Runtime and memory usage in Fast using simulated data compared with publicly available stand-alone implementations (denoted Orig).

<p>All runtimes are in minutes and memory usages are in megabytes. ‘Linear/Logistic’ uses genotype data while ‘Summary’ uses summary data. All indicates running Gwis, Bimbam, Vegas, Minsnp, Minsnp-gene and Single-snp simultaneously in Fast.</p>*<p>No permutations.</p

sj-pdf-1-tae-10.1177_20420188231187493 – Supplemental material for Exploring the mechanism of metformin action in Alzheimer’s disease and type 2 diabetes based on network pharmacology, molecular docking, and molecular dynamic simulation

Supplemental material, sj-pdf-1-tae-10.1177_20420188231187493 for Exploring the mechanism of metformin action in Alzheimer’s disease and type 2 diabetes based on network pharmacology, molecular docking, and molecular dynamic simulation by Xin Shi, Lingling Li, Zhiyao Liu, Fangqi Wang and Hailiang Huang in Therapeutic Advances in Endocrinology and Metabolism</p

Genetic risk score distribution.

<p><b>Histogram of the genetic risk scores (GRS) of mesalamine responders (dashed line) and mesalamine non-responders (solid line).</b> GRS was calculated by summation of the log of the odds ratio at each of 133 ulcerative colitis risk SNPs multiplied by number of risk alleles in each patient.</p

Strongest associations for common transporter gene variants with response to mesalamine.

<p>P values are represented in table were calculated by Chi square analysis with threshold for significance of 0.0013 to correct for multiple testing.</p

Description of cohort under study.

<p>Disease distribution was defined by Paris classification system. All comparisons were made by Chi square analysis or student’s t test.</p

Binding modes assessed by molecular docking studies.

<p>A) The schematic diagram of the interaction of [(dmb)₂Ru(obip)Ru(dmb)₂]⁴⁺ with the antiparallel G-quadruplex structure, B) the mixed parallel/antiparallel G-quadruplex structure. G in green yellow, A in red, T in cyan and [(dmb)₂Ru(obip)Ru(dmb)₂]⁴⁺ in green and blue, C) the complex, the antiparallel G-quadruplex and D) the mixed parallel/antiparallel G-quadruplexare shown in CPK mode.</p

DNA and complex structures.

<p>A) structure of G-quartet with cyclic array of four guanines linked by Hoogsteen H-bonds, B) Anti-paralled G-quadruplex, C) Mixed-hybrid G-quadruplex, D)An ORTEP drawing of [(dmb)₂Ru(obip)Ru(dmb)₂]⁴⁺.</p

Selectivity for G-quadruplex DNA assessed by competition dialysis.

<p>Results of competition dialysis experiment with the amount of [(dmb)₂Ru(obip)Ru(dmb)₂]⁴⁺ bound to each DNA structure plotted as a bar graph.</p

Melting of the G-quadruplex assessed by UV absorbance at 295 nm.

<p>Normalized UV melting curves for 10 µM G-quadruplex (■), 10 µM G-quadruplex + 10 µM [(dmb)₂Ru(obip)Ru(dmb)₂]⁴⁺ (●)in a buffer of 100 mM NaCl, 10 mMNaH₂PO₄/Na₂HPO₄, 1mM Na₂EDTA; 10 µM G-quadruplex (▼) 10 µM G-quadruplex + 10 µM [(dmb)₂Ru(obip)Ru(dmb)₂]⁴⁺ (▲)in a buffer of 100 mM KCl10 mM K₂HPO₄/K₂HPO₄, 1mM K₂EDTA (pH 7.0). </p

Temporal Profiling of the Secretome during Adipogenesis in Humans

Adipose tissue plays a key role as a fat-storage depot and as an endocrine organ. Although mouse adipogenesis has been studied extensively, limited studies have been conducted to characterize this process in humans. We carried out a temporal proteomic analysis to interrogate the dynamic changes in the secretome of primary human preadipocytes as they differentiate into mature adipocytes. Using iTRAQ-based quantitative proteomics, we identified and quantified 420 proteins from the secretome of differentiated human adipocytes. Our results revealed that the majority of proteins showed differential expression during the course of differentiation. In addition to adipokines known to be differentially secreted in the course of adipocyte differentiation, we identified a number of proteins whose dynamic expression in this process has not been previously documented. They include collagen triple helix repeat containing 1, cytokine receptor-like factor 1, glypican-1, hepatoma-derived growth factor, SPARC related modular calcium binding protein 1, SPOCK 1, and sushi repeat-containing protein. A bioinformatics analysis using Human Protein Reference Database and Human Proteinpedia revealed that of the 420 proteins identified, 164 proteins possess signal peptides and 148 proteins are localized to the extracellular compartment. Additionally, we employed antibody arrays to quantify changes in the levels of 182 adipokines during human adipogenesis. This is the first large-scale quantitative proteomic study that combines two platforms, mass spectrometry and antibody arrays, to analyze the changes in the secretome during the course of adipogenesis in humans