Results 171 to 180 of about 665 (203)

STAT Protein Thermal Shift Assays to Monitor Protein‐Inhibitor Interactions

ChemBioChem, 2022
AbstractSTAT3 protein is a sought‐after drug target as it plays a key role in the progression of cancer. Many STAT3 inhibitors (STAT3i) have been reported, but accumulating evidence suggests many of these act as off‐target/indirect inhibitors of STAT signaling. Herein, we describe the STAT protein thermal shift assay (PTSA) as a novel target engagement
Petar Iliev, Danielle Hanke, Brent D. G. Page   +2 more
openaire   +2 more sources

Thermal shift assay for evaluation of transthyretin stability in plasma

Amyloid, 2017
Hereditary (familial) amyloid neuropathy (FAP) is a disease caused by amyloid predominately formed by the accumulation of mutated transthyretin (TTR), mostly in peripheral nerves of patients [1].
Lutz, Fleischhauer, Christoph, Niemietz, Sara, Reinartz Groba, Paula, Ballmaier, Vanessa, Sauer, Sarah, Guttmann, Andree, Zibert, Hartmut, Schmidt   +7 more
openaire   +2 more sources

Determination of Protein–Ligand Binding Affinities by Thermal Shift Assay

ACS Pharmacology and Translational Science
Quantification of protein-ligand interactions is crucial for understanding the protein's biological function and for drug discovery. In this study, we employed three distinct approaches for determination of protein-ligand binding affinities by a thermal shift assay using a single ligand concentration.
Karen Ottemann, Anna Roujeinikova, Brian Smith   +2 more
exaly   +4 more sources

The cellular thermal shift assay for evaluating drug target interactions in cells

Nature Protocols, 2014
Thermal shift assays are used to study thermal stabilization of proteins upon ligand binding. Such assays have been used extensively on purified proteins in the drug discovery industry and in academia to detect interactions. Recently, we published a proof-of-principle study describing the implementation of thermal shift assays in a cellular format ...
Jafari R, Almqvist H, Axelsson H, Ignatushchenko M, Lundbäck T, Nordlund P, Molina DM   +6 more
openaire   +4 more sources

Thermal Shift Assay for Characterizing the Stability of RNA Helicases and Their Interaction with Ligands

2020
Thermofluor or thermal shift assay is an easily implementable, high-throughput method for assessing the thermostability of proteins and the influence of various ligands on that stability. It is particularly useful for the assaying of ligands that may stabilize oligomeric helicases, which rely on both substrates (oligonucleotides) and nucleotide ...
Emmanuel, Saridakis, Franck, Coste
openaire   +2 more sources

Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery

Analytical Biochemistry, 2004
The fluorescence-based thermal shift assay is a general method for identification of inhibitors of target proteins from compound libraries. Using an environmentally sensitive fluorescent dye to monitor protein thermal unfolding, the ligand-binding affinity can be assessed from the shift of the unfolding temperature (Delta Tm) obtained in the presence ...
Rebecca Cowling, Ann Aulabaugh
exaly   +3 more sources

Characterization of Ligand Binding to Pseudokinases Using a Thermal Shift Assay

2017
The protocol herein describes a robust and proven method for the measurement of pseudokinase-ligand interaction using a fluorescence-based thermal shift assay (TSA). Pseudokinases are kinase-like proteins that have recently emerged as crucial regulatory modules of signal transduction pathways and may well represent a novel class of drug targets ...
Isabelle S, Lucet, James M, Murphy
openaire   +2 more sources

Screening of Buffers and Additives for Protein Stabilization by Thermal Shift Assay: A Practical Approach

2023
Thermal shift assay (TSA), also commonly designed by differential scanning fluorimetry (DSF) or ThermoFluor, is a technique relatively easy to implement and perform, useful in a myriad of applications. In addition to versatility, it is also rather inexpensive, making it suitable for high-throughput approaches.
Filipa S S, Engrola, João, Paquete-Ferreira, Teresa, Santos-Silva, Márcia A S, Correia, Francisco, Leisico, Marino F A, Santos   +5 more
openaire   +2 more sources

Matrix Thermal Shift Assay for Fast Construction of Multidimensional Ligand–Target Space

Analytical Chemistry, 2022
Existing thermal shift-based mass spectrometry approaches are able to identify target proteins without chemical modification of the ligand, but they are suffering from complicated workflows with limited throughput. Herein, we present a new thermal shift-based method, termed matrix thermal shift assay (mTSA), for fast deconvolution of ligand-binding ...
Chengfei Ruan, Yan Wang, Xiaolei Zhang, Jiawen Lyu, Na Zhang, Yanni Ma, Chunzhen Shi, Guangbo Qu, Mingliang Ye   +8 more
openaire   +2 more sources

Assessing compound binding to the Eg5 motor domain using a thermal shift assay

Analytical Biochemistry, 2009
Eg5 is a kinesin whose inhibition leads to cycle arrest during mitosis, making it a potential therapeutic target in cancers. Circular dichroism and isothermal titration calorimetry of our pyrrolotriazine-4-one series of inhibitors with Eg5 motor domain revealed enhanced binding in the presence of adenosine 5'-diphosphate (ADP).
Kyoung Min Kim, Robert Borzilleri, Louis Lombardo   +2 more
exaly   +3 more sources