ReviewCurrent opinion in structural biology2014
Putting together structures of epidermal growth factor receptors.
Review in Current opinion in structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 52 citations in OpenAlex.
- EGFR- and Integrin αInternational journal of molecular sciences · 2024Review
- Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes.Cell reports · 2024Article
- Size-dependent activation of CAR-T cells.Science immunology · 2022Article
- Article
- Osimertinib: Another medication related to osteonecrosis of the jaws? A case report and literature review.Frontiers in pharmacology · 2022Article
- The Yin and Yang of ERBB4: Tumor Suppressor and Oncoprotein.Pharmacological reviews · 2022Review
- Structural Basis for Vascular Endothelial Growth Factor Receptor Activation and Implications for Disease Therapy.Biomolecules · 2020Review
- Direct stimulation of ERBB2 highlights a novel cytostatic signaling pathway driven by the receptor ThrScientific reports · 2020Article
- Current Approaches in NSCLC Targeting K-RAS and EGFR.International journal of molecular sciences · 2019Review
- Complex Formation between VEGFR2 and the βCell chemical biology · 2019Article
- Interactions of the EphA2 Kinase Domain with PIPs in Membranes: Implications for Receptor Function.Structure (London, England : 1993) · 2018Article
- Effect of Membrane Composition on Receptor Association: Implications of Cancer Lipidomics on ErbB Receptors.The Journal of membrane biology · 2018Review
- Phosphorylated EGFR Dimers Are Not Sufficient to Activate Ras.Cell reports · 2018Article
- Real-time analysis of the binding of fluorescent VEGFBiochemical pharmacology · 2017Article
- Activation of the EGF Receptor by Ligand Binding and Oncogenic Mutations: The "Rotation Model".Cells · 2017Review
- Free Energy Landscape of Lipid Interactions with Regulatory Binding Sites on the Transmembrane Domain of the EGF Receptor.The journal of physical chemistry. B · 2016Article
- Conformational Changes in the Epidermal Growth Factor Receptor: Role of the Transmembrane Domain Investigated by Coarse-Grained MetaDynamics Free Energy Calculations.Journal of the American Chemical Society · 2016Article
- A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors.The Journal of biological chemistry · 2016Article
- Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain.The Journal of biological chemistry · 2016Article
- Ligand regulation of a constitutively dimeric EGF receptor.Nature communications · 2015Article
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 1 institution in 1 country.
Funding
Abstract
Numerous crystal structures have been reported for the isolated extracellular region and tyrosine kinase domain of the epidermal growth factor receptor (EGFR) and its relatives, in different states of activation and bound to a variety of inhibitors used in cancer therapy. The next challenge is to put these structures together accurately in functional models of the intact receptor in its membrane environment. The intact EGFR has been studied using electron microscopy, chemical biology methods, biochemically, and computationally. The distinct approaches yield different impressions about the structural modes of communication between extracellular and intracellular regions. They highlight possible differences between ligands, and also underline the need to understand how the receptor interacts with the membrane itself.
Indexed as
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.