Structural and functional characterization of Caenorhabditis elegans α-catenin reveals constitutive binding to β-catenin and F-actin.
about
Structural and functional characterization of the α-catenin·β-catenin binding interface in Caenorhabditis elegans reveals conserved requirements for cell-cell adhesion in metazoans.Real-time TIRF observation of vinculin recruitment to stretched α-catenin by AFM.Nonmuscle myosin IIA is involved in recruitment of apical junction components through activation of α-catenin.Analysis of a vinculin homolog in a sponge (phylum Porifera) reveals that vertebrate-like cell adhesions emerged early in animal evolution
P2860
Structural and functional characterization of Caenorhabditis elegans α-catenin reveals constitutive binding to β-catenin and F-actin.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年學術文章
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2017年學術文章
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name
Structural and functional char ...... ding to β-catenin and F-actin.
@en
type
label
Structural and functional char ...... ding to β-catenin and F-actin.
@en
prefLabel
Structural and functional char ...... ding to β-catenin and F-actin.
@en
P2093
P2860
P356
P1476
Structural and functional char ...... ding to β-catenin and F-actin.
@en
P2093
Adam V Kwiatkowski
Hee-Jung Choi
Hyunook Kang
Injin Bang
Jeff Hardin
Jonathon A Heier
Kyeong Sik Jin
W James Nelson
P2860
P304
P356
10.1074/JBC.M116.769778
P407
P577
2017-03-15T00:00:00Z