Shabaz Mohammed

This study reveals a covalent mechanism in a bifunctional glycosyltransferase for hexosyl transfer and reports a novel self-priming function for polymerization.

The paper evaluates photon- and electron-based fragmentation methods for glycopeptide analysis using Omnitrap-LCMS, finding UVPD and EID provide detailed structural information comparable to traditional methods.

This study identifies 104 cellular RNA-binding proteins within HIV-1 particles, revealing their role in viral gene expression and infectivity through interactions with HIV-1 genomic RNA.

The paper develops an improved method to capture ribosome-associated proteins and shows viral infections remodel these proteins in a virus-specific manner, with functional implications for viral propagation.

This study shows that RSV forms condensates by pre-assembling replication centers within viral particles, explaining infection heterogeneity and enabling efficient replication without requiring pre-existing condensates.

This paper develops a high-throughput method to discover a novel photochemical reaction for editing protein side chains and using it to probe protein function through combined photochemical and photophysical approaches.

The paper evaluates nonporous C-18 stationary phases in proteomics workflows, finding they provide comparable or superior performance to traditional porous particles in separation and sensitivity.

This paper introduces FIRESCAPE, a radiolabeling method to study extracellular histone H3 clearance and effects, revealing distinct behaviors compared to intact nucleosomes.

This study identifies 283 RNA-binding proteins whose activity changes in tick cells infected with Uukuniemi virus, revealing new host-virus interactions and a method to silence gene expression in tick cultures.

This study identifies RNA-binding proteins regulated by type I IFN, revealing a new layer of antiviral response involving post-translational regulation of RNA binding.

The paper develops a deep learning model that integrates multiple fragmentation techniques into standard LC-MS workflows, improving proteome coverage and identification rates.

The paper identifies protein networks associated with virus-permissive and hostile cellular states through multi-omics analysis, revealing discrepancies between mRNA and protein levels and the role of phosphorylation in infection control.

This paper introduces a method to track neurodegeneration biomarkers using PET imaging with isosteric protein mimics, revealing spinal fluid dynamics and neuronal loss mechanisms.

The paper shows that XRN1-mediated RNA decay provides nucleotides for alphavirus replication by recycling monophosphate nucleotides through the salvage pathway.

The paper develops a method to efficiently remove over-labelled peptides in proteomics samples, improving identification rates and quantitation precision.

The paper describes a 2D chromatography system for proteomics that improves coverage and intensity with nanogram-scale samples, showing benefits for phosphoproteomics and pull-down experiments.

The paper characterizes an Omnitrap-Orbitrap mass spectrometer with multiple ion activation methods, showing its versatility in peptide and protein analysis.

This paper describes a light-mediated method for stereoretentive post-translational protein editing that generates site-selectively edited proteins with full stereochemistry retention.

The paper identifies Mub1 as an RNA-binding protein that regulates exosome-dependent mRNA degradation, affecting stress response and gene expression.

This study shows that SIK1 activity modulates synaptic phosphoproteome to induce sleep independently of sleep pressure, revealing a causal mechanism for sleep regulation.

This study identifies flg22-responsive RNA-binding proteins in Arabidopsis, revealing their role in plant immunity and uncovering novel immune components.

The paper uses poly(A)+ RNA-protein crosslinking data in fission yeast to analyze RNA-protein complexes and their functional organization.

The paper investigates how RNA-binding proteins (RBPs) change in response to viral infection and identifies RBPs crucial for viral replication.