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1
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0027315405
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Protocadherins: A large family of cadherin-related molecules in central nervous system
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Sano K., Tanihara H., Heimark R.L., Obata S., Davidson M., St John T., Taketani S., Suzuki S. Protocadherins: a large family of cadherin-related molecules in central nervous system. EMBO J. 12:1993;2249-2256.
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EMBO J
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Sano, K.1
Tanihara, H.2
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Obata, S.4
Davidson, M.5
St John, T.6
Taketani, S.7
Suzuki, S.8
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2
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0028875867
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Cloning, expression, and chromosomal localization of a novel cadherin-related protein, protocadherin-3
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Sago H., Kitagawa M., Obata S., Mori N., Taketani S., Rochelle J.M., Seldin M.F., Davidson M., St John T., Suzuki S.T. Cloning, expression, and chromosomal localization of a novel cadherin-related protein, protocadherin-3. Genomics. 29:1995;631-640.
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Genomics
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Sago, H.1
Kitagawa, M.2
Obata, S.3
Mori, N.4
Taketani, S.5
Rochelle, J.M.6
Seldin, M.F.7
Davidson, M.8
St John, T.9
Suzuki, S.T.10
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3
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0031836266
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Cloning, expression analysis, and chromosomal localization of BH-protocadherin (PCDH7), a novel member of the cadherin superfamily
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Yoshida K., Yoshitomo-Nakagawa K., Seki N., Sasaki M., Sugano S. Cloning, expression analysis, and chromosomal localization of BH-protocadherin (PCDH7), a novel member of the cadherin superfamily. Genomics. 49:1998;458-461.
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(1998)
Genomics
, vol.49
, pp. 458-461
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Yoshida, K.1
Yoshitomo-Nakagawa, K.2
Seki, N.3
Sasaki, M.4
Sugano, S.5
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4
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0032191946
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Characterization of two novel protocadherins (PCDH8 and PCDH9) localized on human chromosome 13 and mouse chromosome 14
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Strehl S., Glatt K., Liu Q.M., Glatt H., Lalande M. Characterization of two novel protocadherins (PCDH8 and PCDH9) localized on human chromosome 13 and mouse chromosome 14. Genomics. 53:1998;81-89.
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(1998)
Genomics
, vol.53
, pp. 81-89
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Strehl, S.1
Glatt, K.2
Liu, Q.M.3
Glatt, H.4
Lalande, M.5
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5
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18744433250
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Diversity revealed by a novel family of cadherins expressed in neurons at a synaptic complex
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Kohmura N., Senzaki K., Hamada S., Kai N., Yasuda R., Watanabe M., Ishii H., Yasuda M., Mishina M., Yagi T. Diversity revealed by a novel family of cadherins expressed in neurons at a synaptic complex. Neuron. 20:1998;1137-1151.
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Neuron
, vol.20
, pp. 1137-1151
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Kohmura, N.1
Senzaki, K.2
Hamada, S.3
Kai, N.4
Yasuda, R.5
Watanabe, M.6
Ishii, H.7
Yasuda, M.8
Mishina, M.9
Yagi, T.10
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6
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0032510394
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NF-protocadherin, a novel member of the cadherin superfamily, is required for Xenopus ectodermal differentiation
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Bradley R.S., Espeseth A., Kintner C. NF-protocadherin, a novel member of the cadherin superfamily, is required for Xenopus ectodermal differentiation. Curr Biol. 8:1998;325-334.
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Curr Biol
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Bradley, R.S.1
Espeseth, A.2
Kintner, C.3
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7
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0032440249
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A common protocadherin tail: Multiple protocadherins share the same sequence in their cytoplasmic domains and are expressed in different regions of brain
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Obata S., Sago H., Mori N., Davidson M., St John T., Suzuki S.T. A common protocadherin tail: multiple protocadherins share the same sequence in their cytoplasmic domains and are expressed in different regions of brain. Cell Adhes Commun. 6:1998;323-333.
