Dimerized Domain V of Beta2-Glycoprotein I Is Sufficient to Upregulate Procoagulant Activity in PMA-Treated U937 Monocytes and Require Intact Residues in Two Phospholipid-Binding Loops.

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Dimerized Domain V of Beta2-Glycoprotein I Is Sufficient to Upregulate Procoagulant Activity in PMA-Treated U937 Monocytes and Require Intact Residues in Two Phospholipid-Binding Loops.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

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2017年论文

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2017年论文

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name

Dimerized Domain V of Beta2-Gl ...... wo Phospholipid-Binding Loops.

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Item

label

Dimerized Domain V of Beta2-Gl ...... wo Phospholipid-Binding Loops.

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prefLabel

Dimerized Domain V of Beta2-Gl ...... wo Phospholipid-Binding Loops.

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P1476

Dimerized Domain V of Beta2-Gl ...... wo Phospholipid-Binding Loops.

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P2093

Alexey Kolyada

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David A Barrios

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Natalia Beglova

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P2860

Activated protein C ligation of ApoER2 (LRP8) causes Dab1-dependent signaling in U937 cells

The challenge of lipid rafts

Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids

A Novel Dimeric Inhibitor Targeting Beta2GPI in Beta2GPI/Antibody Complexes Implicated in Antiphospholipid Syndrome

International consensus statement on an update of the classification criteria for definite antiphospholipid syndrome (APS)

Site-directed mutagenesis of recombinant human beta 2-glycoprotein I identifies a cluster of lysine residues that are critical for phospholipid binding and anti-cardiolipin antibody activity

Morbidity and mortality in the antiphospholipid syndrome during a 10-year period: a multicentre prospective study of 1000 patients.

Thrombosis in primary antiphospholipid syndrome: a pivotal role for monocyte tissue factor expression.

Autoantibodies to beta2-glycoprotein I in systemic lupus erythematosus and primary antiphospholipid antibody syndrome: clinical correlations in comparison with other antiphospholipid antibody tests.

Beta2-glycoprotein I can exist in 2 conformations: implications for our understanding of the antiphospholipid syndrome.

P31

scholarly article

P356

10.3390/ANTIB6020008

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2017-06-02T00:00:00Z

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P698

28748111

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P932

5523967

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