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1995, Morphogenetic roles of classic cadherins, Curr Opin Cell Biol, 7, 619, 10.1016\u002F0955-0674(95)80102-2\nSuzuki, 1996, Structural and functional diversity of cadherin superfamily: are new members of cadherin superfamily involved in signal transduction pathway?, J Cell Biochem, 61, 531, 10.1002\u002F(SICI)1097-4644(19960616)61:4\u003C531::AID-JCB6>3.0.CO;2-P\nGallin, 1998, Evolution of the ‘classical’ cadherin family of cell adhesion molecules in vertebrates, Mol Biol Evol, 15, 1099, 10.1093\u002Foxfordjournals.molbev.a026017\nMarrs, 1996, Cadherin cell adhesion molecules in differentiation and embryogenesis, Int Rev Cytol, 165, 159, 10.1016\u002FS0074-7696(08)62222-6\nKnudsen, 1998, A role for cadherins in cellular signaling and differentiation, J Cell Biochem Suppl, 31, 168, 10.1002\u002F(SICI)1097-4644(1998)72:30\u002F31+\u003C168::AID-JCB21>3.0.CO;2-V\nBlaschuk, 1990, Identification of a cadherin cell adhesion recognition sequence, Dev Biol, 139, 227, 10.1016\u002F0012-1606(90)90290-Y\nPertz, 1999, A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation, EMBO J, 18, 1738, 10.1093\u002Femboj\u002F18.7.1738\nShapiro, 1995, Structural basis of cell–cell adhesion by cadherins [see comments], Nature, 374, 327, 10.1038\u002F374327a0\nNose, 1990, Localization of specificity determining sites in cadherin cell adhesion molecules, Cell, 61, 147, 10.1016\u002F0092-8674(90)90222-Z\nOzawa, 1998, The membrane-proximal region of the E cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity, J Cell Biol, 142, 1605, 10.1083\u002Fjcb.142.6.1605\nYap, 1997, Lateral clustering of the adhesive ectodomain: a fundamental determinant of cadherin function, Curr Biol, 7, 308, 10.1016\u002FS0960-9822(06)00154-0\nKatz, 1998, Modulation of cell–cell adherens junctions by surface clustering of the N-cadherin cytoplasmic tail, Exp Cell Res, 243, 415, 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protein mediating the attachment of F-actin to the membrane adhesion complex, Proc Natl Acad Sci USA, 92, 8813, 10.1073\u002Fpnas.92.19.8813\nYamada, 1997, Molecular interactions in cell adhesion complexes, Curr Opin Cell Biol, 9, 76, 10.1016\u002FS0955-0674(97)80155-X\nOzawa, 1998, Identification of the region of α-catenin that plays an essential role in cadherin-mediated cell adhesion, J Biol Chem, 273, 29524, 10.1074\u002Fjbc.273.45.29524\nImamura, 1999, Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion, J Cell Biol, 144, 1311, 10.1083\u002Fjcb.144.6.1311\nChen, 1999, Coupling assembly of the E-cadherin\u002Fβ-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells, J Cell Biol, 144, 687, 10.1083\u002Fjcb.144.4.687\nReynolds, 1992, p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors β-catenin, plakoglobin and armadillo, Oncogene, 7, 2439\nHatzfeld, 1999, The armadillo family of structural proteins, Int Rev Cytol, 186, 179, 10.1016\u002FS0074-7696(08)61054-2\nKeirsebilck, 1998, Molecular cloning of the human p120ctn catenin gene (CTNND1): expression of multiple alternatively spliced isoforms, Genomics, 50, 129, 10.1006\u002Fgeno.1998.5325\nCalautti, 1998, Tyrosine phosphorylation and Src family kinases control keratinocyte cell–cell adhesion, J Cell Biol, 141, 1449, 10.1083\u002Fjcb.141.6.1449\nAono, 1999, p120ctn acts as an inhibitory regulator of cadherin function in colon carcinoma cells, J Cell Biol, 145, 551, 10.1083\u002Fjcb.145.3.551\nDaniel, 1997, Tyrosine phosphorylation and cadherin\u002Fcatenin function, Bioessays, 19, 883, 10.1002\u002Fbies.950191008\nYap, 1998, The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn, J Cell Biol, 141, 779, 10.1083\u002Fjcb.141.3.779\nNavarro, 1998, Differential localization of VE- and N-cadherins in human endothelial cells: VE-cadherin competes with N-cadherin for junctional localization, J Cell Biol, 140, 1475, 10.1083\u002Fjcb.140.6.1475\nDaniel, 1999, The catenin p120ctn interacts with Kaiso, a novel BTB\u002FPOZ domain zinc finger transcription factor, Mol