Differential pathways of claudin oligomerization and integration into tight junctions

References

• Tsukita S, Furuse M, Itoh M. Multifunctional strands in tight junctions. Nat Rev Mol Cell Biol 2001; 2:285 - 93; http://dx.doi.org/10.1038/35067088; PMID: 11283726
   PubMed Web of Science ®Google Scholar
• Anderson JM, Van Itallie CM. Physiology and function of the tight junction. Cold Spring Harb Perspect Biol 2009; 1:a002584; http://dx.doi.org/10.1101/cshperspect.a002584; PMID: 20066090
   PubMed Web of Science ®Google Scholar
• Krause G, Winkler L, Mueller SL, Haseloff RF, Piontek J, Blasig IE. Structure and function of claudins. Biochim Biophys Acta 2008; 1778:631 - 45; http://dx.doi.org/10.1016/j.bbamem.2007.10.018; PMID: 18036336
   PubMed Web of Science ®Google Scholar
• Overgaard CE, Daugherty BL, Mitchell LA, Koval M. Claudins: control of barrier function and regulation in response to oxidant stress. Antioxid Redox Signal 2011; 15:1179 - 93; http://dx.doi.org/10.1089/ars.2011.3893; PMID: 21275791
   PubMed Web of Science ®Google Scholar
• Engelund MB, Yu AS, Li J, Madsen SS, Færgeman NJ, Tipsmark CK. Functional characterization and localization of a gill-specific claudin isoform in Atlantic salmon. Am J Physiol Regul Integr Comp Physiol 2012; 302:R300 - 11; http://dx.doi.org/10.1152/ajpregu.00286.2011; PMID: 21975646
   PubMedGoogle Scholar
• Van Itallie CM, Anderson JM. Claudins and epithelial paracellular transport. Annu Rev Physiol 2006; 68:403 - 29; http://dx.doi.org/10.1146/annurev.physiol.68.040104.131404; PMID: 16460278
   PubMed Web of Science ®Google Scholar
• Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol 1999; 147:1351 - 63; http://dx.doi.org/10.1083/jcb.147.6.1351; PMID: 10601346
   PubMed Web of Science ®Google Scholar
• Poliak S, Matlis S, Ullmer C, Scherer SS, Peles E. Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells. J Cell Biol 2002; 159:361 - 72; http://dx.doi.org/10.1083/jcb.200207050; PMID: 12403818
   PubMed Web of Science ®Google Scholar
• Roh MH, Liu CJ, Laurinec S, Margolis B. The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions. J Biol Chem 2002; 277:27501 - 9; http://dx.doi.org/10.1074/jbc.M201177200; PMID: 12021270
   PubMed Web of Science ®Google Scholar
• Colegio OR, Van Itallie CM, McCrea HJ, Rahner C, Anderson JM. Claudins create charge-selective channels in the paracellular pathway between epithelial cells. Am J Physiol Cell Physiol 2002; 283:C142 - 7; PMID: 12055082
   PubMed Web of Science ®Google Scholar
• Wen H, Watry DD, Marcondes MC, Fox HS. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol Cell Biol 2004; 24:8408 - 17; http://dx.doi.org/10.1128/MCB.24.19.8408-8417.2004; PMID: 15367662
   PubMed Web of Science ®Google Scholar
• Piontek J, Winkler L, Wolburg H, Müller SL, Zuleger N, Piehl C, et al. Formation of tight junction: determinants of homophilic interaction between classic claudins. FASEB J 2008; 22:146 - 58; http://dx.doi.org/10.1096/fj.07-8319com; PMID: 17761522
   PubMed Web of Science ®Google Scholar
• Overgaard CE, Mitchell LA, Koval M. Roles for claudins in alveolar epithelial barrier function. Ann N Y Acad Sci 2012; 1257:167 - 74; http://dx.doi.org/10.1111/j.1749-6632.2012.06545.x; PMID: 22671603
