Structure of protease-cleaved Escherichia coli α-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.
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α2-Macroglobulins: Structure and Function.Hypertrophic cardiomyopathy mutations in the calponin-homology domain of ACTN2 affect actin binding and cardiomyocyte Z-disc incorporation.Oxidation of proteins: is it a programmed process?Assembly of an atypical α-macroglobulin complex from Pseudomonas aeruginosa.CD109 and squamous cell carcinoma.
P2860
Structure of protease-cleaved Escherichia coli α-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.
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2015 nî lūn-bûn
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2015 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունիսին հրատարակված գիտական հոդված
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2015年の論文
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2015年論文
@yue
2015年論文
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2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
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2015年论文
@wuu
name
Structure of protease-cleaved ...... ation for protease entrapment.
@ast
Structure of protease-cleaved ...... ation for protease entrapment.
@en
type
label
Structure of protease-cleaved ...... ation for protease entrapment.
@ast
Structure of protease-cleaved ...... ation for protease entrapment.
@en
prefLabel
Structure of protease-cleaved ...... ation for protease entrapment.
@ast
Structure of protease-cleaved ...... ation for protease entrapment.
@en
P2093
P2860
P50
P1476
Structure of protease-cleaved ...... ation for protease entrapment.
@en
P2093
Aleksander W Roszak
Cameron D Fyfe
Daniel M Wall
Khedidja Mosbahi
Olwyn Byron
P2860
P304
P356
10.1107/S1399004715008548
P577
2015-06-30T00:00:00Z