Structure of the fibrinogen γ-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization
about
A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A.To fuse or not to fuse: what is your purpose?Polymer-driven crystallizationStructural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin α IIb β 3Mechanistic Strategies for Catalysis Adopted by Evolutionary Distinct Family 43 ArabinanasesBinding of a fibrinogen mimetic stabilizes integrin alphaIIbbeta3's open conformationA synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.Preventing Staphylococcus aureus sepsis through the inhibition of its agglutination in blood.Exploring Staphylococcus aureus pathways to disease for vaccine development.Pathogenesis of Staphylococcus aureus Bloodstream Infections.Engineering of plasminogen activators for targeting to thrombus and heightening thrombolytic efficacy.Addition of missing loops and domains to protein models by x-ray solution scattering.Engineered isopeptide bond stabilized fibrin inspired nanoscale peptide based sealants for efficient blood clotting.Thioredoxin as a fusion tag for carrier-driven crystallization.Modeling the Kinetics of Integrin Receptor Binding to Hepatic Extracellular Matrix Proteins.X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site.Effects of snake venom proteases on human fibrinogen chains.Thrombus-targeted nanocarrier attenuates bleeding complications associated with conventional thrombolytic therapy.Serum albumin-protamine conjugate for biocompatible platform for targeted delivery of therapeutic macromolecules.Tissue plasminogen activator-based nanothrombolysis for ischemic stroke.Mechanistic Basis for the Binding of RGD- and AGDV-Peptides to the Platelet Integrin αIIbβ3.The macro domain as fusion tag for carrier-driven crystallization.Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the gamma chain of firbinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation.
P2860
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P2860
Structure of the fibrinogen γ-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structure of the fibrinogen γ- ...... protein driven crystallization
@ast
Structure of the fibrinogen γ- ...... protein driven crystallization
@en
Structure of the fibrinogen γ- ...... protein driven crystallization
@nl
type
label
Structure of the fibrinogen γ- ...... protein driven crystallization
@ast
Structure of the fibrinogen γ- ...... protein driven crystallization
@en
Structure of the fibrinogen γ- ...... protein driven crystallization
@nl
prefLabel
Structure of the fibrinogen γ- ...... protein driven crystallization
@ast
Structure of the fibrinogen γ- ...... protein driven crystallization
@en
Structure of the fibrinogen γ- ...... protein driven crystallization
@nl
P2093
P2860
P356
P1433
P1476
Structure of the fibrinogen γ- ...... protein driven crystallization
@en
P2093
P2860
P304
P356
10.1110/PS.8.12.2663
P577
1999-12-01T00:00:00Z