About: Protein interactions during assembly of the enamel organic extracellular matrix

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rdf:type	Item
description	artículu científicu espublizáu en 1997 (ast) vědecký článek publikovaný v roce 1997 (cs) 1997 թվականի փետրվարին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в лютому 1997 (uk) 1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في فبراير 1997) (ar) vedecký článok (publikovaný 1997/02/01) (sk) scientific journal article (en) wetenschappelijk artikel (gepubliceerd op 1997/02/01) (nl) im Februar 1997 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28586894-9351A7E4-D94C-42F1-96AF-895433D83762
publication date	1997-02-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q28586894-5DBB8D22-D767-4CCE-8C0A-362B4ED5942A
cites work	Full-length sequence, localization, and chromosomal mapping of ameloblastin. A novel tooth-specific gene
author name string	wds:Q28586894-5BC6D6B0-A715-4887-809D-5F56E02ECFCB wds:Q28586894-E1C5A6AD-0F95-4D6B-8A3D-3DC8E27C48C5
author name string	M. L. Snead M. L. Paine
rdfs:label	Protein interactions during assembly of the enamel organic extracellular matrix (en) Protein interactions during assembly of the enamel organic extracellular matrix (nl) Protein interactions during assembly of the enamel organic extracellular matrix (ast)
skos:prefLabel	Protein interactions during assembly of the enamel organic extracellular matrix (en) Protein interactions during assembly of the enamel organic extracellular matrix (nl) Protein interactions during assembly of the enamel organic extracellular matrix (ast)
name	Protein interactions during assembly of the enamel organic extracellular matrix (en) Protein interactions during assembly of the enamel organic extracellular matrix (nl) Protein interactions during assembly of the enamel organic extracellular matrix (ast)
title	wds:Q28586894-BF23EAE3-817C-4A64-A41B-6352FE18E7B8
title	Protein interactions during assembly of the enamel organic extracellular matrix (en)
page(s)	wds:Q28586894-A9B0FA3A-9D3B-49F1-8672-FB19A4DF6637
page(s)	221–227
instance of	wds:Q28586894-1ED7804D-0ABE-46E3-86D5-D7F2AD3AA9CF
instance of	scholarly article
main subject	wds:Q28586894-57759530-E639-45C0-84B7-1515756C09DA
main subject	Amelogenin, X-linked
PubMed ID	wds:Q28586894-BD6ECB3E-C2E9-40A7-ADF5-179C3B63B21B
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9041053
PubMed ID	9041053
published in	wds:Q28586894-E99899F1-5457-4E04-BDA2-B0EF0EF5C461
published in	Journal of Bone and Mineral Research
issue	wds:Q28586894-7128A243-E79F-4269-AE5E-581160F577E4
volume	wds:Q28586894-D2669E06-38EF-4B90-A12E-2CA1EF572AC2
issue	2
volume	12
DOI	wds:Q28586894-6868D7AB-8EC9-4333-8CBE-0FEF2116A48A
DOI	http://dx.doi.org/10.1359/JBMR.1997.12.2.221
DOI	10.1359/JBMR.1997.12.2.221
ResearchGate publication ID	wds:Q28586894-04E12353-63DD-449A-9C4D-99291607038C
ResearchGate publication ID	14170025
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28586894
is cites work of	Regulated gene expression dictates enamel structure and tooth function Biomimetic systems for hydroxyapatite mineralization inspired by bone and enamel Role of macromolecular assembly of enamel matrix proteins in enamel formation Amelogenins: assembly, processing and control of crystal morphology Cellular and chemical events during enamel maturation Amelogenin: a potential regulator of cementum-associated genes. A new frameshift mutation encoding a truncated amelogenin leads to X-linked amelogenesis imperfecta The COOH terminus of the amelogenin, LRAP, is oriented next to the hydroxyapatite surface A tuftelin-interacting protein (TIP39) localizes to the apical secretory pole of mouse ameloblasts Analysis of self-assembly and apatite binding properties of amelogenin proteins lacking the hydrophilic C-terminal A solution NMR investigation into the early events of amelogenin nanosphere self-assembly initiated with sodium chloride or calcium chloride A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein) The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form Interaction of amelogenin with hydroxyapatite crystals: an adherence effect through amelogenin molecular self-association Progressive accretion of amelogenin molecules during nanospheres assembly revealed by atomic force microscopy The enamel protein amelogenin binds to the N-acetyl-D-glucosamine-mimicking peptide motif of cytokeratins Cloning and characterization of the murine ameloblastin promoter pH triggered self-assembly of native and recombinant amelogenins under physiological pH and temperature in vitro Comparative immunochemical analyses of the developmental expression and distribution of ameloblastin and amelogenin in rat incisors. The circadian clock modulates enamel development NF-Y and CCAAT/enhancer-binding protein alpha synergistically activate the mouse amelogenin gene. Role of Cbfa1 in ameloblastin gene transcription Molecular biomimetics: nanotechnology through biology Protein-to-protein interactions: criteria defining the assembly of the enamel organic matrix. Altering biomineralization by protein design Leucine-rich amelogenin peptide induces osteogenesis by activation of the Wnt pathway 3. Protein-protein interactions of the developing enamel matrix Biological synthesis of tooth enamel instructed by an artificial matrix Folding, assembly, and aggregation of recombinant murine amelogenins with T21I and P41T point mutations Amelogenin Promotes the Formation of Elongated Apatite Microstructures in a Controlled Crystallization System. Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry Controlled proteolysis of amelogenins reveals exposure of both carboxy- and amino-terminal regions Biomineralization of a self-assembled-, soft-matrix precursor: Enamel Potential role of the amelogenin N-terminus in the regulation of calcium phosphate formation in vitro. Amelogenin and Enamel Biomimetics Assembly and processing of an engineered amelogenin proteolytic product (rP148). Baculoviral capsid display of His-tagged ZnO inorganic binding peptide How do enamelysin and kallikrein 4 process the 32-kDa enamelin? Identification of amelotin- and ODAM-interacting enamel matrix proteins using the yeast two-hybrid system Determination of protein regions responsible for interactions of amelogenin with CD63 and LAMP1. Intracellular nanosphere subunit assembly as revealed by amelogenin molecular cross-linking studies Preparative SDS PAGE as an Alternative to His-Tag Purification of Recombinant Amelogenin Protein Interaction between Ameloblastin and Proteasome Subunit α Type 3 Can Facilitate Redistribution of Ameloblastin Domains within Forming Enamel. Phosphorylation Modulates Ameloblastin Self-assembly and Ca 2+ Binding In vitro study on the interaction between the 32 kDa enamelin and amelogenin. Spatially related amelogenin interactions in developing rat enamel as revealed by molecular cross-linking studies. Dynamics of Biomineralization and Biodemineralization. Transgene animal model for protein expression and accumulation into forming enamel Altered self-assembly and apatite binding of amelogenin induced by N-terminal proline mutation

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