Identical or overlapping sequences in the primary structure of human alpha(2)-macroglobulin are responsible for the binding of nerve growth factor-beta, platelet-derived growth factor-BB, and transforming growth factor-beta.
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Further evidence for increased macrophage migration inhibitory factor expression in prostate cancer.Targeted Therapies in Liver Fibrosis: Combining the Best Parts of Platelet-Derived Growth Factor BB and Interferon GammaA 16-amino acid peptide from human alpha2-macroglobulin binds transforming growth factor-beta and platelet-derived growth factor-BB.Distinct binding sites in the structure of alpha 2-macroglobulin mediate the interaction with beta-amyloid peptide and growth factors.Alpha2-macroglobulin is a mediator of retinal ganglion cell death in glaucoma.Prostate stem cells and benign prostatic hyperplasiaHepcidin bound to α2-macroglobulin reduces ferroportin-1 expression and enhances its activity at reducing serum iron levels.Molecular dissection of the human alpha2-macroglobulin subunit reveals domains with antagonistic activities in cell signaling.The mosaic receptor sorLA/LR11 binds components of the plasminogen-activating system and platelet-derived growth factor-BB similarly to LRP1 (low-density lipoprotein receptor-related protein), but mediates slow internalization of bound ligand.Binding of alpha2-macroglobulin to GRAB (Protein G-related alpha2-macroglobulin-binding protein), an important virulence factor of group A streptococci, is mediated by two charged motifs in the DeltaA region.Characterization of the interaction between alpha2-macroglobulin and fibroblast growth factor-2: the role of hydrophobic interactions.Identification of the high affinity binding site in transforming growth factor-beta involved in complex formation with alpha 2-macroglobulin. Implications regarding the molecular mechanisms of complex formation between alpha 2-macroglobulin and growTGF-beta impairs renal autoregulation via generation of ROS.Limited mutations in full-length tetrameric human alpha2-macroglobulin abrogate binding of platelet-derived growth factor-BB and transforming growth factor-beta1.
P2860
Q24813097-D5EE87D7-5E9E-4E5F-9565-B3B0AE1C18ACQ26779055-9F28BD51-0C9C-4115-9B93-30F9276E39C3Q30306524-29A6453C-56B9-475D-A6BF-1DE6021BF9D7Q30308620-38CC362D-C5F4-4E0B-B058-770C4A453F03Q36944788-A51C2215-A140-4B1D-844D-B9B10E48DFE0Q37127502-FDE47C27-0736-4371-A2B8-A992D6121080Q37132152-E2EAA19D-D101-43EB-B799-F61F3CBA03CAQ39979231-C74792FD-34BE-4864-B6EF-D822FF0BB9B0Q40571781-B248BFEB-8434-44D5-A5B1-E0FCA805CC3CQ42807143-5A418ECA-AEB8-42B4-AAB3-230E1D3BAE2AQ43003062-AEBB2429-3DD0-4492-B79C-F155F3CD7F19Q43754772-A4873029-939C-4AA8-92FE-407C99258DA9Q45220024-56477ACE-9772-4751-A616-C502908F35E3Q46207609-1C54A0E2-D94E-4D0A-8CA0-0CFF28C0990E
P2860
Identical or overlapping sequences in the primary structure of human alpha(2)-macroglobulin are responsible for the binding of nerve growth factor-beta, platelet-derived growth factor-BB, and transforming growth factor-beta.
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2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Identical or overlapping seque ...... ansforming growth factor-beta.
@ast
Identical or overlapping seque ...... ansforming growth factor-beta.
@en
type
label
Identical or overlapping seque ...... ansforming growth factor-beta.
@ast
Identical or overlapping seque ...... ansforming growth factor-beta.
@en
prefLabel
Identical or overlapping seque ...... ansforming growth factor-beta.
@ast
Identical or overlapping seque ...... ansforming growth factor-beta.
@en
P2093
P356
P1476
Identical or overlapping seque ...... ansforming growth factor-beta.
@en
P2093
A Carmichael
D W Roadcap
J M Mettenburg
S L Gonias
P304
P356
10.1074/JBC.275.8.5826
P407
P577
2000-02-01T00:00:00Z