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  The von Willebrand factor A2 domain disulfide bond exists in oxidized and reduced states in the circulation and regulates function

Hogg, P., Butera, D., Andrews, R., Gardiner, E., Davis, A., Murphy, D., et al. (2015). The von Willebrand factor A2 domain disulfide bond exists in oxidized and reduced states in the circulation and regulates function. Journal of Thrombosis and Haemostasis, 13(S2): PO669-TUE, pp. 750-750. doi:10.1111/jth.12993.

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 Creators:
Hogg, P1, Author
Butera, D1, Author
Andrews, R2, Author
Gardiner, E2, Author
Davis, A3, Author
Murphy, D3, Author
Baker, R4, Author
Thom, J5, Author
Chen, V1, Author
Luken, B6, Author
Wong, J1, Author
Aponte-Santamaria, C7, Author
Bronowska, A7, Author
Baldauf, Carsten8, Author           
Graeter, F7, Author
Affiliations:
1University of New South Wales, Sydney, NSW, Australia, ou_persistent22              
2Monash University, Melbourne, Vic 3004, Australia, ou_persistent22              
3Alfred Hospital, Melbourne, Vic, Australia, ou_persistent22              
4Murdoch University, Murdoch, WA 6150, Australia, ou_persistent22              
5Pathwest Perth, Perth, Australia, ou_persistent22              
6Sanquin Research, Amsterdam, The Netherlands, ou_persistent22              
7Heidelberg Institute of Theoretical Studies, Heidelberg, Germany, ou_persistent22              
8Theory, Fritz Haber Institute, Max Planck Society, ou_634547              

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Language(s): eng - English
 Dates: 2015-062015-06
 Publication Status: Issued
 Pages: 1
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1111/jth.12993
 Degree: -

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Title: Journal of Thrombosis and Haemostasis
  Other : J. Thromb. Haemost.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Oxford : Blackwell
Pages: - Volume / Issue: 13 (S2) Sequence Number: PO669-TUE Start / End Page: 750 - 750 Identifier: ISSN: 1538-7933
CoNE: https://pure.mpg.de/cone/journals/resource/991042728117902