Cell Biol, 19, 3614, 10.1128\u002FMCB.19.5.3614\nWillert, 1998, β-catenin: a key mediator of Wnt signaling, Curr Opin Genet Dev, 8, 95, 10.1016\u002FS0959-437X(98)80068-3\nBullions, 1998, The role of β-catenin in cell adhesion, signal transduction, and cancer, Curr Opin Oncol, 10, 81, 10.1097\u002F00001622-199801000-00013\nHinck, 1994, Dynamics of cadherin\u002Fcatenin complex formation: novel protein interactions and pathways of complex assembly, J Cell Biol, 125, 1327, 10.1083\u002Fjcb.125.6.1327\nAdams, 1998, Mechanisms of epithelial cell–cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein, J Cell Biol, 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E-cadherin-mediated cell–cell adhesion, Science, 281, 832, 10.1126\u002Fscience.281.5378.832\nRatcliffe, 1997, Dephosphorylation of the cadherin-associated p100\u002Fp120 proteins in response to activation of protein kinase C in epithelial cells, J Biol Chem, 272, 31894, 10.1074\u002Fjbc.272.50.31894\nFoty, 1997, Measurement of tumor cell cohesion and suppression of invasion by E- or P-cadherin, Cancer Res, 57, 5033\nFoty, 1996, Surface tensions of embryonic tissues predict their mutual envelopment behavior, Development, 122, 1611, 10.1242\u002Fdev.122.5.1611\nDavis, 1997, Germ-layer surface tensions and ‘tissue affinities’ in Rana pipiens gastrulae: quantitative measurements, Dev Biol, 192, 630, 10.1006\u002Fdbio.1997.8741\nSteinberg, 1994, Experimental specification of cell sorting, tissue spreading, and specific spatial patterning by quantitative differences in cadherin expression, Proc Natl Acad Sci USA, 91, 206, 10.1073\u002Fpnas.91.1.206\nSteinberg, 1996, Adhesion in development: an historical overview, Dev Biol, 180, 377, 10.1006\u002Fdbio.1996.0312\nNakagawa, 1998, Neural crest emigration from the neural tube depends on regulated cadherin expression, Development, 125, 2963, 10.1242\u002Fdev.125.15.2963\nLinask, 1998, N cadherin\u002Fcatenin-mediated morphoregulation of somite formation, Dev Biol, 202, 85, 10.1006\u002Fdbio.1998.9025\nSuzuki, 1997, Neuronal circuits are subdivided by differential expression of type-II classic cadherins in postnatal mouse brains, Mol Cell Neurosci, 9, 433, 10.1006\u002Fmcne.1997.0626\nYap, 1998, The morphogenetic role of cadherin cell adhesion molecules in human cancer: a thematic review, Cancer Invest, 16, 252, 10.3109\u002F07357909809039774\nChristofori, 1999, The role of the cell-adhesion molecule E-cadherin as a tumour-suppressor gene, Trends Biochem Sci, 24, 73, 10.1016\u002FS0968-0004(98)01343-7\nVleminckx, 1991, Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role, Cell, 66, 107, 10.1016\u002F0092-8674(91)90143-M\nLee, 1998, H-cadherin expression inhibits in vitro invasiveness and tumor formation in vivo, Carcinogenesis, 19, 1157, 10.1093\u002Fcarcin\u002F19.6.1157\nMarrs, 1995, Plasticity in epithelial cell phenotype: modulation by expression of different cadherin cell adhesion molecules, J Cell Biol, 129, 507, 10.1083\u002Fjcb.129.2.507\nLarue, 1996, A role for cadherins in tissue formation, Development, 122, 3185, 10.1242\u002Fdev.122.10.3185\nLi, 1998, L-CAM expression induces fibroblast-epidermoid transition in squamous carcinoma cells and downregulates the endogenous N-cadherin, J Cell Sci, 111, 1005, 10.1242\u002Fjcs.111.7.1005\nParker, 1998, Plakoglobin induces desmosome formation and epidermoid phenotype in N-cadherin-expressing squamous carcinoma cells deficient in plakoglobin and E-cadherin, Cell Motil Cytoskeleton, 40, 87, 10.1002\u002F(SICI)1097-0169(1998)40:1\u003C87::AID-CM8>3.0.CO;2-C\nWoodward, 1999, N-cadherin expression and signaling in limb mesenchymal chondrogenesis: stimulation by poly-L-lysine, Dev Genet, 24, 178, 10.1002\u002F(SICI)1520-6408(1999)24:1\u002F2\u003C178::AID-DVG16>3.0.CO;2-M\nHaas, 1999, Chondrogenic differentiation of murine C3H10T1\u002F2 multipotential mesenchymal cells: II. Stimulation by bone morphogenetic protein-2 requires modulation of N-cadherin expression and function, Differentiation, 64, 77, 