Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
about
An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding.Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks.Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights
P2860
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
description
2015 nî lūn-bûn
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2015 թուականի Մարտին հրատարակուած գիտական յօդուած
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2015 թվականի մարտին հրատարակված գիտական հոդված
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
@zh-hk
2015年論文
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2015年論文
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2015年论文
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name
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
@ast
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
@en
type
label
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
@ast
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
@en
prefLabel
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
@ast
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.
@en
P2860
P50
P356
P1476
Role of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function
@en
P2093
Jamie Morris
Xiaodi Deng
P2860
P304
10689-10702
P356
10.1074/JBC.M115.637058
P407
P577
2015-03-02T00:00:00Z