On the public citation graph
Afadin (AF6) in cancer progression: A multidomain scaffold protein with complex and contradictory roles
0 signed · 163 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/ijc.27371openalex-snapshot
Validation of an immunohistochemical signature predictive of 8‐year outcome for patients with breast carcinoma
inferredcites →https://doi.org/10.1002/jcp.20853openalex-snapshot
AF6/s‐afadin is a dual residency protein and localizes to a novel subnuclear compartment
inferredcites →https://doi.org/10.1002/jmr.1042openalex-snapshot
The interaction of Jagged‐1 cytoplasmic tail with afadin PDZ domain is local, folding‐independent, and tuned by phosphorylation
inferredcites →https://doi.org/10.1006/abbi.1999.1448openalex-snapshot
Biochemical Characterization of the Ras-Related GTPases Rit and Rin
inferredcites →https://doi.org/10.1006/bbrc.1999.0731openalex-snapshot
In VivoInteraction of AF-6 with Activated Ras and ZO-1
inferredcites →https://doi.org/10.1007/s004410050062openalex-snapshot
The Canoe protein is necessary in adherens junctions for development of ommatidial architecture in the Drosophila compound eye
inferredcites →https://doi.org/10.1007/s11010-017-3221-8openalex-snapshot
CLDN6 enhances chemoresistance to ADM via AF-6/ERKs pathway in TNBC cell line MDAMB231
inferredcites →https://doi.org/10.1007/s12307-011-0085-4openalex-snapshot
Partial Mesenchymal to Epithelial Reverting Transition in Breast and Prostate Cancer Metastases
inferredcites →https://doi.org/10.1007/s40139-016-0106-6openalex-snapshot
Tight Junctions and the Tumor Microenvironment
inferredcites →https://doi.org/10.1016/b978-0-12-394311-8.00019-4openalex-snapshot
Afadin/AF-6 and Canoe
inferredcites →https://doi.org/10.1016/j.bbamcr.2006.10.001openalex-snapshot
Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance
inferredcites →https://doi.org/10.1016/j.bbamcr.2013.12.013openalex-snapshot
Disrupted interaction between CFTR and AF-6/afadin aggravates malignant phenotypes of colon cancer
inferredcites →https://doi.org/10.1016/j.bbamem.2007.07.012openalex-snapshot
Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton
inferredcites →https://doi.org/10.1016/j.bbamem.2007.12.015openalex-snapshot
Molecular components of the adherens junction
inferredcites →https://doi.org/10.1016/j.bbamem.2020.183399openalex-snapshot
Scaffolding proteins of vertebrate apical junctions: structure, functions and biophysics
inferredcites →https://doi.org/10.1016/j.ceb.2005.08.003openalex-snapshot
Mammalian tight junctions in the regulation of epithelial differentiation and proliferation
inferredcites →https://doi.org/10.1016/j.cell.2005.09.020openalex-snapshot
Deconstructing the Cadherin-Catenin-Actin Complex
inferredcites →https://doi.org/10.1016/j.celrep.2018.10.088openalex-snapshot
A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to Promote α-Toxin Cytotoxicity
inferredcites →https://doi.org/10.1016/j.cub.2004.07.051openalex-snapshot
Proteomic, Functional, and Domain-Based Analysis of In Vivo 14-3-3 Binding Proteins Involved in Cytoskeletal Regulation and Cellular Organization
inferredcites →https://doi.org/10.1016/j.cub.2012.08.024openalex-snapshot
A Genome-wide Functional Screen Shows MAGI-1 Is an L1CAM-Dependent Stabilizer of Apical Junctions in C. elegans
inferredcites →https://doi.org/10.1016/j.mcn.2018.06.006openalex-snapshot
Involvement of l-afadin, but not s-afadin, in the formation of puncta adherentia junctions of hippocampal synapses
inferredcites →https://doi.org/10.1016/j.tcb.2011.06.005openalex-snapshot
Epithelial organization, cell polarity and tumorigenesis
inferredcites →https://doi.org/10.1016/s0014-5793(02)02814-4openalex-snapshot
The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene
inferredcites →https://doi.org/10.1016/s0378-1119(00)00316-4openalex-snapshot
Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadin
inferredcites →https://doi.org/10.1016/s0378-1119(98)00527-7openalex-snapshot
Identification of Ce-AF-6, a novel Caenorhabditis elegans protein, as a putative Ras effector
