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

Allosteric inhibition enhances the efficacy of ABL kinase inhibitors to target unmutated BCR-ABL and BCR-ABL-T315I.

BMC cancer - 17 Sept 2012

Mian Afsar Ali, Metodieva Anna, Badura Susanne, Khateb Mamduh, Ruimi Nili, Najajreh Yousef, Ottmann Oliver Gerhard, Mahajna Jamal, Ruthardt Martin

Abstract excerpt

BACKGROUND: Chronic myelogenous leukemia (CML) and Philadelphia chromosome-positive (Ph+) acute lymphatic leukemia (Ph + ALL) are caused by the t(9;22), which fuses BCR to ABL resulting in deregulated ABL-tyrosine kinase activity. The constitutively activated BCR/ABL-kinase "escapes" the auto-inh...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Colony-Forming Units Assay
Share to Dasatinib

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fusion Proteins, bcr-abl

Share to Hematopoietic Stem Cells

Share to Leukemia, Myelogenous, Chronic, BCR-ABL Positive

Share to Pyrimidines

Share to Thiazoles

Source

Open in PubMed Open full text

Identifiers

PMID: 22985168
DOI: 10.1186/1471-2407-12-411
PMCID: PMC3488316

Genes

BCR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22985168-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Allosteric inhibition enhances the efficacy of ABL kinase inhibitors to target unmutated BCR-ABL and BCR-ABL-T315I.PMID 22985168Read ↗

Overcoming Bcr-Abl T315I mutation by combination of GNF-2 and ATP competitors in an Abl-independent mechanism.Semantic proximity Read ↗

Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors.Semantic proximity Read ↗

Crizotinib acts as ABL1 inhibitor combining ATP-binding with allosteric inhibition and is active against native BCR-ABL1 and its resistance and compound mutants BCR-ABL1T315I and BCR-ABL1T315I-E255K.Semantic proximity Read ↗

Expanding the diversity of allosteric bcr-abl inhibitors.Semantic proximity Read ↗

ABL001, a Potent Allosteric Inhibitor of BCR-ABL, Prevents Emergence of Resistant Disease When Administered in Combination with Nilotinib in an in Vivo Murine Model of Chronic Myeloid LeukemiaSemantic proximity Read ↗

Targeting the BCR-ABL signaling pathway in therapy-resistant Philadelphia chromosome-positive leukemia.Semantic proximity Read ↗

Insight into the allosteric inhibition of Abl kinase.Semantic proximity Read ↗

The growing arsenal of ATP-competitive and allosteric inhibitors of BCR-ABL.Semantic proximity Read ↗

Structure, Regulation, Signaling, and Targeting of Abl Kinases in CancerSemantic proximity Read ↗

Activity of the Aurora Kinase Inhibitor VX-680 against Bcr/Abl-Positive Acute Lymphoblastic LeukemiasSemantic proximity Read ↗

Chemotherapeutic agents circumvent emergence of dasatinib-resistant BCR-ABL kinase mutations in a precise mouse model of Philadelphia chromosome–positive acute lymphoblastic leukemiaSemantic proximity Read ↗

PF-114, a potent and selective inhibitor of native and mutated BCR/ABL is active against Philadelphia chromosome-positive (Ph+) leukemias harboring the T315I mutation.Semantic proximity Read ↗

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