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Upon cellular cholesterol depletion, SREBP leaves the ER to reach the Golgi, where cleavage by site-1 protease (S1P) releases the amino-terminal half of SREBP, which can be further cleaved within its membrane-spanning helix by site-2 metalloproteinase (S2P; Brown & Goldstein, 1999).
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C99 can be further cleaved by BACE1 at its Glu site to produce C89 [ 70].
The 65 kDa core protein can be further cleaved by a furin-like convertase into a 40 kDa protein.
In 4C procedure, the fragment is further cleaved by a second restriction enzyme and subsequently religated to form DNA circles.
P1 is further cleaved into the structural proteins VP4, VP2, VP3 and VP1.
APP is cleaved by β-secretase resulting in the generation of the C-terminal fragment C99, which is further cleaved by the γ-secretase complex generating different Aβ species.
In the cytoplasm, these pre-miRNAs are further cleaved by the endonuclease (Dicer) generating mature miRNAs.
The bulk of APP is cleaved by α-secretase within the A β-domain to produce a C-terminal fragment, which can be further cleaved intramembranously by γ-secretase to produce the peptide P3 and the transcriptionally active APP intracellular domain [ 22].
This is then further cleaved to unspecific hydrocarbons and N-containing hydrocarbons.
In 22Rv1, cytochrome c is released, caspases are activated and PARP is cleaved, within 24 h.
Exochitinases can be further divided into two subcategories: chitobiosidases, which cleave diacetylchitobiose units from the non-reducing end of the chitin chain, and β- 1,4 -N-acetyl-glucosaminidases (NAGase), which cleave the N-acetylglucosamine (NAG) oligomers, generating NAG monomers.
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