inferredcites →https://doi.org/10.1016/s0925-4773(98)00151-8openalex-snapshot
Direct binding between two PDZ domain proteins Canoe and ZO-1 and their roles in regulation of the Jun N-terminal kinase pathway in Drosophila morphogenesis
inferredcites →https://doi.org/10.1016/s0960-9822(02)00922-3openalex-snapshot
Nectin Couples Cell-Cell Adhesion and the Actin Scaffold at Heterotypic Testicular Junctions
inferredcites →https://doi.org/10.1016/s0960-9822(99)80392-3openalex-snapshot
Absence of the tight junctional protein AF-6 disrupts epithelial cell–cell junctions and cell polarity during mouse development
inferredcites →https://doi.org/10.1016/s1535-6108(03)00188-0openalex-snapshot
Dimerization contributes to oncogenic activation of MLL chimeras in acute leukemias
inferredcites →https://doi.org/10.1038/78099openalex-snapshot
Ryk-deficient mice exhibit craniofacial defects associated with perturbed Eph receptor crosstalk
inferredcites →https://doi.org/10.1038/ncb2548openalex-snapshot
Classifying collective cancer cell invasion
inferredcites →https://doi.org/10.1038/ncb3478openalex-snapshot
A mechanically active heterotypic E-cadherin/N-cadherin adhesion enables fibroblasts to drive cancer cell invasion
inferredcites →https://doi.org/10.1038/ncomms8184openalex-snapshot
Loss of polarity protein AF6 promotes pancreatic cancer metastasis by inducing Snail expression
inferredcites →https://doi.org/10.1038/nrc1075openalex-snapshot
Tumour-cell invasion and migration: diversity and escape mechanisms
inferredcites →https://doi.org/10.1038/nrm.2016.80openalex-snapshot
Tight junctions: from simple barriers to multifunctional molecular gates
inferredcites →https://doi.org/10.1038/nsmb.2479openalex-snapshot
Dimer asymmetry defines α-catenin interactions
inferredcites →https://doi.org/10.1038/nsmb.3152openalex-snapshot
Concomitant binding of Afadin to LGN and F-actin directs planar spindle orientation
inferredcites →https://doi.org/10.1038/onc.2010.518openalex-snapshot
Claudin-2 is selectively enriched in and promotes the formation of breast cancer liver metastases through engagement of integrin complexes
inferredcites →https://doi.org/10.1038/onc.2011.106openalex-snapshot
Loss of AF6/afadin, a marker of poor outcome in breast cancer, induces cell migration, invasiveness and tumor growth
inferredcites →https://doi.org/10.1038/onc.2016.289openalex-snapshot
The role of claudins in cancer metastasis
inferredcites →https://doi.org/10.1038/s41467-017-01326-5openalex-snapshot
Evolution of AF6-RAS association and its implications in mixed-lineage leukemia
inferredcites →https://doi.org/10.1038/s41467-020-16978-zopenalex-snapshot
mTOR and S6K1 drive polycystic kidney by the control of Afadin-dependent oriented cell division
inferredcites →https://doi.org/10.1038/s41568-019-0213-xopenalex-snapshot
Controversies around epithelial–mesenchymal plasticity in cancer metastasis
inferredcites →https://doi.org/10.1038/sj.emboj.7601706openalex-snapshot
Regulation of c‐Src by binding to the PDZ domain of AF‐6
inferredcites →https://doi.org/10.1038/sj.onc.1201332openalex-snapshot
Chimeric MLL products with a Ras binding cytoplasmic protein AF6 involved in t(6;11) (q27;q23) leukemia localize in the nucleus
inferredcites →https://doi.org/10.1038/sj.onc.1209772openalex-snapshot
Correlated break at PARK2/FRA6E and loss of AF-6/Afadin protein expression are associated with poor outcome in breast cancer
inferredcites →https://doi.org/10.1046/j.1365-2443.1999.00283.xopenalex-snapshot
Similar and differential behaviour between the nectin‐afadin‐ponsin and cadherin‐catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells
inferredcites →https://doi.org/10.1046/j.1365-2443.2003.00616.xopenalex-snapshot
Antagonistic and agonistic effects of an extracellular fragment of nectin on formation of E‐cadherin‐based cell‐cell adhesion
inferredcites →https://doi.org/10.1073/pnas.92.19.8813openalex-snapshot
Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex.