   PubMed Web of Science ®Google Scholar
• Hemler ME. Tetraspanin functions and associated microdomains. Nat Rev Mol Cell Biol 2005; 6:801 - 11; http://dx.doi.org/10.1038/nrm1736; PMID: 16314869
   PubMed Web of Science ®Google Scholar
• Levy S, Shoham T. Protein-protein interactions in the tetraspanin web. Physiology (Bethesda) 2005; 20:218 - 24; http://dx.doi.org/10.1152/physiol.00015.2005; PMID: 16024509
   PubMed Web of Science ®Google Scholar
• Seigneuret M. Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily. Biophys J 2006; 90:212 - 27; http://dx.doi.org/10.1529/biophysj.105.069666; PMID: 16352525
   PubMed Web of Science ®Google Scholar
• Nusrat A, Parkos CA, Verkade P, Foley CS, Liang TW, Innis-Whitehouse W, et al. Tight junctions are membrane microdomains. J Cell Sci 2000; 113:1771 - 81; PMID: 10769208
   PubMed Web of Science ®Google Scholar
• Lambert D, O’Neill CA, Padfield PJ. Methyl-beta-cyclodextrin increases permeability of Caco-2 cell monolayers by displacing specific claudins from cholesterol rich domains associated with tight junctions. Cell Physiol Biochem 2007; 20:495 - 506; http://dx.doi.org/10.1159/000107533; PMID: 17762176
   PubMed Web of Science ®Google Scholar
• Van Itallie CM, Gambling TM, Carson JL, Anderson JM. Palmitoylation of claudins is required for efficient tight-junction localization. J Cell Sci 2005; 118:1427 - 36; http://dx.doi.org/10.1242/jcs.01735; PMID: 15769849
   PubMed Web of Science ®Google Scholar
• Edidin M. The state of lipid rafts: from model membranes to cells. Annu Rev Biophys Biomol Struct 2003; 32:257 - 83; http://dx.doi.org/10.1146/annurev.biophys.32.110601.142439; PMID: 12543707
   PubMedGoogle Scholar
• Kenworthy AK, Edidin M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer. J Cell Biol 1998; 142:69 - 84; http://dx.doi.org/10.1083/jcb.142.1.69; PMID: 9660864
   PubMed Web of Science ®Google Scholar
• Simons K, Sampaio JL. Membrane organization and lipid rafts. Cold Spring Harb Perspect Biol 2011; 3:a004697; http://dx.doi.org/10.1101/cshperspect.a004697; PMID: 21628426
   PubMed Web of Science ®Google Scholar
• Yamazaki Y, Okawa K, Yano T, Tsukita S, Tsukita S. Optimized proteomic analysis on gels of cell-cell adhering junctional membrane proteins. Biochemistry 2008; 47:5378 - 86; http://dx.doi.org/10.1021/bi8002567; PMID: 18416558
   PubMed Web of Science ®Google Scholar
• Evans MJ, von Hahn T, Tscherne DM, Syder AJ, Panis M, Wölk B, et al. Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry. Nature 2007; 446:801 - 5; http://dx.doi.org/10.1038/nature05654; PMID: 17325668
   PubMed Web of Science ®Google Scholar
• Kovalenko OV, Yang XH, Hemler ME. A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9. Mol Cell Proteomics 2007; 6:1855 - 67; http://dx.doi.org/10.1074/mcp.M700183-MCP200; PMID: 17644758
   PubMed Web of Science ®Google Scholar
• Litvinov SV, Velders MP, Bakker HA, Fleuren GJ, Warnaar SO. Ep-CAM: a human epithelial antigen is a homophilic cell-cell adhesion molecule. J Cell Biol. 1994;125(2):437-46. Epub 1994/04/01.