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Cell Adhes Commun
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Obata, S.1
Sago, H.2
Mori, N.3
Davidson, M.4
St John, T.5
Suzuki, S.T.6
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8
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0033063445
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A striking organization of a large family of human neural cadherin-like cell adhesion genes
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Wu Q., Maniatis T. A striking organization of a large family of human neural cadherin-like cell adhesion genes. Cell. 97:1999;779-790.
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(1999)
Cell
, vol.97
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Wu, Q.1
Maniatis, T.2
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9
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17744391752
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Comparative DNA sequence analysis of mouse and human protocadherin gene clusters
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A largely identical genomic organization of the gene cluster of α-, β- and γ-protocadherin families is found in human and mouse. DNA sequences upstream of each variable exon in these families show high cross-species conservation. This suggests gene regulation by individual, conserved promoter regions.
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Wu Q., Zhang T., Cheng J.F., Kim Y., Grimwood J., Schmutz J., Dickson M., Noonan J.P., Zhang M.Q., Myers R.M., et al. Comparative DNA sequence analysis of mouse and human protocadherin gene clusters. Genome Res. 11:2001;389-404. A largely identical genomic organization of the gene cluster of α-, β- and γ-protocadherin families is found in human and mouse. DNA sequences upstream of each variable exon in these families show high cross-species conservation. This suggests gene regulation by individual, conserved promoter regions.
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(2001)
Genome Res
, vol.11
, pp. 389-404
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Wu, Q.1
Zhang, T.2
Cheng, J.F.3
Kim, Y.4
Grimwood, J.5
Schmutz, J.6
Dickson, M.7
Noonan, J.P.8
Zhang, M.Q.9
Myers, R.M.10
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10
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0034625313
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Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members
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The authors provide a detailed computational comparison of cadherin domain features and discuss their relevance for the evolutionary relationships of the cadherin superfamily. Also, a comprehensive review on expression patterns and functions of cadherins is given.
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Nollet F., Kools P., van Roy F. Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members. J Mol Biol. 299:2000;551-572. The authors provide a detailed computational comparison of cadherin domain features and discuss their relevance for the evolutionary relationships of the cadherin superfamily. Also, a comprehensive review on expression patterns and functions of cadherins is given.
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(2000)
J Mol Biol
, vol.299
, pp. 551-572
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Nollet, F.1
Kools, P.2
Van Roy, F.3
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11
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0035159856
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The mouse Ames waltzer hearing-loss mutant is caused by mutation of Pcdh15, a novel protocadherin gene
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Alagramam K.N., Murcia C.L., Kwon H.Y., Pawlowski K.S., Wright C.G., Woychik R.P. The mouse Ames waltzer hearing-loss mutant is caused by mutation of Pcdh15, a novel protocadherin gene. Nat Genet. 27:2001;99-102.
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(2001)
Nat Genet
, vol.27
, pp. 99-102
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Alagramam, K.N.1
Murcia, C.L.2
Kwon, H.Y.3
Pawlowski, K.S.4
Wright, C.G.5
Woychik, R.P.6
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12
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0034637579
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μ Protocadherin, a novel developmentally regulated protocadherin with mucin-like domains
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Goldberg M., Peshkovsky C., Shifteh A., Al-Awqati Q. μ Protocadherin, a novel developmentally regulated protocadherin with mucin-like domains. J Biol Chem. 275:2000;24622-24629.
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J Biol Chem
, vol.275
, pp. 24622-24629
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Goldberg, M.1
Peshkovsky, C.2
Shifteh, A.3
Al-Awqati, Q.4
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13
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0035914165
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Identification of three novel non-classical cadherin genes through comprehensive analysis of large cDNAs
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Nakajima D., Nakayama M., Kikuno R., Hirosawa M., Nagase T., Ohara O. Identification of three novel non-classical cadherin genes through comprehensive analysis of large cDNAs. Brain Res Mol Brain Res. 94:2001;85-95.
