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The development of a genetic code expansion-based system enables fast protein expression in response to a noncanonical amino acid. The system was implanted into diabetic mice to rescue hyperglycemia with oral delivery of the amino acid.
Discovery of a chemical probe targeting the PWWP domain of NSD2 reveals insight into mechanisms that govern NSD2 localization. The compound and its negative control represent valuable tools for further defining NSD2 biology.
Glyco-PAINT, a super-resolution microscopy approach that images fluorescently tagged glycan interactions with lectins, enables the measurement of sugar–lectin complex densities, residence times and diffusion on cell surfaces.
Mass spectrometric profiling of a glycan library reveals that sialylated glycans, especially sialic acid-containing gangliosides, interact with the RBD of the SARS-CoV-2 spike protein and are involved in ACE2-dependent viral infection.
During the biosynthesis of triacsin, the two N–N bond formation reactions necessary to create the unique N-hydroxytriazene moiety are catalyzed by a glycine-utilizing hydrazine-forming enzyme and a nitrite-utilizing N-nitrosating enzyme.
Post-translational site-selective formation of boronoalanine in proteins enables applications of boron for binding partner capture, footprinting of interactions with reactive oxygen species, proteolytic control and mapping of transient structures.
Structural analysis of the Pepper aptamer in complex with its cognate HBC or HBC-like color variants reveals that it binds fluorophore molecules via one non-G-quadruplex base quadruple and one noncanonical G·U base pair.
Determination of the cryo-EM structures of active neurokinin-1 receptor bound to substance P or the Gq biased peptide SP6–11 reveals that interactions with the receptor extracellular loops regulate G protein signaling selectivity.
CRISPR–Cas9 genome editing is limited in organisms with inefficient homology-directed repair (HDR), but development of a specialized CRISPR platform conferred increased HDR rates in four noncanonical yeasts to enhance strain engineering.
An approach relying on guide RNA pairs encoding the same edits in both sense and antisense DNA strands is developed to improve the editing capability of prime editing in human cells.
Surface protein tagging and mass spectrometry-based proteomics applied in a rabbit cholera model system identifies proteins involved in Vibrio cholera-host cell interactions and defines a cholera toxin-dependent role for host surfactant protein D.
Trivalent PROTACs are reported as a strategy to increase protein degradation efficacy and therapeutic window by combining avidity of target engagement with cooperativity to form highly favorable and productive ternary complexes.
CoraFluors, a class of macrocyclic terbium complexes for use in time-resolved FRET, exhibit physicochemical properties desirable for biological studies, including characterization of Keap1 ligands and HDAC1 target engagement profiling in live cells.
The development of split-engineered base editors (seBEs) enables small-molecule control over DNA deaminase activity, decreasing off-target effects and offering a generalizable solution for temporal control over precise genome editing.
Using short-read sequencing data, Evoracle reconstructs full-length genotypes and fitness during directed evolution experiments, and can identify low-frequency variants before they can be identified using consensus mutations.
TIP60-mediated crotonylation of the microtubule plus-end tracking protein EB1 at Lys66 regulates attachment of astral microtubules to the lateral cell cortex and spindle positioning.
Partial antagonists of the ER transmembrane kinase/endoribonuclease IRE1ɑ were identified that preserve splicing of downstream RNA substrates such as XBP1, enabling cellular survival.
Structures of human cholecystokinin receptors in complex with various ligands or G-proteins reveal how different ligand types are recognized and the basis of peptide selectivity in this receptor family, and suggest a stepwise activation mechanism.
Structural characterization of three paralogous toxin–antitoxin complexes illuminates how each antitoxin specifically targets its cognate toxin, including auxiliary neutralization interfaces that confer evolvability while preventing loss of activity.
Cryo-EM structures of sulfated cholecystokinin 8 bound to the cholecystokinin A receptor in complex with Gs, Gi and Gq heterotrimers reveal structural determinants for G-protein coupling selectivity.