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

Improving the interaction of Myc-interfering peptides with Myc using molecular dynamics simulations.

Journal of peptide science : an official publication of the European Peptide Society - 1 Jan 2009

Jouaux Eva M, Timm Barbara B, Arndt Katja M, Exner Thomas E

Abstract excerpt

Previously, a Myc-interfering peptide (Mip) was identified for the targeted inactivation of the Myc:Max complex by the combination of rational design and an in vivo protein-fragment complementation assay. In the subsequent work presented here, molecular dynamics simulations and free energy calcul...

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 Computer Simulation
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Peptides

Share to Protein Binding

Share to Protein Structure, Quaternary

Share to Proto-Oncogene Proteins c-myc

Source

Identifiers

PMID: 19035580
DOI: 10.1002/psc.1078

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19035580-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Improving the interaction of Myc-interfering peptides with Myc using molecular dynamics simulations.PMID 19035580Read ↗

Structural rationale for the coupled binding and unfolding of the c-Myc oncoprotein by small molecules.Semantic proximity Read ↗

A selective high affinity MYC-binding compound inhibits MYC:MAX interaction and MYC-dependent tumor cell proliferationSemantic proximity Read ↗

Development of DuoMYC: a synthetic cell penetrant miniprotein that efficiently inhibits the oncogenic transcription factor MYCSemantic proximity Read ↗

Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex.Semantic proximity Read ↗

Computer-guided design of Z domain peptides with improved inhibition of VEGFSemantic proximity Read ↗

A novel inhibitor L755507 efficiently blocks c-Myc–MAX heterodimerization and induces apoptosis in cancer cellsSemantic proximity Read ↗

Formation of a structurally-stable conformation by the intrinsically disordered MYC:TRRAP complexSemantic proximity Read ↗

Improving coiled coil stability while maintaining specificity by a bacterial hitchhiker selection system.Semantic proximity Read ↗

In vivo quantification and perturbation of Myc-Max interactions and the impact on oncogenic potentialSemantic proximity Read ↗

Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptide.Semantic proximity Read ↗

Accurate PDZ/Peptide Binding Specificity with Additive and Polarizable Free Energy Simulations.Semantic proximity Read ↗

Computational and experimental studies of the interaction between phospho-peptides and the C-terminal domain of BRCA1.Semantic proximity Read ↗

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