S. Lövgren
Uppsala University
14 Papers
594 Citations
S. Lövgren is an academic researcher from Uppsala University. The author has contributed to research in topics: Carbonic anhydrase & Active site. The author has an hindex of 12, co-authored 14 publications.
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Papers
Crystal structure of human carbonic anhydrase C.
Anders Liljas,Anders Liljas,K.K. Kannan,P.-C. Bergstén,I. Waara,K. Fridborg,B. Strandberg,U. Carlbom,L. Järup,S. Lövgren,M. Petef +10 more
TL;DR: The three dimensional structure of human carbonic anhydrase C has been determined at 2.0 A resolution and the active site has been identified by the binding of inhibitors and the location of the zinc ion.
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Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution
TL;DR: The three-dimensional structure of carbonic anhydrase B (EC 4,2,1,1; carbonate hydro-lyase) from human erythrocytes has been determined to high resolution and the tertiary structure is unique for its folding and is very similar to the structure of the isoenzymes.
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Crystallization of a non-muscle actin
TL;DR: Eukaryotic cells contain a protein which specifically inhibits DNAsae I, and the inhibitor purified from calf spleen consists of two polypeptides which closely resembles muscle actin and whose combination with actin has not been recognized before.
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Crystal structure of human erythrocyte carbonic anhydrase C. VI. The three-dimensional structure at high resolution in relation to other mammalian carbonic anhydrases.
K.K. Kannan,Anders Liljas,I. Waara,P.-C. Bergstén,S. Lövgren,B. Strandberg,Bengtsson U,U. Carlbom,K. Fridborg,L. Järup,M. Petef +10 more
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2.2 å resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains)
Torsten Unge,Stefan D. Knight,Rama Bhikhabhai,S. Lövgren,Zbigniew Dauter,Keith S. Wilson,B. Strandberg +6 more
TL;DR: The RT216 structure provides detailed three-dimensional information of one important part of HIV-1 RT (including the critical active site residues), and a model to explain the inhibitory effect of non-nucleoside inhibitors, which partially accounts for their effect in terms of conformational changes of active site residue.
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