The structure of human DNase I bound to magnesium and phosphate ions points to a catalytic mechanism common to members of the DNase I-like superfamily.
Parsiegla, Goetz
The structure of human DNase I bound to magnesium and phosphate ions points to a catalytic mechanism common to members of the DNase I-like superfamily. [electronic resource] - Biochemistry Dec 2012 - 10250-8 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1520-4995
10.1021/bi300873f doi
Asparagine--metabolism
Catalysis
Catalytic Domain
Crystallography, X-Ray
DNA--metabolism
Deoxyribonuclease I--genetics
Humans
Magnesium--metabolism
Models, Molecular
Phosphates--metabolism
Recombinant Proteins--genetics
Viscosity
The structure of human DNase I bound to magnesium and phosphate ions points to a catalytic mechanism common to members of the DNase I-like superfamily. [electronic resource] - Biochemistry Dec 2012 - 10250-8 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1520-4995
10.1021/bi300873f doi
Asparagine--metabolism
Catalysis
Catalytic Domain
Crystallography, X-Ray
DNA--metabolism
Deoxyribonuclease I--genetics
Humans
Magnesium--metabolism
Models, Molecular
Phosphates--metabolism
Recombinant Proteins--genetics
Viscosity