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

Proteasome inhibitors induce FLT3-ITD degradation through autophagy in AML cells.

Blood - 18 Feb 2016

Larrue Clément, Saland Estelle, Boutzen Héléna, Vergez François, David Marion, Joffre Carine, Hospital Marie-Anne, Tamburini Jérôme, Delabesse Eric, Manenti Stéphane, Sarry Jean Emmanuel, Récher Christian

Abstract excerpt

Internal tandem duplication of the Fms-like tyrosine kinase-3 receptor (FLT3) internal tandem duplication (ITD) is found in 30% of acute myeloid leukemia (AML) and is associated with a poor outcome. In addition to tyrosine kinase inhibitors, therapeutic strategies that modulate the expression of FLT3-ITD are also promising. We show that AML samples bearing FLT3-ITD mutations are more sensitive to proteasome...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy
Share to Bortezomib

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to fms-Like Tyrosine Kinase 3

Share to Mice, Inbred NOD

Share to Mice, SCID

Share to Proteasome Inhibitors

Share to Proteolysis

Share to Xenograft Model Antitumor Assays

Source

Identifiers

PMID: 26286850
DOI: 10.1182/blood-2015-05-646497

Genes

FLT3

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proteasome inhibitors induce FLT3-ITD degradation through autophagy in AML cells.PMID 26286850Read ↗

Inhibition of the proteasome and proteaphagy enhances apoptosis in FLT3-ITD-driven acute myeloid leukemia.Semantic proximity Read ↗

Targeting FLT3-ITD signaling mediates ceramide-dependent mitophagy and attenuates drug resistance in AML.Semantic proximity Read ↗

Oncogenic FLT3-ITD supports autophagy via ATF4 in acute myeloid leukemia.Semantic proximity Read ↗

Autophagy activation mediates resistance to FLT3 inhibitors in acute myeloid leukemia with FLT3-ITD mutation.Semantic proximity Read ↗

Blockade of de novo pyrimidine biosynthesis triggers autophagic degradation of oncoprotein FLT3-ITD in acute myeloid leukemia.Semantic proximity Read ↗

Concomitant targeting of FLT3 and BTK overcomes FLT3 inhibitor resistance in acute myeloid leukemia through the inhibition of autophagy.Semantic proximity Read ↗

ULK1 inhibition as a targeted therapeutic strategy for FLT3-ITD-mutated acute myeloid leukemia.Semantic proximity Read ↗

A combinatorial therapeutic approach to enhance FLT3-ITD AML treatment.Semantic proximity Read ↗

Autophagy and inflammasome activation are associated with poor response to FLT3 inhibitors in patients with FLT3-ITD acute myeloid leukemia.Semantic proximity Read ↗

Potential role of autophagy induced by FLT3-ITD and acid ceramidase in acute myeloid leukemia chemo-resistance: new insights.Semantic proximity Read ↗

Autophagy and inflammasome molecular interplay and activation predict poor response to FLT3 inhibitors in patients with FLT3-ITD acute myeloid leukemiaSemantic proximity Read ↗

The multitargeted receptor tyrosine kinase inhibitor linifanib (ABT-869) induces apoptosis through an Akt and glycogen synthase kinase 3β-dependent pathway.Semantic proximity Read ↗

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