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Article

The tetramerization domain-independent Ras activation by BCR-ABL oncoprotein in hematopoietic cells.

International journal of oncology - 1 Jun 1998

Tauchi T, Okabe S, Miyazawa K, Ohyashiki K

Abstract excerpt

BCR-ABL is a chimeric oncoprotein that exhibits deregulated tyrosine kinase activity and is implicated in the pathogenesis of Philadelphia chromosome-positive human leukemias. We have previously shown that BCR-ABL activates Ras signaling pathways required for transformation. To elucidate the mechanisms whereby BCR-ABL induced transformation in hematopoietic cells, we examined the biological effects of expression...

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Identifiers

PMID: 9592185
DOI: 10.3892/ijo.12.6.1269

Genes

BCR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The tetramerization domain-independent Ras activation by BCR-ABL oncoprotein in hematopoietic cells.PMID 9592185Read ↗

Structural and signaling requirements for BCR-ABL-mediated transformation and inhibition of apoptosis.Semantic proximity Read ↗

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Signal transducer and activator of transcription (STAT)5 activation by BCR/ABL is dependent on intact Src homology (SH)3 and SH2 domains of BCR/ABL and is required for leukemogenesis.Semantic proximity Read ↗

The CRKL Adaptor Protein Transforms Fibroblasts and Functions in Transformation by the BCR-ABL OncogeneSemantic proximity Read ↗

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Autoinhibition of Bcr-Abl through its SH3 domain.Semantic proximity Read ↗

The SH2 domain of P210BCR/ABL is not required for the transformation of hematopoietic factor-dependent cells.Semantic proximity Read ↗

Alternative signals to RAS for hematopoietic transformation by the BCR-ABL oncogene.Semantic proximity Read ↗

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