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

The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibition

16 Dec 2023

Abstract excerpt

Cbl-b is a RING-type E3 ubiquitin ligase that is expressed in several immune cell lineages, where it negatively regulates the activity of immune cells. Cbl-b has specifically been identified as an attractive target for cancer immunotherapy due to its role in promoting an immunosuppressive tumor environment. A Cbl-b inhibitor, Nx-1607, is currently in phase I clinical trials for advanced solid tumor malignancies....

Read the complete abstract on PubMed

Topics

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

Share to Peptidase Inhibition and Analysis
Share to RNA modifications and cancer
Share to Ubiquitin and proteasome pathways

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 38104184
DOI: 10.1038/s42003-023-05655-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibitionPMID 38104184Read ↗

Discovery and characterization of small molecule inhibitors of CBL-B that act as intramolecular glue to enhance T-cell anti-tumor activitySemantic proximity Read ↗

Targeting Cbl-b in cancer immunotherapySemantic proximity Read ↗

Modulation of Immune Cell Functions by the E3 Ligase Cbl-bSemantic proximity Read ↗

Novel c-CBL and CBL-b ubiquitin ligase mutations in human acute myeloid leukemiaSemantic proximity Read ↗

Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.Semantic proximity Read ↗

Discovery of Monovalent Direct Degraders of BRD4 that Act via the Recruitment of DCAF11Semantic proximity Read ↗

A General Strategy for Discovery of Inhibitors and Activators of RING and U-box E3 Ligases with Ubiquitin VariantsSemantic proximity Read ↗

Reinstating targeted protein degradation with DCAF1 PROTACs in CRBN PROTAC resistant settingsSemantic proximity Read ↗

Mining the CRBN Target Space Redefines Rules for Molecular Glue-induced Neosubstrate RecognitionSemantic proximity Read ↗

The role of CBL family ubiquitin ligases in cancer progression and therapeutic strategiesSemantic proximity Read ↗

Locking CBL TKBD in its native conformation presents a novel therapeutic opportunity in mutant CBL-dependent leukemia.Semantic proximity Read ↗

MLN4924: a novel first-in-class inhibitor of NEDD8-activating enzyme for cancer therapySemantic proximity Read ↗

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