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Brain Res Mol Brain Res
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, pp. 85-95
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Nakajima, D.1
Nakayama, M.2
Kikuno, R.3
Hirosawa, M.4
Nagase, T.5
Ohara, O.6
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14
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0035421436
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Mutations in the novel protocadherin PCDH15 cause Usher syndrome type 1F
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This is the first report that identifies a mutated protocadherin as the cause of a human disease. Clinically, Usher syndrome 1F manifests in sensory impairments, (i.e. congenital deafness and progressive retinopathy). Similarly in mice, mutations of protocadherin 15 cause deafness and degeneration of inner ear neuroepithelia in the mutant 'Ames waltzer' [11] . Protocadherin 15 is expressed in several epithelia and in the nervous system, including the retina and the sensory hair cells of the inner ear.
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Alagramam K.N., Yuan H., Kuehn M.H., Murcia C.L., Wayne S., Srisailpathy C.R., Lowry R.B., Knaus R., Van Laer L., Bernier F.P., et al. Mutations in the novel protocadherin PCDH15 cause Usher syndrome type 1F. Hum Mol Genet. 10:2001;1709-1718. This is the first report that identifies a mutated protocadherin as the cause of a human disease. Clinically, Usher syndrome 1F manifests in sensory impairments, (i.e. congenital deafness and progressive retinopathy). Similarly in mice, mutations of protocadherin 15 cause deafness and degeneration of inner ear neuroepithelia in the mutant 'Ames waltzer' [11] . Protocadherin 15 is expressed in several epithelia and in the nervous system, including the retina and the sensory hair cells of the inner ear.
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(2001)
Hum Mol Genet
, vol.10
, pp. 1709-1718
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Alagramam, K.N.1
Yuan, H.2
Kuehn, M.H.3
Murcia, C.L.4
Wayne, S.5
Srisailpathy, C.R.6
Lowry, R.B.7
Knaus, R.8
Van Laer, L.9
Bernier, F.P.10
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15
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0034724368
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Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes
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Wu Q., Maniatis T. Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes. Proc Natl Acad Sci USA. 97:2000;3124-3129.
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Proc Natl Acad Sci USA
, vol.97
, pp. 3124-3129
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Wu, Q.1
Maniatis, T.2
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16
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0035917818
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The human and murine protocadherin-beta one-exon gene families show high evolutionary conservation, despite the difference in gene number
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Vanhalst K., Kools P., Vanden Eynde E., van Roy F. The human and murine protocadherin-beta one-exon gene families show high evolutionary conservation, despite the difference in gene number. FEBS Lett. 495:2001;120-125.
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FEBS Lett
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Vanhalst, K.1
Kools, P.2
Vanden Eynde, E.3
Van Roy, F.4
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17
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0035076508
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The cadherin superfamily
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An instructive and nicely illustrated review, with emphasis on the respective structure/function relationships of the different cadherin subfamilies in adhesion and signaling.
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Angst B.D., Marcozzi C., Magee A.I. The cadherin superfamily. J Cell Sci. 114:2001;625-626. An instructive and nicely illustrated review, with emphasis on the respective structure/function relationships of the different cadherin subfamilies in adhesion and signaling.
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(2001)
J Cell Sci
, vol.114
, pp. 625-626
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Angst, B.D.1
Marcozzi, C.2
Magee, A.I.3
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18
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0033781206
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CDNA cloning, chromosomal mapping, and expression analysis of human VE-Cadherin-2
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Ludwig D., Lorenz J., Dejana E., Bohlen P., Hicklin D.J., Witte L., Pytowski B. cDNA cloning, chromosomal mapping, and expression analysis of human VE-Cadherin-2. Mamm Genome. 11:2000;1030-1033.
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(2000)
Mamm Genome
, vol.11
, pp. 1030-1033
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Ludwig, D.1
Lorenz, J.2
Dejana, E.3
Bohlen, P.4
Hicklin, D.J.5
Witte, L.6
Pytowski, B.7
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19
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0035878392
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Identification and characterization of three members of a novel subclass of protocadherins
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The authors identify a motif conserved in the cytoplasmic portion of many protocadherins, and describe the sequences and genomic organization of three new protocadherins containing this motif. Intriguingly, in some protocadherins the motif is only present in unique splice variants.
