Mechanisms of anterior gradient-2 regulation and function in cancer

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F15%3A%230000626" target="_blank" >RIV/00209805:_____/15:#0000626 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.semcancer.2015.04.005" target="_blank" >http://dx.doi.org/10.1016/j.semcancer.2015.04.005</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.semcancer.2015.04.005" target="_blank" >10.1016/j.semcancer.2015.04.005</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Mechanisms of anterior gradient-2 regulation and function in cancer

Popis výsledku v původním jazyce

Proteins targeted to secretory pathway enter the endoplasmic reticulum where they undergo posttranslational modification and subsequent quality control executed by exquisite catalysts of protein folding, protein disulphide isomerases (PDIs). These enzymes can often provide strict conformational protein folding solutions to highly cysteine-rich cargo as they facilitate disulphide rearrangement in the endoplasmic reticulum. Under conditions when PDI substrates are not isomerised properly, secreted proteins can accumulate in the endoplasmic reticulum leading to endoplasmic reticulum stress initiation with implications for human disease development. Anterior Gradient-2 (AGR2) is an endoplasmic reticulum-resident PDI superfamily member that has emerged as adominant effector of basic biological properties in vertebrates including blastoderm formation and limb regeneration. AGR2 perturbation in mammals influences disease processes including cancer progression and drug resistance, asthma, and

Název v anglickém jazyce

Mechanisms of anterior gradient-2 regulation and function in cancer

Popis výsledku anglicky

Proteins targeted to secretory pathway enter the endoplasmic reticulum where they undergo posttranslational modification and subsequent quality control executed by exquisite catalysts of protein folding, protein disulphide isomerases (PDIs). These enzymes can often provide strict conformational protein folding solutions to highly cysteine-rich cargo as they facilitate disulphide rearrangement in the endoplasmic reticulum. Under conditions when PDI substrates are not isomerised properly, secreted proteins can accumulate in the endoplasmic reticulum leading to endoplasmic reticulum stress initiation with implications for human disease development. Anterior Gradient-2 (AGR2) is an endoplasmic reticulum-resident PDI superfamily member that has emerged as adominant effector of basic biological properties in vertebrates including blastoderm formation and limb regeneration. AGR2 perturbation in mammals influences disease processes including cancer progression and drug resistance, asthma, and

Druh

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

CEP obor

FD - Onkologie a hematologie

OECD FORD obor

—

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

Seminars in cancer biology

ISSN

1044-579X

e-ISSN

—

Svazek periodika

33

Číslo periodika v rámci svazku

August

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

16-24

Kód UT WoS článku

000359887100003

EID výsledku v databázi Scopus

2-s2.0-84938212139