Article

Disruption of IRElα through its Kinase Domain Attenuates Multiple Myeloma

2018-12-13

Abstract excerpt

Multiple myeloma (MM) arises from malignant immunoglobulin-secreting plasma cells and remains an incurable, often lethal disease despite recent therapeutic advances. The unfolded-protein response sensor IRE1α supports protein secretion by deploying a kinase-endoribonuclease module to activate the transcription factor XBP1s. MM cells may coopt the IRE1α-XBP1s pathway; however, the validity of IRE1α as a potential M...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 656f2222-af81-5957-a28f-f11489d925d8
DOI: 10.1101/495242

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Disruption of IRElα through its Kinase Domain Attenuates Multiple MyelomaDOI 10.1101/495242Read

RNA sequencing identifies novel regulated IRE1-dependent decay targets that affect multiple myeloma survival and proliferationSemantic proximity Read

Identification of an Ire1alpha endonuclease specific inhibitor with cytotoxic activity against human multiple myelomaSemantic proximity Read

The role of endoplasmic reticulum stress in maintaining and targeting multiple myeloma: a double-edged sword of adaptation and apoptosisSemantic proximity Read

Distinct Pathway Activities are Associated with Prognosis and Response to Bortezomib- containing Treatment in MCL1-M Based Molecular Subtypes of Multiple MyelomaSemantic proximity Read

IRE1α-XBP1 signaling pathway, a potential therapeutic target in multiple myelomaSemantic proximity Read

XBP1s levels are implicated in the biology and outcome of myeloma mediating different clinical outcomes to thalidomide-based treatmentsSemantic proximity Read

Molecular mechanisms in multiple myeloma drug resistance.Semantic proximity Read

Xbp1s-negative tumor B cells and pre-plasmablasts mediate therapeutic proteasome inhibitor resistance in multiple myeloma.Semantic proximity Read

Targeting degradation of IKZF1 and IKZF3 through modulation of the E3 ligase substrates in the context of cellular therapies for multiple myelomaSemantic proximity Read

The Unfolded Protein Response: A Novel Therapeutic Target in Acute LeukemiasSemantic proximity Read

Novel SLAMF1-derived peptide induces apoptosis in multiple myeloma cells by targeting IRF4 transcription factor for degradationSemantic proximity Read

CRIP1 involves the pathogenesis of multiple myeloma via dual-regulation of proteasome and autophagySemantic proximity Read