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

The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons.

The Journal of biological chemistry - 27 Jan 2006

Shang Limin, Tomasi Thomas B

Abstract excerpt

Interferon signaling pathways are critical to both innate and adaptive immunity. We have demonstrated here that the inhibition of heat shock protein 90 (Hsp90) functions by small interfering RNAs or chemical inhibitors blocking interferon-induced gene expression. Hsp90 was required for signal tra...

Read the complete abstract on PubMed

Topics

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

Share to CD40 Antigens
Share to Chaperonins
Share to HSP90 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoprecipitation

Share to Interferon Type I

Share to Janus Kinase 1

Share to Janus Kinase 2

Share to Proteasome Endopeptidase Complex

Source

Identifiers

PMID: 16280321
DOI: 10.1074/jbc.M509901200

Genes

CDC37
JAK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16280321-2026-09-02.2. 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

The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons.PMID 16280321Read ↗

Role of Heat Shock Proteins (HSP70 and HSP90) in Viral InfectionSemantic proximity Read ↗

HSP90 and HSP70: Implication in Inflammation Processes and Therapeutic Approaches for Myeloproliferative NeoplasmsSemantic proximity Read ↗

Broad action of Hsp90 as a host chaperone required for viral replicationSemantic proximity Read ↗

Heat shock protein 90Semantic proximity Read ↗

Heat shock protein 90 is critical for regulation of phenotype and functional activity of human T lymphocytes and NK cells.Semantic proximity Read ↗

Heat shock protein 90 (Hsp90) inhibition targets canonical TGF-β signalling to prevent fibrosisSemantic proximity Read ↗

Facets of heat shock protein 70 show immunotherapeutic potentialSemantic proximity Read ↗

Hsp90: A New Player in DNA Repair?Semantic proximity Read ↗

Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37.Semantic proximity Read ↗

Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90Semantic proximity Read ↗

HSP70/DNAJA3 chaperone/cochaperone regulates NF-κB activity in immune responsesSemantic proximity Read ↗

An inducible heat shock protein 70 small molecule inhibitor demonstrates anti-dengue virus activity, validating Hsp70 as a host antiviral targetSemantic proximity Read ↗

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