ArticleProteins2009
Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.
Article in Proteins, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- Real-time visualization of collagen assembly uncovers metastable properties in hierarchical organization.Nature communications · 2026Article
- Neuroprotective Potential of Indole-Based Compounds: A Biochemical Study on Antioxidant Properties and Amyloid Disaggregation in Neuroblastoma Cells.Antioxidants (Basel, Switzerland) · 2024Article
- Effects of proline substitution/inclusion on the nanostructure of a self-assembling β-sheet-forming peptide.RSC advances · 2024Article
- The Dynamic Interactions of a Multitargeting Domain in Ameloblastin Protein with Amelogenin and Membrane.International journal of molecular sciences · 2023Article
- Self-assembly study of type I collagen extracted from male Wistar Hannover rat tail tendons.Biomaterials research · 2020Article
- Identification of Key Functional Motifs of Native Amelogenin Protein for Dental Enamel Remineralisation.Molecules (Basel, Switzerland) · 2020Review
- Article
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- Ameloblastin peptide encoded by exon 5 interacts with amelogenin N-terminus.Biochemistry and biophysics reports · 2016Article
- Interactions of amelogenin with phospholipids.Biopolymers · 2015Article
- Amelogenin in Enamel Tissue Engineering.Advances in experimental medicine and biology · 2015Article
- Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micelles.Biopolymers · 2014Article
- Localization and quantitative co-localization of enamelin with amelogenin.Journal of structural biology · 2013Article
- CryoTEM study of effects of phosphorylation on the hierarchical assembly of porcine amelogenin and its regulation of mineralization in vitro.Journal of structural biology · 2013Article
- Self-assembly of filamentous amelogenin requires calcium and phosphate: from dimers via nanoribbons to fibrils.Biomacromolecules · 2012Article
- Structural changes in amelogenin upon self-assembly and mineral interactions.Journal of dental research · 2012Article
- Protein-mediated enamel mineralization.Frontiers in bioscience (Landmark edition) · 2012Review
- The role of amelogenin during enamel-crystallite growth and organization in vivo.European journal of oral sciences · 2011Article
- Phosphorylation of human small heat shock protein HspB8 (Hsp22) by ERK1 protein kinase.Molecular and cellular biochemistry · 2011Article
- Probing the self-association, intermolecular contacts, and folding propensity of amelogenin.Protein science : a publication of the Protein Society · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Amelogenin is a proline-rich enamel matrix protein known to play an important role in the oriented growth of enamel crystals. Amelogenin self-assembles to form nanospheres and higher order structures mediated by hydrophobic interactions. This study aims to obtain a better insight into the relationship between primary-secondary structure and self-assembly of amelogenin by applying computational and biophysical methods. Variable temperature circular dichroism studies indicated that under physiological pH recombinant full-length porcine amelogenin contains unordered structures in equilibrium with polyproline type II (PPII) structure, the latter being more populated at lower temperatures. Increasing the concentration of rP172 resulted in the promotion of folding to an ordered beta-structured assembly. Isothermal titration calorimetry dilution studies revealed that at all temperatures, self-assembly is entropically driven due to the hydrophobic effect and the molar heat of assembly (DeltaH(A)) decreases with temperature. Using a computational approach, a profile of domains in the amino acid sequence that have a high propensity to assemble and to have PPII structures has been identified. We conclude that the assembly properties of amelogenin are due to complementarity between the hydrophobic and PPII helix prone regions.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.