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Elucidating the interactions between serum protein-bound nanoparticles and cell-surface receptors typically operates on a per protein–receptor interaction basis. Integration of omic approaches for testing thousands of interactions unbiasedly reveals important interactions that drive cellular uptake of nanoparticles.
Cas12f1 is a member of type V Cas12 family, which has a hypercompact size. A Cas12f1-based adenine base editor has now been developed that is small enough to be loaded into a single AAV vector without compromising editing activity.
In the post-genomic era, many genes and regulatory elements remain uncharacterized, including riboswitches — RNA structures that control gene expression by directly binding metabolites. Here, a new type of metal-responsive riboswitch that senses sodium cations expands the bacterial Na+ metabolic repertoire.
Biomolecular condensates form and dissolve in response to a wide range of signals. A new study reports a solubility-based phosphoproteome-profiling approach, which uncovers the extensive role of phosphorylation in regulating protein partitioning into condensates across the human proteome.
Chemical probes are powerful tools for the discovery of ligand-binding and drug-target sites on proteins. A new software helps to profile their performance in chemoproteomic applications.
Mutant-selective KRAS-targeting drugs hold great promise for the treatment of some of the most aggressive forms of cancer. Building on the breakthrough success of KRAS-G12C inhibitors, researchers have now found a way to target another mutant KRAS with serine-modifying covalent inhibitors.
A directed evolution approach delivers ribosomes with highly functional tethered subunits. Combining the decoding and peptidyl transferase activities of the ribosome into a single entity sets the scene for more efficient protein engineering technologies.
The Hippo pathway is a key regulator of tissue homeostasis, organ size and cancer. Identification of microcolin B and its analog molecules as Hippo pathway activators connects PtdIns4P-dependent lipid signaling with the Hippo pathway, suggesting potential targets for cancer therapy.
Antigen loading onto class I major histocompatibility complex (MHC-I) proteins relies on chaperones and protein flexibility. Researchers now provide new insight into the process, especially for the intriguing ‘non-classical’ MHC-I protein MR1, with implications for fundamental immunology and the development of novel immunotherapies.
Carbon dioxide (CO2) is a product of cellular respiration that can also serve as a post-translational modification (PTM) through covalent protein modification. A new chemoproteomic strategy enables the capture of functional CO2-dependent carboxylation on lysine residues of proteins.
The rising threat of antifungal resistance means that alternative therapeutics need to be considered. New research explores the biochemical basis of virulence inhibition by mucus glycans against the fungal pathogen Candida albicans.
A fungal ten-eleven translocation (TET) dioxygenase homolog, CcTet, is found to have both 5-methylcytosine (5mC) and N6-methyladenine (6mA) demethylase activity. Structure-based engineering of CcTet yielded a 6mA-specific demethylase, offering a useful tool for the manipulation and functional study of 6mA.
The discovery of long-existing terpenoid biosynthetic pathways in soft corals changes the way specialized metabolism in animals is thought about, and opens unprecedented access to the largely untapped treasure trove of medicinal marine natural products.
Controlling kinase inhibitors’ residence time via reversible covalent binding is of high interest in drug discovery. Tuning reversible covalent binding kinetics using a pan-kinase inhibitor that reacts with the catalytic lysine enabled exquisite temporal selectivity in vitro and in vivo.
Protein arginine methyltransferases (PRMTs) are overexpressed in many cancer types, including triple-negative breast cancer (TNBC). A new study shows that a reversible inhibitor of type I PRMTs suppresses TNBC tumor growth by inducing a viral mimicry response with retained introns.
Natural enzyme complexes can rapidly change configurations to respond to intracellular cues. Now CRISPR enzymes and programmable RNA scaffolds allow synthetic enzyme complexes to be assembled and disassembled on demand.
Microproteins can be generated by a shift in the reading frame during translation. A chemoproteomics approach led to the identification of MINAS-60 as an alternative microprotein that regulates the assembly of the pre-60S ribosome.
The cryo-electron microscopy structure of a fluoroquinolone efflux transporter, NorA, in complex with an antibody fragment provides a new strategy whereby peptide inhibitors derived from antibody loops could be used to block antibiotic efflux in a drug-resistant superbug.
Chemoproteomics reveals a cysteine oxidation event that inhibits the maturation process of a lysosomal protease, enabling its secretion into the extracellular space during infection-induced tumorigenesis. A recent study offers a new mechanistic paradigm for redox-dependent regulation of protein trafficking.
Precision oncology requires an understanding of the genes and pathways that dictate therapeutic response. Through specialized analysis of drug sensitivity patterns across hundreds of genomically annotated cancer cell lines, specific and actionable drivers of intrinsic resistance have been identified.
