Human BACE forms dimers and colocalizes with APP.

@article{Schmechel2004HumanBF,
  title={Human BACE forms dimers and colocalizes with APP.},
  author={Ariane Schmechel and Markus J Strauss and Andrea Schlicksupp and Ruediger Pipkorn and Christian Haass and T. A. Bayer and Gerhard Multhaup},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 38},
  pages={39710-7}
}
Beta-site APP-cleaving enzyme (BACE) is a membrane-bound aspartyl protease with no strict primary preference for cleavage. The molecular mechanisms that link the gamma-secretase multicomponent amyloid precursor protein (APP) processing complex to biochemical properties of BACE generating the N terminus of the amyloid beta-peptide have not, as yet, been identified. We found that in human brain tissue, BACE occurred as a dimer. The overall stability of the BACE homodimer was based on… CONTINUE READING

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