Irit Lax, PhD
Professor of PharmacologyCards
Appointments
Pharmacology
Primary
Contact Info
Pharmacology
PO Box 208066, 333 Cedar Street
New Haven, CT 06520-8066
United States
About
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Titles
Professor of Pharmacology
Appointments
Pharmacology
ProfessorPrimary
Other Departments & Organizations
- Pharmacology
- Primary Faculty
- Schlessinger Lab
- Yale Ventures
Education & Training
- PhD
- Weizmann Institute of Science (1985)
Research
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Research at a Glance
Yale Co-Authors
Frequent collaborators of Irit Lax's published research.
Francisco Tome
Joseph Schlessinger, PhD
Avon Johnson, LCSW
Seong An, PhD
Yoshihisa Suzuki
Publications
2026
Cellular responses to FGF1 are modulated by palmitoylation of the docking protein FRS2α.
An S, Suzuki Y, Mohanty J, Tome F, Lax I, Schlessinger J. Cellular responses to FGF1 are modulated by palmitoylation of the docking protein FRS2α. Proceedings Of The National Academy Of Sciences Of The United States Of America 2026, 123: e2605311123. PMID: 42054356, PMCID: PMC13143043, DOI: 10.1073/pnas.2605311123.Peer-Reviewed Original ResearchAltmetricMeSH Keywords and ConceptsConceptsDocking proteinMitogen-activated protein kinaseReceptor tyrosine kinasesPlasma membranePhosphorylation of multiple tyrosine residuesFormation of signaling complexesMultiple tyrosine residuesCellular responsesDownstream signaling moleculesMembrane rufflingExtracellular cuesPalmitoylation sitesFibroblast growth factorMultiprotein complexesSignaling ComplexTyrosine residuesProtein kinaseResponse to FGF1Ligand stimulationMAPK responsePalmitoylationTyrosine kinasePC12 cellsNeuronal differentiationCellular activities
2009
The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site
Bae J, Lew E, Yuzawa S, Tomé F, Lax I, Schlessinger J. The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site. Journal Of End-to-End-testing 2009, 138: 514-524. DOI: 10.1016/s9999-9994(09)20387-4.Peer-Reviewed Original Research
1988
Chicken Epidermal Growth Factor (EGF) Receptor: cDNA Cloning, Expression in Mouse Cells, and Differential Binding of EGF and Transforming Growth Factor Alpha
Lax I, Johnson A, Howk R, Sap J, Bellot F, Winkler M, Ullrich A, Vennstrom B, Schlessinger J, Givol D. Chicken Epidermal Growth Factor (EGF) Receptor: cDNA Cloning, Expression in Mouse Cells, and Differential Binding of EGF and Transforming Growth Factor Alpha. Molecular And Cellular Biology 1988, 8: 1970-1978. DOI: 10.1128/mcb.8.5.1970-1978.1988.Peer-Reviewed Original ResearchConceptsHuman EGF receptorChicken EGF receptorEpidermal growth factorNIH 3T3 cellsEGF receptorCDNA clonesMammalian epidermal growth factorDifferential bindingTGF-aEndogenous EGF receptorsBinding of epidermal growth factorGrowth factorMurine epidermal growth factorCoding sequenceApparent molecular weightTransforming growth factor-alphaCDNA constructsAvian EGF receptorMouse cellsPrimary structureGrowth factor-alphaCDNAChicken receptorMammalian receptorsFactor-alpha
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Mailing Address
Pharmacology
PO Box 208066, 333 Cedar Street
New Haven, CT 06520-8066
United States