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

Design of drug-resistant alleles of type-III phosphatidylinositol 4-kinases using mutagenesis and molecular modeling.

Biochemistry - 12 Feb 2008

Balla Andras, Tuymetova Galina, Toth Balazs, Szentpetery Zsofia, Zhao Xiaohang, Knight Zachary A, Shokat Kevan, Steinbach Peter J, Balla Tamas

Abstract excerpt

Molecular modeling and site directed mutagenesis were used to analyze the structural features determining the unique inhibitor sensitivities of type-III phosphatidylinositol 4-kinase enzymes (PI4Ks). Mutation of a highly conserved Tyr residue that provides the bottom of the hydrophobic pocket for...

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 Androstadienes
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Share to Wortmannin

Source

Identifiers

PMID: 18205404
DOI: 10.1021/bi7017927

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18205404-2026-09-02.2. 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

Design of drug-resistant alleles of type-III phosphatidylinositol 4-kinases using mutagenesis and molecular modeling.PMID 18205404Read ↗

Somatic mutations in PI3Kα: Structural basis for enzyme activation and drug designSemantic proximity Read ↗

Analysis of the catalytic domain of phosphatidylinositol 4-kinase type II.Semantic proximity Read ↗

Stereo-specific substrate recognition by phosphatidylinositol phosphate kinases is swapped by changing a single amino acid residue.Semantic proximity Read ↗

Targeting the gatekeeper residue in phosphoinositide 3-kinases.Semantic proximity Read ↗

Structural comparisons of class I phosphoinositide 3-kinases.Semantic proximity Read ↗

Capitalizing on tumor genotyping: towards the design of mutation specific inhibitors of phosphoinsitide-3-kinase.Semantic proximity Read ↗

Discovery of drug-resistant and drug-sensitizing mutations in the oncogenic PI3K isoform p110 alpha.Semantic proximity Read ↗

Drug-resistant phosphatidylinositol 3-kinase: guidance for the preemptive strike.Semantic proximity Read ↗

Regulation of class IA PI3Ks.Semantic proximity Read ↗

Mutations in the inter-SH2 domain of the regulatory subunit of phosphoinositide 3-kinase: effects on catalytic subunit binding and holoenzyme function.Semantic proximity Read ↗

Mutant rat phosphatidylinositol/phosphatidylcholine transfer proteins specifically defective in phosphatidylinositol transfer: implications for the regulation of phospholipid transfer activity.Semantic proximity Read ↗

Functional analysis of mutations in the PIS gene, which encodes Saccharomyces cerevisiae phosphatidylinositol synthase.Semantic proximity Read ↗

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