Interaction of enteropathogenic Escherichia coli with human intestinal mucosa: role of effector proteins in brush border remodeling and formation of attaching and effacing lesions
10.1128/iai.73.2.1243-1251.2005 · doi-reference
Entamoeba histolytica EhCP112 dislocates and degrades claudin-1 and claudin-2 at tight junctions of the intestinal epithelium
10.3389/fcimb.2017.00372 · doi-reference
Epithelial cells expressing EhADH, an entamoeba histolytica adhesin, exhibit increased tight junction proteins
10.3389/fcimb.2018.00340 · doi-reference
CagA-ASPP2 complex mediates loss of cell polarity and favors H. pylori colonization of human gastric organoids
10.1073/pnas.1908787117 · doi-reference
Helicobacter pylori CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity
10.1038/nature05765 · doi-reference
Disruption of the epithelial apical-junctional complex by Helicobacter pylori CagA
10.1126/science.1081919 · doi-reference
Enteropathogenic Escherichia coli (EPEC) recruitment of PAR polarity protein atypical PKCζ to pedestals and cell-cell contacts precedes disruption of tight junctions in intestinal epithelial cells
10.3390/ijms21020527 · doi-reference
aPKC: the kinase that phosphorylates cell polarity
10.12688/f1000research.14427.1 · doi-reference
The PAR-aPKC system: lessons in polarity
10.1242/jcs.02898 · doi-reference
Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion
10.1053/gast.2002.36002 · doi-reference
Helicobacter pylori dysregulation of gastric epithelial tight junctions by urease-mediated myosin II activation
10.1053/j.gastro.2008.10.011 · doi-reference
Helicobacter pylori activates myosin light-chain kinase to disrupt claudin-4 and claudin-5 and increase epithelial permeability
10.1128/iai.73.12.7844-7852.2005 · doi-reference
Enteropathogenic Escherichia coli-induced myosin light chain phosphorylation alters intestinal epithelial permeability
10.1016/s0016-5085(97)70006-4 · doi-reference
Listeria adhesion protein induces intestinal epithelial barrier dysfunction for bacterial translocation
10.1016/j.chom.2018.03.004 · doi-reference
Tight junctions as targets and effectors of mucosal immune homeostasis
10.1016/j.jcmgh.2020.04.001 · doi-reference
Myosin light chain phosphorylation regulates barrier function by remodeling tight junction structure
10.1242/jcs.02915 · doi-reference
Epithelial myosin light chain kinase-dependent barrier dysfunction mediates T cell activation-induced diarrhea in vivo
10.1172/jci24970 · doi-reference
A protein kinase A-dependent mechanism by which rotavirus affects the distribution and mRNA level of the functional tight junction-associated protein, occludin, in human differentiated intestinal Caco-2 cells
10.1128/jvi.00263-07 · doi-reference
Rotavirus-induced early activation of the RhoA/ROCK/MLC signaling pathway mediates the disruption of tight junctions in polarized MDCK cells
10.1038/s41598-018-32352-y · doi-reference
The rotavirus surface protein VP8 modulates the gate and fence function of tight junctions in epithelial cells
10.1242/jcs.01425 · doi-reference
The tight junction protein JAM-A functions as coreceptor for rotavirus entry into MA104 cells
10.1016/j.virol.2014.11.016 · doi-reference
Elucidating pathways of Toxoplasma gondii invasion in the gastrointestinal tract: involvement of the tight junction protein occludin
10.1016/j.micinf.2015.07.001 · doi-reference
The coxsackievirus and adenovirus receptor, a required host factor for recovirus infection, is a putative enteric calicivirus receptor
10.1128/jvi.00869-19 · doi-reference
Coxsackievirus entry across epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5
10.1016/j.chom.2007.07.003 · doi-reference
Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions
10.1016/j.cell.2005.10.035 · doi-reference
The coxsackie-adenovirus receptor (CAR) is used by reference strains and clinical isolates representing all six serotypes of coxsackievirus group B and by swine vesicular disease virus
10.1006/viro.2000.0324 · doi-reference
Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5
10.1126/science.275.5304.1320 · doi-reference
The coxsackie- and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis
10.1016/j.yexcr.2006.01.025 · doi-reference
The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction
10.1073/pnas.261452898 · doi-reference
Tight junctions: from simple barriers to multifunctional molecular gates
10.1038/nrm.2016.80 · doi-reference
Signalling to and from tight junctions
10.1038/nrm1055 · doi-reference
Differential response to the course of Cryptosporidium parvum infection and its impact on epithelial integrity in differentiated versus undifferentiated human intestinal enteroids
10.1128/iai.00397-22 · doi-reference
Infection of human and bovine epithelial cells with Cryptosporidium andersoni induces apoptosis and disrupts tight junctional ZO-1: effects of epidermal growth factor
10.1016/s0020-7519(03)00138-3 · doi-reference
Cryptosporidium parvum infection of Caco-2 cell monolayers induces an apical monolayer defect, selectively increases transmonolayer permeability, and causes epithelial cell death
10.1128/iai.62.10.4506-4514.1994 · doi-reference
Tight junction protein occludin is an internalization factor for SARS-CoV-2 infection and mediates virus cell-to-cell transmission
10.1073/pnas.2218623120 · doi-reference
Epithelial junctions and Rho family GTPases: the zonular signalosome
10.4161/21541248.2014.973760 · doi-reference
Rac1, but not RhoA, signaling protects epithelial adherens junction assembly during ATP depletion
10.1152/ajpcell.00604.2001 · doi-reference
Salmonella enterica serovar Typhimurium effectors SopB, SopE, SopE2 and SipA disrupt tight junction structure and function
10.1111/j.1462-5822.2006.00762.x · doi-reference
SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell
10.1074/jbc.m100609200 · doi-reference
Citrobacter rodentium infection causes both mitochondrial dysfunction and intestinal epithelial barrier disruption in vivo: role of mitochondrial associated protein (Map)
10.1111/j.1462-5822.2006.00741.x · doi-reference
