1. A review of improved fixation methods for dental implants
A review of improved fixation methods for dental implants. Part II: Biomechanical integrity at bone–implant interface 
Yo Shibata, DDS, PhD, Yasuhiro Tanimoto, PhD, Noriko Maruyama, DDS, Manamu Nagakura, DDS 
Journal of Prosthodontic Research 
Volume 59, Issue 2, Pages (April 2015)
DOI: /j.jpor
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2. Fig. 1
Schematic representation of events at the bone–implant interface. (a) Protein adsorption from blood and tissue fluids, (b) protein desorption, (c) surface changes and material release, (d) inflammatory and connective tissue cells approach the implant, (e) possible targeted release of matrix proteins and selected adsorption of proteins, (f) formation of lamina limitans and adhesion of osteogenic cells, (g) bone deposition on both the exposed bone and implant surfaces, (h) remodeling of newly formed bone [1,2] (license number: ).
Journal of Prosthodontic Research  , 84-95DOI: ( /j.jpor )
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3. Fig. 2
Schematic illustration of hierarchical structure of bone (license number: ).
Journal of Prosthodontic Research  , 84-95DOI: ( /j.jpor )
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4. Fig. 3
Nanoindentation force displacement curve for measurement of hardness and elastic modulus.
Journal of Prosthodontic Research  , 84-95DOI: ( /j.jpor )
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5. Fig. 4 Viscoelastic hysteresis loop forms during unloading.
Journal of Prosthodontic Research  , 84-95DOI: ( /j.jpor )
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6. Fig. 5
A depth-dependent load/partial unloading load function and consequent effective measurement range on cortical bone.
Journal of Prosthodontic Research  , 84-95DOI: ( /j.jpor )
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7. Fig. 6
Peak assignments on mineralized tissue. the ‘Amide I’ region between 1600 and 1700cm−1 revealed the occurrence of three or more bands at 1623, 1637 and 1656cm−1, attributable to characteristic collagen secondary structures. The band at 1637cm−1 is characteristic of a collagen secondary structure, and is evident as a shoulder at the ‘Amide I’ band in the Raman spectrum of collagen. The increase in the ‘Amide I’ band shoulder at 1656cm−1 was attributable to the maturity of typical α-helix collagen secondary structures. This is related to hydrogen bonding between collagen molecules and subsequent cross-linking of tissues.
Journal of Prosthodontic Research  , 84-95DOI: ( /j.jpor )
Copyright © 2015 Japan Prosthodontic Society Terms and Conditions