Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions (Q28510958)

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Language	Label	Description	Also known as
English	Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions	scientific journal article

Statements

scholarly article

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PubMed publication ID

25 January 2017

Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions (English)

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PubMed publication ID

25 January 2017

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GOA release 2020-03-11

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NMR spectroscopy

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Daniel Häussinger

object named as

Daniel Häussinger

1

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Stephan Grzesiek

object named as

Stephan Grzesiek

6

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object named as

Olivier Pertz

4

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author name string

Thomas Ahrens

2

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PubMed publication ID

25 January 2017

Hans-Jürgen Sass

3

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PubMed publication ID

25 January 2017

Jürgen Engel

5

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PubMed publication ID

25 January 2017

language of work or name

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publication date

6 December 2002

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PubMed publication ID

25 January 2017

Journal of Molecular Biology

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PubMed publication ID

25 January 2017

324

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PubMed publication ID

25 January 2017

4

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PubMed publication ID

25 January 2017

823–839

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PubMed publication ID

25 January 2017

describes a project that uses

NMR spectroscopy

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based on heuristic

inferred from title

Cell surface adhesion receptors

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Cell adhesion: the molecular basis of tissue architecture and morphogenesis

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The molecular structure of cell adhesion molecules

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Morphogenetic roles of classic cadherins

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Homophilic adhesion by cadherins

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Correct proteolytic cleavage is required for the cell adhesive function of uvomorulin

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Structural view of cadherin-mediated cell-cell adhesion

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C-cadherin ectodomain structure and implications for cell adhesion mechanisms

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Calcium binding and homoassociation of E-cadherin domains.

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Lateral self-assembly of E-cadherin directed by cooperative calcium binding

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Cadherin interaction probed by atomic force microscopy

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Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding

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E-cadherin functions as a cis-dimer at the cell-cell adhesive interface in vivo

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A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation

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Expressed recombinant cadherins mediate cell sorting in model systems

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Localization of specificity determining sites in cadherin cell adhesion molecules

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Direct molecular force measurements of multiple adhesive interactions between cadherin ectodomains

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Mechanism of homophilic cadherin adhesion.

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Multiple cadherin extracellular repeats mediate homophilic binding and adhesion

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Structural basis of cell-cell adhesion by cadherins

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Structural basis of calcium-induced E-cadherin rigidification and dimerization

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Solution structure of the epithelial cadherin domain responsible for selective cell adhesion.

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1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin

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Sequence-specific resonance assignments and partial unfolding of extracellular domains II and III of E-cadherin

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Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

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Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

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Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings

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Lateral dimerization is required for the homophilic binding activity of C-cadherin

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Alignment of Biopolymers in Strained Gels: A New Way To Create Detectable Dipole−Dipole Couplings in High-Resolution Biomolecular NMR

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Solution NMR of proteins within polyacrylamide gels: diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes

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Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

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Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

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The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements

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Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme

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Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data

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Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

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Identifiers

10.1016/S0022-2836(02)01137-3

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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