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The mechanical response of talin
by
Hu, Xian
, Sheetz, Michael P.
, Klapholz, Benjamin
, Toseland, Christopher P.
, Yan, Jie
, Cong, Peiwen
, Yao, Mingxi
, Goult, Benjamin T.
, Guo, Yingjian
in
631/45/535
/ 631/57/2272/1590
/ 82
/ 96
/ Adhesion
/ Animals
/ Binding Sites
/ Biomechanical Phenomena
/ Cell adhesion & migration
/ Cloning, Molecular
/ Cytoskeleton
/ Endopeptidases - chemistry
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Extracellular matrix
/ Gene Expression
/ Glutathione Transferase - genetics
/ Glutathione Transferase - metabolism
/ Humanities and Social Sciences
/ Kinetics
/ Mice
/ Models, Molecular
/ multidisciplinary
/ Physiology
/ Protein Binding
/ Protein Folding
/ Protein Interaction Domains and Motifs
/ Protein Refolding
/ Protein Structure, Secondary
/ Proteins
/ Recombinant Fusion Proteins - chemistry
/ Recombinant Fusion Proteins - genetics
/ Recombinant Fusion Proteins - metabolism
/ Science
/ Science (multidisciplinary)
/ Single Molecule Imaging - methods
/ Stress, Mechanical
/ Talin - chemistry
/ Talin - genetics
/ Talin - metabolism
/ Thermodynamics
2016
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The mechanical response of talin
by
Hu, Xian
, Sheetz, Michael P.
, Klapholz, Benjamin
, Toseland, Christopher P.
, Yan, Jie
, Cong, Peiwen
, Yao, Mingxi
, Goult, Benjamin T.
, Guo, Yingjian
in
631/45/535
/ 631/57/2272/1590
/ 82
/ 96
/ Adhesion
/ Animals
/ Binding Sites
/ Biomechanical Phenomena
/ Cell adhesion & migration
/ Cloning, Molecular
/ Cytoskeleton
/ Endopeptidases - chemistry
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Extracellular matrix
/ Gene Expression
/ Glutathione Transferase - genetics
/ Glutathione Transferase - metabolism
/ Humanities and Social Sciences
/ Kinetics
/ Mice
/ Models, Molecular
/ multidisciplinary
/ Physiology
/ Protein Binding
/ Protein Folding
/ Protein Interaction Domains and Motifs
/ Protein Refolding
/ Protein Structure, Secondary
/ Proteins
/ Recombinant Fusion Proteins - chemistry
/ Recombinant Fusion Proteins - genetics
/ Recombinant Fusion Proteins - metabolism
/ Science
/ Science (multidisciplinary)
/ Single Molecule Imaging - methods
/ Stress, Mechanical
/ Talin - chemistry
/ Talin - genetics
/ Talin - metabolism
/ Thermodynamics
2016
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The mechanical response of talin
by
Hu, Xian
, Sheetz, Michael P.
, Klapholz, Benjamin
, Toseland, Christopher P.
, Yan, Jie
, Cong, Peiwen
, Yao, Mingxi
, Goult, Benjamin T.
, Guo, Yingjian
in
631/45/535
/ 631/57/2272/1590
/ 82
/ 96
/ Adhesion
/ Animals
/ Binding Sites
/ Biomechanical Phenomena
/ Cell adhesion & migration
/ Cloning, Molecular
/ Cytoskeleton
/ Endopeptidases - chemistry
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Extracellular matrix
/ Gene Expression
/ Glutathione Transferase - genetics
/ Glutathione Transferase - metabolism
/ Humanities and Social Sciences
/ Kinetics
/ Mice
/ Models, Molecular
/ multidisciplinary
/ Physiology
/ Protein Binding
/ Protein Folding
/ Protein Interaction Domains and Motifs
/ Protein Refolding
/ Protein Structure, Secondary
/ Proteins
/ Recombinant Fusion Proteins - chemistry
/ Recombinant Fusion Proteins - genetics
/ Recombinant Fusion Proteins - metabolism
/ Science
/ Science (multidisciplinary)
/ Single Molecule Imaging - methods
/ Stress, Mechanical
/ Talin - chemistry
/ Talin - genetics
/ Talin - metabolism
/ Thermodynamics
2016
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Journal Article
The mechanical response of talin
2016
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Overview
Talin, a force-bearing cytoplasmic adapter essential for integrin-mediated cell adhesion, links the actin cytoskeleton to integrin-based cell–extracellular matrix adhesions at the plasma membrane. Its C-terminal rod domain, which contains 13 helical bundles, plays important roles in mechanosensing during cell adhesion and spreading. However, how the structural stability and transition kinetics of the 13 helical bundles of talin are utilized in the diverse talin-dependent mechanosensing processes remains poorly understood. Here we report the force-dependent unfolding and refolding kinetics of all talin rod domains. Using experimentally determined kinetics parameters, we determined the dynamics of force fluctuation during stretching of talin under physiologically relevant pulling speeds and experimentally measured extension fluctuation trajectories. Our results reveal that force-dependent stochastic unfolding and refolding of talin rod domains make talin a very effective force buffer that sets a physiological force range of only a few pNs in the talin-mediated force transmission pathway.
Talin is a mechanosensing cytoplasmic adaptor that links integrin cell adhesion receptors to the actin cytoskeleton. Here the authors measure the force-dependent folding and refolding kinetics of all talin rod domains to propose that talin can function as a force buffer under physiologically relevant conditions.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82
/ 96
/ Adhesion
/ Animals
/ Escherichia coli - metabolism
/ Glutathione Transferase - genetics
/ Glutathione Transferase - metabolism
/ Humanities and Social Sciences
/ Kinetics
/ Mice
/ Protein Interaction Domains and Motifs
/ Protein Structure, Secondary
/ Proteins
/ Recombinant Fusion Proteins - chemistry
/ Recombinant Fusion Proteins - genetics
/ Recombinant Fusion Proteins - metabolism
/ Science
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