Retroviral proteases and their roles in virion maturation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10314895" target="_blank" >RIV/00216208:11310/15:10314895 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/15:00444846

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.virol.2015.03.021" target="_blank" >http://dx.doi.org/10.1016/j.virol.2015.03.021</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.virol.2015.03.021" target="_blank" >10.1016/j.virol.2015.03.021</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Retroviral proteases and their roles in virion maturation

Popis výsledku v původním jazyce

Proteolytic processing of viral polyproteins is essential for retrovirus infectivity. Retroviral proteases (PR) become activated during or after assembly of the immature, non-infectious virion. They cleave viral polyproteins at specific sites, inducing major structural rearrangements termed maturation. Maturation converts retroviral enzymes into their functional form, transforms the immature shell into a metastable state primed for early replication events, and enhances viral entry competence. Not onlycleavage at all PR recognition sites, but also an ordered sequence of cleavages is crucial. Proteolysis is tightly regulated, but the triggering mechanisms and kinetics and pathway of morphological transitions remain enigmatic. Here, we outline PR structures and substrate specificities focusing on HIV PR as a therapeutic target. We discuss design and clinical success of HIV PR inhibitors, as well as resistance development towards these drugs. Finally, we summarize data elucidating the ro

Název v anglickém jazyce

Retroviral proteases and their roles in virion maturation

Popis výsledku anglicky

Proteolytic processing of viral polyproteins is essential for retrovirus infectivity. Retroviral proteases (PR) become activated during or after assembly of the immature, non-infectious virion. They cleave viral polyproteins at specific sites, inducing major structural rearrangements termed maturation. Maturation converts retroviral enzymes into their functional form, transforms the immature shell into a metastable state primed for early replication events, and enhances viral entry competence. Not onlycleavage at all PR recognition sites, but also an ordered sequence of cleavages is crucial. Proteolysis is tightly regulated, but the triggering mechanisms and kinetics and pathway of morphological transitions remain enigmatic. Here, we outline PR structures and substrate specificities focusing on HIV PR as a therapeutic target. We discuss design and clinical success of HIV PR inhibitors, as well as resistance development towards these drugs. Finally, we summarize data elucidating the ro

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Virology

ISSN

0042-6822

e-ISSN

—

Svazek periodika

479

Číslo periodika v rámci svazku

May 2015

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

15

Strana od-do

403-417

Kód UT WoS článku

000354909500036

EID výsledku v databázi Scopus

2-s2.0-84937511797