000 01420 a2200373 4500
005 20250515203420.0
264 0 _c20100226
008 201002s 0 0 eng d
022 _a1091-6490
024 7 _a10.1073/pnas.0910144107
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aJohnson, Daniel J D
245 0 0 _aMolecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex.
_h[electronic resource]
260 _bProceedings of the National Academy of Sciences of the United States of America
_cJan 2010
300 _a645-50 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aAnimals
650 0 4 _aAntithrombins
_xchemistry
650 0 4 _aBinding Sites
650 0 4 _aBlood Coagulation
_xphysiology
650 0 4 _aCatalytic Domain
650 0 4 _aCrystallography, X-Ray
650 0 4 _aFactor IXa
_xchemistry
650 0 4 _aHeparin
_xchemistry
650 0 4 _aHumans
650 0 4 _aModels, Molecular
650 0 4 _aProtein Binding
650 0 4 _aProtein Conformation
650 0 4 _aSwine
700 1 _aLangdown, Jonathan
700 1 _aHuntington, James A
773 0 _tProceedings of the National Academy of Sciences of the United States of America
_gvol. 107
_gno. 2
_gp. 645-50
856 4 0 _uhttps://doi.org/10.1073/pnas.0910144107
_zAvailable from publisher's website
999 _c19458046
_d19458046