“Assignment1 of the E-cadherin gene (CDH1) to chromosome 16q22.1 by radiation hybrid mapping”. Cytogenetics and Cell Genetics83 (1–2): 82–83. (Mar 1999). doi:10.1159/000015134. PMID9925936.
“Historical review of the discovery of cadherin, in memory of Tokindo Okada”. Development, Growth & Differentiation60 (1): 3–13. (January 2018). doi:10.1111/dgd.12416. PMID29278270.
“Experimental manipulation of cell surface to affect cellular recognition mechanisms”. Developmental Biology70 (1): 195–205. (May 1979). doi:10.1016/0012-1606(79)90016-2. PMID456740.
“Immunological detection of cell surface components related with aggregation of Chinese hamster and chick embryonic cells”. Developmental Biology70 (1): 206–216. (May 1979). doi:10.1016/0012-1606(79)90017-4. PMID110634.
“Cell-cell adhesion molecule: identification of a glycoprotein relevant to the Ca2+-independent aggregation of Chinese hamster fibroblasts”. Cell20 (2): 363–371. (June 1980). doi:10.1016/0092-8674(80)90622-4. PMID7388946.
“Molecular nature of the calcium-dependent cell-cell adhesion system in mouse teratocarcinoma and embryonic cells studied with a monoclonal antibody”. Developmental Biology101 (1): 19–27. (January 1984). doi:10.1016/0012-1606(84)90112-X. PMID6692973.
“Cell-cell interactions in early embryogenesis: a molecular approach to the role of calcium”. Cell26 (3 Pt 1): 447–454. (1981). doi:10.1016/0092-8674(81)90214-2. PMID6976838.
“Assembly of tight junctions during early vertebrate development”. Seminars in Cell & Developmental Biology11 (4): 291–299. (August 2000). doi:10.1006/scdb.2000.0179. PMID10966863.
“Contact inhibition (of proliferation) redux”. Current Opinion in Cell Biology. Cell-to-cell contact and extracellular matrix 24 (5): 685–694. (October 2012). doi:10.1016/j.ceb.2012.06.009. PMID22835462.
“E-cadherin is required for gastrulation cell movements in zebrafish”. Mechanisms of Development122 (6): 747–763. (June 2005). doi:10.1016/j.mod.2005.03.008. PMID15905076.
“Tensile forces govern germ-layer organization in zebrafish”. Nature Cell Biology10 (4): 429–436. (April 2008). doi:10.1038/ncb1705. PMID18364700.
“Cell surface mechanics and the control of cell shape, tissue patterns and morphogenesis”. Nature Reviews. Molecular Cell Biology8 (8): 633–644. (August 2007). doi:10.1038/nrm2222. PMID17643125.
“The Epithelial Circumferential Actin Belt Regulates YAP/TAZ through Nucleocytoplasmic Shuttling of Merlin” (English). Cell Reports20 (6): 1435–1447. (August 2017). doi:10.1016/j.celrep.2017.07.032. PMID28793266.
“Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex”. Nature Cell Biology4 (3): 222–231. (March 2002). doi:10.1038/ncb758. PMID11836526.
“TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1”. Current Biology13 (17): 1459–1468. (September 2003). doi:10.1016/S0960-9822(03)00581-5. PMID12956947.
“Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions”. Journal of Cell Science113 ( Pt 16) (16): 2829–2836. (August 2000). doi:10.1242/jcs.113.16.2829. PMID10910767.
“HGF/SF modifies the interaction between its receptor c-Met, and the E-cadherin/catenin complex in prostate cancer cells”. International Journal of Molecular Medicine7 (4): 385–388. (April 2001). doi:10.3892/ijmm.7.4.385. PMID11254878.
“Expression and interaction of different catenins in colorectal carcinoma cells”. International Journal of Molecular Medicine8 (6): 695–698. (December 2001). doi:10.3892/ijmm.8.6.695. PMID11712088.
“Expression of E- or P-cadherin is not sufficient to modify the morphology and the tumorigenic behavior of murine spindle carcinoma cells. Possible involvement of plakoglobin”. Journal of Cell Science105 ( Pt 4) (4): 923–934. (August 1993). doi:10.1242/jcs.105.4.923. hdl:10261/78716. PMID8227214.
“FoxM1 is degraded at mitotic exit in a Cdh1-dependent manner”. Cell Cycle7 (17): 2720–2726. (September 2008). doi:10.4161/cc.7.17.6580. PMID18758239.
“WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase”. FEBS Letters575 (1–3): 23–29. (September 2004). doi:10.1016/j.febslet.2004.07.089. PMID15388328.
“IQGAP1 and calmodulin modulate E-cadherin function”. The Journal of Biological Chemistry274 (53): 37885–37892. (December 1999). doi:10.1074/jbc.274.53.37885. PMID10608854.
“Vinculin is associated with the E-cadherin adhesion complex”. The Journal of Biological Chemistry272 (51): 32448–32453. (December 1997). doi:10.1074/jbc.272.51.32448. PMID9405455.
“The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation”. European Journal of Cancer36 (13 Spec No): 1607–1620. (August 2000). doi:10.1016/S0959-8049(00)00158-1. PMID10959047.
“The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells”. Nature Cell Biology2 (2): 84–89. (February 2000). doi:10.1038/35000034. PMID10655587.
“DeltaEF1 is a transcriptional repressor of E-cadherin and regulates epithelial plasticity in breast cancer cells”. Oncogene24 (14): 2375–2385. (March 2005). doi:10.1038/sj.onc.1208429. PMID15674322.
“The two-handed E box binding zinc finger protein SIP1 downregulates E-cadherin and induces invasion”. Molecular Cell7 (6): 1267–1278. (June 2001). doi:10.1016/S1097-2765(01)00260-X. PMID11430829.
“Twist, a master regulator of morphogenesis, plays an essential role in tumor metastasis”. Cell117 (7): 927–939. (June 2004). doi:10.1016/j.cell.2004.06.006. PMID15210113.
“Methylation patterns of the E-cadherin 5' CpG island are unstable and reflect the dynamic, heterogeneous loss of E-cadherin expression during metastatic progression”. The Journal of Biological Chemistry275 (4): 2727–2732. (January 2000). doi:10.1074/jbc.275.4.2727. PMID10644736.
“Expression of E- or P-cadherin is not sufficient to modify the morphology and the tumorigenic behavior of murine spindle carcinoma cells. Possible involvement of plakoglobin”. Journal of Cell Science105 ( Pt 4) (4): 923–934. (August 1993). doi:10.1242/jcs.105.4.923. hdl:10261/78716. PMID8227214.
“Assignment1 of the E-cadherin gene (CDH1) to chromosome 16q22.1 by radiation hybrid mapping”. Cytogenetics and Cell Genetics83 (1–2): 82–83. (Mar 1999). doi:10.1159/000015134. PMID9925936.
“Historical review of the discovery of cadherin, in memory of Tokindo Okada”. Development, Growth & Differentiation60 (1): 3–13. (January 2018). doi:10.1111/dgd.12416. PMID29278270.
“Experimental manipulation of cell surface to affect cellular recognition mechanisms”. Developmental Biology70 (1): 195–205. (May 1979). doi:10.1016/0012-1606(79)90016-2. PMID456740.
“Immunological detection of cell surface components related with aggregation of Chinese hamster and chick embryonic cells”. Developmental Biology70 (1): 206–216. (May 1979). doi:10.1016/0012-1606(79)90017-4. PMID110634.
“Cell-cell adhesion molecule: identification of a glycoprotein relevant to the Ca2+-independent aggregation of Chinese hamster fibroblasts”. Cell20 (2): 363–371. (June 1980). doi:10.1016/0092-8674(80)90622-4. PMID7388946.
“Molecular nature of the calcium-dependent cell-cell adhesion system in mouse teratocarcinoma and embryonic cells studied with a monoclonal antibody”. Developmental Biology101 (1): 19–27. (January 1984). doi:10.1016/0012-1606(84)90112-X. PMID6692973.
“Cell-cell interactions in early embryogenesis: a molecular approach to the role of calcium”. Cell26 (3 Pt 1): 447–454. (1981). doi:10.1016/0092-8674(81)90214-2. PMID6976838.
“Assembly of tight junctions during early vertebrate development”. Seminars in Cell & Developmental Biology11 (4): 291–299. (August 2000). doi:10.1006/scdb.2000.0179. PMID10966863.
“Contact inhibition (of proliferation) redux”. Current Opinion in Cell Biology. Cell-to-cell contact and extracellular matrix 24 (5): 685–694. (October 2012). doi:10.1016/j.ceb.2012.06.009. PMID22835462.
“E-cadherin is required for gastrulation cell movements in zebrafish”. Mechanisms of Development122 (6): 747–763. (June 2005). doi:10.1016/j.mod.2005.03.008. PMID15905076.
