Discover Community Create You

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

Article

BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner.

Cell - 12 Jul 1991

Pendergast A M, Muller A J, Havlik M H, Maru Y, Witte O N

Abstract excerpt

BCR-ABL is a chimeric oncogene implicated in the pathogenesis of Philadelphia chromosome-positive human leukemias. BCR first exon sequences specifically activate the tyrosine kinase and transforming potential of BCR-ABL. We have tested the hypothesis that activation of BCR-ABL may involve direct interaction between BCR sequences and the tyrosine kinase regulatory domains of ABL. Full-length c-BCR as well as BCR...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Line

Share to Cell Transformation, Neoplastic

Share to Genetic Variation

Share to Molecular Sequence Data

Share to Plasmids

Source

Identifiers

PMID: 1712671
DOI: 10.1016/0092-8674(91)90148-r

Genes

BCR

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner.PMID 1712671Read ↗

The SH2-containing adapter protein GRB10 interacts with BCR-ABL.Semantic proximity Read ↗

Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity.Semantic proximity Read ↗

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

Activation of hematopoietic growth factor signal transduction pathways by the human oncogene BCR/ABLSemantic proximity Read ↗

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

Genetic approaches to defining signaling by the CML-associated tyrosine kinase BCR-ABL.Semantic proximity Read ↗

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

The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase.Semantic proximity Read ↗

BCR: a promiscuous fusion partner in hematopoietic disordersSemantic proximity Read ↗

A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins.Semantic proximity Read ↗

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

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 ↗

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