The position of the disulfide bonds in human plasma alpha 2 HS-glycoprotein and the repeating double disulfide bonds in the domain structure
about
Friends and relations of the cystatin superfamily--new members and their evolutionPosttranslational processing of human alpha 2-HS glycoprotein (human fetuin). Evidence for the production of a phosphorylated single-chain form by hepatoma cellsAll-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins.Fluorogenic and fluorescent labeling reagents with a benzofurazan skeleton.The primary structure of cassowary (Casuarius casuarius) goose type lysozyme.The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family.Similar Albeit Not the Same: In-Depth Analysis of Proteoforms of Human Serum, Bovine Serum, and Recombinant Human Fetuin
P2860
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P2860
The position of the disulfide bonds in human plasma alpha 2 HS-glycoprotein and the repeating double disulfide bonds in the domain structure
description
1989 nî lūn-bûn
@nan
1989 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
The position of the disulfide ...... bonds in the domain structure
@ast
The position of the disulfide ...... bonds in the domain structure
@en
The position of the disulfide ...... bonds in the domain structure
@nl
type
label
The position of the disulfide ...... bonds in the domain structure
@ast
The position of the disulfide ...... bonds in the domain structure
@en
The position of the disulfide ...... bonds in the domain structure
@nl
prefLabel
The position of the disulfide ...... bonds in the domain structure
@ast
The position of the disulfide ...... bonds in the domain structure
@en
The position of the disulfide ...... bonds in the domain structure
@nl
P2093
P1476
The position of the disulfide ...... bonds in the domain structure
@en
P2093
P356
10.1016/0167-4838(89)90293-8
P407
P577
1989-02-23T00:00:00Z