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

Molecular characterization of a plant FKBP12 that does not mediate action of FK506 and rapamycin.

The Plant journal : for cell and molecular biology - 1 Aug 1998

Xu Q, Liang S, Kudla J, Luan S

Abstract excerpt

Immuonosuppressive drugs FK506 and rapamycin block a number of signal transduction pathways in eukaryotic systems. The 12 kDa FK506 binding protein (FKBP12) mediates the action of both FK506 and rapamycin against their functional targets. In this report, we cloned, sequenced and characterized a gene encoding FKBP12 in Vicia faba (VfFKBP12). While VfFKBP12 is highly homologous to animal and yeast FKBP12, it does...

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 Cloning, Molecular
Share to Genetic Complementation Test

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Binding

Share to Sequence Analysis, DNA

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 9753776
DOI: 10.1046/j.1365-313x.1998.00232.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular characterization of a plant FKBP12 that does not mediate action of FK506 and rapamycin.PMID 9753776Read ↗

Characterization of the FKBP12-Encoding Genes in Aspergillus fumigatusSemantic proximity Read ↗

The rapamycin-binding domain of the protein kinase mammalian target of rapamycin is a destabilizing domain.Semantic proximity Read ↗

Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP.Semantic proximity Read ↗

FKBP12-Dependent Inhibition of Calcineurin Mediates Immunosuppressive Antifungal Drug Action in MalasseziaSemantic proximity Read ↗

FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.Semantic proximity Read ↗

FKBP12‐rapamycin target TOR2 is a vacuolar protein with an associated phosphatidylinositol‐4 kinase activity.Semantic proximity Read ↗

The human FK506-binding proteins: characterization of human FKBP19Semantic proximity Read ↗

Physiological function of FKBP12, a primary target of rapamycin/FK506: a newly identified role in transcription of ribosomal protein genes in yeastSemantic proximity Read ↗

FKBP12 dimerization mutations effect FK506 binding and differentially alter calcineurin inhibition in the human pathogen Aspergillus fumigatus.Semantic proximity Read ↗

Molecular cloning and overexpression of the human FK506-binding protein FKBPSemantic proximity Read ↗

Leveraging Fungal Calcineurin-Inhibitor Structures, Biophysics and Dynamics to Design Selective and Non-Immunosuppressive FK506 AnalogsSemantic proximity Read ↗

Rapamycin-FKBP12 blocks proliferation, induces differentiation, and inhibits cdc2 kinase activity in a myogenic cell line.Semantic proximity Read ↗

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