inferredcites →https://doi.org/10.1073/pnas.95.17.9779openalex-snapshot
PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor
inferredcites →https://doi.org/10.1073/pnas.97.16.9064openalex-snapshot
The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin
inferredcites →https://doi.org/10.1074/jbc.271.2.607openalex-snapshot
Identification of AF-6 and Canoe as Putative Targets for Ras
inferredcites →https://doi.org/10.1074/jbc.274.19.13556openalex-snapshot
Thermodynamic and Kinetic Characterization of the Interaction between the Ras Binding Domain of AF6 and Members of the Ras Subfamily
inferredcites →https://doi.org/10.1074/jbc.274.34.23850openalex-snapshot
M-Ras/R-Ras3, a Transforming Ras Protein Regulated by Sos1, GRF1, and p120 Ras GTPase-activating Protein, Interacts with the Putative Ras Effector AF6
inferredcites →https://doi.org/10.1074/jbc.274.43.30914openalex-snapshot
nArgBP2, a Novel Neural Member of Ponsin/ArgBP2/Vinexin Family That Interacts with Synapse-associated Protein 90/Postsynaptic Density-95-associated Protein (SAPAP)
inferredcites →https://doi.org/10.1074/jbc.275.14.10291openalex-snapshot
Nectin-3, a New Member of Immunoglobulin-like Cell Adhesion Molecules That Shows Homophilic and Heterophilic Cell-Cell Adhesion Activities
inferredcites →https://doi.org/10.1074/jbc.m002363200openalex-snapshot
Junctional Adhesion Molecule Interacts with the PDZ Domain-containing Proteins AF-6 and ZO-1
inferredcites →https://doi.org/10.1074/jbc.m103810200openalex-snapshot
Nectin4/PRR4, a New Afadin-associated Member of the Nectin Family That Trans-interacts with Nectin1/PRR1 through V Domain Interaction
inferredcites →https://doi.org/10.1074/jbc.m109.016436openalex-snapshot
Regulation by Afadin of Cyclical Activation and Inactivation of Rap1, Rac1, and RhoA Small G Proteins at Leading Edges of Moving NIH3T3 Cells
inferredcites →https://doi.org/10.1074/jbc.m109.043760openalex-snapshot
Involvement of the Interaction of Afadin with ZO-1 in the Formation of Tight Junctions in Madin-Darby Canine Kidney Cells
inferredcites →https://doi.org/10.1074/jbc.m111.261768openalex-snapshot
Cooperative Role of Nectin-Nectin and Nectin-Afadin Interactions in Formation of Nectin-based Cell-Cell Adhesion
inferredcites →https://doi.org/10.1074/jbc.m111.308858openalex-snapshot
Role of Scaffold Protein Afadin Dilute Domain-interacting Protein (ADIP) in Platelet-derived Growth Factor-induced Cell Movement by Activating Rac Protein through Vav2 Protein
inferredcites →https://doi.org/10.1074/jbc.m113.453464openalex-snapshot
Binding between the Junctional Proteins Afadin and PLEKHA7 and Implication in the Formation of Adherens Junction in Epithelial Cells
inferredcites →https://doi.org/10.1074/jbc.m201463200openalex-snapshot
Biochemical and Structural Definition of the l-Afadin- and Actin-binding Sites of α-Catenin
inferredcites →https://doi.org/10.1074/jbc.m209832200openalex-snapshot
ADIP, a Novel Afadin- and α-Actinin-Binding Protein Localized at Cell-Cell Adherens Junctions
inferredcites →https://doi.org/10.1074/jbc.m211888200openalex-snapshot
AF-6 Controls Integrin-mediated Cell Adhesion by Regulating Rap1 Activation through the Specific Recruitment of Rap1GTP and SPA-1
inferredcites →https://doi.org/10.1074/jbc.m401957200openalex-snapshot
Involvement of LMO7 in the Association of Two Cell-Cell Adhesion Molecules, Nectin and E-cadherin, through Afadin and α-Actinin in Epithelial Cells
inferredcites →https://doi.org/10.1074/jbc.m510070200openalex-snapshot
Regulation of the Assembly and Adhesion Activity of E-cadherin by Nectin and Afadin for the Formation of Adherens Junctions in Madin-Darby Canine Kidney Cells
inferredcites →https://doi.org/10.1074/jbc.m707461200openalex-snapshot
Regulation of Platelet-derived Growth Factor Receptor Activation by Afadin through SHP-2
