Electrochemical Investigations of Tau Protein Phosphorylations and Interactions with Pin1

Martić, Sanela; Beheshti, Samaneh; Kraatz, Heinz‐Bernhard; Litchfield, David W.

doi:10.1002/cbdv.201100418

Cited by 24 publications

(12 citation statements)

References 33 publications

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“…Furthermore, most of methods attempted the detection of protein phosphorylation by measuring the addition of negative charges changes of the protein after phosphorylation or the release of protons in the reaction buffer upon phosphorylation of protein . These methods noted as mass spectroscopy, phosphor‐specific antibody, radioisotope labelling, the sensitive and selective electrochemical and optical detection methodologies, etc.…”

Section: Introductionmentioning

confidence: 99%

Multi‐iPPseEvo: A Multi‐label Classifier for Identifying Human Phosphorylated Proteins by Incorporating Evolutionary Information into Chou′s General PseAAC via Grey System Theory

Qiu

Zheng

Sun

et al. 2016

Molecular Informatics

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Predicting phosphorylation protein is a challenging problem, particularly when query proteins have multi-label features meaning that they may be phosphorylated at two or more different type amino acids. In fact, human protein usually be phosphorylated at serine, threonine and tyrosine. By introducing the "multi-label learning" approach, a novel predictor has been developed that can be used to deal with the systems containing both single- and multi-label phosphorylation protein. Here we proposed a predictor called Multi-iPPseEvo by (1) incorporating the protein sequence evolutionary information into the general pseudo amino acid composition (PseAAC) via the grey system theory, (2) balancing out the skewed training datasets by the asymmetric bootstrap approach, and (3) constructing an ensemble predictor by fusing an array of individual random forest classifiers thru a voting system. Rigorous cross-validations via a set of multi-label metrics indicate that the multi-label phosphorylation predictor is very promising and encouraging. The current approach represents a new strategy to deal with the multi-label biological problems, and the software is freely available for academic use at http://www.jci-bioinfo.cn/Multi-iPPseEvo.

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Section: Introductionmentioning

confidence: 99%

Multi‐iPPseEvo: A Multi‐label Classifier for Identifying Human Phosphorylated Proteins by Incorporating Evolutionary Information into Chou′s General PseAAC via Grey System Theory

Qiu

Zheng

Sun

et al. 2016

Molecular Informatics

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“…In this respect, kinase inhibitors are intensively investigated in drug discovery (Cohen and Alessi, 2013). Current methods for understanding kinase activity are based on mass spectroscopy (Zhang et al, 2005), electrochemical impedance spectroscopy (Martić et al, 2012a(Martić et al, , 2012b, isotope labelling technique (Stasyk and Huber, 2012), or immunoassays (Nadler et al, 2008). The above techniques are time consuming, laborious, cost inefficient or require the usage of toxic chemical reagents (e.g.…”

Section: Introductionmentioning

confidence: 99%

Protein phosphorylation analysis based on proton release detection: Potential tools for drug discovery

Bhalla

Lorenzo

Pula

et al. 2014

Biosensors and Bioelectronics

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Phosphorylation is the most important post-translational modification of proteins in eukaryotic cells and it is catalysed by enzymes called kinases. The balance between protein phosphorylation and dephosphorylation is critical for the regulation of physiological processes and its unbalance is the cause of several diseases. Conventional assays used to analyse the kinase activity are limited as they rely heavily on phospho-specific antibodies and radioactive tags. This makes their use impractical for high throughput drug discovery platforms. We have developed two versatile methods to detect the release of protons (H(+)) associated with the protein phosphorylation catalysed by kinases. The first approach is based on the pH-sensitive response of oxide-semiconductor interfaces and the second method detects the pH changes in phosphorylation reaction using a commercial micro-pH electrode. The proposed methods successfully detected phosphorylation of myelin basic protein by PKC-α kinase. These techniques can be readily adopted for multiplexed arrays and high throughput analysis of kinase activity, which will represent an important innovation in biomedical research and drug discovery.

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“…Radioisotope-labelling entails the use of expensive and hazardous reagents and is not easily available for all investigators. In recent times, some groups have described the development of sensitive and selective electrochemical 10 11 12 13 14 15 and optical detection methodologies 16 for investigating kinase activity. These methodologies offer several advantages in terms of reagent requirement, multiplexing and screening throughput, adaptability to different kinase targets, routine cost and time for the analysis.…”

mentioning

confidence: 99%

Protein phosphorylation detection using dual-mode field-effect devices and nanoplasmonic sensors

Bhalla

Lorenzo

Pula

et al. 2015

Sci Rep

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Phosphorylation by kinases is an important post-translational modification of proteins. It is a critical control for the regulation of vital cellular activities, and its dysregulation is implicated in several diseases. A common drug discovery approach involves, therefore, time-consuming screenings of large libraries of candidate compounds to identify novel inhibitors of protein kinases. In this work, we propose a novel method that combines localized surface plasmon resonance (LSPR) and electrolyte insulator semiconductor (EIS)-based proton detection for the rapid identification of novel protein kinase inhibitors. In particular, the selective detection of thiophosphorylated proteins by LSPR is achieved by changing their resonance properties via a pre-binding with gold nanoparticles. In parallel, the EIS field-effect structure allows the real-time electrochemical monitoring of the protein phosphorylation by detecting the release of protons associated with the kinases activity. This innovative combination of both field-effect and nanoplasmonic sensing makes the detection of protein phosphorylation more reliable and effective. As a result, the screening of protein kinase inhibitors becomes more rapid, sensitive, robust and cost-effective.

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Electrochemical Investigations of Tau Protein Phosphorylations and Interactions with Pin1

Cited by 24 publications

References 33 publications

Multi‐iPPseEvo: A Multi‐label Classifier for Identifying Human Phosphorylated Proteins by Incorporating Evolutionary Information into Chou′s General PseAAC via Grey System Theory

Multi‐iPPseEvo: A Multi‐label Classifier for Identifying Human Phosphorylated Proteins by Incorporating Evolutionary Information into Chou′s General PseAAC via Grey System Theory

Protein phosphorylation analysis based on proton release detection: Potential tools for drug discovery

Protein phosphorylation detection using dual-mode field-effect devices and nanoplasmonic sensors

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