10.1046\u002Fj.1432-0436.1999.6420077.x\nGeorge-Weinstein, 1997, N-cadherin promotes the commitment and differentiation of skeletal muscle precursor cells, Dev Biol, 185, 14, 10.1006\u002Fdbio.1997.8542\nRedfield, 1997, Cadherins promote skeletal muscle differentiation in three-dimensional cultures, J Cell Biol, 138, 1323, 10.1083\u002Fjcb.138.6.1323\nGoichberg, 1998, Direct involvement of N-cadherin-mediated signaling in muscle differentiation, Mol Biol Cell, 9, 3119, 10.1091\u002Fmbc.9.11.3119\nImanaka-Yoshida, 1998, N-cadherin is required for the differentiation and initial myofibrillogenesis of chick cardiomyocytes, Cell Motil Cytoskeleton, 39, 52, 10.1002\u002F(SICI)1097-0169(1998)39:1\u003C52::AID-CM5>3.0.CO;2-I\nInoue, 1998, Cadherin-6 in the developing mouse brain: expression along restricted connection systems and synaptic localization suggest a 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mechanisms in cell-mediated cytotoxicity, Annu Rev Cell Dev Biol, 23, 495, 10.1146\u002Fannurev.cellbio.23.090506.123521\nFinetti, 2009, Intraflagellar transport is required for polarized recycling of the TCR\u002FCD3 complex to the immune synapse, Nat Cell Biol, 11, 1332, 10.1038\u002Fncb1977\nStinchcombe, 2001, The immunological synapse of CTL contains a secretory domain and membrane bridges, Immunity, 15, 751, 10.1016\u002FS1074-7613(01)00234-5",{"EN":192},"Cell polarisation and the immunological 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10.1016\u002Fj.gene.2005.06.019",{"doi":704},"10.1016\u002Fj.gene.2005.06.019",{"id":18,"text":706,"url":18,"identifiers":707},"Prasanth, 2007, Eukaryotic regulatory RNAs: an answer to the ‘genome complexity’ conundrum, Genes Dev, 21, 11, 10.1101\u002Fgad.1484207",{"doi":708},"10.1101\u002Fgad.1484207",{"id":18,"text":710,"url":18,"identifiers":711},"Faghihi, 2008, Expression of a noncoding RNA is elevated in Alzheimer's disease and drives rapid feed-forward regulation of beta-secretase, Nat Med, 14, 723, 10.1038\u002Fnm1784",{"doi":712},"10.1038\u002Fnm1784",{"id":18,"text":714,"url":18,"identifiers":715},"Khalil, 2008, A novel RNA transcript with antiapoptotic function is silenced in fragile X syndrome, PLoS One, 3, e1486, 10.1371\u002Fjournal.pone.0001486",{"doi":716},"10.1371\u002Fjournal.pone.0001486",{"id":718,"createTime":719,"updateTime":719,"relativeEntities":720,"slug":18,"properties":721,"entityType":109,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":728,"fullTextUrl":18,"authors":729,"publicationType":150,"publisherRelationship":757,"citationCount":18,"citationInfo":18,"publishDate":785,"publishYear":786,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":181},"f7e47bb6-ee73-4dc0-b93f-f1307e95a59e","2024-01-09T23:56:59.685+00:00",[],{"references":722,"title":724,"doi":726},{"VOID":723},"Oegema, 1997, Rappaport rules: cleavage furrow induction in animal cells, Proc Natl Acad Sci USA, 94, 4817, 10.1073\u002Fpnas.94.10.4817\nEichinger, 1999, Dictyostelium as model system for studies of the actin cytoskeleton by molecular genetics, Microsc 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10.1083\u002Fjcb.146.2.439\nGuo, 1996, A non-muscle myosin required for embryonic polarity in Caenorhabditis elegans, Nature, 382, 455, 10.1038\u002F382455a0\nZurek, 1990, Differential effects of myosin-antibody complexes on contractile rings and circumferential belts in epitheloid cells, J Cell Sci, 97, 297, 10.1242\u002Fjcs.97.2.297\nKomatsu, 2000, Effects of the regulatory light chain phosphorylation of myosin II on mitosis and cytokinesis of mammalian cells, J Biol Chem, 275, 34512, 10.1074\u002Fjbc.M003019200\nSomma, 2002, Molecular dissection of cytokinesis by RNA interference in Drosophila cultured cells, Mol Biol Cell, 13, 2448, 10.1091\u002Fmbc.01-12-0589\nYoung, 1993, Morphogenesis in Drosophila requires nonmuscle myosin heavy chain function, Genes Dev, 7, 29, 10.1101\u002Fgad.7.1.29\nStraight, 2003, Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor, Science, 299, 1743, 10.1126\u002Fscience.1081412\nPierini, 