“Multiplex” rheostat positions cluster around allosterically critical regions of the lactose repressor protein
Leonidas E. Bantis(University of Kansas Medical Center), Liskin Swint‐Kruse(University of Kansas Medical Center)
Cited by 6
Related Papers
Identification of a covert evolutionary pathway between two protein folds
|Nature Communications|2023|34
Rheostat positions: A new classification of protein positions relevant to pharmacogenomics
|Medicinal Chemistry Research|2020|29
Reconciling <i>in vitro</i> and <i>in vivo</i> activities of engineered, LacI-based repressor proteins: Contributions of DNA looping and operator sequence variation
|bioRxiv (Cold Spring Harbor Laboratory)|2018|1
Dissecting the effects of single amino acid substitutions in <scp>SARS</scp>‐<scp>CoV‐2</scp> Mpro
|Protein Science|2025|1
The intrinsically disordered transcriptional activation domain of CIITA is functionally tuneable by single substitutions: An exception or a new paradigm?
|bioRxiv (Cold Spring Harbor Laboratory)|2023|0