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CDH1 (cadherin 1, type 1, E-cadherin (epithelial))

Identity

Other namesArc-1
CD324
CDHE
Cadherin-1
E-cadherin
ECAD
LCAM
UVO
Uvomorulin
HGNC (Hugo) CDH1
LocusID (NCBI) 999
Location 16q22.1
Location_base_pair Starts at 68771195 and ends at 68869444 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

 
  DNA of CDH1 gene composed of 16 coding exons.
Description DNA contains 98250 bp composed of 16 coding exons.
Transcription 4828 bp mRNA transcribed in centromeric to telomeric orientation; 2649 bp open reading frame.
Pseudogene Yes, for example, the repeat sequence named c41-cad is a pseudogene of the cadherin family. c41-cad is localizated on 5q13

Protein

 
  Three-dimensional structure of the beta-catenin arm repeat region in complex with the E-cadherin cytoplasmic domain (Huber and Weis, 2001). The arm repeats are formed by three helices, H1 and H2 (both gray) and H3 (blue). Residues 134-161, which include part of the alpha-catenin-binding site and a portion of the first arm repeat, form a single helix in this particular crystal structure (cyan). E-cadherin is divided into five regions of primary structure (1-5) that are indicated in distinct colors (Pokutta S and Weis WI, 2007).
Description The cadherins are a family of calcium-dependent transmembrane linker proteins; the first three that were discovered were named according to their tissue origin (E-cadherin from epithelium, N-cadherin from neural tissue and P-cadherin from placenta). The mature E-cadherin protein consists of three major domains: a large extracellular portion (exons 4-13), which mediates homophilic cellular interactions; and smaller transmembrane (exons 13-14) and cytoplasmic domains (exons 14-16), the latter providing a link to the actin cytoskeleton through an association with various catenins, such as B-catenin. The protein E-cadherin is a calcium-dependent cell-cell adhesion molecule expressed in adherents junctions between epithelial cells. It is a transmembrane glycoprotein with five extracellular domains that mediate intercellular adhesion through homophilic binding. The cytoplasmatic domain is bound to the actin cytoskeleton via intracellular attachment proteins, the catenins. The actin cytoskeleton forms a transcellular network mediating structural integrity, cellular polarity and epithelial morphogenesis.
Expression Present tissue specificity for non-neural epithelial tissues and there are high levels in solid tissues.
Localisation Cell junction; single-pass type I membrane protein. Anchored to actin microfilaments through association with alpha-catenin, beta-catenin and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm.
Function One of the most important and ubiquitous types of adhesive interactions required for the maintenance of solid tissues is that mediated by the classic cadherin adhesion molecules. Cadherins are transmembrane Ca2+- dependent homophilic adhesion receptors that are well known to play important roles in cell recognition and cell sorting during development. However, they continue to be expressed at high levels in virtually all solid tissues. There are many members of the classic cadherin family (which is a subset of the larger cadherin superfamily), but E-cadherin in epithelial tissues has been the most studied in the context of stable adhesions. Continued expression and functional activity of E-cadherin are required for cells to remain tightly associated in the epithelium, and in its absence the many other cell adhesion and cell junction proteins expressed in epithelial cells (see below) are not capable of supporting intercellular adhesion. In its capacity to maintain the overall state of adhesion between epithelial cells, E-cadherin is thought to act as an important suppressor of epithelial tumor cell invasiveness and metastasis.
Homology Pan troglodytes - CDH1; Canis lupus familiaris - CDH1; Mus musculus - Cdh1; Rattus norvegicus - Cdh1; Gallus gallus - LOC415860; Danio rerio - cdh1

