ArticleThe protein journal2006
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".
Article in The protein journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 35 citations in OpenAlex.
- Electrochemical detection of different p53 conformations by using nanostructured surfaces.Scientific reports · 2019Article
- Amperometric Sensor for Detection of Chloride Ions.Sensors (Basel, Switzerland) · 2008Article
- Utilizing of Adsorptive Transfer Stripping Technique Brdicka Reaction for Determination of Metallothioneins Level in Melanoma Cells, Blood Serum and Tissues.Sensors (Basel, Switzerland) · 2008Article
- An Electrochemical Detection of Metallothioneins at the Zeptomole Level in Nanolitre Volumes.Sensors (Basel, Switzerland) · 2008Article
- Lactoferrin Isolation Using Monolithic Column Coupled with Spectrometric or Micro-Amperometric Detector.Sensors (Basel, Switzerland) · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Presence of mutated and/or structurally modified (e.g., denatured, aggregated) protein p53 form is associated with several disorders such as Alzheimer's disease, Parkinson's 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 flow 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 mul injection; 3 x 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, approach of more electroactive centers - aminoacid residues - towards electrode surface) in comparison with native form. On the other hand, aggregated form offers lower response (steric eclipse of electroactive protein parts) when compared with the signal of native form. The obtained data show that we are not only able to sensitively determine native, denatured, and aggregated structural forms of p53 protein but also to distinguish them.
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