The preferential heterodimerization of human small heat shock proteins HSPB1 and HSPB6 is dictated by the N-terminal domain.
about
The growing world of small heat shock proteins: from structure to functions.An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins.Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP familyTerminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3
P2860
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P2860
The preferential heterodimerization of human small heat shock proteins HSPB1 and HSPB6 is dictated by the N-terminal domain.
description
2016 nî lūn-bûn
@nan
2016年の論文
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2016年学术文章
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2016年学术文章
@zh
2016年学术文章
@zh-cn
2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
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2016年學術文章
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name
The preferential heterodimeriz ...... ated by the N-terminal domain.
@en
The preferential heterodimeriz ...... ated by the N-terminal domain.
@nl
type
label
The preferential heterodimeriz ...... ated by the N-terminal domain.
@en
The preferential heterodimeriz ...... ated by the N-terminal domain.
@nl
prefLabel
The preferential heterodimeriz ...... ated by the N-terminal domain.
@en
The preferential heterodimeriz ...... ated by the N-terminal domain.
@nl
P2093
P50
P1154
2-s2.0-84992111128
P1476
The preferential heterodimeriz ...... ated by the N-terminal domain.
@en
P2093
Esther M Martin
Michelle Heirbaut
Sergei V Strelkov
Steven Beelen
Tim Verschueren
P356
10.1016/J.ABB.2016.10.002
P407
P577
2016-10-04T00:00:00Z