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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.
The more exposed structure and the absence of the disulfide bridge in the short form could make this protein more susceptible to degradation.
These properties make this protein an attractive candidate for single-molecule force spectroscopy (smFS) studies, which, to our knowledge, have been previously conducted for just two other ultrafast folders (villin18 and α3D19).
From my perspective, the next step is not to discuss how we can make this protein into a profitable pill, but rather to discuss how we can become more active in our day-to-day lives.
These properties, combined with the small, monomeric, cysteine-free and highly stable structure of FNfn10-3JCLI4, makemake this protein useful in future applications involving detection and targeting of αvβ3-positive cells.
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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.
It shows a high content of essential amino acids, making this protein important from a nutritional viewpoint.
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.
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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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com