inferredcites →https://doi.org/10.1074/jbc.rev119.007759openalex-snapshot
Cell adhesion in cancer: Beyond the migration of single cells
inferredcites →https://doi.org/10.1083/jcb.139.2.517openalex-snapshot
Afadin: A Novel Actin Filament–binding Protein with One PDZ Domain Localized at Cadherin-based Cell-to-Cell Adherens Junction
inferredcites →https://doi.org/10.1083/jcb.139.3.785openalex-snapshot
The Ras Target AF-6 Interacts with ZO-1 and Serves as a Peripheral Component of Tight Junctions in Epithelial Cells
inferredcites →https://doi.org/10.1083/jcb.142.4.1053openalex-snapshot
The Ras Target AF-6 is a Substrate of the Fam Deubiquitinating Enzyme
inferredcites →https://doi.org/10.1083/jcb.144.2.361openalex-snapshot
The Junction-associated Protein AF-6 Interacts and Clusters with Specific Eph Receptor Tyrosine Kinases at Specialized Sites of Cell–Cell Contact in the Brain
inferredcites →https://doi.org/10.1083/jcb.144.5.1001openalex-snapshot
Ponsin/SH3P12: An l-Afadin– and Vinculin-binding Protein Localized at Cell–Cell and Cell–Matrix Adherens Junctions
inferredcites →https://doi.org/10.1083/jcb.145.3.539openalex-snapshot
Nectin/PRR: An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin-based Adherens Junctions through Interaction with Afadin, a PDZ Domain–containing Protein
inferredcites →https://doi.org/10.1083/jcb.147.7.1569openalex-snapshot
Cingulin Contains Globular and Coiled-Coil Domains and Interacts with Zo-1, Zo-2, Zo-3, and Myosin
inferredcites →https://doi.org/10.1083/jcb.150.5.1161openalex-snapshot
Two Cell Adhesion Molecules, Nectin and Cadherin, Interact through Their Cytoplasmic Domain–Associated Proteins
inferredcites →https://doi.org/10.1083/jcb.200904001openalex-snapshot
The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction
inferredcites →https://doi.org/10.1083/jcb.201907079openalex-snapshot
Afadin regulates actomyosin organization through αE-catenin at adherens junctions
inferredcites →https://doi.org/10.1083/jcb.201907083openalex-snapshot
Clathrin’s adaptor interaction sites are repurposed to stabilize microtubules during mitosis
inferredcites →https://doi.org/10.1091/mbc.e02-08-0486openalex-snapshot
NZO-3 Expression Causes Global Changes to Actin Cytoskeleton in Madin-Darby Canine Kidney Cells: Linking a Tight Junction Protein to Rho GTPases
inferredcites →https://doi.org/10.1091/mbc.e08-10-1014openalex-snapshot
Junctional Adhesion Molecule A Interacts with Afadin and PDZ-GEF2 to Activate Rap1A, Regulate β1 Integrin Levels, and Enhance Cell Migration
inferredcites →https://doi.org/10.1091/mbc.e12-02-0103openalex-snapshot
R-Ras controls axon branching through afadin in cortical neurons
inferredcites →https://doi.org/10.1091/mbc.e13-06-0298openalex-snapshot
JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function
inferredcites →https://doi.org/10.1093/dnares/5.2.115openalex-snapshot
Complete Genomic Structure, DNA Polymorphisms, and Alternative Splicing of the Human AF-6 Gene
inferredcites →https://doi.org/10.1093/emboj/19.5.843openalex-snapshot
Tumorigenesis in mice with a fusion of the leukaemia oncogene Mll and the bacterial lacZ gene
inferredcites →https://doi.org/10.1093/jb/mvx048openalex-snapshot
ERK signalling as a regulator of cell motility
inferredcites →https://doi.org/10.1093/nar/gky1015openalex-snapshot
COSMIC: the Catalogue Of Somatic Mutations In Cancer
inferredcites →https://doi.org/10.1101/cshperspect.a002899openalex-snapshot
Adherens Junction: Molecular Architecture and Regulation
inferredcites →https://doi.org/10.1101/gad.319194.118openalex-snapshot
Afadin cooperates with Claudin-2 to promote breast cancer metastasis
inferredcites →https://doi.org/10.1101/gad.9.5.612openalex-snapshot
canoe encodes a novel protein containing a GLGF/DHR motif and functions with Notch and scabrous in common developmental pathways in Drosophila.
