Phage display reveals a novel interaction of human tear lipocalin and thioredoxin which is relevant for ligand binding.
about
Human tear lipocalin acts as an oxidative-stress-induced scavenger of potentially harmful lipid peroxidation products in a cell culture systemRestoration of structural stability and ligand binding after removal of the conserved disulfide bond in tear lipocalin.Tear lipocalin: structure and function.Is dimerization a common feature in thioredoxins? The case of thioredoxin from Litopenaeus vannamei.Translationally controlled tumor protein of Brugia malayi functions as an antioxidant protein.Sumoylation of human translationally controlled tumor protein is important for its nuclear transportThe conserved disulfide bond of human tear lipocalin modulates conformation and lipid binding in a ligand selective manner.Functional cavity dimensions of tear lipocalin.Tear Lipocalin: Structure, Function and Molecular Mechanisms of Action
P2860
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P2860
Phage display reveals a novel interaction of human tear lipocalin and thioredoxin which is relevant for ligand binding.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Phage display reveals a novel ...... s relevant for ligand binding.
@ast
Phage display reveals a novel ...... s relevant for ligand binding.
@en
type
label
Phage display reveals a novel ...... s relevant for ligand binding.
@ast
Phage display reveals a novel ...... s relevant for ligand binding.
@en
prefLabel
Phage display reveals a novel ...... s relevant for ligand binding.
@ast
Phage display reveals a novel ...... s relevant for ligand binding.
@en
P2093
P2860
P1433
P1476
Phage display reveals a novel ...... s relevant for ligand binding.
@en
P2093
P2860
P304
P356
10.1016/S0014-5793(99)01331-9
P407
P577
1999-10-01T00:00:00Z