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Wolverton T., Lalande M. Identification and characterization of three members of a novel subclass of protocadherins. Genomics. 76:2001;66-72. The authors identify a motif conserved in the cytoplasmic portion of many protocadherins, and describe the sequences and genomic organization of three new protocadherins containing this motif. Intriguingly, in some protocadherins the motif is only present in unique splice variants.
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(2001)
Genomics
, vol.76
, pp. 66-72
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Wolverton, T.1
Lalande, M.2
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20
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0033808650
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Conservation of PCDHX in mammals; Expression of human X/Y genes predominantly in brain
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Blanco P., Sargent C.A., Boucher C.A., Mitchell M., Affara N.A. Conservation of PCDHX in mammals; expression of human X/Y genes predominantly in brain. Mamm Genome. 11:2000;906-914.
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(2000)
Mamm Genome
, vol.11
, pp. 906-914
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Blanco, P.1
Sargent, C.A.2
Boucher, C.A.3
Mitchell, M.4
Affara, N.A.5
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21
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0033572510
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Identification of a novel protocadherin gene (PCDH11) on the human XY homology region in Xq21.3
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Yoshida K., Sugano S. Identification of a novel protocadherin gene (PCDH11) on the human XY homology region in Xq21.3. Genomics. 62:1999;540-543.
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(1999)
Genomics
, vol.62
, pp. 540-543
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Yoshida, K.1
Sugano, S.2
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22
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0033999020
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Genomic organization of the family of CNR cadherin genes in mice and humans
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Sugino H., Hamada S., Yasuda R., Tuji A., Matsuda Y., Fujita M., Yagi T. Genomic organization of the family of CNR cadherin genes in mice and humans. Genomics. 63:2000;75-87.
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(2000)
Genomics
, vol.63
, pp. 75-87
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Sugino, H.1
Hamada, S.2
Yasuda, R.3
Tuji, A.4
Matsuda, Y.5
Fujita, M.6
Yagi, T.7
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23
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0035793213
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Cadherin superfamily proteins in Caenorhabditis elegans and Drosophila melanogaster
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A thorough analysis of cadherin-related genes in the sequenced genomes of both model organisms provides new insight into the evolution of the cadherin superfamily. The study suggests that Fat, seven-pass transmembrane cadherins and a cadherin molecule with two ectodomains are of ancient type, as is the cytoplasmic domain of classic cadherins. Interestingly, the presence of many unique types of cadherins indicates convergent evolutionary selection of species- or phylum-specific cadherins.
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Hill E., Broadbent I.D., Chothia C., Pettitt J. Cadherin superfamily proteins in Caenorhabditis elegans and Drosophila melanogaster. J Mol Biol. 305:2001;1011-1024. A thorough analysis of cadherin-related genes in the sequenced genomes of both model organisms provides new insight into the evolution of the cadherin superfamily. The study suggests that Fat, seven-pass transmembrane cadherins and a cadherin molecule with two ectodomains are of ancient type, as is the cytoplasmic domain of classic cadherins. Interestingly, the presence of many unique types of cadherins indicates convergent evolutionary selection of species- or phylum-specific cadherins.
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(2001)
J Mol Biol
, vol.305
, pp. 1011-1024
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Hill, E.1
Broadbent, I.D.2
Chothia, C.3
Pettitt, J.4
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24
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0035147474
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Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain
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Vogt L., Schrimpf S.P., Meskenaite V., Frischknecht R., Kinter J., Leone D.P., Ziegler U., Sonderegger P. Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain. Mol Cell Neurosci. 17:2001;151-166.
