Overall work flow.

<p>Overall work flow.</p

The essential and downstream common proteins of amyotrophic lateral sclerosis: A protein-protein interaction network analysis

<div><p>Amyotrophic Lateral Sclerosis (ALS) is a devastative neurodegenerative disease characterized by selective loss of motoneurons. While several breakthroughs have been made in identifying ALS genetic defects, the detailed molecular mechanisms are still unclear. These genetic defects involve in numerous biological processes, which converge to a common destiny: motoneuron degeneration. In addition, the common comorbid Frontotemporal Dementia (FTD) further complicates the investigation of ALS etiology. In this study, we aimed to explore the protein-protein interaction network built on known ALS-causative genes to identify essential proteins and common downstream proteins between classical ALS and ALS+FTD (classical ALS + ALS/FTD) groups. The results suggest that classical ALS and ALS+FTD share similar essential protein set (VCP, FUS, TDP-43 and hnRNPA1) but have distinctive functional enrichment profiles. Thus, disruptions to these essential proteins might cause motoneuron susceptible to cellular stresses and eventually vulnerable to proteinopathies. Moreover, we identified a common downstream protein, ubiquitin-C, extensively interconnected with ALS-causative proteins (22 out of 24) which was not linked to ALS previously. Our <i>in silico</i> approach provides the computational background for identifying ALS therapeutic targets, and points out the potential downstream common ground of ALS-causative mutations.</p></div

Downstream proteins ranked by number of direct interactions with ALS-causative proteins.

<p>Downstream proteins ranked by number of direct interactions with ALS-causative proteins.</p

Degree centrality ranking in ALS PPI network.

<p>Degree centrality ranking in ALS PPI network.</p

Most significantly enriched KEGG pathways.

<p>Most significantly enriched KEGG pathways.</p

Profiles of the interacting proteins.

<p>A) Profile of C9orf72 with only direct interaction B) The profiles include both direct and indirect interactions of important downstream proteins. Red, blue and green denote direct, secondary and tertiary contact proteins respectively. Yellow highlights ALS/FTD proteins.</p

ALS-causative genes from OMIM.

<p>ALS-causative genes from OMIM.</p

Most significantly enriched GO terms.

<p>Most significantly enriched GO terms.</p

Protein involvement based on participated cluster number.

<p>Protein involvement based on participated cluster number.</p

Time-Resolved Synchrotron X-ray Scattering Study on Propylene–1-Butylene Random Copolymer Subjected to Uniaxial Stretching at High Temperatures

Synchrotron wide-angle X-ray diffraction (WAXD) and small-angle X-ray scattering (SAXS) were used to characterize the structure evolution of propylene–1-butylene (P–B) random copolymer subjected to uniaxial tensile deformation at 100 °C. Polymorphism and preferred orientation of the crystal phases were examined quantitatively by 2D WAXD. The results indicated that three ensembles of crystalline modifications with distinctive orientation modes coexisted during stretching. The orthorhombic γ-form adopted a tilted cross-β configuration, in which the <i>c</i>-axis had a tilt angle with respect to the fiber axis. The monoclinic α-form in the mother lamellae had a <i>c</i>-axis orientation with polymer chains parallel to the fiber axis. In the α-phase daughter lamellae, the unit cell assumed an <i>a-</i>axis orientation, where the <i>c</i>-axis had an 80° angle with respect to the fiber axis. Stretching transformed the γ-phase into the energetically more stable α-phase. In the late stage, the system was dominated by the α-phase with parallel chain packing. Complemented by qualitative SAXS analysis, simultaneous inter- and intralamellar chain slips were observed during the early stage of stretching. After yielding, a fibrillation process followed. The formation of fibril bundles together with a cross-linked network after yielding might account for the stress-hardening behavior in the late stage of stretching