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

Targeting subcellular localization through the polo-box domain: non-ATP competitive inhibitors recapitulate a PLK1 phenotype.

Molecular cancer therapeutics - 1 Aug 2012

McInnes Campbell, Estes Kara, Baxter Merissa, Yang Zhengguan, Farag Doaa Boshra, Johnston Paul, Lazo John S, Wang Jianjun, Wyatt Michael D

Abstract excerpt

The polo-box domain (PBD) has critical roles in the mitotic functions of polo-like kinase 1 (PLK1). The replacement with partial ligand alternative through computational enrichment (REPLACE) strategy to develop inhibitors of protein-protein interactions has identified alternatives for the N-terminal tripeptide of a Cdc25C substrate. In addition, a peptide structure-activity relationship described key determinants...

Read the complete abstract on PubMed

Topics

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

Share to cdc25 Phosphatases
Share to HeLa Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Intracellular Space

Share to Mitosis

Share to Molecular Docking Simulation

Share to Peptides

Share to Polo-Like Kinase 1

Share to Protein Interaction Domains and Motifs

Source

Open in PubMed Open full text

Identifiers

PMID: 22848093
DOI: 10.1158/1535-7163.MCT-12-0006-T
PMCID: PMC3711794

Genes

PLK1
PLK3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeting subcellular localization through the polo-box domain: non-ATP competitive inhibitors recapitulate a PLK1 phenotype.PMID 22848093Read ↗

Modulating Protein-Protein Interactions of the Mitotic Polo-like Kinases to Target Mutant KRAS.Semantic proximity Read ↗

A coupled chemical-genetic and bioinformatic approach to Polo-like kinase pathway exploration.Semantic proximity Read ↗

Polo-like kinase inhibitors: an emerging opportunity for cancer therapeuticsSemantic proximity Read ↗

Enabling and Disabling Polo-like Kinase 1 Inhibition through Chemical GeneticsSemantic proximity Read ↗

Polo-like Kinase 1 as an emerging drug target: structure, function and therapeutic implicationsSemantic proximity Read ↗

PLK-1 Targeted Inhibitors and Their Potential against TumorigenesisSemantic proximity Read ↗

Polo-Like Kinase (PLK) Inhibitors in Preclinical and Early Clinical Development in OncologySemantic proximity Read ↗

Selective blockade of cancer cell proliferation and anchorage-independent growth by Plk1 activity-dependent suicidal inhibition of its polo-box domain.Semantic proximity Read ↗

Current progress and future perspectives in the development of anti-polo-like kinase 1 therapeutic agentsSemantic proximity Read ↗

Design and synthesis of 2-amino-pyrazolopyridines as Polo-like kinase 1 inhibitors.Semantic proximity Read ↗

A review of Plks: Thinking outside the (polo) boxSemantic proximity Read ↗

Probing cell-division phenotype space and Polo-like kinase function using small molecules.Semantic proximity Read ↗

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