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Dipeptidyl peptidase i controls survival from Klebsiella pneumoniae lung infection by processing surfactant protein D

Autor: Sutherland, RE, Barry, SS, Olsen, JS, Salantes, DB, Caughey, GH, Wolters, PJ

Publikováno v: Sutherland, RE; Barry, SS; Olsen, JS; Salantes, DB; Caughey, GH; & Wolters, PJ. (2014). Dipeptidyl peptidase i controls survival from Klebsiella pneumoniae lung infection by processing surfactant protein D. Biochemical and Biophysical Research Communications, 450(1), 818-823. doi: 10.1016/j.bbrc.2014.06.062. UCSF: Retrieved from: http://www.escholarship.org/uc/item/38r08416

Prior work established that a deficiency in the cysteine protease dipeptidyl peptidase I (DPPI) improves survival following polymicrobial septic peritonitis. To test whether DPPI regulates survival from severe lung infections, DPPI-/-mice were studie

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::3012c90df0ced7c2dd0aae10b358fdd9
http://www.escholarship.org/uc/item/38r08416

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Bronchoalveolar lavage cell immunophenotyping facilitates diagnosis of lung allograft rejection

Autor: Greenland, JR, Jewell, NP, Gottschall, M, Trivedi, NN, Kukreja, J, Hays, SR, Singer, JP, Golden, JA, Caughey, GH

Publikováno v: Greenland, JR; Jewell, NP; Gottschall, M; Trivedi, NN; Kukreja, J; Hays, SR; et al.(2014). Bronchoalveolar lavage cell immunophenotyping facilitates diagnosis of lung allograft rejection. American Journal of Transplantation, 14(4), 831-840. doi: 10.1111/ajt.12630. UCSF: Retrieved from: http://www.escholarship.org/uc/item/0gv4k5v4
American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons, vol 14, iss 4

Supplementary methods to identify acute rejection and to distinguish rejection from infection may improve clinical outcomes for lung allograft recipients. We hypothesized that distinct bronchoalveolar lavage (BAL) cell profiles are associated with re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::5cadb65a998b5523f91e2ac908b5cb31
http://www.escholarship.org/uc/item/0gv4k5v4

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Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type i serine proteases Fromtransmembrane anchors

Autor: Raman, K, Trivedi, NN, Raymond, WW, Ganesan, R, Kirchhofer, D, Verghese, GM, Craik, CS, Schneider, EL, Nimishakavi, S, Caughey, GH

Publikováno v: Raman, K; Trivedi, NN; Raymond, WW; Ganesan, R; Kirchhofer, D; Verghese, GM; et al.(2013). Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type i serine proteases Fromtransmembrane anchors. Journal of Biological Chemistry, 288(15), 10588-10598. doi: 10.1074/jbc.M112.449033. UCSF: Retrieved from: http://www.escholarship.org/uc/item/6dm6m1c8

Human and mouse marapsins (Prss27) are serine proteases preferentially expressed by stratified squamous epithelia. However, mouse marapsin contains a transmembrane anchor absent from the human enzyme. To gain insights into physical forms, activities,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::b2a68e20d44e556fe72ba95a9333f9d1
http://www.escholarship.org/uc/item/6dm6m1c8

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