Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch. - Wikidata - wikimedia - TriplyDB

Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch.

Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch.

http://www.wikidata.org/entity/Q34990340

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Mineral and Protein-Bound Water and Latching Action Control Mechanical Behavior at Protein-Mineral Interfaces in Biological Nanocomposites Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism Fibronectin Mechanobiology Regulates Tumorigenesis Utilizing Fibronectin Integrin-Binding Specificity to Control Cellular Responses Extracellular matrix as an inductive scaffold for functional tissue reconstruction Fibronectin unfolding revisited: modeling cell traction-mediated unfolding of the tenth type-III repeat Cancer cell invasion is enhanced by applied mechanical stimulation Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates The interplay between cell signalling and mechanics in developmental processes Single-Cell Migration in Complex Microenvironments: Mechanics and Signaling Dynamics Native topology determines force-induced unfolding pathways in globular proteins.Mechanically untying a protein slipknot: multiple pathways revealed by force spectroscopy and steered molecular dynamics simulations.Designing a nano-interface in a microfluidic chip to probe living cells: challenges and perspectives.Sugar transport across lactose permease probed by steered molecular dynamics.The allosteric role of the Ca2+ switch in adhesion and elasticity of C-cadherin.Assembly of fibronectin extracellular matrix.Unfolding proteins by external forces and temperature: the importance of topology and energetics.Extending a spectrin repeat unit. I: linear force-extension response Insulin-response element-binding protein 1: a novel Akt substrate involved in transcriptional action of insulin.Energy landscape distortions and the mechanical unfolding of proteins Unfolding and extraction of a transmembrane alpha-helical peptide: dynamic force spectroscopy and molecular dynamics simulations.Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy: theory and applications Forced unbinding of GPR17 ligands from wild type and R255I mutant receptor models through a computational approach.Fluid- or surface-phase human salivary scavenger protein gp340 exposes different bacterial recognition properties.Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer.Role of altered sialylation of the I-like domain of beta1 integrin in the binding of fibronectin to beta1 integrin: thermodynamics and conformational analyses Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension.Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule.The key event in force-induced unfolding of Titin's immunoglobulin domains.Simulated refolding of stretched titin immunoglobulin domains Forced detachment of the CD2-CD58 complex.Steered molecular dynamics simulation on the binding of NNRTI to HIV-1 RT.Molecular dynamics simulations of forced conformational transitions in 1,6-linked polysaccharides.Extending a spectrin repeat unit. II: rupture behavior Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Sequential unfolding of individual helices of bacterioopsin observed in molecular dynamics simulations of extraction from the purple membrane Epitope topography controls bioactivity in supramolecular nanofibers Non-muscle myosin II induces disassembly of actin stress fibres independently of myosin light chain dephosphorylation Calculating potentials of mean force from steered molecular dynamics simulations.

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P2860

Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch.

http://www.wikidata.org/entity/Q34990340

description

1999 nî lūn-bûn

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1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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1999 թվականի փետրվարին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Forced unfolding of the fibron ...... molecular recognition switch.

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Forced unfolding of the fibron ...... molecular recognition switch.

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Forced unfolding of the fibron ...... molecular recognition switch.

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type

label

Forced unfolding of the fibron ...... molecular recognition switch.

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Forced unfolding of the fibron ...... molecular recognition switch.

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Forced unfolding of the fibron ...... molecular recognition switch.

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Forced unfolding of the fibron ...... molecular recognition switch.

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Forced unfolding of the fibron ...... molecular recognition switch.

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Forced unfolding of the fibron ...... molecular recognition switch.

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Proceedings of the National Academy of Sciences of the United States of America

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Forced unfolding of the fibron ...... molecular recognition switch.

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A Krammer

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P2860

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Comparison of simple potential functions for simulating liquid water

Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme

2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region

All-atom empirical potential for molecular modeling and dynamics studies of proteins

The anatomy and taxonomy of protein structure

Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy

Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation

Reconstructing potential energy functions from simulated force-induced unbinding processes.

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1351-1356

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