Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Hadler, Kieran"'
Autor:
Daumann, Lena J., McCarthy, Bianca Y., Hadler, Kieran S., Murray, Tracy P., Gahan, Lawrence R., Larrabee, James A., Ollis, David L., Schenk, Gerhard
Publikováno v:
In BBA - Proteins and Proteomics January 2013 1834(1):425-432
Autor:
Hume David A, Guddat Luke W, Kelly Gregory, Burrows Allan, Robinson Jodie, Weber Jane, Cassady A Ian, Huber Thomas, Hadler Kieran S, Schenk Gerhard, Flanagan Jack U
Publikováno v:
BMC Research Notes, Vol 1, Iss 1, p 78 (2008)
Abstract Background Tartrate-resistant acid phosphatases (TRAcPs), also known as purple acid phosphatases (PAPs), are a family of binuclear metallohydrolases that have been identified in plants, animals and fungi. The human enzyme is a major histoche
Externí odkaz:
https://doaj.org/article/3596ca8544914cc2b1088790b1c273c6
Autor:
Ely, Fernanda1, Hadler, Kieran1, Mitić, Nataša, Gahan, Lawrence1, Ollis, David2, Plugis, Nicholas3, Russo, Marie3, Larrabee, James3 larrabee@middlebury.edu, Schenk, Gerhard schenk@uq.edu.au
Publikováno v:
Journal of Biological Inorganic Chemistry (JBIC). May2011, Vol. 16 Issue 5, p777-787. 11p.
Publikováno v:
FEBS Journal. Sep2007, Vol. 274 Issue 18, p4742-4751. 10p. 2 Color Photographs, 2 Diagrams, 2 Charts.
Autor:
Hadler, Kieran S., Mitic, Natasa, Yip, Sylvia Hsu-Chen, Gahan, Lawrence R., Ollis, David L., Schenk, Gerhard, Larrabee, James A.
The glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes is a promiscuous, dinuclear metallohydrolase that has potential application in the remediation of organophosphate nerve agents and pesticides. GpdQ employs an unusual reaction mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______223::8402e8d32a814ce05354c0f96d555bbc
http://eprints.maynoothuniversity.ie/3716/
http://eprints.maynoothuniversity.ie/3716/
Autor:
Jackson, Colin J., Hadler, Kieran S., Carr, Paul D., Oakley, Aaron J., Yip, Sylvia, Schenk, Gerhard, Ollis, David L.
The structure of a malonate-bound form of the glycerophosphodiesterase from Enterobacter aerogenes, GpdQ, has been refined at a resolution of 2.2 A ° to a final R factor of 17.1%. The structure was originally solved to 2.9 A ° resolution using SAD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______223::1eaeb62f08c7c66bfefdce6c0e45640a
http://eprints.maynoothuniversity.ie/3714/
http://eprints.maynoothuniversity.ie/3714/
Autor:
Hadler, Kieran S., Tanifum, Eric A., Hsu-Chen Yip, Sylvia, Mitic, Natasa, Guddat, Luke W., Jackson, Colin J., Gahan, Lawrence R., Nguyen, Kelly, Carr, Paul D., Ollis, David L., Hengge, Alvan C., Larrabee, James A., Schenk, Gerhard
The glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes is a promiscuous binuclear metallohydrolase that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______223::e4f2eb7610298ebbb7191d1841faa3c0
http://eprints.maynoothuniversity.ie/3701/
http://eprints.maynoothuniversity.ie/3701/
Publikováno v:
In Journal of Inorganic Biochemistry 2010 104(2):211-213
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