Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
about
Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defectsCrystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptideStructure and interactions of the translation initiation factor eIF1High-resolution structures of bacterially expressed soluble human CD59Structural and phylogenetic characterization of human SLURP-1, the first secreted mammalian member of the Ly-6/uPAR protein superfamilySolution structure of the alpha-subunit of human chorionic gonadotropinNMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1Identification and Structural Characterization of a New Three-Finger Toxin Hemachatoxin from Hemachatus haemachatus VenomStructural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59The urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/Endo180): membrane proteins engaged in matrix turnover during tissue remodelingThe Caenorhabditis elegans odr-2 gene encodes a novel Ly-6-related protein required for olfactionMolecular cloning of the rat analogue of human CD59: structural comparison with human CD59 and identification of a putative active siteCell signaling, post-translational protein modifications and NMR spectroscopyOverview of protein structural and functional folds.Overview of protein folds in the immune system.Effects of autoclaving and high pressure on allergenicity of hazelnut proteins.PATE, a gene expressed in prostate cancer, normal prostate, and testis, identified by a functional genomic approach.Structure and distribution of modules in extracellular proteins.GPIHBP1, an endothelial cell transporter for lipoprotein lipase.Complement System Part I - Molecular Mechanisms of Activation and Regulation.Assessing the role of the glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) three-finger domain in binding lipoprotein lipaseMapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9Role of complement and complement regulatory proteins in the complications of diabetesInhibition of the complement membrane attack complex by Schistosoma mansoni paramyosinMapping the active site of CD59Biochemistry and pathophysiology of intravascular and intracellular lipolysis.Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis.Molecular basis for a link between complement and the vascular complications of diabetesA specific and sensitive assay for blood levels of glycated CD59: a novel biomarker for diabetes.Mapping part of the functional epitope for ligand binding on the receptor for urokinase-type plasminogen activator by site-directed mutagenesis.The mystery behind membrane insertion: a review of the complement membrane attack complexPlasminogen activator inhibitor type 1 in cancer: therapeutic and prognostic implications.Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom alpha-neurotoxins.CD59 blocks not only the insertion of C9 into MAC but inhibits ion channel formation by homologous C5b-8 as well as C5b-9.Removal of domain D2 or D3 of the human urokinase receptor does not affect ligand affinity.Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59Conserved structural determinants in three-fingered protein domains.A distinctive histidine residue is essential for in vivo glycation-inactivation of human CD59 transgenically expressed in mice erythrocytes: Implications for human diabetes complications.Insights into the human CD59 complement binding interface toward engineering new therapeutics.Complement regulation.
P2860
Q24298184-3A5590CD-37E7-4E5D-A413-B9C6AFBA20D7Q24529128-16521475-8A39-4D2C-A4A8-208EB856E1D0Q24534133-134B7ED1-7149-4964-89B3-501E4007BA65Q24657819-D42A09E5-130E-4872-A1E1-D05D71B954CEQ24672686-CD93A3E0-2E30-404B-B68F-5D24A9D5E19FQ27617774-913BB917-68C4-4FFD-A6D8-93594F17C384Q27666667-CC4B3442-FCD6-47B7-8466-F98625738EA5Q27675088-6F843F75-7982-4759-971B-A407FC32582BQ27678091-99B5CCA4-4547-4EB0-8075-BB1DFCBCFA14Q28257803-4BC8CD5B-4169-47C1-8127-0EC2F29B2993Q28345584-D34C4D86-15C7-4199-930B-6CB7134A09EFQ28572539-6CB1DB3F-2C17-4E56-9ED1-DC64FCC0A519Q28830783-4CF820E7-A3B8-4937-9351-643B6CD5CC58Q30368988-9E3F3D66-8628-49FE-966C-B3291B10B350Q30369011-CEE44EA3-DF74-4C97-89D6-16AB1E2701FCQ30417102-6F2F963F-533D-461C-9A1B-A19E1BBCCC03Q34016309-999BC2BD-D353-4D2F-BF85-2082D9DAB2B4Q34063457-8DB2998D-C61D-47EE-9484-2D6F9752F336Q34208235-65D08E3D-970B-477F-AF43-209D80945E4DQ34481071-8E485EE7-6585-40A8-9C85-ED25035FA7CDQ35011033-DB19593C-D2CA-4054-A821-8D464CA95F43Q35063359-6CF935C2-A1C1-4E1C-A4CB-ACF54468FC54Q35657115-C162AD4D-91DE-428B-BB86-0B6BA993F195Q36375634-0A07B5FC-51D7-42D1-9F79-5CB8356F3D0BQ36376823-8105B264-7D74-4E38-A854-2EB5F38B9E21Q36708030-007DB42F-5DA9-404F-AC9B-38841A2EECC2Q36803615-49E49954-5A53-4250-9280-954BF550150BQ36977373-B701768B-E16E-4082-9DF7-76EB11A71B4FQ37178439-118200F3-056C-4443-9F74-A52AA9C0DE3CQ38317155-ABFDAD2C-BF99-40D2-BC45-756AF6E1FCC9Q39384364-EDE99B07-529A-430B-B14D-6D87E692702BQ40475372-046F6C60-7F4A-41ED-92EC-C4BC33210462Q40683497-64FC4D55-56F1-4500-82EB-24D74FB7622CQ40746391-E4BE4A63-777F-41D2-B7EF-300DA80E5DEEQ41226527-F117193A-8BB2-4E49-A183-71608763512DQ41909754-FDA6EFEB-5EA1-4642-A608-432674D8DEBBQ45106348-512E958F-E44B-4DC1-89BF-48F80EBDAA05Q46319885-BE5A8D53-5F30-4D0A-B69B-129B2EF68E70Q46633558-682650F4-F364-445A-A49A-E8F67285D3A3Q47686748-CD5C3A59-0171-408E-92C8-2275D1A61179
P2860
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
description
1994 nî lūn-bûn
@nan
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@ast
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@en
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@nl
type
label
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@ast
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@en
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@nl
prefLabel
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@ast
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@en
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@nl
P2093
P1433
P1476
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
@en
P2093
C M Fletcher
P J Lachmann
P304
P356
10.1016/S0969-2126(00)00020-4
P50
P577
1994-03-01T00:00:00Z