Mutations

 
  57 CDH1 mutations have been found to date. 50 of these are listed in Human Gene Mutation Database. Truncating (27) and splice site (7) mutations are found above the Schema (34/45, 76%), missense mutations below it (11/45, 24%). Two marked with an asterisk have been reported as somatic mutations in sporadic diffuse gastric cancer. No Polymorphisms. No Gross deletions/duplications, complex rearrangements, repeat variations been reported. They spread out all over CDH1 gene (Brooks-Wilson et al., 2004).
Germinal 30 CDH1 germline mutations have been described in hereditary diffuse gastric cancer families. 25 have been inactivating (frameshift, nonsense, and splice-site), the remainders are missense. The mutations are distributed equally throughout the gene.
Somatic Somatically acquired mutations in CDH1 were found in about 56% of lobular breast tumors, generally (>90%) in combination with loss of the wild-type allele, while no mutations were found in ductal primary breast carcinomas. Most of these somatic mutations result in premature stop codons as a consequence of insertions, deletions and nonsense mutations. As the majority of these frameshift and nonsense mutations is predicted to generate secreted E-cadherin fragments, the functionality of this major cell-cell adhesion protein is lost. Other cancer-confined E-cadherin mutations also result in crippled proteins. The distinctive invasive growth pattern, which is typical for lobular breast cancers, is fully compatible with this functional inactivation.
472 human tumors and 15 different cancer cell lines derived from 10 different tissues have been screened for CDH1 mutation. So far, frequent somatic mutations (50%) have been identified only in sporadic diffuse gastric cancer (DGC), Lobular Breast Cancer. For sporadic DGC, most somatic mutations are missense (exons 8, 9) or exon skipping. For sporadic Lobular Breast Cancer, most somatic mutations are truncating.472 human tumors and 15 different cancer cell lines derived from 10 different tissues have been screened for CDH1 mutation. So far, frequent somatic mutations (50%) have been identified only in sporadic Diffuse Gastric Cancer, Lobular Breast Cancer.
Interestingly, there is a major difference between the mutation types identified in these two carcinoma types. In diffuse gastric carcinomas, the predominant mutations are exon skippings causing in-frame deletions. By contrast, most mutations identified in lobular breast cancer result in premature stop codons. In the case of the diffuse gastric carcinomas, a mutation cluster region is suggested as more than 60% of mutations cause exon skipping of exon 8 and 9. Preliminary in vitro studies using transfected cell lines suggest that tumor-associated E-cadherin mutations reduce cell adhesion, increase cell motility, and change cell morphology possibly by dominant negative mechanisms. On the contrary, the truncating mutations present in lobular breast cancers are obviously scattered over the entire E-cadherin gene. In line with this finding is the observation that the expression of E-cadherin protein is lost in lobular breast cancers, in contrast to the retention of expression of the mutant E-cadherin proteins in diffuse gastric carcinomas. Surprisingly, so far almost no E-cadherin mutations have been found to be located in the highly conserved cytoplasmic domain. In most cases, E-cadherin mutations are found in combination with loss of the wild-type allele.

Implicated in

Entity Non-small cell lung cancer
Prognosis Reduced E-cadherin correlates with lymph node metastasis. The rate of vascular invasion was statistically high in cases with the reduced expression of E-cadherin. Reduction of E-cadherin is associated with the degree of differentiation. Bohm et al. found a correlation between differentiation and E-cadherin expression in lung squamous cell carcinoma, and Bongiorno et al. found that well-differentiated lung cancers express E-cadherin, in a preserved fashion, and that poorly differentiated tumors exhibited a reduced or disorganized staining pattern. Sulzer et al. also found that E-cadherin expression significantly correlated with increasing tumor differentiation. In general, undifferentiated or poorly differentiated cancer cells tend to have a strong potential to invade tissues. These results suggest that reduction of E-cadherin correlates with tumor invasion.
Oncogenesis Reduced E-cadherin expression weakens cell-to-cell attachment, and tumor cells detach from the primary tumor, invade vessels, and migrate to lymph nodes. Once tumor cells reattach to lymph nodes, E-cadherin is strongly expressed, and lymph nodes are subject to metastases.
  
Entity Melanoma
Oncogenesis The major adhesion mediator between keratinocytes and normal melanocytes is E-cadherin, which disappears during melanoma progression. While normal melanocytes express E-cadherin, this molecule is not found on nevus or melanoma cells. The loss of E-cadherin likely plays a crucial role in tumor progression. Cells that have lost epithelial differentiation, as manifested by the loss of functional E-cadherin, show increased mobility and invasiveness. Keratinocytes can no longer control melanoma cells that have lost E-cadherin. When melanoma cells are forced to express E-cadherin and are cocultured with keratinocytes, they dramatically change: melanomas adhere to keratinocytes, no longer express invasion-related molecules, and lose their invasive capacities
  
Entity Oesophageal adenocarcinoma
Prognosis Reduction in the expression of E-cadherin in patients with OSCC was shown to be strongly associated with postoperative blood borne recurrence, resulting in a poorer prognosis than in those patients with tumours showing normal expression before surgery. This finding suggested that in patients with reduced E-cadherin immunoreactivity, the metastatic potential of the oesophageal cancer cells may be increased. Therefore, the evaluation of E-cadherin immunoreactivity may be useful in predicting haematogenous spread and hence recurrence, thus serving as an aid for planning adjuvant treatment after surgery in patients with OSCC. It has also been reported that E-cadherin might be an independent predictor of micrometastasis in lymph nodes that are classified as N0 by routine histopathological analysis.
  