2003, Membrane lipid organization is critical for human neutrophil polarization, J Biol Chem, 278, 10831, 10.1074\u002Fjbc.M212386200\nO’Connell, 1999, The small GTP-binding protein Rho regulates cortical activities in cultured cells during division, J Cell Biol, 144, 305, 10.1083\u002Fjcb.144.2.305\nO’Connell, 2001, Distinct roles of the equatorial and polar cortices in the cleavage of adherent cells, Curr Biol, 11, 702, 10.1016\u002FS0960-9822(01)00181-6",{"EN":725},"Variations on a theme: the many modes of cytokinesis",{"VOID":727},"10.1016\u002Fj.ceb.2003.11.004","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0955067403001601",[730,745],{"id":731,"sortIndex":19,"researcher":18,"roles":732,"affiliations":733,"properties":742},"00942417-cbac-4aeb-b0d1-e62355a2d497",[118],[734],{"id":18,"sortIndex":19,"affiliation":735,"properties":18},{"id":736,"createTime":737,"updateTime":737,"relativeEntities":738,"slug":18,"properties":739,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"f4c73b9f-2cb5-4374-af4c-07312e23bbb8","2024-01-09T23:56:59.716+00:00",[],{"title":740},{"VI":741},"Gene Function Research Center, Tsukuba Central 4, AIST, Tsukuba, Ibaraki 305-8562, Japan",{"title":743},{"VI":744},"Taro QP Uyeda",{"id":746,"sortIndex":116,"researcher":18,"roles":747,"affiliations":748,"properties":754},"9c3ed7f1-4db4-42b7-8f1c-5370ff3be299",[118],[749],{"id":18,"sortIndex":19,"affiliation":750,"properties":18},{"id":736,"createTime":737,"updateTime":737,"relativeEntities":751,"slug":18,"properties":752,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":753},{"VI":741},{"title":755},{"VI":756},"Akira Nagasaki",{"url":728,"publisher":758,"properties":780},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":759,"slug":10,"properties":760,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":763,"manageAffiliations":764,"indexDatabases":765,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":761,"title":762},{"VOID":13},{"EN":15},[],[],[766,773],{"id":55,"indexDatabase":767,"url":70,"indexYears":18,"academicFieldIds":772,"indexDatabaseRanking":18},{"id":57,"createTime":58,"updateTime":59,"relativeEntities":768,"label":769,"description":770,"key":66,"publicationTags":771,"standard":18},[],{"EN":62,"VI":62},{"VI":64,"EN":65},[68,69],[72],{"id":74,"indexDatabase":774,"url":87,"indexYears":88,"academicFieldIds":779,"indexDatabaseRanking":91},{"id":76,"createTime":77,"updateTime":78,"relativeEntities":775,"label":776,"description":777,"key":84,"publicationTags":778,"standard":18},[],{"EN":81,"VI":81},{"EN":81,"VI":83},[86],[90],{"volume":781,"pages":783},{"VOID":782},"16",{"VOID":784},"55-60","2004-02-01",2004,{"id":788,"createTime":789,"updateTime":790,"relativeEntities":791,"slug":792,"properties":793,"entityType":109,"verifyStatus":17,"verifyTime":790,"verifyNote":802,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":803,"fullTextUrl":18,"authors":804,"publicationType":150,"publisherRelationship":826,"citationCount":18,"citationInfo":18,"publishDate":853,"publishYear":495,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":181},"e5a7cd1d-d474-4f6e-9fd0-6d3255cce7fd","2023-11-14T22:35:34.468+00:00","2025-01-21T23:56:16.675+00:00",[],"Control-of-the-oocyte-to-embryo-transition-by-the-ubiquitin-proteolytic-system-in-mouse-and-C-elegans",{"pii":794,"abstract":796,"title":798,"doi":800},{"VOID":795},"S0955067410001596",{"EN":797},"In metazoans the oocyte-to-embryo transition occurs in the absence of mRNA transcription and relies entirely on maternally provided mRNA and proteins. We review here recent findings illustrating the importance of degradation of key proteins allowing essential cell cycle transitions as well as important remodelling of the oocyte to produce a totipotent zygote. By following the chronological order of events, we update recent discoveries on the instrumental role of the cullin-RING and APC\u002FC ubiquitin-ligases in promoting meiosis resumption and the oocyte-to-embryo transition.",{"EN":799},"Control of the