Analysis of human follistatin structure: identification of two discontinuous N-terminal sequences coding for activin A binding and structural consequences of activin binding to native proteins.

@article{Wang2000AnalysisOH,
  title={Analysis of human follistatin structure: identification of two discontinuous N-terminal sequences coding for activin A binding and structural consequences of activin binding to native proteins.},
  author={Qing Feng Wang and Henry T. Keutmann and Alan L. Schneyer and Patrick M. Sluss},
  journal={Endocrinology},
  year={2000},
  volume={141 9},
  pages={3183-93}
}
A primary physiological function of follistatin is the binding and neutralization of activin, a transforming growth factor-beta family growth factor, and loss of function mutations are lethal. Despite the critical biological importance of follistatin's neutralization of activin, the structural basis of activin's binding to follistatin is poorly understood. The purposes of these studies were 1) to identify the primary sequence(s) within the N-terminal domain of the follistatin coding for activin… CONTINUE READING
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The preparation of 131Ilabeled human growth hormone of high specific radioactivity

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