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Structural basis of cell-cell adhesion by cadherins
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instance of
scholarly article
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title
Structural basis of cell-cell adhesion by cadherins
(English)
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main subject
cell adhesion
1 reference
based on heuristic
inferred from title
author
Jens Als-Nielsen
series ordinal
8
object named as
J Als-Nielsen
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Peter D. Kwong
series ordinal
3
object named as
P D Kwong
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author name string
L Shapiro
series ordinal
1
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A M Fannon
series ordinal
2
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A Thompson
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4
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M S Lehmann
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5
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G Grübel
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6
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J F Legrand
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7
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D R Colman
series ordinal
9
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W A Hendrickson
series ordinal
10
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language of work or name
English
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publication date
23 March 1995
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published in
Nature
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volume
374
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page(s)
327-37
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issue
6520
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cites work
A Drosophila homolog of cadherin associated with armadillo and essential for embryonic cell-cell adhesion.
1 reference
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Cadherin cell adhesion receptors as a morphogenetic regulator
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Cloning and expression of cDNA encoding a neural calcium-dependent cell adhesion molecule: its identity in the cadherin gene family
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Localization of specificity determining sites in cadherin cell adhesion molecules
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Cadherin subclasses: differential expression and their roles in neural morphogenesis
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inferred from DOI database lookup
Cadherins: a molecular family important in selective cell-cell adhesion
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Autoantibodies against the amino-terminal cadherin-like binding domain of pemphigus vulgaris antigen are pathogenic
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Identification of a cadherin cell adhesion recognition sequence
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Functional correlation between cell adhesive properties and some cell surface proteins
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Teratocarcinoma cell adhesion: identification of a cell-surface protein involved in calcium-dependent cell aggregation
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Transmembrane molecular assemblies regulated by the greater cadherin family
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Unraveling the cytoplasmic interactions of the cadherin superfamily
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Regulation of embryonic cell adhesion by the cadherin cytoplasmic domain
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Disruption of epithelial cell-cell adhesion by exogenous expression of a mutated nonfunctional N-cadherin
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Target Specifications and Performance of the ESRF Source
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Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
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Purification and spectroscopic characterization of a recombinant amino-terminal polypeptide fragment of mouse epithelial cadherin
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Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution
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Single amino acid substitutions in one Ca2+ binding site of uvomorulin abolish the adhesive function
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Junctional complexes in various epithelia
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Membrane ultrastructure at mammalian intercellular junctions
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7 January 2021
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inferred from DOI database lookup
Transmembrane control of cadherin-mediated cell-cell adhesion
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inferred from DOI database lookup
Microfilaments in Cellular and Developmental Processes
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An electron microscope study of the parathyroid gland of the frog (Ràna clamitans)
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Fine structure of desmosomes. , hemidesmosomes, and an adepidermal globular layer in developing newt epidermis
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Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts
1 reference
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Changes in membrane-microfilament interaction in intercellular adherens junctions upon removal of extracellular Ca2+ ions
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A-CAM: a 135-kD receptor of intercellular adherens junctions. II. Antibody-mediated modulation of junction formation
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Ultrastructure of intercellular junctions in adult and developing cardiac muscle
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R-cadherin: a novel Ca(2+)-dependent cell-cell adhesion molecule expressed in the retina
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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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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
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Solution structure of the epithelial cadherin domain responsible for selective cell adhesion.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F374327A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1038/374327A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1810538
Dimensions Publication ID
1010829113
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OpenCitations bibliographic resource ID
1810538
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1810538
PubMed ID
7885471
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1810538
Springer Nature article ID
10.1038/374327a0
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