The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.
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Protein-mediated enamel mineralizationInsights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free waterA solution NMR investigation into the impaired self-assembly properties of two murine amelogenins containing the point mutations T21→I or P41→TA solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein)Matching 4.7-Å XRD spacing in amelogenin nanoribbons and enamel matrix.Elongated polyproline motifs facilitate enamel evolution through matrix subunit compaction.Molecular dynamics simulations of the intrinsically disordered protein amelogenin.Hierarchical self-assembly of amelogenin and the regulation of biomineralization at the nanoscale.Amelogenin-collagen interactions regulate calcium phosphate mineralization in vitroHow amelogenin orchestrates the organization of hierarchical elongated microstructures of apatiteProtein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.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.Selective and specific ion binding on proteins at physiologically-relevant concentrations.Amelogenin supramolecular assembly in nanospheres defined by a complex helix-coil-PPII helix 3D-structure.Intrinsically disordered proteins and biomineralization.Human osteoblastic cells discriminate between 20-kDa amelogenin isoforms.Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesPerturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins.The expanded amelogenin polyproline region preferentially binds to apatite versus carbonate and promotes apatite crystal elongationProbing the self-association, intermolecular contacts, and folding propensity of amelogenin.Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite.Dissecting amelogenin protein nanospheres: characterization of metastable oligomers.The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution.Biological response on a titanium implant-grade surface functionalized with modular peptidesKinetics of nanochain formation in a simplified model of amelogenin biomacromolecules.Cementomimetics-constructing a cementum-like biomineralized microlayer via amelogenin-derived peptidesImproved protocol to purify untagged amelogenin - Application to murine amelogenin containing the equivalent P70→T point mutation observed in human amelogenesis imperfectaAmelogenin in Enamel Tissue Engineering.The role of bioactive nanofibers in enamel regeneration mediated through integrin signals acting upon C/EBPα and c-Jun.Phosphorylation and ionic strength alter the LRAP-HAP interface in the N-terminus.Localization and quantitative co-localization of enamelin with amelogenin.Mineral association changes the secondary structure and dynamics of murine amelogeninIntrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5Why do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water.Biominerals--hierarchical nanocomposites: the example of bone.Prospects and Pits on the Path of Biomimetics: The case of tooth enamel.Cryogenic transmission electron microscopy study of amelogenin self-assembly at different pHAmelogenin and Enamel Biomimetics.Hydrolysis of amelogenin by matrix metalloprotease-20 accelerates mineralization in vitro.Solvation driven conformational transitions in the second transmembrane domain of mycobacteriophage holin.
P2860
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P2860
The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.
description
2009 nî lūn-bûn
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2009 թուականի Մարտին հրատարակուած գիտական յօդուած
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2009 թվականի մարտին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
The tooth enamel protein, porc ...... uration in the monomeric form.
@ast
The tooth enamel protein, porc ...... uration in the monomeric form.
@en
type
label
The tooth enamel protein, porc ...... uration in the monomeric form.
@ast
The tooth enamel protein, porc ...... uration in the monomeric form.
@en
prefLabel
The tooth enamel protein, porc ...... uration in the monomeric form.
@ast
The tooth enamel protein, porc ...... uration in the monomeric form.
@en
P2093
P2860
P356
P1433
P1476
The tooth enamel protein, porc ...... uration in the monomeric form.
@en
P2093
Craig Harcup
Janet Moradian-Oldak
John Spencer Evans
Katya Delak
Rajamani Lakshminarayanan
Yuwwei Fan
P2860
P304
P356
10.1021/BI802175A
P407
P577
2009-03-01T00:00:00Z