Mechanism of the Interaction of β2-Glycoprotein I with Negatively Charged Phospholipid Membranes

M Hammel, R Schwarzenbacher, A Gries… - Biochemistry, 2001 - ACS Publications
In an attempt to understand the multifunctional involvement of β2-glycoprotein I (β2GPI) in
autoimmune diseases, thrombosis, atherosclerosis, and inflammatory processes, substantial …

Membrane binding of β2-glycoprotein I can be described by a two-state reaction model: an atomic force microscopy and surface plasmon resonance study

R Gamsjaeger, A Johs, A Gries, HJ Gruber… - Biochemical …, 2005 - portlandpress.com
Complexes formed between β2GPI (β2-glycoprotein I), a human plasma protein, and
biological membranes are considered to be targets of macrophages and antiphospholipid …

[HTML][HTML] Crystal structure of human β2‐glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome

R Schwarzenbacher, K Zeth, K Diederichs… - The EMBO …, 1999 - embopress.org
The high affinity of human plasma β2‐glycoprotein I (β 2 GPI), also known as apolipoprotein‐
H (ApoH), for negatively charged phospholipids determines its implication in a variety of …

Structure–Function Studies on β2-glycoprotein I

PG de Groot, B Bouma, BCH Lutters… - Journal of …, 2000 - Elsevier
Human β2-glycoprotein I is a heavily glycosylated plasma protein which has been
implicated in the binding of antiphospholipid antibodies to negatively charged …

Aggregation of β2-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Y Hagihara, DP Hong, M Hoshino, K Enjyoji, H Kato… - Biochemistry, 2002 - ACS Publications
β2-Glycoprotein I (β2-GPI) is a plasma protein that binds to negatively charged substances
such as DNA, heparin, and anionic phospholipids. The interaction of β2-GPI with anionic …

Characterization of β2-glycoprotein I binding to phospholipid membranes

MF Harper, PM Hayes, BR Lentz… - Thrombosis and …, 1998 - thieme-connect.com
The plasma protein β 2-glycoprotein I (β 2-GPI) is a major target of autoantibodies in patients
with the antiphospholipid syndrome. To understand the physiological function of β 2-GPI and …

Microheterogeneity of beta-2 glycoprotein I: implications for binding to anionic phospholipids

TA BRIGHTON, YP DAI, PJ HOGG… - Biochemical …, 1999 - portlandpress.com
Considerable interest is currently focused on the interactions of beta-2 glycoprotein I (β2GPI)
and anti-phospholipid antibodies with anionic phospholipids in an attempt to understand the …

Identification of the phospholipid-binding site of human β2-glycoprotein I domain V by heteronuclear magnetic resonance

M Hoshino, Y Hagihara, I Nishii, T Yamazaki… - Journal of Molecular …, 2000 - Elsevier
To understand the mechanism of the interaction between human β2-glycoprotein I (β2-GPI)
and negatively charged phospholipids, we determined the three-dimensional solution …

[HTML][HTML] β2‐Glycoprotein I: evolution, structure and function

PG De Groot, JCM Meijers - Journal of Thrombosis and Haemostasis, 2011 - Elsevier
Summary β 2‐Glycoprotein I (β 2‐GPI) is a protein that circulates in blood at high
concentrations. The function of β 2‐GPI has long been an enigma. More than 20 years ago …

Anti-β2-glycoprotein I autoantibodies from patients with the “antiphospholipid” syndrome bind to β2-glycoprotein I with low affinity: dimerization of β2-glycoprotein I …

Y Sheng, DA Kandiah, SA Krilis - The Journal of Immunology, 1998 - journals.aai.org
Abstract “Antiphospholipid” autoantibodies are associated with arterial and venous
thrombosis, recurrent fetal loss, and thrombocytopenia. At present, the best-characterized …