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The structural and biochemical data described here provides a clear understanding of the mechanism of binding to the active site and how this interaction confers stabilization to the enzyme.
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The data described here were collected from April through August 2014.
The data described here are simply programmatic.
The data described here are derived from 2 separate experiments.
Taken together, the data described here suggest the following model.
The biochemical data described above suggest that Aha1 selectively associates with Hsp90α and Rab3GAP1.
As such, the data describe here were somewhat surprising.
The biochemical system described here retains the key characteristics of somatic expansions from non-proliferating tissues in humans and mice.
The original data is described here, but we recommend using the data here.
The biochemical detection methods described here should translate easily to direct and rapid measurements of changes in current flow using chip-based methods.
The task is explained here, and the data release is described here.
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