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The ease of preparation and scale-up makes this protein delivery platform attractive for clinical translation.
The exclusive expression of E7, a viral oncogene, in infected cells makes this protein an ideal target for immunotherapy.
QR1's ability to bioactivate quinones and its elevated expression in many human solid tumors makes this protein an excellent target for enzyme-directed drug development.
The molecular orientation makes this protein form a semi-crystalline structure which contains two phases: highly crystalline antiparallel β-sheet structure and non-crystalline part (Wang et al. 2004).
Mice carrying a mutation in the gene that makes this protein have fewer mature T cells than normal mice.
Moreover, the diversity of regulatory mechanisms that have been unravelled by structural studies makes this protein family still a very interesting target for structural investigations.
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Because people make this protein in their own bodies, no one is allergic to it.
One DNA molecule encodes a protein found in the myelin sheath; the first-responders make this protein, which acts as bait for the rogue immune cells.
It shows a high content of essential amino acids, making this protein important from a nutritional viewpoint.
The more exposed structure and the absence of the disulfide bridge in the short form could make this protein more susceptible to degradation.
After further investigation, they determined that the protein binds to SAM and indirectly gauges the pool of available methionine, making this protein — SAMTOR — a specific and unique nutrient sensor that informs the mTOR pathway.
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Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com