Given a context passage, generate a question from the passage such that its answer is shortest continous span from the passage.
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Question: The motion of an object can be represented by a position-time graph like Graph 1 in the Figure 1.1. In this type of graph, the y-axis represents position relative to the starting point, and the x-axis represents time. A position-time graph shows how far an object has traveled from its starting position at any given time since it started moving. Q: In the Figure 1.1, what distance has the object traveled from the starting point by the time 5 seconds have elapsed? A: The object has traveled a distance of 50 meters. In a position-time graph, the velocity of the moving object is represented by the slope, or steepness, of the graph line. If the graph line is horizontal, like the line after time = 5 seconds in Graph 2 in the Figure 1.2, then the slope is zero and so is the velocity. The position of the object is not changing. The steeper the line is, the greater the slope of the line is and the faster the objects motion is changing. Its easy to calculate the average velocity of a moving object from a position-time graph. Average velocity equals the change in position (represented by d) divided by the corresponding change in time (represented by t): velocity = d t For example, in Graph 2 in the Figure 1.2, the average velocity between 0 seconds and 5 seconds is: d t 25 m 0 m = 5 s0 s 25 m = 5s = 5 m/s velocity =

Answer: the slope of a position-time graph can be used to find the moving objects


Question: Diabetic nephropathy is the leading cause of end-stage renal disease in humans in the Western world. The recent development of Na+-glucose cotransporter 2 (SGLT2) inhibitors offers a new antidiabetic therapy via enhanced glucose excretion. Whether this strategy exerts beneficial effects on the development of type 2 diabetic nephropathy is still largely unclear. We investigated the effects of the specific SGLT2 inhibitor empagliflozin in BTBR.Cg-Lep<ob>/WiscJ (BTBR ob/ob) mice, which spontaneously develop type 2 diabetic nephropathy. In the first experiment, BTBR ob/ob mice received either a diet containing 300 ppm empagliflozin or equicaloric placebo chow for 12 wk. In the second experiment, BTBR ob/ob mice received 1 gkg body wt(-1)day(-1) ANG II to induce arterial hypertension and were separated into the same two diet groups for 6 wk. In both experiments, empagliflozin treatment enhanced glucosuria, thereby lowering blood glucose. Independently of hypertension, empagliflozin reduced albuminuria in diabetic mice. However, empagliflozin treatment affected diabetes-related glomerular hypertrophy, markers of renal inflammation, and mesangial matrix expansion only in BTBR ob/ob mice without hypertension. In summary, empagliflozin demonstrated significant antihyperglycemic effects, differentially ameliorating early features of diabetic nephropathy in BTBR ob/ob mice with and without hypertension.

Answer: Which protein does empagliflozin inhibit?


Question: Polycomb gene silencing requires histone methyltransferase activity of Polycomb repressive complex 2 (PRC2), which methylates lysine 27 of histone H3. Information on how PRC2 works is limited by lack of structural data on the catalytic subunit, Enhancer of zeste (E(Z)), and the paucity of E(z) mutant alleles that alter its SET domain. Here we analyze missense alleles of Drosophila E(z), selected for molecular study because of their dominant genetic effects. Four missense alleles identify key E(Z) SET domain residues, and a fifth is located in the adjacent CXC domain. Analysis of mutant PRC2 complexes in vitro, and H3-K27 methylation in vivo, shows that each SET domain mutation disrupts PRC2 histone methyltransferase. Based on known SET domain structures, the mutations likely affect either the lysine-substrate binding pocket, the binding site for the adenosylmethionine methyl donor, or a critical tyrosine predicted to interact with the substrate lysine epsilon-amino group. In contrast, the CXC mutant retains catalytic activity, Lys-27 specificity, and trimethylation capacity. Deletion analysis also reveals a functional requirement for a conserved E(Z) domain N-terminal to CXC and SET. These results identify critical SET domain residues needed for PRC2 enzyme function, and they also emphasize functional inputs from outside the SET domain.

Answer:
What is the characteristic domain of histone methyltransferases?