inferredcites →https://doi.org/10.1111/gtc.12185openalex-snapshot
s‐Afadin binds more preferentially to the cell adhesion molecules nectins than l‐afadin
inferredcites →https://doi.org/10.1111/gtc.12566openalex-snapshot
Requirement of the F‐actin‐binding activity of l‐afadin for enhancing the formation of adherens and tight junctions
inferredcites →https://doi.org/10.1111/j.1460-9568.2011.07947.xopenalex-snapshot
The effector and scaffolding proteins AF6 and MUPP1 interact with connexin36 and localize at gap junctions that form electrical synapses in rodent brain
inferredcites →https://doi.org/10.1111/j.1742-4658.2010.07609.xopenalex-snapshot
Mixed lineage leukemia: a structure–function perspective of the MLL1 protein
inferredcites →https://doi.org/10.1126/science.aaf6546openalex-snapshot
A collective route to metastasis: Seeding by tumor cell clusters
inferredcites →https://doi.org/10.1128/mcb.00299-12openalex-snapshot
Claudin-2 Promotes Breast Cancer Liver Metastasis by Facilitating Tumor Cell Interactions with Hepatocytes
inferredcites →https://doi.org/10.1128/mcb.23.13.4663-4672.2003openalex-snapshot
The Bcr Kinase Downregulates Ras Signaling by Phosphorylating AF-6 and Binding to Its PDZ Domain
inferredcites →https://doi.org/10.1146/annurev.cellbio.24.110707.175339openalex-snapshot
The Immunoglobulin-Like Cell Adhesion Molecule Nectin and Its Associated Protein Afadin
inferredcites →https://doi.org/10.1158/0008-5472.can-13-2381openalex-snapshot
ERKs in Cancer: Friends or Foes?
inferredcites →https://doi.org/10.1158/1541-7786.mcr-13-0398openalex-snapshot
The Adherens Junction Protein Afadin Is an AKT Substrate that Regulates Breast Cancer Cell Migration
inferredcites →https://doi.org/10.1161/atvbaha.118.310991openalex-snapshot
Afadin Facilitates Vascular Endothelial Growth Factor–Induced Network Formation and Migration of Vascular Endothelial Cells by Inactivating Rho-Associated Kinase Through ArhGAP29
inferredcites →https://doi.org/10.1182/blood-2009-09-243386openalex-snapshot
Self-association mediated by the Ras association 1 domain of AF6 activates the oncogenic potential of MLL-AF6
inferredcites →https://doi.org/10.1182/blood-2012-11-465120openalex-snapshot
Leukemic transformation by the MLL-AF6 fusion oncogene requires the H3K79 methyltransferase Dot1l
inferredcites →https://doi.org/10.1182/blood-2013-09-525741openalex-snapshot
MLL-AF6 fusion oncogene sequesters AF6 into the nucleus to trigger RAS activation in myeloid leukemia
inferredcites →https://doi.org/10.1186/1478-811x-8-8openalex-snapshot
PDZ domains and their binding partners: structure, specificity, and modification
inferredcites →https://doi.org/10.1186/s12885-015-1286-xopenalex-snapshot
Loss of AF-6/afadin induces cell invasion, suppresses the formation of glandular structures and might be a predictive marker of resistance to chemotherapy in endometrial cancer
inferredcites →https://doi.org/10.1186/s12935-018-0662-4openalex-snapshot
CLDN2 inhibits the metastasis of osteosarcoma cells via down-regulating the afadin/ERK signaling pathway
inferredcites →https://doi.org/10.1242/dev.087957openalex-snapshot
De novo lumen formation and elongation in the developing nephron: a central role for afadin in apical polarity
inferredcites →https://doi.org/10.1242/dev.189241openalex-snapshot
Disruption of the nectin-afadin complex recapitulates features of the human cleft lip/palate syndrome CLPED1
inferredcites →https://doi.org/10.1242/jcs.00167openalex-snapshot
Nectin and afadin: novel organizers of intercellular junctions
inferredcites →https://doi.org/10.1242/jcs.016634openalex-snapshot
Cell polarity and cancer – cell and tissue polarity as a non-canonical tumor suppressor
inferredcites →https://doi.org/10.1242/jcs.024620openalex-snapshot
Involvement of the nectin-afadin complex in PDGF-induced cell survival
