Exploring affinity chromatography in proteomics: A comprehensive review

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F24%3A00599846" target="_blank" >RIV/61389030:_____/24:00599846 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/24:73627372

Výsledek na webu

<a href="https://doi.org/10.1016/j.aca.2024.342513" target="_blank" >https://doi.org/10.1016/j.aca.2024.342513</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.aca.2024.342513" target="_blank" >10.1016/j.aca.2024.342513</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Exploring affinity chromatography in proteomics: A comprehensive review

Popis výsledku v původním jazyce

Over the past decades, the proteomics field has undergone rapid growth. Progress in mass spectrometry and bioinformatics, together with separation methods, has brought many innovative approaches to the study of the molecular biology of the cell. The potential of affinity chromatography was recognized immediately after its first application in proteomics, and since that time, it has become one of the cornerstones of many proteomic protocols. Indeed, this chromatographic technique exploiting the specific binding between two molecules has been employed for numerous purposes, from selective removal of interfering (over)abundant proteins or enrichment of scarce biomarkers in complex biological samples to mapping the post-translational modifications and protein interactions with other proteins, nucleic acids or biologically active small molecules. This review presents a comprehensive survey of this versatile analytical tool in current proteomics. To navigate the reader, the haphazard space of affinity separations is classified according to the experiment's aims and the separated molecule's nature. Different types of available ligands and experimental strategies are discussed in further detail for each of the mentioned procedures.

Název v anglickém jazyce

Exploring affinity chromatography in proteomics: A comprehensive review

Popis výsledku anglicky

Over the past decades, the proteomics field has undergone rapid growth. Progress in mass spectrometry and bioinformatics, together with separation methods, has brought many innovative approaches to the study of the molecular biology of the cell. The potential of affinity chromatography was recognized immediately after its first application in proteomics, and since that time, it has become one of the cornerstones of many proteomic protocols. Indeed, this chromatographic technique exploiting the specific binding between two molecules has been employed for numerous purposes, from selective removal of interfering (over)abundant proteins or enrichment of scarce biomarkers in complex biological samples to mapping the post-translational modifications and protein interactions with other proteins, nucleic acids or biologically active small molecules. This review presents a comprehensive survey of this versatile analytical tool in current proteomics. To navigate the reader, the haphazard space of affinity separations is classified according to the experiment's aims and the separated molecule's nature. Different types of available ligands and experimental strategies are discussed in further detail for each of the mentioned procedures.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

<a href="/cs/project/LO1204" target="_blank" >LO1204: Udržitelný rozvoj výzkumu v Centru regionu Haná</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

Analytica Chimica Acta

ISSN

0003-2670

e-ISSN

1873-4324

Svazek periodika

1306

Číslo periodika v rámci svazku

JUN 1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

23

Strana od-do

342513

Kód UT WoS článku

001236188000001

EID výsledku v databázi Scopus

2-s2.0-85189076424