Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides-Reference-Cited by-同舟云学术

Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides

Published:2018-07-17 Issue:1 Volume:9 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Saravanan Rathi^ORCID,Holdbrook Daniel A,Petrlova Jitka,Singh Shalini,Berglund Nils A,Choong Yeu Khai^ORCID,Kjellström Sven^ORCID,Bond Peter J,Malmsten Martin,Schmidtchen Artur^ORCID

Funder

Lee Kong Chian School of Medicine Postdoctoral Fellowship,Nanyang Technological University, Singapore

Svenska Forskningsrådet Formas (Swedish Research Council Formas)

LEO Foundation Center for Cutaneous Drug Delivery (2016-11-01)

Singapore Ministry of Education Academic Research Fund Tier 1 (2015-T1-001-082)

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-05242-0.pdf

Reference70 articles.

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3. Li, Y. D. et al. NF-kappaB transcription factor p50 critically regulates tissue factor in deep vein thrombosis. J. Biol. Chem. 284, 4473–4483 (2009).

4. Petrlova, J. et al. Aggregation of thrombin-derived C-terminal fragments as a previously undisclosed host defense mechanism. Proc. Natl Acad. Sci. USA 114, E4213–E4222 (2017).

5. van der Plas, M. J. et al. Pseudomonas aeruginosa elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses. Nat. Commun. 7, 11567 (2016).

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