Eric S. Fischer

The paper presents an unbiased surfaceome atlas of leukemic cell lines, identifying novel surface proteins and discordant gene expression patterns, with CD70 highlighted as a potential therapeutic target in AML.

The paper identifies two proteasomal mechanisms that target proteins with exposed cysteines, revealing their role in quality control and linking them to human diseases.

This paper designs an orthogonal self-labeling protein, LUCI-tag, using deep learning, which enables rapid and payload-agnostic labeling of proteins in live cells.

The paper shows that covalent modification of CRBN by EM12-FS creates a new interface for NTAQ1 recruitment, expanding degrader specificity beyond the G-loop degron.

This study shows that truncating mutations in PPM1D shift its degradation pathway from ubiquitin-independent to UBR5-mediated, leading to increased PPM1D levels and oncogenic effects.

Z-TAC converts IgG antibodies into cell-surface protein degraders, enabling efficient and sustained degradation of multiple receptors and receptor combinations.

The paper discovers a charged molecular glue, c-Glue, through targeted degron display, enabling the development of Molecular Glue Degraders (MGDs) for protein degradation.

This paper identifies a bifunctional small molecule that can induce both transactivation and repression of gene expression depending on cellular context.

This study uses high-throughput chemistry to discover chemical inducers of proximity by modifying pre-existing ligands and screening for degrader activity.

This study identifies the structural basis of VCP-VCPIP1-p47 complex formation and demonstrates the role of VCPID in enhancing DUB activity and Golgi reassembly.

This paper develops chemical probes for FBXO22, including a degrader and a recruitment ligand, to enable targeted protein degradation applications.

The paper identifies O-mannosylation and protein maturation as therapeutic targets in BRAF fusion oncogenesis by showing their necessity for fusion-induced transformation.

The paper develops a large yeast surface display library to identify high-affinity peptide ligands for various protein targets, revealing binding motifs and novel clones.

This study identifies FGFR alterations in pediatric gliomas, their association with specific histologies, and their response to targeted therapies.

The paper identifies 298 protein targets of CRBN-binding molecular glues using a high-throughput affinity purification mass spectrometry workflow and demonstrates a lead compound for the new target PPIL4.

The paper shows that structural ubiquitin contributes to K48 linkage-specificity in Tom1 through a non-canonical binding site identified via cryo-EM.

This study develops potent and selective CK1α molecular glue degraders through scaffold hopping and structure-activity relationship analysis of a glutarimide-based library.

This study shows SMAC mimetics, when combined with IFN{psi}, enable human macrophages to phagocytose live cancer cells across multiple donors.

This study develops a kinetic scout approach to accelerate targeted protein degrader development by tuning ligand residence time through chemical proteomics and mechanistic assays.

The paper identifies CRBN-dependent WEE1 molecular glue degraders through combinatorial library screening and medicinal chemistry, providing structural insights into kinase selectivity.

This study develops electrophilic degraders using SNAr chemistry, enabling selective protein degradation without requiring a defined E3 ligase recruiter.

This study evaluates how electrophilic modifications to JQ1 affect DCAF16 trans-labeling and BRD4 degradation, showing a correlation between warhead exposure and degradation efficiency.

This study develops small molecule degraders of the dengue virus envelope protein, demonstrating their ability to induce proteosome-mediated degradation and providing a foundation for antiviral drug development.

This paper identifies HUWE1 as a ubiquitin ligase that enhances ubiquitin modifications on proteins and aggregates, promoting their degradation via proteasome and autophagy pathways.

This study identifies HAPSTR1 as a HUWE1 substrate that facilitates its nuclear localization, thereby regulating stress signaling pathways and cell proliferation.

The paper presents cryo-EM structures of BIRC6-client complexes to elucidate the mechanism of Smac-mediated caspase release and BIRC6 function in apoptosis regulation.

This paper develops a scalable method to identify E3-specific degraders by tracing substrate receptor abundance changes induced by pharmacological auto-degradation.

The paper develops a machine learning model to predict protein degradability for targeted protein degradation, identifying key features and extending predictions to the proteome.

The paper presents the cryo-EM structure of HUWE1, revealing its modular architecture and its role in degrading cell-fate decision factors.