ArticleMethods in molecular biology (Clifton, N.J.)2019
Use of Microscale Thermophoresis (MST) to Measure Binding Affinities of Components of the Fusion Machinery.
Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
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- Measuring Interactions Between Proteins and Small Molecules or Nucleic Acids.Current protocols · 2024Review
- Hepatic COX1 loss leads to impaired autophagic flux and exacerbates nonalcoholic steatohepatitis.Acta pharmaceutica Sinica. B · 2023Article
- Structural basis for TRIM72 oligomerization during membrane damage repair.Nature communications · 2023Article
- SAR insights into TET2 catalytic domain inhibition: Synthesis of 2-Hydroxy-4-Methylene-pentanedicarboxylates.Bioorganic & medicinal chemistry · 2021Article
- A Therapeutic Strategy for Preferential Targeting of TET2 Mutant and TET-dioxygenase Deficient Cells in Myeloid Neoplasms.Blood cancer discovery · 2021Article
- An Allosteric Binding Site on Sortilin Regulates the Trafficking of VLDL, PCSK9, and LDLR in Hepatocytes.Biochemistry · 2020Article
- A novel anti-platelet aggregation target of chinensinaphthol methyl ether and neojusticin B obtained from Rostellularia procumbens (L.) Nees.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- A small-molecule competitive inhibitor of phosphatidic acid binding by the AAA+ protein NSF/Sec18 blocks the SNARE-priming stage of vacuole fusion.The Journal of biological chemistry · 2019Article
- Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming.The Journal of biological chemistry · 2019Article
- A Novel Antiplatelet Aggregation Target of Justicidin B Obtained FromFrontiers in pharmacology · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Microscale thermophoresis is a relatively new technique used by an increasing number of academic laboratories to estimate relative binding affinities between ligand (analyte) that is titrated and a target (generally protein) that is either fluorescently labeled exogenously in the red or blue channel (labeled thermophoresis) or endogenously labeled via the presence of sufficient aromatic amino acid residues such as tryptophan (label-free thermophoresis). There are advantages and disadvantages to each technique; however, one major disadvantage of label-free thermophoresis is that protein-protein interactions cannot be measured, as generally most proteins have enough aromatic residues to generate an interfering signal. Thermophoresis can be used to determine steady-state binding affinities as between SNAREs and relevant binding partners of SNAREs and labeled thermophoresis is increasingly becoming a reliable technique to screen binding partners of fusion machinery to determine relevance in terms of direct biochemical interactions.
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