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Mol Cell Neurosci
, vol.17
, pp. 151-166
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Vogt, L.1
Schrimpf, S.P.2
Meskenaite, V.3
Frischknecht, R.4
Kinter, J.5
Leone, D.P.6
Ziegler, U.7
Sonderegger, P.8
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25
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0033544706
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Proteins of the CNR family are multiple receptors for Reelin
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Senzaki K., Ogawa M., Yagi T. Proteins of the CNR family are multiple receptors for Reelin. Cell. 99:1999;635-647.
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Cell
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Senzaki, K.1
Ogawa, M.2
Yagi, T.3
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26
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0033081489
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Expression of a novel protocadherin, OL-protocadherin, in a subset of functional systems of the developing mouse brain
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Hirano S., Yan Q., Suzuki S.T. Expression of a novel protocadherin, OL-protocadherin, in a subset of functional systems of the developing mouse brain. J Neurosci. 19:1999;995-1005.
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, vol.19
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Hirano, S.1
Yan, Q.2
Suzuki, S.T.3
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27
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0029616019
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Protocadherin Pcdh2 shows properties similar to, but distinct from, those of classical cadherins
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Obata S., Sago H., Mori N., Rochelle J.M., Seldin M.F., Davidson M., St John T., Taketani S., Suzuki S.T. Protocadherin Pcdh2 shows properties similar to, but distinct from, those of classical cadherins. J Cell Sci. 108:1995;3765-3773.
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J Cell Sci
, vol.108
, pp. 3765-3773
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Obata, S.1
Sago, H.2
Mori, N.3
Rochelle, J.M.4
Seldin, M.F.5
Davidson, M.6
St John, T.7
Taketani, S.8
Suzuki, S.T.9
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28
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0033516668
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Arcadlin is a neural activity-regulated cadherin involved in long-term potentiation
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Yamagata K., Andreasson K.I., Sugiura H., Maru E., Dominique M., Irie Y., Miki N., Hayashi Y., Yoshioka M., Kaneko K., et al. Arcadlin is a neural activity-regulated cadherin involved in long-term potentiation. J Biol Chem. 274:1999;11979-19473.
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J Biol Chem
, vol.274
, pp. 11979-19473
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Yamagata, K.1
Andreasson, K.I.2
Sugiura, H.3
Maru, E.4
Dominique, M.5
Irie, Y.6
Miki, N.7
Hayashi, Y.8
Yoshioka, M.9
Kaneko, K.10
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29
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0032504260
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Identification of a novel cadherin (vascular endothelial cadherin-2) located at intercellular junctions in endothelial cells
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Telo P., Breviario F., Huber P., Panzeri C., Dejana E. Identification of a novel cadherin (vascular endothelial cadherin-2) located at intercellular junctions in endothelial cells. J Biol Chem. 273:1998;17565-17572.
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J Biol Chem
, vol.273
, pp. 17565-17572
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Telo, P.1
Breviario, F.2
Huber, P.3
Panzeri, C.4
Dejana, E.5
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30
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0037090984
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Axial protocadherin is a mediator of prenotochord cell sorting in Xenopus
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Xenopus axial protocadherin (AXPC) mediates homophilic cell adhesion and is crucial for proper notochord formation in the neurula stage, as shown by injection of dominant-negative constructs and morpholino oligonucleotides. Possibly, AXPC-mediated cell sorting is also involved in the morphogenesis of other structures, as expression of AXPC is found in the nervous system, the somites and the pronephros later in development.
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Kuroda H., Inui M., Sugimoto K., Hayata T., Asashima M. Axial protocadherin is a mediator of prenotochord cell sorting in Xenopus. Dev Biol. 244:2002;267-277. Xenopus axial protocadherin (AXPC) mediates homophilic cell adhesion and is crucial for proper notochord formation in the neurula stage, as shown by injection of dominant-negative constructs and morpholino oligonucleotides. Possibly, AXPC-mediated cell sorting is also involved in the morphogenesis of other structures, as expression of AXPC is found in the nervous system, the somites and the pronephros later in development.
