ArticleThe EMBO journal1992
Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 50 citations in OpenAlex.
- The interplay of helminthic neuropeptides and proteases in parasite survival and host immunomodulation.Biochemical Society transactions · 2022Review
- Synthesis, cloning and expression of a novel pre-miniproinsulin analogue gene in Escherichia coli.Journal of advanced research · 2015Article
- Genetics of the first seven proprotein convertase enzymes in health and disease.Current genomics · 2013Article
- Deorphanization of novel peptides and their receptors.The AAPS journal · 2010Review
- Processing of peptide and hormone precursors at the dibasic cleavage sites.Cellular and molecular life sciences : CMLS · 2009Review
- Two cleavage products of the Drosophila accessory gland protein ovulin can independently induce ovulation.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Effects of L- and D-REKR amino acid-containing peptides on HIV and SIV envelope glycoprotein precursor maturation and HIV and SIV replication.The Biochemical journal · 2002Article
- Temperature-induced conformational changes in prosomatostatin-II: implications for processing.The Biochemical journal · 1998Article
- Sequence requirements for proinsulin processing at the B-chain/C-peptide junction.The Biochemical journal · 1995Article
- Structure determination of a tetradecapeptide mimicking the RXVRG consensus sequence recognized by a Xenopus laevis skin endoprotease: an approach based on simulated annealing and 1H NMR.Journal of computer-aided molecular design · 1995Article
- Sorting and processing of secretory proteins.The Biochemical journal · 1994Review
- Expression of mutant ELH prohormones in AtT-20 cells: the relationship between prohormone processing and sorting.The Journal of cell biology · 1993Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bioactivation of pro-proteins by limited proteolysis is a general mechanism in the biosynthesis of hormones, receptors and viral protein precursors. This proceeds by cleavage of peptide bonds at the level of single or pairs of basic residues in the proforms. Examination of a number of cleavage loci in various precursors failed to reveal any consensus primary sequence around the dibasic cleavage sites. Thus it has been proposed, on the basis of secondary structure predictions [Rholam, M., Nicolas, P. and Cohen, P. (1986) FEBS Lett., 207, 1-6], that those basic residues which operate as signal loci for the proteolytic enzyme machinery are situated in, or next to, privileged precursor regions most often constituted by flexible and exposed motifs, e.g. beta-turns and/or loops. Peptides reproducing the N-terminal processing domain of the hormone precursor, pro-ocytocin-neurophysin, were examined by a combination of spectroscopical techniques including circular dichroism, infrared Fourier transform and one- and two-dimensional proton NMR. The results indicate that: (i) the region situated on the N terminus of the Lys-Arg doublet is organized as a beta-turn in solution; (ii) the sequential organization of the residues participating in the beta-turn determines the privileged relative orientation of the basic amino acid side chains and the subtype of turn; (iii) the peptide segment situated on the C-terminal side of the dibasic, corresponding to the N-terminal octapeptide of neurophysin, is organized as an alpha-helix.(ABSTRACT TRUNCATED AT 250 WORDS)
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