Other Solid tumors implicated (Data extracted from papers in the Atlas)

Solid Tumors AmeloblastomID5945 MedulloblastomaID5065 rhab5004 rhabID5004 blad5001
bladID5001

External links

Nomenclature
HGNC (Hugo)CDH1   1748
Cards
AtlasCDH1ID166ch16q22
Entrez_Gene (NCBI)CDH1  999  cadherin 1, type 1, E-cadherin (epithelial)
GeneCards (Weizmann)CDH1
Ensembl (Hinxton)ENSG00000039068 [Gene_View]  chr16:68771195-68869444 [Contig_View]  CDH1 [Vega]
ICGC DataPortalENSG00000039068
AceView (NCBI)CDH1
Genatlas (Paris)CDH1
WikiGenes999
SOURCE (Princeton)NM_004360
Genomic and cartography
GoldenPath (UCSC)CDH1  -  16q22.1   chr16:68771195-68869444 +  16q22.1   [Description]    (hg19-Feb_2009)
EnsemblCDH1 - 16q22.1 [CytoView]
Mapping of homologs : NCBICDH1 [Mapview]
OMIM114480   137215   167000   176807   192090   608089   
Gene and transcription
Genbank (Entrez)AB025105 AB025106 AI890107 AK290012 AK297913
RefSeq transcript (Entrez)NM_004360
RefSeq genomic (Entrez)AC_000148 NC_000016 NC_018927 NG_008021 NT_010498 NW_001838290 NW_004929402
Consensus coding sequences : CCDS (NCBI)CDH1
Cluster EST : UnigeneHs.461086 [ NCBI ]
CGAP (NCI)Hs.461086
Alternative Splicing : Fast-db (Paris)GSHG0011307
Alternative Splicing GalleryENSG00000039068
Gene ExpressionCDH1 [ NCBI-GEO ]     CDH1 [ SEEK ]   CDH1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP12830 (Uniprot)
NextProtP12830  [Medical]
With graphics : InterProP12830
Splice isoforms : SwissVarP12830 (Swissvar)
Domaine pattern : Prosite (Expaxy)CADHERIN_1 (PS00232)    CADHERIN_2 (PS50268)   
Domains : Interpro (EBI)Cadherin    Cadherin-like    Cadherin_CS    Cadherin_cytoplasmic-dom    Cadherin_pro_dom    Catenin_binding_dom   
Related proteins : CluSTrP12830
Domain families : Pfam (Sanger)Cadherin (PF00028)    Cadherin_C (PF01049)    Cadherin_pro (PF08758)   
Domain families : Pfam (NCBI)pfam00028    pfam01049    pfam08758   
Domain families : Smart (EMBL)CA (SM00112)  Cadherin_pro (SM01055)  
DMDM Disease mutations999
Blocks (Seattle)P12830
PDB (SRS)1O6S    2O72    2OMT    2OMU    2OMV    2OMX    2OMY    2OMZ    3FF7    3FF8    3L6X    3L6Y   
PDB (PDBSum)1O6S    2O72    2OMT    2OMU    2OMV    2OMX    2OMY    2OMZ    3FF7    3FF8    3L6X    3L6Y   
PDB (IMB)1O6S    2O72    2OMT    2OMU    2OMV    2OMX    2OMY    2OMZ    3FF7    3FF8    3L6X    3L6Y   
PDB (RSDB)1O6S    2O72    2OMT    2OMU    2OMV    2OMX    2OMY    2OMZ    3FF7    3FF8    3L6X    3L6Y   
Human Protein AtlasENSG00000039068
Peptide AtlasP12830
HPRD01885
IPIIPI00025861   IPI01010829   IPI00911003   IPI00744889   IPI00000513   
Protein Interaction databases
DIP (DOE-UCLA)P12830
IntAct (EBI)P12830
FunCoupENSG00000039068
BioGRIDCDH1
IntegromeDBCDH1
STRING (EMBL)CDH1
Ontologies - Pathways
QuickGOP12830
Ontology : AmiGOtrophectodermal cell differentiation  glycoprotein binding  epithelial cell morphogenesis  calcium ion binding  protein binding  extracellular region  cytoplasm  endosome  trans-Golgi network  plasma membrane  plasma membrane  cell-cell adherens junction  focal adhesion  apoptotic process  cellular component disassembly involved in execution phase of apoptosis  homophilic cell adhesion  synapse assembly  sensory perception of sound  beta-catenin binding  response to toxic substance  cytoplasmic side of plasma membrane  cell surface  actin cytoskeleton  integral component of membrane  aggresome  basolateral plasma membrane  lateral plasma membrane  single organismal cell-cell adhesion  catenin complex  protein metabolic process  protein phosphatase binding  protein domain specific binding  pituitary gland development  negative regulation of cell-cell adhesion  extracellular matrix disassembly  cell junction  cell junction  extracellular matrix organization  ankyrin binding  neuron projection development  GTPase activating protein binding  node of Ranvier  regulation of water loss via skin  cell junction assembly  adherens junction organization  response to drug  positive regulation of transcription factor import into nucleus  lateral loop  Schmidt-Lanterman incisure  regulation of cysteine-type endopeptidase activity involved in apoptotic process  apical junction complex  axon terminus  apical part of cell  cell-cell junction organization  gamma-catenin binding  positive regulation of transcription, DNA-templated  perinuclear region of cytoplasm  negative regulation of epithelial cell proliferation  regulation of immune response  cell adhesion molecule binding  protein homooligomerization  intestinal epithelial cell development  salivary gland cavitation  regulation of branching involved in salivary gland morphogenesis  extracellular vesicular exosome  tight junction assembly  cellular response to amino acid stimulus  cellular response to lithium ion  cellular response to indole-3-methanol  protein localization to plasma membrane  establishment of protein localization to plasma membrane  negative regulation of canonical Wnt signaling pathway  cochlea development  regulation of protein localization to cell surface  
