Structural basis of calcium-induced E-cadherin rigidification and dimerization (Q27732599)

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English	Structural basis of calcium-induced E-cadherin rigidification and dimerization	scientific article

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scholarly article

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Structural basis of calcium-induced E-cadherin rigidification and dimerization (English)

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Michael Overduin

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M Overduin

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Mitsuhiko Ikura

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M Ikura

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author name string

B Nagar

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J M Rini

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language of work or name

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publication date

28 March 1996

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380

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6572

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360-4

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Cadherins: a molecular family important in selective cell-cell adhesion

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

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Localization of specificity determining sites in cadherin cell adhesion molecules

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From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion

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

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Structural basis of cell-cell adhesion by cadherins

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Purification and spectroscopic characterization of a recombinant amino-terminal polypeptide fragment of mouse epithelial cadherin

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Single amino acid substitutions in one Ca2+ binding site of uvomorulin abolish the adhesive function

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Calcium ions as extracellular messengers

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E-cadherin gene mutations in human gastric carcinoma cell lines

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Identification of a cadherin cell adhesion recognition sequence

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Changes in membrane-microfilament interaction in intercellular adherens junctions upon removal of extracellular Ca2+ ions

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Preliminary X-ray analysis of Escherichia coli GMP synthetase: determination of anomalous scattering factors for a cysteinyl mercury derivative.

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Improved methods for building protein models in electron density maps and the location of errors in these models

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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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

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Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector

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Identifiers

10.1038/380360A0

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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Springer Nature article ID

10.1038/380360a0

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