oocyte-to-embryo transition by the ubiquitin–proteolytic system in mouse and C. elegans",{"VOID":801},"10.1016\u002Fj.ceb.2010.09.003","Author affiliation is blank","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0955067410001596",[805,812,819],{"id":806,"sortIndex":19,"researcher":18,"roles":807,"affiliations":808,"properties":809},"5a8d5e2b-b7b7-4e90-8216-95ec257a9a43",[118],[],{"title":810},{"VI":811},"Terret  Marie-Emilie",{"id":813,"sortIndex":19,"researcher":18,"roles":814,"affiliations":815,"properties":816},"e4fc2897-1f5c-4d76-8f1b-efa450188d20",[118],[],{"title":817},{"VI":818},"Verlhac  Marie-Hélène",{"id":820,"sortIndex":19,"researcher":18,"roles":821,"affiliations":822,"properties":823},"694dceb4-9417-40ca-9e6d-4f1b89cb4010",[118],[],{"title":824},{"VI":825},"Pintard  Lionel",{"url":803,"publisher":827,"properties":849},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":828,"slug":10,"properties":829,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":832,"manageAffiliations":833,"indexDatabases":834,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":830,"title":831},{"VOID":13},{"EN":15},[],[],[835,842],{"id":55,"indexDatabase":836,"url":70,"indexYears":18,"academicFieldIds":841,"indexDatabaseRanking":18},{"id":57,"createTime":58,"updateTime":59,"relativeEntities":837,"label":838,"description":839,"key":66,"publicationTags":840,"standard":18},[],{"EN":62,"VI":62},{"VI":64,"EN":65},[68,69],[72],{"id":74,"indexDatabase":843,"url":87,"indexYears":88,"academicFieldIds":848,"indexDatabaseRanking":91},{"id":76,"createTime":77,"updateTime":78,"relativeEntities":844,"label":845,"description":846,"key":84,"publicationTags":847,"standard":18},[],{"EN":81,"VI":81},{"EN":81,"VI":83},[86],[90],{"volume":850,"pages":851},{"VOID":476},{"VOID":852},"758","2010-12-31",{"id":855,"createTime":856,"updateTime":857,"relativeEntities":858,"slug":859,"properties":860,"entityType":109,"verifyStatus":110,"verifyTime":857,"verifyNote":111,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":867,"fullTextUrl":18,"authors":868,"publicationType":150,"publisherRelationship":933,"citationCount":18,"citationInfo":18,"publishDate":961,"publishYear":962,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":181},"1952a482-8ad9-449f-b110-6b9415bc8ff8","2023-12-11T23:09:40.500+00:00","2025-02-19T23:55:36.132+00:00",[],"Mechanics-of-the-cellular-actin-cortex-From-signalling-to-shape-change",{"references":861,"title":863,"doi":865},{"VOID":862},"Ramanathan, 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involved in mitotic rounding, Nat Commun, 8, 1266, 10.1038\u002Fs41467-017-01147-6\nLi, 2016, The F-actin bundler alpha-actinin Ain1 is tailored for ring assembly and constriction during cytokinesis in fission yeast, Mol Biol Cell, 27, 1821, 10.1091\u002Fmbc.e16-01-0010\nDescovich, 2018, Cross-linkers both drive and brake cytoskeletal remodeling and furrowing in cytokinesis, Mol Biol Cell, 29, 622, 10.1091\u002Fmbc.E17-06-0392\nTerry, 2018, Capping protein regulates actin dynamics during cytokinetic midbody maturation, Proc Natl Acad Sci USA, 115, 2138, 10.1073\u002Fpnas.1722281115\nDurkin, 2017, RhoD inhibits RhoC-ROCK-dependent cell contraction via PAK6, Dev Cell, 41, 315, 10.1016\u002Fj.devcel.2017.04.010\nAoki, 2016, A RhoA and Rnd3 cycle regulates actin reassembly during membrane blebbing, Proc Natl Acad Sci U S A, 113, E1863, 10.1073\u002Fpnas.1600968113\nJiao, 2018, Myosin II-interacting guanine nucleotide exchange factor promotes bleb retraction via stimulating cortex reassembly at the bleb membrane, Mol Biol Cell, 29, 643, 10.1091\u002Fmbc.E17-10-0579\nMichaux, 2018, Excitable RhoA dynamics drive pulsed contractions in the early C. elegans embryo, J Cell Biol, 217, 4230, 10.1083\u002Fjcb.201806161\nRamkumar, 2016, Coupling changes in cell shape to chromosome segregation, Nat Rev Mol Cell Biol, 17, 511, 10.1038\u002Fnrm.2016.75\nMatthews, 2012, Changes in Ect2 localization couple actomyosin-dependent cell shape changes to mitotic progression, Dev Cell, 23, 