Ontology : EGO-EBItrophectodermal cell differentiation  glycoprotein binding  epithelial cell morphogenesis  calcium ion binding  protein binding  extracellular region  cytoplasm  endosome  trans-Golgi network  plasma membrane  plasma membrane  cell-cell adherens junction  focal adhesion  apoptotic process  cellular component disassembly involved in execution phase of apoptosis  homophilic cell adhesion  synapse assembly  sensory perception of sound  beta-catenin binding  response to toxic substance  cytoplasmic side of plasma membrane  cell surface  actin cytoskeleton  integral component of membrane  aggresome  basolateral plasma membrane  lateral plasma membrane  single organismal cell-cell adhesion  catenin complex  protein metabolic process  protein phosphatase binding  protein domain specific binding  pituitary gland development  negative regulation of cell-cell adhesion  extracellular matrix disassembly  cell junction  cell junction  extracellular matrix organization  ankyrin binding  neuron projection development  GTPase activating protein binding  node of Ranvier  regulation of water loss via skin  cell junction assembly  adherens junction organization  response to drug  positive regulation of transcription factor import into nucleus  lateral loop  Schmidt-Lanterman incisure  regulation of cysteine-type endopeptidase activity involved in apoptotic process  apical junction complex  axon terminus  apical part of cell  cell-cell junction organization  gamma-catenin binding  positive regulation of transcription, DNA-templated  perinuclear region of cytoplasm  negative regulation of epithelial cell proliferation  regulation of immune response  cell adhesion molecule binding  protein homooligomerization  intestinal epithelial cell development  salivary gland cavitation  regulation of branching involved in salivary gland morphogenesis  extracellular vesicular exosome  tight junction assembly  cellular response to amino acid stimulus  cellular response to lithium ion  cellular response to indole-3-methanol  protein localization to plasma membrane  establishment of protein localization to plasma membrane  negative regulation of canonical Wnt signaling pathway  cochlea development  regulation of protein localization to cell surface  
Pathways : BIOCARTASUMOylation as a mechanism to modulate CtBP-dependent gene responses [Genes]    Downregulated of MTA-3 in ER-negative Breast Tumors [Genes]    TGF beta signaling pathway [Genes]   
Pathways : KEGGRap1 signaling pathway    Hippo signaling pathway    Cell adhesion molecules (CAMs)    Adherens junction    Bacterial invasion of epithelial cells    Pathogenic Escherichia coli infection    Pathways in cancer    Endometrial cancer    Thyroid cancer    Melanoma    Bladder cancer   
REACTOMEP12830 [protein]
REACTOME PathwaysREACT_578 Apoptosis [pathway]
REACTOME PathwaysREACT_111155 Cell-Cell communication [pathway]
REACTOME PathwaysREACT_118779 Extracellular matrix organization [pathway]
REACTOME PathwaysREACT_6900 Immune System [pathway]
Protein Interaction DatabaseCDH1
Wikipedia pathwaysCDH1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)CDH1
SNP (GeneSNP Utah)CDH1
SNP : HGBaseCDH1
Genetic variants : HAPMAPCDH1
1000_GenomesCDH1 
ICGC programENSG00000039068 
Cancer Gene: CensusCDH1 
CONAN: Copy Number AnalysisCDH1 
Somatic Mutations in Cancer : COSMICCDH1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
LOVD (Leiden Open Variation Database)Colon cancer gene variant databases
LOVD (Leiden Open Variation Database)Zhejiang University Center for Genetic and Genomic Medicine (ZJU-CGGM)
DECIPHER (Syndromes)16:68771195-68869444
Mutations and Diseases : HGMDCDH1
OMIM114480    137215    167000    176807    192090    608089   
MedgenCDH1
GENETestsCDH1
Disease Genetic AssociationCDH1
Huge Navigator CDH1 [HugePedia]  CDH1 [HugeCancerGEM]
Genomic VariantsCDH1  CDH1 [DGVbeta]
Exome VariantCDH1
dbVarCDH1
ClinVarCDH1
snp3D : Map Gene to Disease999
General knowledge
Homologs : HomoloGeneCDH1
Homology/Alignments : Family Browser (UCSC)CDH1
Phylogenetic Trees/Animal Genes : TreeFamCDH1
Chemical/Protein Interactions : CTD999
Chemical/Pharm GKB GenePA26282
Drug Sensitivity CDH1
Clinical trialCDH1
Cancer Resource (Charite)ENSG00000039068
Other databases
Other databasehttp://cancergenome.broadinstitute.org/index.php?tgene=CDH1
Probes
Litterature
PubMed499 Pubmed reference(s) in Entrez
CoreMineCDH1
GoPubMedCDH1
iHOPCDH1

