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Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.

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Structure2018PMID 29478821PMC5846801stubpubmedProvenance
Source
PubMed
Retrieved
Sep 8, 2026
Layer
normalized (units and labels harmonized; values unchanged)
Run
ING-CIVIC-20260908-000001
Published

Abstract

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Linked entities

Linked entities (2)

How each link was made (MeSH, dictionary, registry reference, curation…) and whether it has been validated. Candidate links are not counted in entity statistics.

Validated 2

Curated evidence

Evidence citing this paper (4)

civicProvenance
Source
CIViC — Clinical Interpretation of Variants in Cancer
Dataset
CIViC evidence items
Version
civic-2026-09-08
Retrieved
Sep 8, 2026
Layer
normalized (units and labels harmonized; values unchanged)
Evidence
expert curation
License
CC0 1.0
PMID
29478821
Run
ING-CIVIC-20260908-000001
Open at source
CuratedShowing 1–4 of 4 evidence items · levels, directions and significance as curated at the source; each row links to its CIViC record.
TherapyCancerTypeLevelDirection · significanceRating (1–5)StatusEvidenceSource
FGFR3 E466K1
(functional)—UNRESOLVEDFunctionalDSupports Gain Of Function3submitted
EID10390

Protein co-chaperone Cdc37 is required in FGFR3 remodeling for recognition by chaperone protein Hsp90. Cdc37 must partially deactivate the kinase and present it in a particular orientation to Hsp90. S… (full text at CIViC)

PMID 29478821 · Bunney et al., 2018 · Open in CIViC

civic
FGFR3 I538F1
(functional)—UNRESOLVEDFunctionalDSupports Gain Of Function3submitted
EID10388

Protein co-chaperone Cdc37 is required in FGFR3 remodeling for recognition by chaperone protein Hsp90. Cdc37 must partially deactivate the kinase and present it in a particular orientation to Hsp90. … (full text at CIViC)

PMID 29478821 · Bunney et al., 2018 · Open in CIViC

civic
FGFR3 K650E1
(functional)—UNRESOLVEDFunctionalDSupports Unaltered Function2submitted
EID10391

Protein co-chaperone Cdc37 is required in FGFR3 remodeling for recognition by chaperone protein Hsp90. Cdc37 must partially deactivate the kinase and present it in a particular orientation to Hsp90. A… (full text at CIViC)

PMID 29478821 · Bunney et al., 2018 · Open in CIViC

civic
FGFR3 N540K1
(functional)—UNRESOLVEDFunctionalDSupports Gain Of Function3accepted
EID10389

FGFR3 N540K exhibited increased kinase activity compared to wild-type FGFR3, as reported in prior characterization of the mutation. In this study, FGFR3 N540K demonstrated enhanced incorporation into … (full text at CIViC)

PMID 29478821 · Bunney et al., 2018 · Open in CIViC

civic