open...n/vavai/riv/zamer
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| issn
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| number of pages
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| http://localhost/t...ganizacniJednotka
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