Bibliography

Differences of E-cadherin expression levels and patterns in primary and metastatic human lung cancer.
Bhm M, Totzeck B, Birchmeier W, Wieland I
Clinical & experimental metastasis. 1994 ; 12 (1) : 55-62.
PMID 8287621
 
E-cadherin is a tumour/invasion suppressor gene mutated in human lobular breast cancers.
Berx G, Cleton-Jansen AM, Nollet F, de Leeuw WJ, van de Vijver M, Cornelisse C, van Roy F
The EMBO journal. 1995 ; 14 (24) : 6107-6115.
PMID 8557030
 
Cloning and characterization of the human invasion suppressor gene E-cadherin (CDH1).
Berx G, Staes K, van Hengel J, Molemans F, Bussemakers MJ, van Bokhoven A, van Roy F
Genomics. 1995 ; 26 (2) : 281-289.
PMID 7601454
 
E-cadherin expression in primary and metastatic thoracic neoplasms and in Barrett's oesophagus.
Bongiorno PF, al-Kasspooles M, Lee SW, Rachwal WJ, Moore JH, Whyte RI, Orringer MB, Beer DG
British journal of cancer. 1995 ; 71 (1) : 166-172.
PMID 7819034
 
Expressed cadherin pseudogenes are localized to the critical region of the spinal muscular atrophy gene.
Selig S, Bruno S, Scharf JM, Wang CH, Vitale E, Gilliam TC, Kunkel LM
Proceedings of the National Academy of Sciences of the United States of America. 1995 ; 92 (9) : 3702-3706.
PMID 7731968
 
