Interacting recruitment domains bring methylation and repressor fusions together to improve recruitment efficiency and target gene inhibition.
A single polypeptide combines target recognition, DNA cleavage, and reverse transcription to insert longer sequences at defined genomic sites.
Adenine deaminase fusion proteins pair catalytic editing with nucleic acid targeting for precise A-T to G-C conversion in eukaryotic cells.
MMR inhibition with MLH1dn or nearby silent mutations helps prime editing increase efficiency while reducing indel byproducts.
Fusion proteins pair DNA-binding domains with methyltransferases to modify gene regulation without double-strand breaks or indels.
Interacting recruitment domains address weak recruitment and limited modification range by pairing DNA methylation and repressor fusions for target gene inhibition.
CRISPR-Cas fusion proteins target multiple HBV DNA sites to repress viral transcription and reduce replication and protein levels.
Combining Pfu, KOD, T4, and phi29 domains balances proofreading fidelity, processivity, amplification speed, and inhibitor tolerance in PCR.
A compact Casδ endonuclease addresses large CRISPR proteins and multi-RNA guidance through a truncated catalytic core for precise editing.
Modular PPR repeats recognize target ssDNA sequences, enabling programmable gene-expression regulation beyond natural ssDNA-binding proteins.