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Herein we describe the development of a novel engineered TEVp mutant designed to be active in the secretory pathway.
This growth arrest can be rescued by exogenous expression of the fusion and a mutant designed to prevent translation of the ELK4 protein.
Bungarus fasciatus acetylcholinesterase (BfAChE) was engineered to acquire organophosphate hydrolase (OPase) activity by reproducing the features of the human butyrylcholinesterase G117H mutant, the first mutant designed to hydrolyse OPs.
To study the role of AKAP5 in behavior and synaptic plasticity, we created two AKAP5 mutant lines of mice, a null allele, or knockout (KO) and an AKAP5 mutant designed to express a truncated protein missing the PKA binding domain (D36).
The mutant designed to knock out binding mode A (Q1), showed a single event probability of ~77%, and a double event probability of ~23%.
A mutant unable to hydrolyse ATP (K304A in the Walker A box) and a mutant designed to abrogate the nuclease activity (D10A/E12A) were generated by directed mutagenesis.
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We investigated four new λ6 85⁎ mutants designed to fold especially rapidly.
Influenza haemagglutinin (HA) and HA-derived mutants designed to locate primarily to secretory or endocytic membranes were present in PLD1-positive membranes.
Here, we describe the analysis of the pH-dependent stability of 13 mutants designed to probe the nature of the Lys12 denatured state interaction.
Recently, functional analysis of a series of site-specific mutants, designed to mimic missense mutations found in ATP2C1, uncovered specific defects in Ca2+ and/or Mn2+ transport and protein expression in mutant hSPCA1 polypeptides.
Mutants designed to impeded cell-to-cell movement failed to accumulate at PD indicating that basic residues in both R1 and R2 are critical for binding the MP at PD.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com