Domain structure of human alpha 2-macroglobulin. Characterization of a receptor-binding domain obtained by digestion with papain
about
Binding of alpha2ML1 to the low density lipoprotein receptor-related protein 1 (LRP1) reveals a new role for LRP1 in the human epidermisHuman alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3Structure of a rat α1-macroglobulin receptor-binding domain dimerMutations in CPAMD8 Cause a Unique Form of Autosomal-Recessive Anterior Segment DysgenesisA 16-amino acid peptide from human alpha2-macroglobulin binds transforming growth factor-beta and platelet-derived growth factor-BB.Characterization and immunohistochemical localization of alpha 2-macroglobulin receptor (low-density lipoprotein receptor-related protein) in human brain.The structure of alpha 2-macroglobulin-methylamine after papain digestion as determined by electron microscopy.An alpha 2-macroglobulin receptor-dependent mechanism for the plasma clearance of transforming growth factor-beta 1 in miceBinding 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.C3bi receptor (complement receptor type 3) recognizes a region of complement protein C3 containing the sequence Arg-Gly-Asp.Analysis of Alpha-2 Macroglobulin from the Long-Lived and Cancer-Resistant Naked Mole-Rat and Human PlasmaAcute phase proteins are major clients for the chaperone action of α₂-macroglobulin in human plasmaUnique features of a Pseudomonas aeruginosa α2-macroglobulin homolog.Altered interaction of Cis-dichlorodiammineplatinum(II)--modified alpha 2-macroglobulin (alpha 2M) with the low density lipoprotein receptor-related protein/alpha 2M receptor but not the alpha 2M signaling receptor.Molecular dissection of the human alpha2-macroglobulin subunit reveals domains with antagonistic activities in cell signaling.Surfactant protein D interacts with alpha2-macroglobulin and increases its innate immune potential.Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin
P2860
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P2860
Domain structure of human alpha 2-macroglobulin. Characterization of a receptor-binding domain obtained by digestion with papain
description
1986 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1986
@ast
im September 1986 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: September 1986)
@en
vedecký článok (publikovaný 1986/09/01)
@sk
vědecký článek publikovaný v roce 1986
@cs
wetenschappelijk artikel (gepubliceerd op 1986/09/01)
@nl
наукова стаття, опублікована у вересні 1986
@uk
научни чланак (објављен 1986/09/01)
@sr
name
Domain structure of human alph ...... ained by digestion with papain
@ast
Domain structure of human alph ...... ained by digestion with papain
@en
Domain structure of human alph ...... ained by digestion with papain
@nl
type
label
Domain structure of human alph ...... ained by digestion with papain
@ast
Domain structure of human alph ...... ained by digestion with papain
@en
Domain structure of human alph ...... ained by digestion with papain
@nl
prefLabel
Domain structure of human alph ...... ained by digestion with papain
@ast
Domain structure of human alph ...... ained by digestion with papain
@en
Domain structure of human alph ...... ained by digestion with papain
@nl
P2093
P1433
P1476
Domain structure of human alph ...... ained by digestion with papain
@en
P2093
F Van Leuven
J Gliemann
L Sottrup-Jensen
P407
P577
1986-09-01T00:00:00Z