Solution structure of Compstatin, a potent complement inhibitor
about
Compstatin: a complement inhibitor on its way to clinical applicationStructure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibitionDesign of a modified mouse protein with ligand binding properties of its human analog by molecular dynamics simulations: the case of C3 inhibition by compstatinA simple, yet highly accurate, QSAR model captures the complement inhibitory activity of compstatinNew compstatin variants through two de novo protein design frameworks.Novel analogues of the therapeutic complement inhibitor compstatin with significantly improved affinity and potency.Complement System Part I - Molecular Mechanisms of Activation and Regulation.Complement and its implications in cardiac ischemia/reperfusion: strategies to inhibit complement.A new generation of potent complement inhibitors of the Compstatin family.New compstatin peptides containing N-terminal extensions and non-natural amino acids exhibit potent complement inhibition and improved solubility characteristicsSpecies specificity of the complement inhibitor compstatin investigated by all-atom molecular dynamics simulationsMolecular dynamics in drug design: new generations of compstatin analogs.New analogs of the clinical complement inhibitor compstatin with subnanomolar affinity and enhanced pharmacokinetic propertiesNatural IgM-mediated innate autoimmunity: a new target for early intervention of ischemia-reperfusion injury.Peptide redesign for inhibition of the complement system: Targeting age-related macular degeneration.Structure-kinetic relationship analysis of the therapeutic complement inhibitor compstatin.Recent developments in low molecular weight complement inhibitorsComplement component C3 mediates Th1/Th17 polarization in human T-cell activation and cutaneous GVHD.C3b and factor H: key components of the complement system.The key roles of complement and tissue factor in Escherichia coli-induced coagulation in human whole blood.Novel compstatin family peptides inhibit complement activation by drusen-like deposits in human retinal pigmented epithelial cell cultures.Development of a new pharmacophore model that discriminates active compstatin analogs.Thermodynamic studies on the interaction of the third complement component and its inhibitor, compstatin.The structural basis of compstatin activity examined by structure-function-based design of peptide analogs and NMR.
P2860
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P2860
Solution structure of Compstatin, a potent complement inhibitor
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Solution structure of Compstatin, a potent complement inhibitor
@ast
Solution structure of Compstatin, a potent complement inhibitor
@en
Solution structure of Compstatin, a potent complement inhibitor
@nl
type
label
Solution structure of Compstatin, a potent complement inhibitor
@ast
Solution structure of Compstatin, a potent complement inhibitor
@en
Solution structure of Compstatin, a potent complement inhibitor
@nl
prefLabel
Solution structure of Compstatin, a potent complement inhibitor
@ast
Solution structure of Compstatin, a potent complement inhibitor
@en
Solution structure of Compstatin, a potent complement inhibitor
@nl
P2093
P2860
P356
P1433
P1476
Solution structure of Compstatin, a potent complement inhibitor
@en
P2093
P2860
P304
P356
10.1002/PRO.5560070311
P407
P577
1998-03-01T00:00:00Z