High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin

2001 ◽  
Vol 314 (2) ◽  
pp. 279-291 ◽  
Author(s):  
Ole Andreas Andersen ◽  
Torgeir Flatmark ◽  
Edward Hough
1997 ◽  
Vol 4 (12) ◽  
pp. 995-1000 ◽  
Author(s):  
Heidi Erlandsen ◽  
Fabrizia Fusetti ◽  
Aurora Martinez ◽  
Edward Hough ◽  
Torgeir Flatmark ◽  
...  

1999 ◽  
Vol 82 (08) ◽  
pp. 271-276 ◽  
Author(s):  
Glen Spraggon ◽  
Stephen Everse ◽  
Russell Doolittle

IntroductionAfter a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved. * Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide


2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Guixing Ma ◽  
Yifan Zhu ◽  
Zhicheng Yu ◽  
Ashfaq Ahmad ◽  
Hongmin Zhang

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