371, 10.1016\u002Fj.devcel.2012.06.003\nMaddox, 2003, RhoA is required for cortical retraction and rigidity during mitotic cell rounding, J Cell Biol, 160, 255, 10.1083\u002Fjcb.200207130\nFededa, 2012, Molecular control of animal cell cytokinesis, Nat Cell Biol, 14, 440, 10.1038\u002Fncb2482\nZanin, 2013, A conserved RhoGAP limits M phase contractility and coordinates with microtubule asters to confine RhoA during cytokinesis, Dev Cell, 26, 496, 10.1016\u002Fj.devcel.2013.08.005\nKiyomitsu, 2013, Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase, Cell, 154, 391, 10.1016\u002Fj.cell.2013.06.010\nRodrigues, 2015, Kinetochore-localized PP1-Sds22 couples chromosome segregation to polar relaxation, Nature, 524, 489, 10.1038\u002Fnature14496\nAsiedu, 2009, Centrosome\u002Fspindle pole-associated protein regulates cytokinesis via promoting the recruitment of MyoGEF to the central spindle, Mol Biol Cell, 20, 1428, 10.1091\u002Fmbc.e08-01-0001\nMartz, 2013, Leukemia-associated RhoGEF (LARG) is a novel RhoGEF in cytokinesis and required for the proper completion of abscission, Mol Biol Cell, 24, 2785, 10.1091\u002Fmbc.e12-07-0533\nSchiel, 2012, FIP3-endosome-dependent formation of the secondary ingression mediates ESCRT-III recruitment during cytokinesis, Nat Cell Biol, 14, 1068, 10.1038\u002Fncb2577\nWagner, 2016, Local RhoA activation induces cytokinetic furrows independent of spindle position and cell cycle stage, J Cell Biol, 213, 641, 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Cell Mol Neurobiol, 12, 333, 10.1007\u002FBF00734934\nMarcus, 1991, Significance of C-Terminal Cysteine Modifications to the Biological Activity of the Saccharomyces cerevisiae a-Factor Mating Pheromone, Mol Cell Biol, 11, 3603, 10.1128\u002FMCB.11.7.3603\nChelsky, 1989, Lamin B Methylation and Assembly into the Nuclear Envelope, J Biol Chem, 264, 11368, 10.1016\u002FS0021-9258(18)83282-3\nSobotka-Briner, 1992, COOH-Terminal Methylation of Lamin B and Inhibition of Methylation by Farnesylated Peptides Corresponding to Lamin B and Other CAAX Motif Proteins, J Biol Chem, 267, 12122, 10.1016\u002FS0021-9258(19)49813-X\nBacklund, 1992, GTP-Stimulated Carboxyl Methylation of a Soluble Form of the GTP-Binding Protein G25K in Brain, J Biol Chem, 267, 18432, 10.1016\u002FS0021-9258(19)36981-9\nHuzoor-Akbar Winegar, 1991, Carboxyl Methylation of Platelet rapl Proteins is Stimulated by Guanosine 5′-(3-O-thio)triphosphate, J Biol Chem, 266, 4387, 10.1016\u002FS0021-9258(20)64334-4\nPhilips, 1993, 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Biochem Sci, 12, 155, 10.1016\u002F0968-0004(87)90073-9\nGeiger, 1987, Deamidation, Isomerization, and Racemization at Asparaginyl and Aspartyl Residues in Peptides: Succinimide-Linked Reactions that Contribute to Protein Degradation, J Biol Chem, 262, 785, 10.1016\u002FS0021-9258(19)75855-4\nStephenson, 1989, Succinimide Formation from Aspartyl and Asparaginyl Peptides as a Model for the Spontaneous Degradation of Proteins, J Biol Chem, 264, 6164, 10.1016\u002FS0021-9258(18)83327-0\nMcFadden, 1982, Methylation at d-Aspartyl Residues in Erythrocytes: Possible Step in the Repair of Aged Membrane Proteins, 79, 2460\nJohnson, 1987, Partial Repair of Deamidation-Damaged Calmodulin by Protein Carboxyl Methyltransferase, J Biol Chem, 262, 12283, 10.1016\u002FS0021-9258(18)45348-3\nJohnson, 1987, Protein Carboxyl Methyltransferase Facilitates Conversion of Atypical l-Isoaspartyl Peptides to Normal l-Aspartyl Peptides, J Biol Chem, 262, 5622, 10.1016\u002FS0021-9258(18)45619-0\nMcFadden, 1987, Conversion of Isoaspartyl Peptides to Normal Peptides: Implications for the Cellular Repair of Damaged Proteins, 84, 2595\nGalletti, 1988, Repair of Isopeptide Bonds by Protein Carboxyl O-Methyltransferase: Seminal Ribonuclease as a Model System, Biochemistry, 27, 1752, 10.1021\u002Fbi00405a055\nLi, 1992, A Protein Methyltransferase Specific for Altered Aspartyl Residues is Important in Escherichia coli Stationary-Phase Survival and Heat-Shock Resistance, 89, 