Membrane-induced conformational change in human apolipoprotein H.

Membrane-induced conformational change in human apolipoprotein H.

Item
http://www.wikidata.org/entity/Q41908801
Pathophysiology of the antiphospholipid syndromeMembrane binding of Escherichia coli RNase E catalytic domain stabilizes protein structure and increases RNA substrate affinity.Human apolipoprotein H may have various orientations when attached to lipid layer.Antiphospholipid antibodies: effects on trophoblast and endothelial cells.γδ T cell receptor ligands and modes of antigen recognitionBiotinylation of glycan chains in beta2 glycoprotein I induces dimerization of the molecule and its detection by the human autoimmune anti-cardiolipin antibody EY2C9Covalent attachment of functionalized cardiolipin on a biosensor gold surface allows repetitive measurements of anticardiolipin antibodies in serum.Membrane binding of beta2-glycoprotein I can be described by a two-state reaction model: an atomic force microscopy and surface plasmon resonance study.The binding site in {beta}2-glycoprotein I for ApoER2' on platelets is located in domain V.
P2860

Membrane-induced conformational change in human apolipoprotein H.

Item
http://www.wikidata.org/entity/Q41908801
description
2000 nî lūn-bûn
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name
Membrane-induced conformational change in human apolipoprotein H.
@en
type
label
Membrane-induced conformational change in human apolipoprotein H.
@en
prefLabel
Membrane-induced conformational change in human apolipoprotein H.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P478
P577
P5875
P698
P932
P356
P1433
P1476
Membrane-induced conformational change in human apolipoprotein H.
@en
P2093
P2860
P304
P31
P356
P407
P478
P577
P5875
P698
P932