About: The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation     Goto   Sponge   NotDistinct   Permalink

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Description
  • Retroviral proteases are translated as a part of Gag-related polyproteins, and are released and activated during particle release. Mason-Pfizer monkey virus (M-PMV) Gag polyproteins assemble into immature capsids within the cytoplasmof the host cells; however, their processing occurs only after transport to the plasma membrane and subsequent release. Thus, the activity of M-PMV protease is expected to be highly regulated during the replication cycle. It has been proposed that reversible oxidation of protease cysteine residues might be responsible for such regulation. We show that cysteine residues in M-PMV protease can form an intramolecular S-S bridge. The disulfide bridge shifts the monomer/dimer equilibrium in favor of the dimer, and increases the proteolytic activity significantly. To investigate the role of this disulfide bridge in virus maturation and replication, we engineered an M-PMV clone in which both protease cysteine residues were replaced by alanine (M-PMVPRC7A/C106A). Surpr
  • Retroviral proteases are translated as a part of Gag-related polyproteins, and are released and activated during particle release. Mason-Pfizer monkey virus (M-PMV) Gag polyproteins assemble into immature capsids within the cytoplasmof the host cells; however, their processing occurs only after transport to the plasma membrane and subsequent release. Thus, the activity of M-PMV protease is expected to be highly regulated during the replication cycle. It has been proposed that reversible oxidation of protease cysteine residues might be responsible for such regulation. We show that cysteine residues in M-PMV protease can form an intramolecular S-S bridge. The disulfide bridge shifts the monomer/dimer equilibrium in favor of the dimer, and increases the proteolytic activity significantly. To investigate the role of this disulfide bridge in virus maturation and replication, we engineered an M-PMV clone in which both protease cysteine residues were replaced by alanine (M-PMVPRC7A/C106A). Surpr (en)
  • Retrovirové proteasy jsou translatovány jako součást polyproteinů Retroviral proteases are translated as a part of Gag-related polyproteins, and are released and activated during particle release. Mason-Pfizer monkey virus (M-PMV) Gag polyproteins assemble into immature capsids within the cytoplasmof the host cells; however, their processing occurs only after transport to the plasma membrane and subsequent release. Thus, the activity of M-PMV protease is expected to be highly regulated during the replication cycle. It has been proposed that reversible oxidation of protease cysteine residues might be responsible for such regulation. We show that cysteine residues in M-PMV protease can form an intramolecular S-S bridge. The disulfide bridge shifts the monomer/dimer equilibrium in favor of the dimer, and increases the proteolytic activity significantly. To investigate the role of this disulfide bridge in virus maturation and replication, we engineered an M-PMV clone in which both protease c (cs)
Title
  • The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation
  • The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation (en)
  • Úloha S-S můstku v retrovirové protease a maturaci viru (cs)
skos:prefLabel
  • The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation
  • The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation (en)
  • Úloha S-S můstku v retrovirové protease a maturaci viru (cs)
skos:notation
  • RIV/60461373:22330/07:00019201!RIV08-AV0-22330___
http://linked.open.../vavai/riv/strany
  • 1493-1504
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(1M0520), P(IAA4055304), Z(MSM6046137305)
http://linked.open...iv/cisloPeriodika
  • 365
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 448239
http://linked.open...ai/riv/idVysledku
  • RIV/60461373:22330/07:00019201
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • retroviral protease; Mason-Pfizer monkey virus; disulfide; dimerization; maturation (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • BE - Belgické království
http://linked.open...ontrolniKodProRIV
  • [296DF7D2B5E0]
http://linked.open...i/riv/nazevZdroje
  • Journal of molecular biology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Pichová, Iva
  • Zábranská, Helena
  • Hrabal, Richard
  • Ruml, Tomáš
  • Svatoš, Aleš
  • Kluh, Ivan
  • Tůma, Roman
http://linked.open...n/vavai/riv/zamer
issn
  • 0022-2836
number of pages
http://localhost/t...ganizacniJednotka
  • 22330
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