about
High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexesAtomic resolution structures of trypsin provide insight into structural radiation damageThe structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation featuresStructural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicidaStructure of uracil-DNAN-glycosylase (UNG) fromVibrio cholerae: mapping temperature adaptation through structural and mutational analysisThermodynamics and structure of a salmon cold active goose-type lysozymeStructural and biophysical analysis of interactions between cod and human uracil-DNAN-glycosylase (UNG) and UNG inhibitor (Ugi)Structural and functional characterization of two unusual endonuclease III enzymes from Deinococcus radioduransCold adaption of enzymes: structural comparison between salmon and bovine trypsinsThe crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitorThe primary structure and specificity determining residues displayed by recombinant salmon antibody domains.High quality draft genome sequence of Streptomyces sp. strain AW19M42 isolated from a sea squirt in Northern NorwayCold adapted enzymes.Computational analysis of binding of P1 variants to trypsin.Draft Genome Sequence of the Actinomycete Rhodococcus sp. Strain AW25M09, Isolated from the Hadsel Fjord, Northern Norway.Characterization of the N-acetylneuraminic acid synthase (NeuB) from the psychrophilic fish pathogen Moritella viscosa.Probing the effect of point mutations at protein-protein interfaces with free energy calculationsComparative studies of endonuclease I from cold-adapted Vibrio salmonicida and mesophilic Vibrio cholerae.Electrostatic interactions play an essential role in DNA repair and cold-adaptation of uracil DNA glycosylase.Electrostatic effects play a central role in cold adaptation of trypsin.Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua).Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants.Structural evidence for lack of inhibition of fish goose-type lysozymes by a bacterial inhibitor of lysozyme.Increased flexibility as a strategy for cold adaptation: a comparative molecular dynamics study of cold- and warm-active uracil DNA glycosylase.Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans.The 1.8 A crystal structure of a proteinase K-like enzyme from a psychrotroph Serratia species.Predicting proteinase specificities from free energy calculations.Structure of anionic salmon trypsin in a second crystal form.Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution.Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 A resolution.Crystallization and preliminary X-ray crystallographic studies of native elastase from North Atlantic salmon (Salmo salar).Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: qualitative evaluation of electrostatic differences at the substrate binding site.Evaluation of protein-protein association energies by free energy perturbation calculations.Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus mykiss).Ion pairs and their role in modulating stability of cold- and warm-active uracil DNA glycosylaseCrystallization and preliminary X-ray crystallographic studies of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar)The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallographyTemperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsinComparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solutionInterscaffolding additivity: binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases
P50
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P50
description
hulumtues
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researcher
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ricercatore
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wetenschapper
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հետազոտող
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name
Arne O Smalås
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Arne O Smalås
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Arne O Smalås
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Arne O Smalås
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type
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Arne O Smalås
@ast
Arne O Smalås
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Arne O Smalås
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Arne O Smalås
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Arne O Smalås
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Arne O Smalås
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Arne O Smalås
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Arne O Smalås
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P1053
C-4131-2016
P106
P21
P214
276149106194068491411
P31
P3829
P496
0000-0002-4651-9911