F
Fabrizia Fusetti
Researcher at University of Groningen
Publications - 53
Citations - 3546
Fabrizia Fusetti is an academic researcher from University of Groningen. The author has contributed to research in topics: Membrane protein & Lipase. The author has an hindex of 29, co-authored 52 publications receiving 3195 citations. Previous affiliations of Fabrizia Fusetti include University of Milan & University of California, Berkeley.
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Journal ArticleDOI
Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone.
Wangsa T. Ismaya,Henriëtte J. Rozeboom,A. Weijn,Jurriaan J. Mes,Fabrizia Fusetti,Harry J. Wichers,Bauke W. Dijkstra +6 more
TL;DR: The first structure of the full fungal tyrosinase complex from the mushroom Agaricus bisporus is presented, explaining how calcium ions stabilize the tetrameric state of the enzyme.
Journal ArticleDOI
Crystal Structure of the Copper-Containing Quercetin 2,3-Dioxygenase from Aspergillus japonicus
Fabrizia Fusetti,Klaus H Schröter,Roberto A. Steiner,Paula I. van Noort,Tjaard Pijning,Henriëtte J. Rozeboom,Kor H. Kalk,Maarten R. Egmond,Bauke W Dijkstra +8 more
TL;DR: Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance.
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Crystal Structure and Carbohydrate-binding Properties of the Human Cartilage Glycoprotein-39
TL;DR: The binding features observed in the complex structures suggest that either chitin or a closely related oligosaccharide could act as the physiological ligand for HCgp-39.
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Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins.
Fabrizia Fusetti,Holger von Moeller,Douglas R. Houston,Henriëtte J. Rozeboom,Bauke W. Dijkstra,Rolf G. Boot,Johannes M. F. G. Aerts,Daan M. F. van Aalten +7 more
TL;DR: The crystal structure of the human chitotriosidase and complexes with a chitooligosaccharide and allosamidin reveal an elongated active site cleft, compatible with the binding of long chitin polymers, and explain the inactivation of the enzyme through an inherited genetic deficiency.
Journal ArticleDOI
Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.
Heidi Erlandsen,Fabrizia Fusetti,Fabrizia Fusetti,Fabrizia Fusetti,Aurora Martinez,Edward Hough,Torgeir Flatmark,Raymond C. Stevens,Raymond C. Stevens +8 more
TL;DR: The 2.0 A crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals a fold similar to that of tyrosine hydrogenase, providing the first structural view of where mutations occur and a rationale to explain molecular mechanisms of the enzymatic phenotypes in the autosomal recessive disorder phenylketoneuria.