Furin at the cutting edge: From protein traffic to embryogenesis and disease
By G. Thomas. Nature reviews. Molecular cell biology, 2002
1,210 citations recorded by the source corpus.
Subfields: Biotechnology, Cell Biology
View Paper: https://www.semanticscholar.org/paper/383fa9c0ae7c32a6f5dabdb77e407892c3b2e718
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Citations in the corpus
- Fusion Protein Linkers: Property, Design and Functionality (2012, background): “Furin is mainly localized in the trans-golgi network (TGN) and also recycles between TGN, early endosomes, and the cell surface [69].”
- Control of matrix metalloproteinase catalytic activity. (2007, background): “Furin is a type 1 membrane, subtilisin-like serine protease present in the trans-Golgi network (Thomas, 2002), and thus, MMPs with a furin cleavage site are processed intracellularly before secretion (Illman et al., 2003;Kang et al., 2002;Pei and Weiss, 1995;Sato et al., 1996).”
- Neurotrophin secretion: current facts and future prospects. (2003, background): “The second group consists of PACE4, PC5/6B, PC7, and furin, which mostly contain a single transmembrane domain near the C-terminus and which are selectively found in the TGN, endosomes, and in rare cases also in constitutive secretory vesicles (Zhou et al., 1999; Thomas, 2002).”
- Feature-based prediction of non-classical and leaderless protein secretion. (2004, background): “This is puzzling, since propeptide cleavage usually takes place in secreted proteins (Thomas, 2002).”
- Host cell proteases: critical determinants of coronavirus tropism and pathogenesis (2014, background): “Because furin can be viewed as a representative PC (Thomas, 2002), and because it is the most frequently characterized PC to be involved in processing and activating coronavirus S proteins, we will focus on this protease.”
- Middle East Respiratory Syndrome Coronavirus: Another Zoonotic Betacoronavirus Causing SARS-Like Disease (2015, background): “Furin and furin-like proprotein convertases are broadly expressed serine endoproteases that cleave the multibasic motifs RX(R/K/X)R and process proproteins into their biologically active forms (55).”