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One-Pot Time-Induced Proteome Integral Solubility Alteration Assay for Automated and Sensitive Drug-Target Identification.
Anal Chem
December 2024
Division of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, 17177 Stockholm, Sweden.
The proteome integral solubility alteration (PISA) assay is widely used for identifying drug targets, but it is labor-intensive and time-consuming and requires a substantial amount of biological sample. Aiming at enabling automation and greatly reducing the sample amount, we developed one-pot time-induced (OPTI)-PISA. Here, we demonstrate OPTI-PISA performance on identifying targets of multiple drugs in cell lysate and scaling down the sample amount to sub-microgram levels, making the PISA method suitable for NanoProteomics.
View Article and Find Full Text PDFIonic liquid-assisted sample preparation mediates sensitive proteomic analysis of Bacillus subtilis spores.
Sci Rep
July 2024
Faculty of Pharmaceutical Science, Setsunan University, Osaka, 573-0101, Japan.
Endospore-forming bacteria are ubiquitous. Bacterial endospores are multilayered proteinaceous structures that protects the bacterial genome during stress conditions. They are also responsible for a wide range of critical clinical infections in humans.
View Article and Find Full Text PDFIntegrated MICROFASP Method with CZE-Based Fractionation Technique and NanoRPLC-ESI-MS/MS for a Comprehensive Proteomics Analysis of a Submicrogram Sample.
J Proteome Res
August 2024
Institute of Drug Discovery Technology, Ningbo University, Ningbo, Zhejiang 315211, China.
Article Synopsis
- A new two-dimensional (2D) separation platform combines capillary zone electrophoresis (CZE) and nanoRPLC-ESI-MS/MS for advanced proteomics analysis using very small sample sizes.
- This method allows for extensive protein coverage by directly collecting peptide fractions, which minimizes sample loss and contamination, leading to identification of thousands of unique peptides and protein groups.
- The platform successfully analyzed protein digests from the MICROFASP method, revealing a high level of proteome profiling efficiency with just 200 ng of starting material.
An Optimized Miniaturized Filter-Aided Sample Preparation Method for Sensitive Cross-Linking Mass Spectrometry Analysis of Microscale Samples.
Anal Chem
July 2024
Institute of Drug Discovery Technology, Ningbo University, Ningbo, Zhejiang 315211, China.
Article Synopsis
- Cross-linking mass spectrometry (XL-MS) is an important technique for studying protein structures and their interactions, but analyzing low-abundance samples can result in sample loss during preparation.
- The study introduces an optimized method called O-MICROFASP that enhances XL-MS analysis for tiny samples, significantly increasing the identification of cross-linked peptides from minimal amounts of protein.
- By using various cross-linkers and an advanced sample preparation technique, researchers identified over 2700 unique cross-linked peptides from just 5 μg of HeLa cell lysates, confirming the method's effectiveness for detailed protein analysis and interaction mapping.
An ionic liquid-assisted sample preparation method for sensitive integral-membrane proteome analysis.
Anal Biochem
December 2023
Department of Applied Chemistry, National Defense Academy, Yokosuka, 239-8686, Japan. Electronic address:
Many ion channels and receptor proteins are potential targets for new drugs. However, standard methods for profiling these integral membrane proteins (IMPs) have not been fully established, especially when applied to rare and quantity-limited biological samples. We previously demonstrated that a mixture containing 1-butyl-3-methylimidazolium cyanate, an ionic liquid (IL), and NaOH (termed i-soln) is an excellent solubilizer for insoluble aggregates.
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