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Article

Redundancy and specificity of the metalloprotease system mediating oncogenic NOTCH1 activation in T-ALL.

Leukemia - 1 Oct 2011

Sulis M L, Saftig P, Ferrando A A

Abstract excerpt

Oncogenic mutations in NOTCH1 are present in over 50% of T-cell lymphoblastic leukemias (T-ALLs). Activation of NOTCH1 requires a double proteolytic processing in the extracellular region of the receptor (S2) and in the transmembrane domain (S3). Currently, anti-NOTCH1 therapies based on the inhibition of S3 processing via small molecule γ-secretase inhibitors are in development. Here we report on the...

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Share to ADAM Proteins
Share to Amyloid Precursor Protein Secretases
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Precursor T-Cell Lymphoblastic Leukemia-Lymphoma

Share to Real-Time Polymerase Chain Reaction

Share to Receptor, Notch1

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Source

Open in PubMed Open full text

Identifiers

PMID: 21625236
DOI: 10.1038/leu.2011.130
PMCID: PMC3165074

Genes

NOTCH1
ADAM10
ADAM17

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Redundancy and specificity of the metalloprotease system mediating oncogenic NOTCH1 activation in T-ALL.PMID 21625236Read ↗

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