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Human serum-derived protein removes the need for coating in defined human pluripotent stem cell culture.Structure and function of inter-alpha-trypsin inhibitor heavy chains.Unmasking a hyaluronan-binding site of the BX(7)B type in the H3 heavy chain of the inter-alpha-inhibitor family.Constitutive expression of pentraxin 3 (PTX3) protein by human amniotic membrane cells leads to formation of the heavy chain (HC)-hyaluronan (HA)-PTX3 complex.Inter-alpha inhibitor protein administration improves survival from neonatal sepsis in miceThe link module from human TSG-6 inhibits neutrophil migration in a hyaluronan- and inter-alpha -inhibitor-independent manner.Inter-alpha-trypsin inhibitor, a covalent protein-glycosaminoglycan-protein complex.Incorporation of pentraxin 3 into hyaluronan matrices is tightly regulated and promotes matrix cross-linking.Serum Inter-α-inhibitor activates the Yes tyrosine kinase and YAP/TEAD transcriptional complex in mouse embryonic stem cells.TSG-6 potentiates the antitissue kallikrein activity of inter-alpha-inhibitor through bikunin release.Constitutive expression of inter-α-inhibitor (IαI) family proteins and tumor necrosis factor-stimulated gene-6 (TSG-6) by human amniotic membrane epithelial and stromal cells supporting formation of the heavy chain-hyaluronan (HC-HA) complex.Heavy chains of inter alpha inhibitor (IαI) inhibit the human complement system at early stages of the cascade.The Compact and Biologically Relevant Structure of Inter-α-inhibitor Is Maintained by the Chondroitin Sulfate Chain and Divalent CationsTumor Necrosis Factor-stimulated Gene 6 (TSG-6)-mediated Interactions with the Inter-α-inhibitor Heavy Chain 5 Facilitate Tumor Growth Factor β1 (TGFβ1)-dependent Fibroblast to Myofibroblast DifferentiationBiochemical characterization and function of complexes formed by hyaluronan and the heavy chains of inter-alpha-inhibitor (HC*HA) purified from extracts of human amniotic membrane.Positive Mode LC-MS/MS Analysis of Chondroitin Sulfate Modified Glycopeptides Derived from Light and Heavy Chains of The Human Inter-α-Trypsin Inhibitor Complex.Molecular heterogeneity of the SHAP-hyaluronan complex. Isolation and characterization of the complex in synovial fluid from patients with rheumatoid arthritis.Characterization of the interaction between tumor necrosis factor-stimulated gene-6 and heparin: implications for the inhibition of plasmin in extracellular matrix microenvironments.Equivalent involvement of inter-alpha-trypsin inhibitor heavy chain isoforms in forming covalent complexes with hyaluronan.Urine protein markers distinguish stone-forming from non-stone-forming relatives of calcium stone formers.Pig MAP/ITIH4 and haptoglobin are interleukin-6-dependent acute-phase plasma proteins in porcine primary cultured hepatocytes
P2860
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P2860
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im Januar 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в січні 1999
@uk
name
Structural Characterization of Inter-α-inhibitor
@en
Structural Characterization of Inter-α-inhibitor
@nl
type
label
Structural Characterization of Inter-α-inhibitor
@en
Structural Characterization of Inter-α-inhibitor
@nl
prefLabel
Structural Characterization of Inter-α-inhibitor
@en
Structural Characterization of Inter-α-inhibitor
@nl
P2093
P2860
P356
P1476
Structural characterization of inter-alpha-inhibitor. Evidence for an extended shape
@en
P2093
P2860
P304
P356
10.1074/JBC.274.1.298
P407
P577
1999-01-01T00:00:00Z