Structural analysis of lipid complexes of GM2-activator protein
about
The role of hydrophobic interactions in positioning of peripheral proteins in membranesThe liganding of glycolipid transfer protein is controlled by glycolipid acyl structurePoint mutational analysis of the liganding site in human glycolipid transfer protein. Functionality of the complex.Crystal structures of saposins A and CStructural basis for glycosphingolipid transfer specificityGlycolipid transfer proteinsStructural and mechanistic analyses of endo-glycoceramidase II, a membrane-associated family 5 glycosidase in the Apo and GM3 ganglioside-bound formsStructural Basis of Sterol Binding by NPC2, a Lysosomal Protein Deficient in Niemann-Pick Type C2 DiseaseCrystal structure of soluble MD-1 and its interaction with lipid IVaTranscription factor Bcl11b controls selection of invariant natural killer T-cells by regulating glycolipid presentation in double-positive thymocytesDiscovery of novel membrane binding structures and functionsCharacterizing solution surface loop conformational flexibility of the GM2 activator protein.Photoaffinity labelling of the human GM2-activator protein. Mechanistic insight into ganglioside GM2 degradation.Synthetic toll-like receptor 4 agonists stimulate innate resistance to infectious challenge.Editing of CD1d-bound lipid antigens by endosomal lipid transfer proteins.Ganglioside biochemistryDrosophila melanogaster NPC2 proteins bind bacterial cell wall components and may function in immune signal pathways.Lipid-binding proteins in membrane digestion, antigen presentation, and antimicrobial defense.Sphingolipid transfer proteins defined by the GLTP-fold.TLR4-MD-2 complex is negatively regulated by an endogenous ligand, globotetraosylceramide.Isolation of monomeric and dimeric secreted MD-2. Endotoxin.sCD14 and Toll-like receptor 4 ectodomain selectively react with the monomeric form of secreted MD-2.A Drosophila protein family implicated in pheromone perception is related to Tay-Sachs GM2-activator protein.Identification of ganglioside GM2 activator playing a role in cancer cell migration through proteomic analysis of breast cancer secretomes.Ligand extraction properties of the GM2 activator protein and its interactions with lipid vesiclesInteractions of the GM2 activator protein with phosphatidylcholine bilayers: a site-directed spin-labeling power saturation study.The immunological functions of saposins.My journey into the world of sphingolipids and sphingolipidoses.Paclitaxel binding to human and murine MD-2.The enzyme-binding region of human GM2-activator protein.Combined replacement effects of human modified β-hexosaminidase B and GM2 activator protein on GM2 gangliosidoses fibroblasts.Saposin B binds and transfers phospholipids.Ganglioside GM2 activator presents GM2 to hexosaminidase for cleavageMolecular pathology of Sandhoff disease with p.Arg505Gln in HEXB: application of simulation analysis.
P2860
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P2860
Structural analysis of lipid complexes of GM2-activator protein
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structural analysis of lipid complexes of GM2-activator protein
@ast
Structural analysis of lipid complexes of GM2-activator protein
@en
Structural analysis of lipid complexes of GM2-activator protein
@nl
type
label
Structural analysis of lipid complexes of GM2-activator protein
@ast
Structural analysis of lipid complexes of GM2-activator protein
@en
Structural analysis of lipid complexes of GM2-activator protein
@nl
prefLabel
Structural analysis of lipid complexes of GM2-activator protein
@ast
Structural analysis of lipid complexes of GM2-activator protein
@en
Structural analysis of lipid complexes of GM2-activator protein
@nl
P2093
P3181
P1476
Structural analysis of lipid complexes of GM2-activator protein
@en
P2093
Christine Schubert Wright
Fraydoon Rastinejad
Qiang Zhao
P304
P3181
P356
10.1016/S0022-2836(03)00794-0
P407
P577
2003-08-22T00:00:00Z