Janet Moradian-Oldak

Analysis of self-assembly and apatite binding properties of amelogenin proteins lacking the hydrophilic C-terminal.

Supramolecular assembly of amelogenin nanospheres into birefringent microribbons.

Amelogenin supra-molecular assembly in vitro compared with the architecture of the forming enamel matrix.

Assembly and processing of an engineered amelogenin proteolytic product (rP148).

On the formation of amelogenin microribbons.

Control of apatite crystal growth by the co-operative effect of a recombinant porcine amelogenin and fluoride.

Dynamic light scattering study of an amelogenin gel-like matrix in vitro.

Tissue engineering strategies for the future generation of dental implants.

3. Protein-protein interactions of the developing enamel matrix.

Enamel inspired nanocomposite fabrication through amelogenin supramolecular assembly.

The emergence of "nanospheres" as basic structural components adopted by amelogenin.

Polyelectrolyte-mediated adsorption of amelogenin monomers and nanospheres forming mono- or multilayers.

The role of secondary structure in the entropically driven amelogenin self-assembly.

Tooth regeneration: challenges and opportunities for biomedical material research.

The 32kDa enamelin undergoes conformational transitions upon calcium binding.

Immunogold labeling of amelogenin in developing porcine enamel revealed by field emission scanning electron microscopy.

Controlled remineralization of enamel in the presence of amelogenin and fluoride.

Mimicking the Self-Organized Microstructure of Tooth Enamel.

The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.

In vitro study on the interaction between the 32 kDa enamelin and amelogenin.

Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.

How amelogenin orchestrates the organization of hierarchical elongated microstructures of apatite.

Amelogenin Promotes the Formation of Elongated Apatite Microstructures in a Controlled Crystallization System.

The REGENERATION of TOOTH ENAMEL.

Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins.

Probing the self-association, intermolecular contacts, and folding propensity of amelogenin.

Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin.

Tooth enamel proteins enamelin and amelogenin cooperate to regulate the growth morphology of octacalcium phosphate crystals.

The cooperation of enamelin and amelogenin in controlling octacalcium phosphate crystal morphology.

A multistage pathway for human prion protein aggregation in vitro: from multimeric seeds to β-oligomers and nonfibrillar structures.

Folding, assembly, and aggregation of recombinant murine amelogenins with T21I and P41T point mutations.

Single-molecule determination of the face-specific adsorption of Amelogenin's C-terminus on hydroxyapatite.

Preface.

Amelogenin "nanorods" formation during proteolysis by Mmp-20.

Dissecting amelogenin protein nanospheres: characterization of metastable oligomers.

In situ AFM study of amelogenin assembly and disassembly dynamics on charged surfaces provides insights on matrix protein self-assembly.

Amelogenin-enamelin association in phosphate-buffered saline.

Protein-mediated enamel mineralization.

Amelogenin processing by MMP-20 prevents protein occlusion inside calcite crystals.

Localization and quantitative co-localization of enamelin with amelogenin.

An amelogenin-chitosan matrix promotes assembly of an enamel-like layer with a dense interface.

Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micelles.