inferredcites →https://doi.org/10.1242/jcs.03027openalex-snapshot
Regulation of epithelial wound closure and intercellular adhesion by interaction of AF6 with actin cytoskeleton
inferredcites →https://doi.org/10.1242/jcs.048439openalex-snapshot
Localization of nectin-free afadin at the leading edge and its involvement in directional cell movement induced by platelet-derived growth factor
inferredcites →https://doi.org/10.1242/jcs.081000openalex-snapshot
Involvement of afadin in barrier function and homeostasis of mouse intestinal epithelia
inferredcites →https://doi.org/10.1242/jcs.129437openalex-snapshot
Drebrin preserves endothelial integrity by stabilizing nectin at adherens junctions
inferredcites →https://doi.org/10.1242/jcs.188169openalex-snapshot
EphA2 proteomics in human keratinocytes reveals a novel association with afadin and epidermal tight junctions
inferredcites →https://doi.org/10.1371/journal.pone.0000066openalex-snapshot
The PDZ Protein Canoe/AF-6 Links Ras-MAPK, Notch and Wingless/Wnt Signaling Pathways by Directly Interacting with Ras, Notch and Dishevelled
inferredcites →https://doi.org/10.1371/journal.pone.0034343openalex-snapshot
Dysregulation of Cell Polarity Proteins Synergize with Oncogenes or the Microenvironment to Induce Invasive Behavior in Epithelial Cells
inferredcites →https://doi.org/10.1371/journal.pone.0080356openalex-snapshot
Genetic Deletion of Afadin Causes Hydrocephalus by Destruction of Adherens Junctions in Radial Glial and Ependymal Cells in the Midbrain
inferredcites →https://doi.org/10.1371/journal.pone.0089763openalex-snapshot
Afadin Regulates Puncta Adherentia Junction Formation and Presynaptic Differentiation in Hippocampal Neurons
inferredcites →https://doi.org/10.1371/journal.pone.0110549openalex-snapshot
Genetic Ablation of Afadin Causes Mislocalization and Deformation of Paneth Cells in the Mouse Small Intestinal Epithelium
inferredcites →https://doi.org/10.1517/14728222.2011.639361openalex-snapshot
The RAS/RAF/MEK/ERK and the PI3K/AKT signalling pathways: role in cancer pathogenesis and implications for therapeutic approaches
inferredcites →https://doi.org/10.15252/embr.201948216openalex-snapshot
Afadin is a scaffold protein repressing insulin action via HDAC6 in adipose tissue
inferredcites →https://doi.org/10.1634/theoncologist.2009-0009openalex-snapshot
The Role of Src in Solid Tumors
inferredcites →https://doi.org/10.3389/fmicb.2018.02712openalex-snapshot
Afadin Downregulation by Helicobacter pylori Induces Epithelial to Mesenchymal Transition in Gastric Cells
inferredcites →https://doi.org/10.3389/fped.2017.00004openalex-snapshot
MLL-Rearranged Leukemias—An Update on Science and Clinical Approaches
inferredcites →https://doi.org/10.3892/ol.2016.5110openalex-snapshot
The Ras/Raf/MEK/ERK signaling pathway and its role in the occurrence and development of HCC
inferredcites →https://doi.org/10.3892/ol.2017.7461openalex-snapshot
PI3K/AKT/Afadin signaling pathway contributes to pathological vascularization in glioblastomas
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4730364openalex-extracted
Transcriptomics and Proteomics Analysis Reveals Damage to the Intestine and Gill Of Larimichthys Crocea Exposed to Iridovirus
inferred← citeshttps://doi.org/10.1002/path.6394openalex-snapshot
Afadin loss induces breast cancer metastasis through destabilisation of E‐cadherin to F‐actin linkage
inferred← citeshttps://doi.org/10.1007/82_2025_333openalex-snapshot
Akt/PKB Functions in Cell Migration and Invasion
inferred← citeshttps://doi.org/10.1007/s12272-026-01598-wopenalex-snapshot
Neuroinflammation and blood–brain barrier disruption in Japanese encephalitis virus infection: mechanisms, therapeutic targets, and intervention strategies
inferred← citeshttps://doi.org/10.1016/bs.acc.2024.11.006openalex-snapshot
Cell-cell junctional proteins in cancer
inferred← citeshttps://doi.org/10.1016/j.celrep.2025.115335openalex-snapshot
