ArticleStructure (London, England : 1993)2008
Mechanism of activation and inhibition of the HER4/ErbB4 kinase.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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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.
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Who cites it
103 citing papers in PubMed, 188 citations in OpenAlex.
- Deep3D-DTA: A Tri-Modal Deep Learning Framework for Binding Affinity Prediction Leveraging 3D Structural Representations of Drugs and Targets.Interdisciplinary sciences, computational life sciences · 2026Article
- Recurrent cancer-associated ERBB4 mutations are transforming and confer resistance to targeted therapies.Molecular oncology · 2026Article
- Thiourea Derivatives for the Potential Treatment of Lung Cancer via the Inhibition of EGFR and Efflux Pumps: Synthesis,Anti-cancer agents in medicinal chemistry · 2026Article
- Development and validation of a prognostic prediction model based on coagulation-related genes and clinical factors in acute leukemia.Translational pediatrics · 2025Article
- Cross-Talk between NOK and EGFR: Juxtamembrane and Kinase domain interactions enhancing STAT3/5 signaling in breast cancer tumorigenesis.Translational oncology · 2025Article
- Vitamin D ameliorates prediabetic cardiac injure via modulation of the ErbB4/ferroptosis signaling axis.Frontiers in immunology · 2025Article
- Multiple ligands simultaneous molecular docking and dynamics approach to study the synergetic inhibitory of curcumin analogs on ErbB4 tyrosine phosphorylation.Research in pharmaceutical sciences · 2024Article
- HER4 is a high-affinity dimerization partner for all EGFR/HER/ErbB family proteins.Protein science : a publication of the Protein Society · 2024Article
- Enabling target-aware molecule generation to follow multi objectives with Pareto MCTS.Communications biology · 2024Article
- Identification of kinase modulators as host-directed therapeutics against intracellular methicillin-resistantFrontiers in cellular and infection microbiology · 2024Article
- Anticancer pan-ErbB inhibitors reduce inflammation and tissue injury and exert broad-spectrum antiviral effects.The Journal of clinical investigation · 2023Article
- Suppression of Ah Receptor (AhR) increases the aggressiveness of TNBC cells and 11-Cl-BBQ-activated AhR inhibits their growth.Biochemical pharmacology · 2023Article
- Design, Synthesis, ADME, and Anticancer Studies of NewerACS omega · 2023Article
- Structure and dynamics of the EGFR/HER2 heterodimer.Cell discovery · 2023Article
- Inhibition of mutationally activated HER2.Chemical biology & drug design · 2023Article
- Targetable HER3 functions driving tumorigenic signaling in HER2-amplified cancers.Cell reports · 2022Article
- The Yin and Yang of ERBB4: Tumor Suppressor and Oncoprotein.Pharmacological reviews · 2022Review
- An Unbiased Functional Genetics Screen Identifies Rare Activating ERBB4 Mutations.Cancer research communications · 2022Article
- Network-based approach for targeting human kinases commonly associated with amyotrophic lateral sclerosis and cancer.Frontiers in molecular neuroscience · 2022Article
- A Review of HER4 (ErbB4) Kinase, Its Impact on Cancer, and Its Inhibitors.Molecules (Basel, Switzerland) · 2021Review
43 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
HER4/ErbB4 is a ubiquitously expressed member of the EGF/ErbB family of receptor tyrosine kinases that is essential for normal development of the heart, nervous system, and mammary gland. We report here crystal structures of the ErbB4 kinase domain in active and lapatinib-inhibited forms. Active ErbB4 kinase adopts an asymmetric dimer conformation essentially identical to that observed to be important for activation of the EGF receptor/ErbB1 kinase. Mutagenesis studies of intact ErbB4 in Ba/F3 cells confirm the importance of this asymmetric dimer for activation of intact ErbB4. Lapatinib binds to an inactive form of the ErbB4 kinase in a mode equivalent to its interaction with the EGF receptor. All ErbB4 residues contacted by lapatinib are conserved in the EGF receptor and HER2/ErbB2, which lapatinib also targets. These results demonstrate that key elements of kinase activation and inhibition are conserved among ErbB family members.
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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.