8 research outputs found

    RMS<sub>a</sub> inter-component relationships for the two groups (TD in light grey and CP in black).

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    <p>The inter-component comparison graphs characterized by significant different regression lines between the TD and CP groups are reported in figure: RMS<sub>a</sub>AP vs RMS<sub>a</sub>ML for head (p = 0.007), RMS<sub>a</sub>ML vs RMSaCC for sternum (p = 0.048), and RMS<sub>a</sub>AP vs RMSaCC for pelvis (p = 0.043).</p

    On the left, RMS of the acceleration components at the three levels.

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    <p>On the right, attenuation coefficients from pelvis to head (C<sub>PH</sub>), from pelvis to sternum (C<sub>PS</sub>), and from sternum to head (C<sub>SH</sub>) along the three anatomical axes. Parameters computed for the TD and CP groups are represented with empty and filled box-plots, respectively. Significant between-groups differences (p < 0.05 or p < 0.01) are reported with the symbol § or §§, respectively.</p

    IPA analysis.

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    <p>In the figure are shown the top 6 signaling networks: 1) Cellular Movement, Hematological System Development and Function and Immune Cell Trafficking; 2) Cell Morphology, Cellular Movement, Digestive System Development and Function; 3) Free Radical Scavenging, Connective Tissue Disorders and Inflammatory Disease; 4) Cell-To-Cell Signaling and Interaction, Cellular Function and Maintenance, Hematological System Development and Function; 5) Organ Morphology, Skeletal and Muscular System Development and Function, Tissue Morphology; 6) Organ Morphology, Skeletal and Muscular System Development and Function, Cancer.</p

    Gene Ontology annotation of protein.

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    <p>To have a general picture of the molecular functions (a), biological processes (b), and protein class (c), of identified proteins, the Protein ANalysis THrough Evolutionary Relationships (PANTHER) Database was used.</p

    1d-SDS-PAGE.

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    <p>Proteins were resolved by Any kD Mini-PROTEAN TGX precast polyacrylamide gels. Gel line was sliced up in 7 pieces; gel bands were destained, reduced, alkylated, and digested with trypsin; peptides were resuspended and analyzed by LC-MS/MS.</p
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