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Isolation of placental cadherin cDNA: identification of a novel gene family of cell-cell adhesion molecules.
Nose A, Nagafuchi A, Takeichi M. Nose A, et al. EMBO J. 1987 Dec 1;6(12):3655-61. EMBO J. 1987. PMID: 3428270 Free PMC article.
We report the cloning of cDNA encoding a cadherin present in the placenta which is called P-cadherin. The deduced sequence encodes a polypeptide of 822 amino acids with the characteristic features of integral membrane proteins. ...These results provide evidence for …
We report the cloning of cDNA encoding a cadherin present in the placenta which is called P-cadherin. The deduced sequence encodes …
Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a human cancer cell line.
Oda T, Kanai Y, Shimoyama Y, Nagafuchi A, Tsukita S, Hirohashi S. Oda T, et al. Biochem Biophys Res Commun. 1993 Jun 30;193(3):897-904. doi: 10.1006/bbrc.1993.1710. Biochem Biophys Res Commun. 1993. PMID: 8323564
., one of 957 bp deletion resulting in a 319-amino-acid deletion and another of 761 bp deletion resulting in a frameshift, were identified. ...
., one of 957 bp deletion resulting in a 319-amino-acid deletion and another of 761 bp deletion resulting in a frameshift, wer …
alpha-catenin-independent recruitment of ZO-1 to nectin-based cell-cell adhesion sites through afadin.
Yokoyama S, Tachibana K, Nakanishi H, Yamamoto Y, Irie K, Mandai K, Nagafuchi A, Monden M, Takai Y. Yokoyama S, et al. Mol Biol Cell. 2001 Jun;12(6):1595-609. doi: 10.1091/mbc.12.6.1595. Mol Biol Cell. 2001. PMID: 11408571 Free PMC article.
The nectin-afadin complex has a potency to recruit the E-cadherin-beta-catenin complex through alpha-catenin in a manner independent of ponsin. ...Nectin showed a potency to recruit not only alpha-catenin but also ZO-1 to nectin-based cell-cell adhesion sites …
The nectin-afadin complex has a potency to recruit the E-cadherin-beta-catenin complex through alpha-catenin in a manner indep …
Structure, expression and chromosome assignment of the human catenin (cadherin-associated protein) alpha 1 gene (CTNNA1).
Furukawa Y, Nakatsuru S, Nagafuchi A, Tsukita S, Muto T, Nakamura Y, Horii A. Furukawa Y, et al. Cytogenet Cell Genet. 1994;65(1-2):74-8. doi: 10.1159/000133603. Cytogenet Cell Genet. 1994. PMID: 8404069
We have isolated the human alpha-catenin gene (CTNNA1), which encodes a cadherin-associated protein, and have determined its primary structure and chromosomal localization. ...
We have isolated the human alpha-catenin gene (CTNNA1), which encodes a cadherin-associated protein, and have determined its primary …
Structural diversity of band 4.1 superfamily members.
Takeuchi K, Kawashima A, Nagafuchi A, Tsukita S. Takeuchi K, et al. J Cell Sci. 1994 Jul;107 ( Pt 7):1921-8. J Cell Sci. 1994. PMID: 7983158
Several proteins contain the domain homologous to the N-terminal half of band 4.1 protein, indicating the existence of a superfamily. ...The deduced amino acid sequence revealed a myristoylation site, as well as phosphorylation sites for A-kinase and tyrosine …
Several proteins contain the domain homologous to the N-terminal half of band 4.1 protein, indicating the existence of a superfamily. …
Radixin is a novel member of the band 4.1 family.
Funayama N, Nagafuchi A, Sato N, Tsukita S, Tsukita S. Funayama N, et al. J Cell Biol. 1991 Nov;115(4):1039-48. doi: 10.1083/jcb.115.4.1039. J Cell Biol. 1991. PMID: 1955455 Free PMC article.
The composite cDNA is 4,241 nucleotides long and codes for a 583-amino acid polypeptide with a calculated molecular mass of 68.5 kD. ...In erythrocytes the band 4.1 protein acts as a key protein in the association of short actin filaments with a plasma …
The composite cDNA is 4,241 nucleotides long and codes for a 583-amino acid polypeptide with a calculated molecular mass of 68 …
A 220-kD undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites.
Itoh M, Yonemura S, Nagafuchi A, Tsukita S, Tsukita S. Itoh M, et al. J Cell Biol. 1991 Dec;115(5):1449-62. doi: 10.1083/jcb.115.5.1449. J Cell Biol. 1991. PMID: 1955485 Free PMC article.
The affinity-purified 220-kD protein molecule looked like a spherical particle, and its binding site on the spectrin molecule was shown to be in the position approximately 10-20 nm from the midpoint of spectrin tetramer by low-angle rotary-shadowing electron microscopy. Ta …
The affinity-purified 220-kD protein molecule looked like a spherical particle, and its binding site on the spectrin molecule was sho …
Posttranscriptional regulation of alpha-catenin expression is required for Wnt signaling in L cells.
Takahashi N, Ishihara S, Takada S, Tsukita S, Nagafuchi A. Takahashi N, et al. Biochem Biophys Res Commun. 2000 Nov 2;277(3):691-8. doi: 10.1006/bbrc.2000.3748. Biochem Biophys Res Commun. 2000. PMID: 11062015
These results suggested that the low-efficiency of translation and unidentified degradation mechanisms maintained the low levels of alpha-catenin expression in the cytoplasm as a necessary condition for the Wnt signaling pathway....
These results suggested that the low-efficiency of translation and unidentified degradation mechanisms maintained the low levels of alpha-ca …
E-cadherin and alpha-catenin expression in human esophageal cancer.
Kadowaki T, Shiozaki H, Inoue M, Tamura S, Oka H, Doki Y, Iihara K, Matsui S, Iwazawa T, Nagafuchi A, et al. Kadowaki T, et al. Cancer Res. 1994 Jan 1;54(1):291-6. Cancer Res. 1994. PMID: 8261454
Intercellular adhesion of the epithelial tissue is mainly regulated by the E-cadherin (E-cad) molecule. alpha-Catenin (alpha-cat) is one of the E-cad-associated cytoplasmic proteins that forms a linkage to the cytoskeleton and regulates E-cad function. ...Twenty-five (54%) …
Intercellular adhesion of the epithelial tissue is mainly regulated by the E-cadherin (E-cad) molecule. alpha-Catenin (alpha-cat) is one of …
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