Extracellular domains drive homo- but not hetero-dimerization of erbB receptors

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Extracellular domains drive homo- but not hetero-dimerization of erbB receptors is …
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scholarly articleQ13442814

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P356DOI10.1093/EMBOJ/19.17.4632
P932PMC publication ID302059
P698PubMed publication ID10970856
P5875ResearchGate publication ID12350966

P50authorMark A. LemmonQ24076870
P2093author name stringK M Ferguson
T L Macatee
M J Mohan
P J Darling
P2860cites workNeuregulin-4: a novel growth factor that acts through the ErbB-4 receptor tyrosine kinaseQ22009917
Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulinQ24305421
Binding of Neu Differentiation Factor with the Extracellular Domain of Her2 and Her3Q24315647
HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimersQ24336345
Identification of heregulin, a specific activator of p185erbB2Q24338146
SH2 domains recognize specific phosphopeptide sequencesQ27860748
Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2Q28279061
The epidermal growth factor receptor couples transforming growth factor-alpha, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4Q28513922
ErbB4 signaling in the mammary gland is required for lobuloalveolar development and Stat5 activation during lactationQ28594099
The cellular response to neuregulins is governed by complex interactions of the erbB receptor familyQ28609130
Intermolecular association of the p185neu protein and EGF receptor modulates EGF receptor functionQ28678683
ErbB-2 is a common auxiliary subunit of NDF and EGF receptors: implications for breast cancerQ28678776
Growth factor signaling by receptor tyrosine kinasesQ29618315
SH2/SH3 signaling proteinsQ30194539
An incomplete program of cellular tyrosine phosphorylations induced by kinase-defective epidermal growth factor receptorsQ30463969
Nonclinical studies addressing the mechanism of action of trastuzumab (Herceptin).Q33730975
Two EGF molecules contribute additively to stabilization of the EGFR dimerQ33885990
ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signalingQ33886341
Bivalence of EGF-like ligands drives the ErbB signaling networkQ33887274
Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptorQ34180911
Neuregulins and their receptors: a versatile signaling module in organogenesis and oncogenesisQ34431223
Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylationQ35054357
EGF-stimulated tyrosine phosphorylation of p185neu: a potential model for receptor interactionsQ35980208
Interaction between proteins localized in membranesQ37396417
Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor. A low resolution projection structure of the ligand-binding domainQ38334256
Epidermal growth factor binding induces a conformational change in the external domain of its receptorQ38342722
Local aggregation of hormone–receptor complexes is required for activation by epidermal growth factorQ40226398
Dimerization of cell surface receptors in signal transductionQ40579106
Regulation of signal transduction and signal diversity by receptor oligomerizationQ40592846
A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signalingQ40673334
Formation of a high affinity heregulin binding site using the soluble extracellular domains of ErbB2 with ErbB3 or ErbB4.Q41020913
Egf binding to its receptor triggers a rapid tyrosine phosphorylation of the erbB-2 protein in the mammary tumor cell line SK-BR-3Q41107277
The extracellular domain of the epidermal growth factor receptor. Studies on the affinity and stoichiometry of binding, receptor dimerization and a binding-domain mutantQ41438473
The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand-receptor interactionsQ41554100
The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complexQ41710005
Heterodimerization of the erbB-1 and erbB-2 receptors in human breast carcinoma cells: a mechanism for receptor transregulationQ41710300
Specificity within the EGF family/ErbB receptor family signaling networkQ41721612
Autoregulatory mechanisms in protein-tyrosine kinasesQ41758716
Evidence for epidermal growth factor (EGF)-induced intermolecular autophosphorylation of the EGF receptors in living cellsQ42025518
Proxy activation of protein ErbB2 by heterologous ligands implies a heterotetrameric mode of receptor tyrosine kinase interactionQ42141978
Expression of dominant-negative ErbB2 in the mammary gland of transgenic mice reveals a role in lobuloalveolar development and lactationQ42814150
Heterodimerization of c-erbB2 with different epidermal growth factor receptor mutants elicits stimulatory or inhibitory responsesQ42819990
EGF induces increased ligand binding affinity and dimerization of soluble epidermal growth factor (EGF) receptor extracellular domain.Q52444456
Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteinsQ68139662
Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activationQ68818445
Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activationQ72871521
Secondary dimerization between members of the epidermal growth factor receptor familyQ73257880
Binding specificities and affinities of egf domains for ErbB receptorsQ77360929
P433issue17
P407language of work or nameEnglishQ1860
P304page(s)4632-4643
P577publication date2000-09-01
P1433published inThe EMBO JournalQ1278554
P1476titleExtracellular domains drive homo- but not hetero-dimerization of erbB receptors
P478volume19

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cites work (P2860)
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Q37643945erbB3 is an active tyrosine kinase capable of homo- and heterointeractions

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