Multivalent afadin interaction promotes IDR-mediated condensate formation and junctional separation of epithelial cells
inferred← citeshttps://doi.org/10.1016/j.isci.2025.112658openalex-snapshot
AF6 regulates intestinal IgA via crosstalk between intestinal epithelial cells and immune cells in inflammatory bowel disease
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102426openalex-snapshot
Identification of lysophosphatidic acid in serum as a factor that promotes epithelial apical junctional complex organization
inferred← citeshttps://doi.org/10.1039/d5md00203fopenalex-snapshot
The relationship between cancer risk and cystic fibrosis: the role of CFTR in cell growth and cancer development
inferred← citeshttps://doi.org/10.1080/21688370.2022.2077620openalex-snapshot
Tight junctions: from molecules to gastrointestinal diseases
inferred← citeshttps://doi.org/10.1080/21688370.2022.2133880openalex-snapshot
Trans-Compartmental Regulation of Tight Junction Barrier Function
inferred← citeshttps://doi.org/10.1101/2023.07.04.547654openalex-snapshot
Somatic mutation of Afadin leads to anchorage independent survival and metastatic growth of breast cancer through αE-catenin dependent destabilization of the adherens junction
inferred← citeshttps://doi.org/10.1101/2025.11.14.688534openalex-snapshot
Remodeling of KRAS interactome induced by clinically relevant RAS inhibitors reveals convergent responses and a KRAS-mediated regulation of directional cell migration
inferred← citeshttps://doi.org/10.1111/gtc.12940openalex-snapshot
Stimulatory role of nectin‐4 and p95‐ErbB2 in multilayered T47D cell proliferation
inferred← citeshttps://doi.org/10.1126/sciadv.adu0989openalex-snapshot
Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature
inferred← citeshttps://doi.org/10.1158/0008-5472.can-23-3140openalex-snapshot
AFDN Deficiency Promotes Liver Tropism of Metastatic Colorectal Cancer
inferred← citeshttps://doi.org/10.1186/s12943-022-01498-9openalex-snapshot
The circROBO1/KLF5/FUS feedback loop regulates the liver metastasis of breast cancer by inhibiting the selective autophagy of afadin
inferred← citeshttps://doi.org/10.1186/s12974-024-03266-6openalex-snapshot
Japanese encephalitis virus-induced DNA methylation contributes to blood-brain barrier permeability by modulating tight junction protein expression
inferred← citeshttps://doi.org/10.21037/jtd-23-396openalex-snapshot
Construction of a prognostic model for lung adenocarcinoma based on membrane-tension-related genes
inferred← citeshttps://doi.org/10.2147/ijgm.s459418openalex-snapshot
Identification of PDZD11 as a Potential Biomarker Associated with Immune Infiltration for Diagnosis and Prognosis in Epithelial Ovarian Cancer
inferred← citeshttps://doi.org/10.31579/2768-0487/162openalex-snapshot
Insights into the t (6;11) (q27; q23) translocation in acute leukemia by Cytogenetic & Fluorescence in Situ Hybridization Technique
inferred← citeshttps://doi.org/10.3389/fcell.2022.866200openalex-snapshot
Potential Therapeutic Applications of N-Cadherin Antagonists and Agonists
inferred← citeshttps://doi.org/10.3389/fonc.2024.1320766openalex-snapshot
Antibody-mediated targeting of Claudins in cancer
inferred← citeshttps://doi.org/10.3390/biom14121596openalex-snapshot
Regulation of Vascular Injury and Repair by P21-Activated Kinase 1 and P21-Activated Kinase 2: Therapeutic Potential and Challenges
inferred← citeshttps://doi.org/10.3390/ijms25115601openalex-snapshot
The Basic Requirement of Tight Junction Proteins in Blood-Brain Barrier Function and Their Role in Pathologies
inferred← citeshttps://doi.org/10.64898/2026.05.20.726717openalex-snapshot
Polarity remodeling of ventricular cardiomyocyte precursors during heart morphogenesis is required for ventricular chamber formation
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.