Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.
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Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular InflammationProline isomerization in the C-terminal region of HSP27.Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.Chaperone activity of human small heat shock protein-GST fusion proteins.Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau
P2860
Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.
description
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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
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2015年论文
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2015年论文
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2015年论文
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name
Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.
@en
type
label
Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.
@en
prefLabel
Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.
@en
P2093
P2860
P1476
Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1
@en
P2093
Amanda F Clouser
Ponni Rajagopal
P2860
P2888
P304
P356
10.1007/S10858-015-9973-0
P577
2015-08-05T00:00:00Z
P6179
1050396120