9885\nLadino, 1992, Methylation of Atypical Protein Aspartyl Residues During the Stress Response of HcLa Cells, J Cell Physiol, 153, 297, 10.1002\u002Fjcp.1041530209\nJohnson, 1993, Accumulation of Substrates for Protein l-Isoaspartyl Methyltransferase in Adenosine Dialdehyde-Treated PC12 Cells, J Biol Chem, 268, 6174, 10.1016\u002FS0021-9258(18)53235-X\nLadino, 1990, Protein Carboxyl Methylation and Methyl Ester Turnover in Density-Fractionated Human Erythrocytes, Mechan Ageing Develop, 55, 123, 10.1016\u002F0047-6374(90)90020-G\nO'Connor, 1988, Enhanced Carboxyl Methylation of Membrane-Associated Hemoglobin in Human Erythrocytes, J Biol Chem, 263, 1380, 10.1016\u002FS0021-9258(19)57315-X\nJohnson, 1991, Protein l-Isoaspartyl Methyltransferase in Postmortem Brains of Aged Humans, Neurobiol Aging, 12, 19, 10.1016\u002F0197-4580(91)90034-H\nOkamoto, 1985, Identification of an Active Site Peptide of Skeletal Myosin After Photoaffinity Labeling with N-(4-Azido-2-Nitrophenyl)-2-Aminoethyl Diphosphate, 82, 1575\nRoberts, 1986, Trimethyllysine and Protein Function: Effect of Methylation and Mutagenesis of Lysine 115 of Calmodulin on NAD Kinase Activation, J Biol Chem, 261, 1491, 10.1016\u002FS0021-9258(17)35963-X\nRoberts, 1992, Expression of a Calmodulin Methylation Mutant Affects the Growth and Development of Transgenic Tobacco Plants, 89, 8394\nWang, 1992, Methylations of 70,000-Da Heat Shock Proteins in 3T3 Cells: Alterations by Arsenite Treatments, by Different Stages of Growth and by Virus Transformation, Arch Biochem Biophys, 297, 169, 10.1016\u002F0003-9861(92)90656-H\nLischwe, 1985, Clustering of Glycine and NG,NG-Dimethylarginine in Nucleolar Protein C23, Biochemistry, 24, 6025, 10.1021\u002Fbi00343a001\nLischwe, 1985, Purification and Partial Characterization of a Nucleolar Scleroderma Antigen (Mr = 34,000; pl, 8.5) Rich in NG,NG-Dimethylarginine, J Biol Chem, 260, 14304, 10.1016\u002FS0021-9258(17)38718-5\nNajbauer, 1993, Peptides with Sequences Similar to Glycine, Arginine-Rich Motifs in Proteins Interacting with RNA Are Efficiently Recognized by Methyltransferase(s) Modifying Arginine in Numerous Proteins, J Biol Chem, 268, 10501, 10.1016\u002FS0021-9258(18)82227-X\nCalnan, 1991, Arginine-Mediated RNA Recognition — The Arginine Fork, Science, 252, 1167, 10.1126\u002Fscience.252.5009.1167\nSolomon, 1987, Studies on the Role of Actin's Ntao-Methylhistidine Using Oligodeoxynucleotide-Directed Site-Specific Mutagenesis, J Viol Chem, 262, 11382, 10.1016\u002FS0021-9258(18)60971-8\nMattheakis, 1992, DPH5, a Methyltransferase Gene Required for Diphthamide Biosynthesis in Saccharomyces cerevisiae, Mol Cell Biol, 12, 4026, 10.1128\u002FMCB.12.9.4026\nPhan, 1993, Saccharromyces cerevisiae Elongation Factor 2. Mutagenesis of the Histidine Precursor of Diphthamide Yields a Functional Protein that is Resistant to Diphtheria Toxin, J Biol Chem, 268, 8665, 10.1016\u002FS0021-9258(18)52926-4\nSwanson, 1990, Phycobiliprotein Methylation: Effect of the γN-Methylasparagine Residue on Energy Transfer in Phycocyanin and the Phycobilisome, J Mol Biol, 214, 787, 10.1016\u002F0022-2836(90)90293-U\nIngrosso, 1989, Sequence of the d-Aspartyl\u002Fl-Isoaspartyl Protein Methyltransferase from Human Erythrocytes: Common Sequence Motifs for Protein, DNA, RNA, and Small. Molecule S-Adenosylmethionine-Dependent Methyltransferases, J Biol Chem, 264, 20131, 10.1016\u002FS0021-9258(19)47228-1\nThomas, 1993, Post-Translational Methylation of Phycobilisomes and Oxygen Evolution Efficiency in Cyanobacteria, Biochim Biophys Acta, 1143, 104, 10.1016\u002F0005-2728(93)90222-2\nLee, 1993, Protein Phosphatase 2A Catalytic Subunit Is Methylesterified at its Carboxyl Terminus By a Novel Methyltransferase, J Biol Chem, 268, 19192, 10.1016\u002FS0021-9258(19)36497-X\nXie, 1993, Protein Phosphatase 2A Is Reversibly Modified by Methyl Esterification at its C-Terminal Leucine Residue in Bovine Brain, J Biol Chem",{"EN":973},"Protein 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The minimal