Discover Community Create You

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

Exploiting Transient Protein States for the Design of Small-Molecule Stabilizers of Mutant p53.

Structure (London, England : 1993) - 1 Dec 2015

Joerger Andreas C, Bauer Matthias R, Wilcken Rainer, Baud Matthias G J, Harbrecht Hannes, Exner Thomas E, Boeckler Frank M, Spencer John, Fersht Alan R

Abstract excerpt

The destabilizing p53 cancer mutation Y220C creates an extended crevice on the surface of the protein that can be targeted by small-molecule stabilizers. Here, we identify different classes of small molecules that bind to this crevice and determine their binding modes by X-ray crystallography. These structures reveal two major conformational states of the pocket and a cryptic, transiently open hydrophobic...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Antineoplastic Agents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Molecular Dynamics Simulation

Share to Molecular Sequence Data

Share to Protein Binding

Share to Protein Stability

Share to Tumor Suppressor Protein p53

Source

Open in PubMed Open full text

Identifiers

PMID: 26636255
DOI: 10.1016/j.str.2015.10.016
PMCID: PMC4671956

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploiting Transient Protein States for the Design of Small-Molecule Stabilizers of Mutant p53.PMID 26636255Read ↗

Toward the rational design of p53-stabilizing drugs: probing the surface of the oncogenic Y220C mutant.Semantic proximity Read ↗

Harnessing Fluorine-Sulfur Contacts and Multipolar Interactions for the Design of p53 Mutant Y220C Rescue Drugs.Semantic proximity Read ↗

Targeting Cavity-Creating p53 Cancer Mutations with Small-Molecule Stabilizers: the Y220X Paradigm.Semantic proximity Read ↗

An in silico algorithm for identifying stabilizing pockets in proteins: test case, the Y220C mutant of the p53 tumor suppressor protein.Semantic proximity Read ↗

Discovery of Nanomolar-Affinity Pharmacological Chaperones Stabilizing the Oncogenic p53 Mutant Y220CSemantic proximity Read ↗

A Structure-Guided Molecular Chaperone Approach for Restoring the Transcriptional Activity of the p53 Cancer Mutant Y220CSemantic proximity Read ↗

Small molecule induced reactivation of mutant p53 in cancer cells.Semantic proximity Read ↗

Markov State Models and NMR Uncover an Overlooked Allosteric Loop in p53Semantic proximity Read ↗

Targeting the p53 cancer mutants Y220C, Y220N, and Y220S with the small-molecule stabilizer rezatapopt.Semantic proximity Read ↗

Towards In Situ Dynamics of DNA-bound Full-Length p53 TetramerSemantic proximity Read ↗

Structural basis of p53 inactivation by cavity-creating cancer mutations and its implications for the development of mutant p53 reactivators.Semantic proximity Read ↗

Targeted rescue of a destabilized mutant of p53 by an in silico screened drug.Semantic proximity Read ↗

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