“Tensile forces govern germ-layer organization in zebrafish”. Nature Cell Biology10 (4): 429–436. (April 2008). doi:10.1038/ncb1705. PMID18364700.
“Cell surface mechanics and the control of cell shape, tissue patterns and morphogenesis”. Nature Reviews. Molecular Cell Biology8 (8): 633–644. (August 2007). doi:10.1038/nrm2222. PMID17643125.
“The Epithelial Circumferential Actin Belt Regulates YAP/TAZ through Nucleocytoplasmic Shuttling of Merlin” (English). Cell Reports20 (6): 1435–1447. (August 2017). doi:10.1016/j.celrep.2017.07.032. PMID28793266.
“Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex”. Nature Cell Biology4 (3): 222–231. (March 2002). doi:10.1038/ncb758. PMID11836526.
“TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1”. Current Biology13 (17): 1459–1468. (September 2003). doi:10.1016/S0960-9822(03)00581-5. PMID12956947.
“Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions”. Journal of Cell Science113 ( Pt 16) (16): 2829–2836. (August 2000). doi:10.1242/jcs.113.16.2829. PMID10910767.
“HGF/SF modifies the interaction between its receptor c-Met, and the E-cadherin/catenin complex in prostate cancer cells”. International Journal of Molecular Medicine7 (4): 385–388. (April 2001). doi:10.3892/ijmm.7.4.385. PMID11254878.
“Expression and interaction of different catenins in colorectal carcinoma cells”. International Journal of Molecular Medicine8 (6): 695–698. (December 2001). doi:10.3892/ijmm.8.6.695. PMID11712088.
“Expression of E- or P-cadherin is not sufficient to modify the morphology and the tumorigenic behavior of murine spindle carcinoma cells. Possible involvement of plakoglobin”. Journal of Cell Science105 ( Pt 4) (4): 923–934. (August 1993). doi:10.1242/jcs.105.4.923. hdl:10261/78716. PMID8227214.
“FoxM1 is degraded at mitotic exit in a Cdh1-dependent manner”. Cell Cycle7 (17): 2720–2726. (September 2008). doi:10.4161/cc.7.17.6580. PMID18758239.
“WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase”. FEBS Letters575 (1–3): 23–29. (September 2004). doi:10.1016/j.febslet.2004.07.089. PMID15388328.
“IQGAP1 and calmodulin modulate E-cadherin function”. The Journal of Biological Chemistry274 (53): 37885–37892. (December 1999). doi:10.1074/jbc.274.53.37885. PMID10608854.
“Vinculin is associated with the E-cadherin adhesion complex”. The Journal of Biological Chemistry272 (51): 32448–32453. (December 1997). doi:10.1074/jbc.272.51.32448. PMID9405455.
“The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation”. European Journal of Cancer36 (13 Spec No): 1607–1620. (August 2000). doi:10.1016/S0959-8049(00)00158-1. PMID10959047.
“E-cadherin is inactivated in a majority of invasive human lobular breast cancers by truncation mutations throughout its extracellular domain”. Oncogene13 (9): 1919–1925. (November 1996). PMID8934538.
“E-cadherin gene mutations provide clues to diffuse type gastric carcinomas”. Cancer Research54 (14): 3845–3852. (July 1994). PMID8033105.
“The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells”. Nature Cell Biology2 (2): 84–89. (February 2000). doi:10.1038/35000034. PMID10655587.
“DeltaEF1 is a transcriptional repressor of E-cadherin and regulates epithelial plasticity in breast cancer cells”. Oncogene24 (14): 2375–2385. (March 2005). doi:10.1038/sj.onc.1208429. PMID15674322.
“The two-handed E box binding zinc finger protein SIP1 downregulates E-cadherin and induces invasion”. Molecular Cell7 (6): 1267–1278. (June 2001). doi:10.1016/S1097-2765(01)00260-X. PMID11430829.
“Twist, a master regulator of morphogenesis, plays an essential role in tumor metastasis”. Cell117 (7): 927–939. (June 2004). doi:10.1016/j.cell.2004.06.006. PMID15210113.
“Methylation patterns of the E-cadherin 5' CpG island are unstable and reflect the dynamic, heterogeneous loss of E-cadherin expression during metastatic progression”. The Journal of Biological Chemistry275 (4): 2727–2732. (January 2000). doi:10.1074/jbc.275.4.2727. PMID10644736.