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Article

Hematoxylin binds to mutant calreticulin and disrupts its abnormal interaction with thrombopoietin receptor.

Blood - 8 Apr 2021

Jia Ruochen, Balligand Thomas, Atamanyuk Vasyl, Nivarthi Harini, Xu Erica, Kutzner Leon, Weinzierl Jakob, Nedelec Audrey, Kubicek Stefan, Lesyk Roman, Zagrijtschuk Oleh, Constantinescu Stefan N, Kralovics Robert

Abstract excerpt

Somatic mutations of calreticulin (CALR) have been identified as a main disease driver of myeloproliferative neoplasms, suggesting that development of drugs targeting mutant CALR is of great significance. Site-directed mutagenesis in the N-glycan binding domain (GBD) abolishes the ability of mutant CALR to oncogenically activate the thrombopoietin receptor (MPL). We therefore hypothesized that a small molecule...

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Identifiers

PMID: 33202418
DOI: 10.1182/blood.2020006264
PMCID: PMC8118640

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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