Norman E. Davey

The paper identifies a non-canonical helical binding motif in MAD1 that specifically interacts with Cyclin B1 to recruit CDK1 to the SAC, revealing a mechanism for B-type cyclin recognition.

This paper develops a stable RPE1 cell line with inducible and dose-dependent transgene expression using CRISPR/Cas9 and FRT/Tet-On systems, validated through multi-omics analysis.

The paper identifies pH-sensing amyloid core motifs in yeast and human proteomes, showing they enable reversible protein assembly under stress.

This study identifies ZATT/ZNF451 as a key factor in resolving stalled TOP2 cleavage complexes without relying on TDP2, proteolysis, or DSB repair pathways.

The paper maps over 20,000 human protein-protein interactions mediated by short linear motifs using a peptide library screening approach.

The paper systematically identifies SLiM-binding interactions of USP family auxiliary domains using proteomic and biochemical methods, revealing functional redundancy and motif specificity.

The paper screens peptide-binding pockets across cancer cell lines to identify therapeutic vulnerabilities and dependencies, finding that peptide inhibition can reveal hidden dependencies and enhance drug efficacy.

The paper systematically assesses the function of short linear motifs (SLiMs) by mutating and screening them in human cells, identifying essential SLiMs for cell proliferation and uncovering novel classes and binding partners.

This study identifies POLE2 as a general NPF-motif receptor, revealing its role in recruiting proteins involved in replication, DNA repair, and transcription through SLiM-mediated interactions.

The paper identifies and characterizes cyclin-CDK docking motifs through high-throughput peptide binding assays and structural analysis, revealing a broader repertoire of motif types and binding mechanisms.

This study uses phage-based deep mutational scanning to identify binding determinants of short linear motifs between human and SARS-CoV-2 proteins, refining motifs and identifying affinity-enhancing mutations.

This study presents a proteomic and phosphoproteomic analysis of the human cell cycle in non-transformed cells, revealing new insights into cell cycle-dependent protein and phosphorylation oscillations.

The paper identifies CYB5R4 as an evolutionarily conserved reductase that activates PP4 and PP6 by reducing their catalytic metal ions, essential for cell viability under oxidative stress.

The paper introduces SIMBA, a functional assay to quantify SLiM binding, showing in vivo binding strength correlates with in vitro affinity and revealing context-dependent recognition determinants.

The paper characterizes how disease mutations in intrinsically disordered regions modulate protein interactions mediated by short linear motifs, identifying both loss and gain of interactions.

This study benchmarks five motif discovery tools and seven sequence alignment tools on their ability to find short linear motifs in peptides, identifying DEME, SLiMFinder, and Opal as top performers.

This study identifies catalytic and non-catalytic functions of DNA polymerase kappa in translesion DNA synthesis using CRISPR screening and TLS analysis.

The paper identifies SARS-CoV-2 protein domains that interact with human peptides and discovers antiviral peptides targeting Nsp9 and Nsp16.

The paper evaluates 43 methods for predicting intrinsically disordered regions and binding regions in proteins, finding that deep learning methods outperform older physicochemical approaches but binding prediction remains challenging.

The paper analyzes fungal G1 cyclin docking motifs to determine their sequence features and regulatory potency in vivo.

The paper identifies conserved SQ and QS motifs in bacterial effectors that may mimic ATM kinase substrates, suggesting a mechanism by which pathogens modulate host signaling during infection.