Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.
about
Protein-mediated enamel mineralizationElongated polyproline motifs facilitate enamel evolution through matrix subunit compaction.The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.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.Human osteoblastic cells discriminate between 20-kDa amelogenin isoforms.Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins.Probing the self-association, intermolecular contacts, and folding propensity of amelogenin.Proline-glutamate chimera's side chain conformation directs the type of β-hairpin structure.The role of amelogenin during enamel-crystallite growth and organization in vivo.Amelogenin in Enamel Tissue Engineering.Localization and quantitative co-localization of enamelin with amelogenin.Survey of the year 2009: applications of isothermal titration calorimetry.Large potentials of small heat shock proteins.Prospects and Pits on the Path of Biomimetics: The case of tooth enamel.Amelogenin and Enamel Biomimetics.Interactions of amelogenin with phospholipids.Full length amelogenin binds to cell surface LAMP-1 on tooth root/periodontium associated cellsSelf-assembly of filamentous amelogenin requires calcium and phosphate: from dimers via nanoribbons to fibrils.Ameloblastin peptide encoded by exon 5 interacts with amelogenin N-terminus.CryoTEM study of effects of phosphorylation on the hierarchical assembly of porcine amelogenin and its regulation of mineralization in vitro.Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micellesStructural changes in amelogenin upon self-assembly and mineral interactions.Circular dichroism and electron microscopy studies in vitro of 33-mer gliadin peptide revealed secondary structure transition and supramolecular organization.Phosphorylation of human small heat shock protein HspB8 (Hsp22) by ERK1 protein kinase.Peptide-Based Bioinspired Approach to Regrowing Multilayered Aprismatic Enamel.
P2860
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P2860
Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.
description
2009 nî lūn-bûn
@nan
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
2009年论文
@zh
2009年论文
@zh-cn
name
Analysis of secondary structur ...... thermal titration calorimetry.
@en
Analysis of secondary structur ...... thermal titration calorimetry.
@nl
type
label
Analysis of secondary structur ...... thermal titration calorimetry.
@en
Analysis of secondary structur ...... thermal titration calorimetry.
@nl
prefLabel
Analysis of secondary structur ...... thermal titration calorimetry.
@en
Analysis of secondary structur ...... thermal titration calorimetry.
@nl
P2093
P2860
P356
P1433
P1476
Analysis of secondary structur ...... thermal titration calorimetry.
@en
P2093
Balachandra G Hegde
Daming Fan
Janet Moradian-Oldak
Rajamani Lakshminarayanan
P2860
P304
P356
10.1002/PROT.22369
P407
P50
P577
2009-08-01T00:00:00Z