Evidence for similar conformational changes in alpha 2-macroglobulin on reaction with primary amines or proteolytic enzymes.
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Alpha-2-macroglobulin functions as an inhibitor of fibrinolytic, clotting, and neutrophilic proteinases in sepsis: studies using a baboon modelBinding of transforming growth factor-beta 1 to methylamine-modified alpha 2-macroglobulin and to binary and ternary alpha 2-macroglobulin-proteinase complexesAlpha 2-macroglobulin functions as a cytokine carrier to induce nitric oxide synthesis and cause nitric oxide-dependent cytotoxicity in the RAW 264.7 macrophage cell line.Binding of platelet-derived growth factor-BB and transforming growth factor-beta 1 to alpha 2-macroglobulin in vitro and in vivo: comparison of receptor-recognized and non-recognized alpha 2-macroglobulin conformations.Differences in the binding of transforming growth factor beta 1 to the acute-phase reactant and constitutively synthesized alpha-macroglobulins of rat.Activated alpha 2-macroglobulin promotes mitogenesis in rat vascular smooth muscle cells by a mechanism that is independent of growth-factor-carrier activity.Proteinases are isoform-specific regulators of the binding of transforming growth factor beta to alpha 2-macroglobulin.Chemical modification of alpha2-macroglobulin to generate derivatives that bind transforming growth factor-beta with increased affinity.Localization of the binding site for transforming growth factor-beta in human alpha2-macroglobulin to a 20-kDa peptide that also contains the bait region.alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli.Low resolution X-ray structure of human methylamine-treated alpha 2-macroglobulin.Effect of methylamine and plasmin on the conformation of human alpha 2-macroglobulin as revealed by differential scanning calorimetric analysisStructural analysis of acute-phase alpha 2-macroglobulin.Inactivation of human gamma interferon by Pseudomonas aeruginosa proteases: elastase augments the effects of alkaline protease despite the presence of alpha 2-macroglobulinThe human alpha 2-macroglobulin receptor: identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin.Molecular cloning of Limulus alpha 2-macroglobulin.Common evolutionary origin of alpha 2-macroglobulin and complement components C3 and C4.The proteinase-binding reaction of alpha 2M.Electron microscopy of the conformational changes of alpha 2-macroglobulin from human plasmaThe structure around the thioester bond in bovine alpha 2-macroglobulin. Possible implications for the conformational stability of the inhibitor on thioester cleavage.Role of the scavenger receptor in the uptake of methylamine-activated alpha 2-macroglobulin by rat liver.Stoichiometry of reactions of alpha 2-macroglobulin with trypsin and chymotrypsin.Native conformations of human complement components C3 and C4 show different dependencies on thioester formation.Purification and characterization of human alpha 2-macroglobulin conformational variants by non-ideal high performance size-exclusion chromatography.Interaction of transforming growth factor-beta-1 with alpha-2-macroglobulin from normal and inflamed equine joints.Further characterization of the platinum-reactive component of the alpha 2-macroglobulin-receptor recognition site.The conformational changes of alpha 2-macroglobulin induced by methylamine or trypsin. Characterization by extrinsic and intrinsic spectroscopic probes.Limulus alpha 2-macroglobulin. First evidence in an invertebrate for a protein containing an internal thiol ester bond.Binding of proteinases to human alpha 2-macroglobulin with its thioester bonds cleaved by methylamine in the presence of a thiol-group-cyanylating reagent.Uric acid mediates photodynamic inactivation of caprine alpha-2-macroglobulin.A derivative of the plasma protease inhibitor alpha(2)-macroglobulin regulates the response to peripheral nerve injury.Limited mutations in full-length tetrameric human alpha2-macroglobulin abrogate binding of platelet-derived growth factor-BB and transforming growth factor-beta1.The properties of rabbit alpha1-macroglobulin upon activation are distinct from those of rabbit and human alpha2-macroglobulins.Similar architectures of native and transformed human alpha2-macroglobulin suggest the transformation mechanism.
P2860
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P2860
Evidence for similar conformational changes in alpha 2-macroglobulin on reaction with primary amines or proteolytic enzymes.
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年論文
@yue
1982年論文
@zh-hant
1982年論文
@zh-hk
1982年論文
@zh-mo
1982年論文
@zh-tw
1982年论文
@wuu
1982年论文
@zh
1982年论文
@zh-cn
name
Evidence for similar conformat ...... amines or proteolytic enzymes.
@en
type
label
Evidence for similar conformat ...... amines or proteolytic enzymes.
@en
prefLabel
Evidence for similar conformat ...... amines or proteolytic enzymes.
@en
P2860
P356
P1433
P1476
Evidence for similar conformat ...... amines or proteolytic enzymes.
@en
P2093
P2860
P304
P356
10.1042/BJ2070347
P407
P577
1982-11-01T00:00:00Z