Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

High-throughput interrogation of ligand binding mode using a fluorescence-based assay.

Angewandte Chemie (International ed. in English) - 27 Jul 2012

Śledź Paweł, Lang Steffen, Stubbs Christopher J, Abell Chris

Abstract excerpt

Probing the pocket: A high-throughput fluorescence-based thermal shift (FTS) assay utilized different forms of a protein (in gray) to establish the binding mode of a ligand (see picture). The assay serves in the rapid evaluation of structure-activity binding-mode relationships for a series of ligands of Plk1, an important target of anticancer therapy.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Calorimetry
Share to Fluorescence
Share to High-Throughput Screening Assays

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Molecular Structure

Share to Proteins

Share to Structure-Activity Relationship

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 22730171
DOI: 10.1002/anie.201202660
PMCID: PMC3556687

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

High-throughput interrogation of ligand binding mode using a fluorescence-based assay.PMID 22730171Read ↗

Allosteric activation of the protein kinase PDK1 with low molecular weight compounds.Semantic proximity Read ↗

Investigating protein-ligand interactions with a mutant FKBP possessing a designed specificity pocket.Semantic proximity Read ↗

FLiK: a direct-binding assay for the identification and kinetic characterization of stabilizers of inactive kinase conformations.Semantic proximity Read ↗

Structural studies of a hyperthermophilic thymidylate kinase enzyme reveal conformational substates along the reaction coordinate.Semantic proximity Read ↗

An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering.Semantic proximity Read ↗

DFG-1 Residue Controls Inhibitor Binding Mode and Affinity, Providing a Basis for Rational Design of Kinase Inhibitor Selectivity.Semantic proximity Read ↗

Structural changes induced by ligand binding drastically increase the thermostability of the Ser/Thr protein kinase TpkD from Thermus thermophilus HB8.Semantic proximity Read ↗

HTRF Kinase Assay Development and Methods in Inhibitor Characterization.Semantic proximity Read ↗

Discovery and optimization of 1,3,5-trisubstituted pyrazolines as potent and highly selective allosteric inhibitors of protein kinase C-ζ.Semantic proximity Read ↗

Fragment-Based Discovery of a Qualified Hit Targeting the Latency-Associated Nuclear Antigen of the Oncogenic Kaposi’s Sarcoma-Associated Herpesvirus/Human Herpesvirus 8Semantic proximity Read ↗

Evaluating the Therapeutic Viability of Bacterially Expressed Human TLK1B-Kinase Domain for Cancer Drug DesignSemantic proximity Read ↗

Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.