ArticleExperimental and therapeutic medicine2010
Genome-wide comparison of FGFRL1 with structurally related surface receptors.
Article in Experimental and therapeutic medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- FGFR Like1 drives esophageal cancer progression via EMT, PI3K/Akt, and notch signalling: insights from clinical data and next-generation sequencing analysis.FEBS open bio · 2026Article
- FGFRL1: Structure, Molecular Function, and Involvement in Human Disease.Current issues in molecular biology · 2025Review
- Understanding Neovascularization in Glioblastoma: Insights from the Current Literature.International journal of molecular sciences · 2025Review
- Predictive Value of Serum VEGF Levels in Non-Small Cell Lung Cancer: A Review.Oncology research · 2025Review
- Clinical advances and challenges in targeting FGF/FGFR signaling in lung cancer.Molecular cancer · 2024Review
- Receptor FGFRL1 acts as a tumor suppressor in nude mice when overexpressed in HEK 293 Tet-On cells.Oncology letters · 2016Article
- Biology of FGFRL1, the fifth fibroblast growth factor receptor.Cellular and molecular life sciences : CMLS · 2011Review
- Rapid fusion and syncytium formation of heterologous cells upon expression of the FGFRL1 receptor.The Journal of biological chemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FGFRL1 (FGFR5) is a member of the fibroblast growth factor receptor family, which lacks the intracellular tyrosine kinase domain required for signal transduction by trans-phosphorylation. Since it still contains a cytoplasmic domain of 100 amino acid residues with a peculiar histidine-rich element, it might be involved in an alternative pathway of downstream signaling. To get a clue about a possible mechanism, we compared the overall structure of FGFRL1 with all proteins from the UniProt databank. We found that the human genome encodes 42 structurally related proteins with a signal peptide, three Ig-like domains and a transmembrane domain. These proteins can be grouped in seven families, fibroblast growth factor receptors (FGFRs), Fc receptor-like proteins, IL-1 receptor-like proteins, killer cell Ig-like receptors (KIRs), nectin-like proteins, sialic acid binding lectins (SIGLECs) and signal regulatory proteins (SIRPs). The 7 families utilize four different strategies for signaling, namely a protein tyrosine kinase domain, a TIR (Toll/IL-1 receptor) domain, ITIM/ITAM motifs as well as carboxy-terminal peptides that interact with the PDZ domain of an adaptor protein. It remains to be determined whether FGFRL1 might also utilize one of these strategies for signaling.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.