E-cadherin is inactivated in a majority of invasive human lobular breast cancers by truncation mutations throughout its extracellular domain.
Berx G, Cleton-Jansen AM, Strumane K, de Leeuw WJ, Nollet F, van Roy F, Cornelisse C
Oncogene. 1996 ; 13 (9) : 1919-1925.
PMID 8934538
 
Cell adhesion: the molecular basis of tissue architecture and morphogenesis.
Gumbiner BM
Cell. 1996 ; 84 (3) : 345-357.
PMID 8608588
 
An efficient and reliable multiplex PCR-SSCP mutation analysis test applied to the human E-cadherin gene.
Berx G, Nollet F, Strumane K, van Roy F
Human mutation. 1997 ; 9 (6) : 567-574.
PMID 9195232
 
Mutations of the human E-cadherin (CDH1) gene.
Berx G, Becker KF, Hfler H, van Roy F
Human mutation. 1998 ; 12 (4) : 226-237.
PMID 9744472
 
Reduced E-cadherin expression is associated with increased lymph node metastasis and unfavorable prognosis in non-small cell lung cancer.
Sulzer MA, Leers MP, van Noord JA, Bollen EC, Theunissen PH
American journal of respiratory and critical care medicine. 1998 ; 157 (4 Pt 1) : 1319-1323.
PMID 9563756
 
Expression of E-cadherin and beta-catenin in human non-small cell lung cancer and the clinical significance.
Kase S, Sugio K, Yamazaki K, Okamoto T, Yano T, Sugimachi K
Clinical cancer research : an official journal of the American Association for Cancer Research. 2000 ; 6 (12) : 4789-4796.
PMID 11156236
 
The E-cadherin/catenin complex: an important gatekeeper in breast cancer tumorigenesis and malignant progression.
Berx G, Van Roy F
Breast cancer research : BCR. 2001 ; 3 (5) : 289-293.
PMID 11597316
 
E-cadherin and loss of heterozygosity at chromosome 16 in breast carcinogenesis: different genetic pathways in ductal and lobular breast cancer?
Cleton-Jansen AM
Breast cancer research : BCR. 2002 ; 4 (1) : 5-8.
PMID 11879552
 
Germline E-cadherin mutations in hereditary diffuse gastric cancer: assessment of 42 new families and review of genetic screening criteria.
Brooks-Wilson AR, Kaurah P, Suriano G, Leach S, Senz J, Grehan N, Butterfield YS, Jeyes J, Schinas J, Bacani J, Kelsey M, Ferreira P, MacGillivray B, MacLeod P, Micek M, Ford J, Foulkes W, Australie K, Greenberg C, LaPointe M, Gilpin C, Nikkel S, Gilchrist D, Hughes R, Jackson CE, Monaghan KG, Oliveira MJ, Seruca R, Gallinger S, Caldas C, Huntsman D
Journal of medical genetics. 2004 ; 41 (7) : 508-517.
PMID 15235021
 
Recent advances in melanoma biology.
Perlis C, Herlyn M
The oncologist. 2004 ; 9 (2) : 182-187.
PMID 15047922
 
Genetic aetiology of diffuse gastric cancer: so near, yet so far.
Sweet KM, Lynch HT
Journal of medical genetics. 2004 ; 41 (7) : 481-483.
PMID 15235018
 
Expression of cell adhesion molecules in oesophageal carcinoma and its prognostic value.
Nair KS, Naidoo R, Chetty R
Journal of clinical pathology. 2005 ; 58 (4) : 343-351.
PMID 15790695
 
Structure and mechanism of cadherins and catenins in cell-cell contacts.
Pokutta S, Weis WI
Annual review of cell and developmental biology. 2007 ; 23 : 237-261.
PMID 17539752
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written10-2007Marilia de Freitas Calmon, Paula Rahal
Laboratory of Genomics studies, So Paulo State University, Departament of Biology, So Jos do Rio Preto, SP, Brasil

Citation

This paper should be referenced as such :
Calmon, MF ; Rahal, P
CDH1 (cadherin 1, type 1, E-cadherin (epithelial))
Atlas Genet Cytogenet Oncol Haematol. 2008;12(3):204-207.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/CDH1ID166ch16q22.html

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indexed on : Sat Nov 8 16:55:23 CET 2014

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