Antithrombin III-beta associates more readily than antithrombin III-alpha with uninjured and de-endothelialized aortic wall in vitro and in vivo

scientific article published on 01 May 1991

Antithrombin III-beta associates more readily than antithrombin III-alpha with uninjured and de-endothelialized aortic wall in vitro and in vivo is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1161/01.ATV.11.3.530
P698PubMed publication ID2029494

P2093author name stringM R Witmer
M W Hatton
P433issue3
P304page(s)530-539
P577publication date1991-05-01
P1433published inArteriosclerosis and thrombosis : a journal of vascular biologyQ27709770
P1476titleAntithrombin III-beta associates more readily than antithrombin III-alpha with uninjured and de-endothelialized aortic wall in vitro and in vivo
P478volume11

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cites work (P2860)
Q74079042Comparative catabolism of prothrombin and antithrombin in normal and alloxan-diabetic rabbits
Q24528208Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a β-like variant in baculovirus-infected insect cells
Q43588743Heparin cofactor II, antithrombin-beta and their complexes with thrombin in human tissues
Q79910337Intracellular retention of hepatic serpins caused by severe hyperlipidemia
Q54038989Mutation of any site of N-linked glycosylation accelerates the in vivo clearance of recombinant rabbit antithrombin.
Q88762817Revisiting antithrombin in health and disease, congenital deficiencies and genetic variants, and laboratory studies on α and β forms
Q73158699Separation between the alpha and beta forms of human antithrombin by hydroxyapatite high-performance liquid chromatography
Q27640482Structure of beta-antithrombin and the effect of glycosylation on antithrombin's heparin affinity and activity

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