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(2002)
Dev Biol
, vol.244
, pp. 267-277
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Kuroda, H.1
Inui, M.2
Sugimoto, K.3
Hayata, T.4
Asashima, M.5
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31
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0032414392
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The role of paraxial protocadherin in selective adhesion and cell movements of the mesoderm during Xenopus gastrulation
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Kim S.H., Yamamoto A., Bouwmeester T., Agius E., Robertis E.M. The role of paraxial protocadherin in selective adhesion and cell movements of the mesoderm during Xenopus gastrulation. Development. 125:1998;4681-4690.
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(1998)
Development
, vol.125
, pp. 4681-4690
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Kim, S.H.1
Yamamoto, A.2
Bouwmeester, T.3
Agius, E.4
Robertis, E.M.5
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32
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0032860770
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BH-protocadherin-c, a member of the cadherin superfamily, interacts with protein phosphatase 1 alpha through its intracellular domain
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Yoshida K., Watanabe M., Kato H., Dutta A., Sugano S. BH-protocadherin-c, a member of the cadherin superfamily, interacts with protein phosphatase 1 alpha through its intracellular domain. FEBS Lett. 460:1999;93-98.
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FEBS Lett
, vol.460
, pp. 93-98
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Yoshida, K.1
Watanabe, M.2
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Dutta, A.4
Sugano, S.5
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33
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0035976795
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Disabled-1 interacts with a novel developmentally regulated protocadherin
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The cloning of protocadherin 18 (see also Wolverton and Lalande 2001 [19•] ) resulted from a yeast two-hybrid screen for novel interaction partners of Dab1. It exhibits typical features of the protocadherin family in its genomic organization. The phosphotyrosine-binding (PTB) domain of Disabled is relevant for interaction with protocadherin 18, suggesting that other PTB-domain proteins might interact with this protocadherin in different tissues.
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Homayouni R., Rice D.S., Curran T. Disabled-1 interacts with a novel developmentally regulated protocadherin. Biochem Biophys Res Commun. 289:2001;539-547. The cloning of protocadherin 18 (see also Wolverton and Lalande 2001 [19•] ) resulted from a yeast two-hybrid screen for novel interaction partners of Dab1. It exhibits typical features of the protocadherin family in its genomic organization. The phosphotyrosine-binding (PTB) domain of Disabled is relevant for interaction with protocadherin 18, suggesting that other PTB-domain proteins might interact with this protocadherin in different tissues.
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(2001)
Biochem Biophys Res Commun
, vol.289
, pp. 539-547
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Homayouni, R.1
Rice, D.S.2
Curran, T.3
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34
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0035021654
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Juxtaposition of CNR protocadherins and reelin expression in the developing spinal cord
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Carroll P., Gayet O., Feuillet C., Kallenbach S., de Bovis B., Dudley K., Alonso S. Juxtaposition of CNR protocadherins and reelin expression in the developing spinal cord. Mol Cell Neurosci. 17:2001;611-623.
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(2001)
Mol Cell Neurosci
, vol.17
, pp. 611-623
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Carroll, P.1
Gayet, O.2
Feuillet, C.3
Kallenbach, S.4
De Bovis, B.5
Dudley, K.6
Alonso, S.7
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35
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0034918597
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Dynamic expression patterns of the new protocadherin families CNRs and Pcdh-gamma during mouse odontogenesis: Comparison with reelin expression
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Heymann R., Kallenbach S., Alonso S., Carroll P., Mitsiadis T.A. Dynamic expression patterns of the new protocadherin families CNRs and Pcdh-gamma during mouse odontogenesis: comparison with reelin expression. Mech Dev. 106:2001;181-184.
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(2001)
Mech Dev
, vol.106
, pp. 181-184
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Heymann, R.1
Kallenbach, S.2
Alonso, S.3
Carroll, P.4
Mitsiadis, T.A.5
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36
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0031697445
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Zebrafish paraxial protocadherin is a downstream target of spadetail involved in morphogenesis of gastrula mesoderm
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