Aberrant disulphide bonding contributes to the ER retention of alpha1-antitrypsin deficiency variants.
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Cysteines as Redox Molecular Switches and Targets of Disease.The pathological Trento variant of alpha-1-antitrypsin (E75V) shows nonclassical behaviour during polymerization.Intermittent C1-Inhibitor Deficiency Associated with Recessive Inheritance: Functional and Structural Insight.Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases.The Multifaceted Effects of Alpha1-Antitrypsin on Neutrophil Functions.Alpha-1 antitrypsin deficiency: outstanding questions and future directions.EDEM1's mannosidase-like domain binds ERAD client proteins in a redox-sensitive manner and possesses catalytic activityDynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation
P2860
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P2860
Aberrant disulphide bonding contributes to the ER retention of alpha1-antitrypsin deficiency variants.
description
2015 nî lūn-bûn
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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
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
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2015年论文
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name
Aberrant disulphide bonding co ...... titrypsin deficiency variants.
@en
type
label
Aberrant disulphide bonding co ...... titrypsin deficiency variants.
@en
prefLabel
Aberrant disulphide bonding co ...... titrypsin deficiency variants.
@en
P2093
P2860
P50
P356
P1476
Aberrant disulphide bonding co ...... ntitrypsin deficiency variants
@en
P2093
Daniela Medicina
Riccardo Ronzoni
Romina Berardelli
P2860
P304
P356
10.1093/HMG/DDV501
P577
2015-12-08T00:00:00Z