Discovery of KT-413, a Targeted Protein Degrader of IRAK4 and IMiD Substrates Targeting MYD88 Mutant Diffuse Large B-Cell Lymphoma.

doi:10.1021/acs.jmedchem.3c01823

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

Community

Back to search

Article

Discovery of KT-413, a Targeted Protein Degrader of IRAK4 and IMiD Substrates Targeting MYD88 Mutant Diffuse Large B-Cell Lymphoma.

Journal of medicinal chemistry - 11 Jul 2024

Weiss Matthew M, Zheng Xiaozhang, Ji Nan, Browne Chris M, Campbell Veronica, Chen Dapeng, Enerson Brad, Fei Xue, Huang Xin, Klaus Christine R, Li Haoran, Mayo Michele, McDonald Alice A, Paul Atanu, Rong Haojing, Sharma Kirti, Shi Yatao, Slavin Anthony, Walther Dirk M, Yuan Karen, Zhang Yi, Zhu Xiao, Kelleher Joe, Walker Duncan, Mainolfi Nello

Abstract excerpt

Developing therapies for the activated B-cell like (ABC) subtype of diffuse large B-cell lymphomas (DLBCL) remains an area of unmet medical need. A subset of ABC DLBCL tumors is driven by activating mutations in myeloid differentiation primary response protein 88 (MYD88), which lead to constitutive activation of interleukin-1 receptor associated kinase 4 (IRAK4) and cellular proliferation. IRAK4 signaling is...

Read the complete abstract on PubMed

Topics

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

Share to Antineoplastic Agents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Discovery

Share to Imidazoles

Share to Interleukin-1 Receptor-Associated Kinases

Share to Lymphoma, Large B-Cell, Diffuse

Share to Myeloid Differentiation Factor 88

Share to Proteolysis

Share to Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 38920289
DOI: 10.1021/acs.jmedchem.3c01823

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Discovery of KT-413, a Targeted Protein Degrader of IRAK4 and IMiD Substrates Targeting MYD88 Mutant Diffuse Large B-Cell Lymphoma.PMID 38920289Read ↗

Integrated proteomic screening reveals design principles of CRBN molecular glue degradersSemantic proximity Read ↗

Design and synthesis of Imidazo[1,2-b]pyridazine IRAK4 inhibitors for the treatment of mutant MYD88 L265P diffuse large B-cell lymphoma.Semantic proximity Read ↗

A multiprotein supercomplex controlling oncogenic signalling in lymphoma.Semantic proximity Read ↗

Oncogenically active MYD88 mutations in human lymphoma.Semantic proximity Read ↗

Kinase-impaired BTK mutations are susceptible to clinical-stage BTK and IKZF1/3 degrader NX-2127.Semantic proximity Read ↗

Bexobrutideg: A Selective, Catalytic Degrader of Bruton’s Tyrosine Kinase Overcomes Inhibitor Resistance and Suppresses Autoantibody-Mediated DiseaseSemantic proximity Read ↗

Identification and Characterization of Von Hippel-Lindau-Recruiting Proteolysis Targeting Chimeras (PROTACs) of TANK-Binding Kinase 1.Semantic proximity Read ↗

Breaking Bad Proteins – Discovery Approaches and the Road to Clinic for DegradersSemantic proximity Read ↗

Biological Functions and Clinical Implications of CFLAR: From Cell Death Mechanisms to Therapeutic Targeting in Immune RegulationSemantic proximity Read ↗

Discovery and Optimization of Pyrrolopyrimidine Inhibitors of Interleukin-1 Receptor Associated Kinase 4 (IRAK4) for the Treatment of Mutant MYD88L265P Diffuse Large B-Cell Lymphoma.Semantic proximity Read ↗

MYD88 L265P elicits mutation-specific ubiquitination to drive NF-κB activation and lymphomagenesis.Semantic proximity Read ↗

Catalytic Degraders Effectively Address Kinase Site Mutations in EML4-ALK Oncogenic Fusions.Semantic proximity Read ↗

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