cadherin-catenin complex binds to actin filaments under force, Science, 346, 1254211, 10.1126\u002Fscience.1254211\nDupont, 2011, Role of YAP\u002FTAZ in mechanotransduction, Nature, 474, 179, 10.1038\u002Fnature10137\nWada, 2011, Hippo pathway regulation by cell morphology and stress fibers, Development, 138, 3907, 10.1242\u002Fdev.070987\nSkamagki, 2013, Asymmetric localization of Cdx2 mRNA during the first cell-fate decision in early mouse development, Cell Rep, 3, 442, 10.1016\u002Fj.celrep.2013.01.006\nRossi, 2015, Genetic compensation induced by deleterious mutations but not gene knockdowns, Nature, 524, 230, 10.1038\u002Fnature14580\nShahbazi, 2016, Self-organization of the human embryo in the absence of maternal tissues, Nat Cell Biol, 18, 700, 10.1038\u002Fncb3347\nDeglincerti, 2016, Self-organization of the in vitro attached human embryo, Nature, 533, 251, 10.1038\u002Fnature17948",{"EN":1035},"How cells change shape and position in the early mammalian embryo",{"VOID":1037},"10.1016\u002Fj.ceb.2016.11.002","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0955067416302149",[1040,1055,1068,1080],{"id":1041,"sortIndex":888,"researcher":18,"roles":1042,"affiliations":1043,"properties":1052},"0ec2c99e-49c3-41da-a63c-1cb4e7240cf2",[118],[1044],{"id":18,"sortIndex":19,"affiliation":1045,"properties":18},{"id":1046,"createTime":1047,"updateTime":1047,"relativeEntities":1048,"slug":18,"properties":1049,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"72c1964d-ca82-4541-b60d-d482cd8bd2da","2024-02-09T14:52:49.441+00:00",[],{"title":1050},{"VI":1051},"Institute of Molecular and Cell Biology, A*STAR, 61 Biopolis Drive, Singapore 138673, Singapore",{"title":1053},{"VI":1054},"Stephanie Bissiere",{"id":1056,"sortIndex":1057,"researcher":18,"roles":1058,"affiliations":1059,"properties":1065},"9510f16c-dc6e-4a38-9a90-bda3cdaea154",3,[118],[1060],{"id":18,"sortIndex":19,"affiliation":1061,"properties":18},{"id":1046,"createTime":1047,"updateTime":1047,"relativeEntities":1062,"slug":18,"properties":1063,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1064},{"VI":1051},{"title":1066},{"VI":1067},"Nicolas Plachta",{"id":1069,"sortIndex":116,"researcher":18,"roles":1070,"affiliations":1071,"properties":1077},"25cec458-6b7c-40ea-b4ff-6a1d7ae4ab25",[118],[1072],{"id":18,"sortIndex":19,"affiliation":1073,"properties":18},{"id":1046,"createTime":1047,"updateTime":1047,"relativeEntities":1074,"slug":18,"properties":1075,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1076},{"VI":1051},{"title":1078},{"VI":1079},"Jennifer Zenker",{"id":1081,"sortIndex":19,"researcher":18,"roles":1082,"affiliations":1083,"properties":1089},"ed1983f4-4276-4f16-827b-0ff566d5d063",[118],[1084],{"id":18,"sortIndex":19,"affiliation":1085,"properties":18},{"id":1046,"createTime":1047,"updateTime":1047,"relativeEntities":1086,"slug":18,"properties":1087,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1088},{"VI":1051},{"title":1090},{"VI":1091},"Melanie D White",{"url":1038,"publisher":1093,"properties":1115},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1094,"slug":10,"properties":1095,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1098,"manageAffiliations":1099,"indexDatabases":1100,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1096,"title":1097},{"VOID":13},{"EN":15},[],[],[1101,1108],{"id":55,"indexDatabase":1102,"url":70,"indexYears":18,"academicFieldIds":1107,"indexDatabaseRanking":18},{"id":57,"createTime":58,"updateTime":59,"relativeEntities":1103,"label":1104,"description":1105,"key":66,"publicationTags":1106,"standard":18},[],{"EN":62,"VI":62},{"VI":64,"EN":65},[68,69],[72],{"id":74,"indexDatabase":1109,"url":87,"indexYears":88,"academicFieldIds":1114,"indexDatabaseRanking":91},{"id":76,"createTime":77,"updateTime":78,"relativeEntities":1110,"label":1111,"description":1112,"key":84,"publicationTags":1113,"standard":18},[],{"EN":81,"VI":81},{"EN":81,"VI":83},[86],[90],{"volume":1116,"pages":1118},{"VOID":1117},"44",{"VOID":1119},"7-13","2017-02-01",2017]