Factor IX oligomerization underlies reduced activity upon disruption of physiological conditions-Reference-Cited by-同舟云学术

Factor IX oligomerization underlies reduced activity upon disruption of physiological conditions

Published:2014-01-13 Issue:2 Volume:20 Page:e157-e163
ISSN:1351-8216
Container-title:Haemophilia
language:en
Short-container-title:Haemophilia

Author:

Simhadri V. L.¹,Hamasaki-Katagiri N.¹,Tseng S. C.¹,Bentley A. A.²,Zichel R.¹,Hershko A. Y.³,Komar A. A.²,Kimchi-Sarfaty C.¹

Affiliation:

1. Laboratory of Hemostasis; Division of Hematology; Center for Biologics Evaluation & Research; US FDA; Bethesda MD USA

2. Department of Biological, Geological & Environmental Sciences; Center for Gene Regulation in Health and Disease; Cleveland State University; Cleveland OH USA

3. Department of Medicine; Meir Medical Center; Kfar Saba Israel

Publisher

Wiley

Subject

Genetics (clinical),Hematology,General Medicine

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/hae.12356/fullpdf

Reference26 articles.

1. Structure, function, and molecular defects of factor IX;Thompson;Blood,1986

2. The molecular basis of haemophilia B;Lillicrap;Haemophilia,1998

3. Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy;Freedman;J Biol Chem,1995

4. A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S;Scipio;Biochemistry,1977

5. Analysis of F9 point mutations and their correlation to severity of haemophilia B disease;Hamasaki-Katagiri;Haemophilia,2012

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1. Single synonymous mutation in factor IX alters protein properties and underlies haemophilia B;Journal of Medical Genetics;2016-12-22