Biochemical and Structural Characterization

This paper introduces a programmable protein editing platform using split intein-mediated recombination to enable precise modification of mature proteins in living cells.

This paper investigates AbpX, a microbial biomatrix protein that forms thermostable hydrogels through calcium ion-dependent self-assembly and provides an atomic model of its fibril lattice.

The paper uses machine learning to engineer conditional split inteins for light-controlled protein splicing in mammalian cells.

This paper introduces split inteins to enable modular NRPS engineering, generating 324 hybrid NRPS and over 200 novel peptides through combinatorial transformation.

The paper introduces CHalo reagents that conditionally ligate to HaloTag proteins, enabling light- or enzyme-triggered labeling, protein recruitment control, and enzyme activity recording.

The paper reports the cryo-EM structure of the RP4 conjugation pilus, revealing it is functional without phospholipid modification, challenging previous assumptions about pilus biogenesis.

The paper introduces a method to control protein activity through dimerization-based conditional reconstitution, demonstrating its application in inducing cell death, virus detection, and immune cell stimulation.

This study identifies distinct molecular mechanisms for DNA-binding by competence T4P in Gram-positive and Gram-negative bacteria using Streptococcus pneumoniae as a model.

This paper develops a system for anchoring and controlled release of proteins in Chlamydomonas reinhardtii using GP1 PPSPX motifs and pH-sensitive inteins.

This study investigates how thioamide substitutions in SpyTag affect ligation kinetics with SpyCatcher, showing both faster and slower complex formation depending on substitution position.

This paper introduces a protein actuator platform that performs Boolean logic operations on cell surfaces using proximity-gated trans-splicing, enabling selective recruitment of enzymatic and cytotoxic activities to specific cells.

The paper identifies Ffp1 as the sole fimbrillin in Porphyromonas species, showing it is ancestral and structurally similar to Bacteroides ovatus fimbrillin.

The paper uses LanM enzymes and leader peptides to modify D-Ala in GLP-1 and GLP-2 in E. coli, showing how precursor design affects modification patterns.

The paper identifies new split sites in Npu DnaE and gp41-1 inteins, enabling functional three-piece versions for biotechnological applications.

The paper identifies myxosortases as proteases processing C-terminal sorting signals with invariant cysteine residues in bacteria.

The paper improves the signal peptide of the Ag43 autotransporter in E. coli to enhance surface display of sfGFP using epPCR and single-cell sorting.

This paper develops a DNA-encoded method to display multivalent proteins on phage and demonstrates its use to study in vivo clearance rates of L-asparaginase.

This paper introduces IBM, a method that systematically splits proteins into logic gates using inteins, enabling inducible control of protein function.

This study investigates how SrtA inhibitors' activity depends on the closed lid conformation of SrtA from Bacillus anthracis through molecular dynamics and docking analyses.