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Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity

Autor: Craik, Charles, Skala, W, Utzschneider, DT, Magdolen, V, Debela, M, Guo, S, Craik, CS, Brandstetter, H, Goettig, P

Publikováno v: Craik, Charles; Skala, W; Utzschneider, DT; Magdolen, V; Debela, M; Guo, S; et al.(2014). Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/56j989h8

© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.Human kallikrein-related peptidase 2 (KLK2) is a tryptic serine protease predominantly expressed in prostatic tissue and secreted into prostatic fluid, a major component of s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::e1002715f9bfbd6a1613b6a0247e8f7d
http://www.escholarship.org/uc/item/56j989h8

Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation

Autor: Christoph Becker-Pauly, Magdolen, Anke Ohler, Stefan Wagner, Debela M

The metalloproteases meprin α and β are expressed in several tissues, leukocytes, and cancer cells. In skin, meprins are located in separate layers of human epidermis indicating distinct physiological functions, supported by effects on cultured ker

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7479dfef25657c4fa823757adf6c2fb6
https://mediatum.ub.tum.de/1323925

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