Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor.

By L. Hong, G. Koelsch, Xinli Lin, Shili Wu, S. Terzyan, Arun K. Ghosh, Xuenjun C. Zhang, Jordan Tang. Science, 2000

677 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/9cafec6d5f412d8c45d63a1f8271f673192c150f

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Computational Theory and Mathematics

1. Christian Haass
2. Sangram S. Sisodia

In Molecular Biology

1. Christian Haass

In Physiology

1. Christian Haass
2. Sangram S. Sisodia
3. G. Thinakaran
4. C. Kaether
5. D. Holtzman
6. J. Long

Citations in the corpus

• Trafficking and proteolytic processing of APP. (2012, background): “BACE1 is a membrane-bound aspartyl protease with its active site in the lumen/extracellular space and with structural similarities to the pepsin family (Hong et al. 2000).”