ArticleBiophysical journal2008
The structure and orientation of the C-terminus of LRAP.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.
- Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review.International journal of molecular sciences · 2021Pooled it
- Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing.International journal of molecular sciences · 2023Review
- Biomedical applications of solid-binding peptides and proteins.Materials today. Bio · 2023Review
- Binding Mode Characterization of Osteopontin on Hydroxyapatite by Solution NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2021Article
- Solid-State NMR and MD Study of the Structure of the Statherin Mutant SNa15 on Mineral Surfaces.Journal of the American Chemical Society · 2019Article
- Meeting report: a hard look at the state of enamel research.International journal of oral science · 2017Article
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- Solid-state NMR studies of proteins immobilized on inorganic surfaces.Solid state nuclear magnetic resonance · 2015Review
- The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength.Frontiers in physiology · 2014Article
- Phosphorylation and ionic strength alter the LRAP-HAP interface in the N-terminus.Biochemistry · 2013Article
- Neutron reflectometry studies of the adsorbed structure of the amelogenin, LRAP.The journal of physical chemistry. B · 2013Article
- Biophysical characterization of synthetic amelogenin C-terminal peptides.European journal of oral sciences · 2012Article
- Leucine-rich amelogenin peptides regulate mineralization in vitro.Journal of dental research · 2011Article
- Single-molecule determination of the face-specific adsorption of Amelogenin's C-terminus on hydroxyapatite.Angewandte Chemie (International ed. in English) · 2011Article
- Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite.The journal of physical chemistry. C, Nanomaterials and interfaces · 2011Article
- Potential role of the amelogenin N-terminus in the regulation of calcium phosphate formation in vitro.Cells, tissues, organs · 2011Article
- Toward a structure determination method for biomineral-associated protein using combined solid- state NMR and computational structure prediction.Structure (London, England : 1993) · 2010Article
- A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein).Biochimica et biophysica acta · 2010Article
- Sum frequency generation and solid-state NMR study of the structure, orientation, and dynamics of polystyrene-adsorbed peptides.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces.Journal of structural biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Amelogenin is the predominant protein found during enamel development and is thought to be the biomineralization protein controlling the unique elongated hydroxyapatite crystals that constitute enamel. The secondary structure of biomineralization proteins is thought to be important in the interaction with hydroxyapatite. Unfortunately, very little data are available on the structure or the orientation of amelogenin, either in solution or bound to hydroxyapatite. The C-terminus contains the majority of the charged residues and is predicted to interact with hydroxyapatite; thus, we used solid-state NMR dipolar recoupling techniques to investigate the structure and orientation of the C-terminus of LRAP, a naturally occurring splice variant of full-length amelogenin. Using (13)C{(15)N} Rotational Echo DOuble Resonance (REDOR), the structure of the C-terminus was found to be largely random coil, both on the surface of hydroxyapatite as well as lyophilized from solution. The orientation of the C-terminal region with respect to hydroxyapatite was investigated for two alanine residues (Ala(46) and Ala(49)) using (13)C{(31)P} REDOR and one lysine residue (Lys(52)) using (15)N{(31)P} REDOR. The residues examined were found to be 7.0, 5.7, and 5.8 A from the surface of hydroxyapatite for Ala(46), Ala(49), and Lys(52), respectively. This provides direct evidence that the charged C-terminus is interacting closely with hydroxyapatite, positioning the acidic amino acids to aid in controlling crystal growth. However, solid-state NMR dynamics measurements also revealed significant mobility in the C-terminal region of the protein, in both the side chains and the backbone, suggesting that this region alone is not responsible for binding.
Indexed as
Identifiers
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.