Změna elektrochemického signálu proteinu P53 podle jeho strukturní formy - rychlé a citlivé rozlišení nativní, denaturované a agregované formy -Strážce genomu.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F06%3A00015697" target="_blank" >RIV/00216224:14310/06:00015697 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/62156489:43210/06:00103383 RIV/00216208:11130/06:471

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the "Guardian of the Genome"

Popis výsledku v původním jazyce

Presence of mutated and/or structurally modi.ed (e.g., denatured, aggregated) protein p53 form is associated with several disorders such as Alzheimers disease, Parkinsons disease, prion diseases, and many types of tumours. The aim of this work was to distinguish native, denatured and aggregated form of full-length p53 by .ow injection analysis coupled with electrochemical detector (FIA-ED). Firstly FIA-ED method used for protein native form determination was optimized (detection limit 45.8 amol per 5 llinjection; 3_S/N). In addition the technique was applied to identify p53 structural forms (denatured and aggregated). It was found out that denatured form provides about three times higher electrochemical response (protein structure unfolding, approachof more electroactive centers - aminoacid residues - towards electrode surface) in comparison with native form. On the other hand, aggregated form o.ers lower response (steric eclipse of electroactive protein parts) when compared with the

Název v anglickém jazyce

Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the "Guardian of the Genome"

Popis výsledku anglicky

Presence of mutated and/or structurally modi.ed (e.g., denatured, aggregated) protein p53 form is associated with several disorders such as Alzheimers disease, Parkinsons disease, prion diseases, and many types of tumours. The aim of this work was to distinguish native, denatured and aggregated form of full-length p53 by .ow injection analysis coupled with electrochemical detector (FIA-ED). Firstly FIA-ED method used for protein native form determination was optimized (detection limit 45.8 amol per 5 llinjection; 3_S/N). In addition the technique was applied to identify p53 structural forms (denatured and aggregated). It was found out that denatured form provides about three times higher electrochemical response (protein structure unfolding, approachof more electroactive centers - aminoacid residues - towards electrode surface) in comparison with native form. On the other hand, aggregated form o.ers lower response (steric eclipse of electroactive protein parts) when compared with the

Druh

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

CEP obor

CG - Elektrochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GP525%2F04%2FP132" target="_blank" >GP525/04/P132: Studium obranných mechanismů rostlin při stresu způsobeném těžkými kovy</a><br>

Návaznosti

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

Rok uplatnění

2006

Kód důvěrnosti údajů

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

Název periodika

The Protein Journal

ISSN

1572-3887

e-ISSN

—

Svazek periodika

25

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

10

Strana od-do

23-32

Kód UT WoS článku

—

EID výsledku v databázi Scopus

—