Control of blood proteins by functional disulfide bonds.
about
Inflammatory and oxidative stress in rotavirus infectionCD44 Binding to Hyaluronic Acid Is Redox Regulated by a Labile Disulfide Bond in the Hyaluronic Acid Binding SiteVascular thiol isomerases.From structure to redox: The diverse functional roles of disulfides and implications in disease.Caspase-1-mediated pathway promotes generation of thromboinflammatory microparticles.Redox regulation of methionine aminopeptidase 2 activityRevisiting the mechanistic basis of the French Paradox: Red wine inhibits the activity of protein disulfide isomerase in vitro.Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.Photonic activation of plasminogen induced by low dose UVB.Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.Differential Receptor Binding and Regulatory Mechanisms for the Lymphangiogenic Growth Factors Vascular Endothelial Growth Factor (VEGF)-C and -D.Protein disulfide isomerase secretion following vascular injury initiates a regulatory pathway for thrombus formation.Using biomaterials to rewire the process of wound repair.Identification of allosteric disulfides from prestress analysis.Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy.Biosystems Study of the Molecular Networks Underlying Hippocampal Aging Progression and Anti-aging Treatment in Mice.Recent mass spectrometry-based techniques and considerations for disulfide bond characterization in proteins.One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor.Heterogeneous nuclear ribonucleoprotein E1 regulates protein disulphide isomerase translation in oxidized low-density lipoprotein-activated endothelial cells.An allosteric disulfide bond is involved in enhanced activation of factor XI by protein disulfide isomerase.Identification of allosteric disulfides from labile bonds in X-ray structures.An isomerase completes the circuit for a redox switch.Mechano-redox control of integrin de-adhesionReduction of leucocyte cell surface disulfide bonds during immune activation is dynamic as revealed by a quantitative proteomics workflow (SH-IQ)
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Control of blood proteins by functional disulfide bonds.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 12 February 2014
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Control of blood proteins by functional disulfide bonds.
@en
Control of blood proteins by functional disulfide bonds.
@nl
type
label
Control of blood proteins by functional disulfide bonds.
@en
Control of blood proteins by functional disulfide bonds.
@nl
prefLabel
Control of blood proteins by functional disulfide bonds.
@en
Control of blood proteins by functional disulfide bonds.
@nl
P2860
P50
P1433
P1476
Control of blood proteins by functional disulfide bonds
@en
P2093
Diego Butera
P2860
P304
P356
10.1182/BLOOD-2014-01-549816
P407
P577
2014-02-12T00:00:00Z