Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors.
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Summary
This work integrated the available structural information with phylogenetic, biochemical, biophysical, genetic, and computational data into a suggested model for the regulation and activation of these receptors and offers molecular interpretations of the effects of various oncogenic alterations that interfere with the regulatory mechanism.
- Type
- review
- Published
- 2008-01-01
- Cited by
- 57
- References
- 130
- OpenAlex
- https://openalex.org/W1963781866
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:33003316
Keywords
Receptor tyrosine kinase, ErbB, Extracellular, Intracellular, Biology
References
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Cited by
- Co-Conserved Features Associated with cis Regulation of ErbB Tyrosine Kinases
- Oncogenic mutant forms of EGFR: lessons in signal transduction and targets for cancer therapy
- GxxxG motifs, phenylalanine, and cholesterol guide the self-association of transmembrane domains of ErbB2 receptors.
- Molecular dynamics of the asymmetric dimers of EGFR: simulations on the active and inactive conformations of the kinase domain.
- Molecular dynamics simulation reveals structural and thermodynamic features of kinase activation by cancer mutations within the epidermal growth factor receptor
- IGF2 Overexpression in Solitary Fibrous Tumors is Independent of Anatomic Location and is Related to Loss of Imprinting
- Architecture and membrane interactions of the EGF receptor
- Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.
- The ErbB Kinase Domain: Structural Perspectives into Kinase Activation and Inhibition
- Protein logic: a statistical mechanical study of signal integration at the single-molecule level.
- Self-association of models of transmembrane domains of ErbB receptors in a lipid bilayer.
- Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases.
- Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
- Physical-chemical principles underlying RTK activation, and their implications for human disease
- Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies
- Kinase‐mediated quasi‐dimers of EGFR
- EGFR juxtamembrane domain, membranes, and calmodulin: kinetics of their interaction.
- Endogenous RhoG Is Rapidly Activated after Epidermal Growth Factor Stimulation through Multiple Guanine-Nucleotide Exchange Factors
- Conformational dynamics of the EGFR kinase domain reveals structural features involved in activation
- HER2 Transmembrane Domain Dimerization Coupled with Self-Association of Membrane-Embedded Cytoplasmic Juxtamembrane Regions.
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