Enhancement of tyrosine kinase activity of the Drosophila epidermal growth factor receptor homolog by alterations of the transmembrane domain.

doi:10.1111/j.1432-1033.1990.tb15532.x

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Enhancement of tyrosine kinase activity of the Drosophila epidermal growth factor receptor homolog by alterations of the transmembrane domain.

European journal of biochemistry - 20 May 1990

Wides R J, Zak N B, Shilo B Z

Abstract excerpt

The Drosophila epidermal growth factor receptor homolog (DER) displays sequence similarity to both the epidermal growth factor (EGF) receptor and the neu vertebrate proteins. We have examined the possibility of deregulating the tyrosine kinase activity of DER by introducing structural changes which mimic the oncogenic alterations in the vertebrate counterparts. Substitution of valine by glutamic acid in the...

Topics

Amino Acid Sequence
Animals
Base Sequence
Chimera
Drosophila
Drosophila Proteins
Enzyme Activation
ErbB Receptors
Gene Expression Regulation, Enzymologic
Genes
Glutamates

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Glutamic Acid

Molecular Sequence Data

Mutation

Phosphorylation

Protein Kinases

Protein-Tyrosine Kinases

Receptors, Invertebrate Peptide

Source

Open in PubMed

Identifiers

PMID: 1972062
DOI: 10.1111/j.1432-1033.1990.tb15532.x

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1972062-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Enhancement of tyrosine kinase activity of the Drosophila epidermal growth factor receptor homolog by alterations of the transmembrane domain.PMID 1972062Read ↗

Oncogenic activating mutations in the neu/erbB-2 oncogene are involved in the induction of mammary tumors.Semantic proximity Read ↗

Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation.Semantic proximity Read ↗

Developmental control by the Drosophila EGF receptor homolog DER.Semantic proximity Read ↗

NIH/3T3 cells transformed with the activated erbB-2 oncogene can be phenotypically reverted by a kinase deficient, dominant negative erbB-2 variant.Semantic proximity Read ↗

Ligand-independent dimerization and activation of the oncogenic Xmrk receptor by two mutations in the extracellular domain.Semantic proximity Read ↗

Mutational analysis of the role of the carboxy-terminal region of the v-erbB protein in erythroid cell transformation.Semantic proximity Read ↗

DroVav, the Drosophila melanogaster homologue of the mammalian Vav proteins, serves as a signal transducer protein in the Rac and DER pathways.Semantic proximity Read ↗

Three dimensional structure of the transmembrane region of the proto-oncogenic and oncogenic forms of the neu protein.Semantic proximity Read ↗

Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors.Semantic proximity Read ↗

Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation.Semantic proximity Read ↗

Activating mutations in the extracellular domain of the melanoma inducing receptor Xmrk are tumorigenic in vivo.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.