ArticleBiochemistry2016
Deletion of the N- or C-Terminal Helix of Apolipophorin III To Create a Four-Helix Bundle Protein.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.
- Impact of statin use on cancer-specific mortality and recurrence: A meta-analysis of 60 observational studies.Medicine · 2020Pooled it
- Insights into the C-terminal domain of apolipoprotein E from chimera studies with apolipophorin III.Molecular and cellular biochemistry · 2023Article
- Purification and membrane interactions of human KCNQ1Biochimica et biophysica acta. Biomembranes · 2022Article
- Vitamin E Derivative with Modified Side Chain Induced Apoptosis by Modulating the Cellular Lipids and Membrane Dynamics in MCF7 Cells.Cell biochemistry and biophysics · 2021Article
- Terminal Peptide Extensions Augment the Retinal IMPDH1 Catalytic Activity and Attenuate the ATP-induced Fibrillation Events.Cell biochemistry and biophysics · 2021Article
- A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.Cell biochemistry and biophysics · 2021Review
- Fragments ofBBA advances · 2021Article
- Structural and Functional Characterisation of the Domains of Ubiquitin-Activating Enzyme (E1) of Saccharomyces cerevisiae.Cell biochemistry and biophysics · 2020Article
- The membrane protein KCNQ1 potassium ion channel: Functional diversity and current structural insights.Biochimica et biophysica acta. Biomembranes · 2020Review
- Lipoprotein Particle Formation by Proapoptotic tBid.Biophysical journal · 2018Article
- Expression of the C-terminal domain of human apolipoprotein A-I using a chimeric apolipoprotein.Protein expression and purification · 2017Article
- Transfer of C-terminal residues of human apolipoprotein A-I to insect apolipophorin III creates a two-domain chimeric protein with enhanced lipid binding activity.Biochimica et biophysica acta. Biomembranes · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Apolipophorin III (apoLp-III) is an exchangeable apolipoprotein found in insects and plays an important function in lipid transport. The protein has an unusual five-helix bundle architecture, deviating from the common four-helix bundle motif. To understand the role of the additional helix in apoLp-III, the N-terminal or C-terminal helix was deleted to create a putative four-helix bundle protein. While the protein lacking helix-1 could be expressed in bacteria albeit at reduced yields, apoLp-III lacking helix-5 could not be produced. Mutational analysis by truncating helix-5 showed that a minimum segment of approximately one-third of the C-terminal helix is required for protein expression. The variant lacking helix-5 was produced by inserting a methionine residue between helix-4 and -5; subsequent cyanogenbromide cleavage generated the four-helix variant. Both N- and C-terminal helix deletion variants displayed significantly reduced helical content, protein stability, and tertiary structure. Despite the significantly altered structure, the variants were still fully functional. The rate of dimyristoylphosphatidylcholine vesicle solubilization was enhanced 4-5-fold compared to the wild-type protein, and the deletion variants were effective in binding to lipolyzed low density lipoprotein thereby preventing lipoprotein aggregation. These results show that the additional helix of apoLp-III is not essential for lipid binding but is required for proper folding to keep the protein into a stable conformation.
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Registered trials
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