   Google Scholar
• Ladwein M, Pape UF, Schmidt DS, Schnölzer M, Fiedler S, Langbein L, et al. The cell-cell adhesion molecule EpCAM interacts directly with the tight junction protein claudin-7. Exp Cell Res 2005; 309:345 - 57; http://dx.doi.org/10.1016/j.yexcr.2005.06.013; PMID: 16054130
   PubMed Web of Science ®Google Scholar
• Kuhn S, Koch M, Nübel T, Ladwein M, Antolovic D, Klingbeil P, et al. A complex of EpCAM, claudin-7, CD44 variant isoforms, and tetraspanins promotes colorectal cancer progression. Mol Cancer Res 2007; 5:553 - 67; http://dx.doi.org/10.1158/1541-7786.MCR-06-0384; PMID: 17579117
   PubMed Web of Science ®Google Scholar
• Wu CJ, Mannan P, Lu M, Udey MC. Epithelial Cell Adhesion Molecule (EpCAM) Regulates Claudin Dynamics and Tight Junctions. J Biol Chem 2013; http://dx.doi.org/10.1074/jbc.M113.457499; PMID: 23486470
   PubMed Web of Science ®Google Scholar
• Nübel T, Preobraschenski J, Tuncay H, Weiss T, Kuhn S, Ladwein M, et al. Claudin-7 regulates EpCAM-mediated functions in tumor progression. Mol Cancer Res 2009; 7:285 - 99; http://dx.doi.org/10.1158/1541-7786.MCR-08-0200; PMID: 19276185
   PubMed Web of Science ®Google Scholar
• Thuma F, Zöller M. EpCAM-associated claudin-7 supports lymphatic spread and drug resistance in rat pancreatic cancer. Int J Cancer 2013; http://dx.doi.org/10.1002/ijc.28085; PMID: 23390083
   PubMed Web of Science ®Google Scholar
• Lei Z, Maeda T, Tamura A, Nakamura T, Yamazaki Y, Shiratori H, et al. EpCAM contributes to formation of functional tight junction in the intestinal epithelium by recruiting claudin proteins. Dev Biol 2012; 371:136 - 45; http://dx.doi.org/10.1016/j.ydbio.2012.07.005; PMID: 22819673
   PubMed Web of Science ®Google Scholar
• Daugherty BL, Ward C, Smith T, Ritzenthaler JD, Koval M. Regulation of heterotypic claudin compatibility. J Biol Chem 2007; 282:30005 - 13; http://dx.doi.org/10.1074/jbc.M703547200; PMID: 17699514
   PubMed Web of Science ®Google Scholar
• Furuse M, Sasaki H, Tsukita S. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J Cell Biol 1999; 147:891 - 903; http://dx.doi.org/10.1083/jcb.147.4.891; PMID: 10562289
   PubMed Web of Science ®Google Scholar
• Coyne CB, Gambling TM, Boucher RC, Carson JL, Johnson LG. Role of claudin interactions in airway tight junctional permeability. Am J Physiol Lung Cell Mol Physiol 2003; 285:L1166 - 78; PMID: 12909588
   PubMed Web of Science ®Google Scholar
• Blasig IE, Winkler L, Lassowski B, Mueller SL, Zuleger N, Krause E, et al. On the self-association potential of transmembrane tight junction proteins. Cell Mol Life Sci 2006; 63:505 - 14; http://dx.doi.org/10.1007/s00018-005-5472-x; PMID: 16456617
   PubMed Web of Science ®Google Scholar
• Angelow S, Schneeberger EE, Yu AS. Claudin-8 expression in renal epithelial cells augments the paracellular barrier by replacing endogenous claudin-2. J Membr Biol 2007; 215:147 - 59; http://dx.doi.org/10.1007/s00232-007-9014-3; PMID: 17516019
   PubMed Web of Science ®Google Scholar
• Sengoku A, Inai T, Shibata Y. Formation of aberrant TJ strands by overexpression of claudin-15 in MDCK II cells. Histochem Cell Biol 2008; 129:211 - 22; http://dx.doi.org/10.1007/s00418-007-0354-y; PMID: 17989991
   PubMed Web of Science ®Google Scholar
• Nunes FD, Lopez LN, Lin HW, Davies C, Azevedo RB, Gow A, et al. Distinct subdomain organization and molecular composition of a tight junction with adherens junction features. J Cell Sci 2006; 119:4819 - 27; http://dx.doi.org/10.1242/jcs.03233; PMID: 17130295
   PubMed Web of Science ®Google Scholar
• Simon DB, Lu Y, Choate KA, Velazquez H, Al-Sabban E, Praga M, et al. Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption. Science 1999; 285:103 - 6; http://dx.doi.org/10.1126/science.285.5424.103; PMID: 10390358
   PubMed Web of Science ®Google Scholar
• Konrad M, Schaller A, Seelow D, Pandey AV, Waldegger S, Lesslauer A, et al. Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement. Am J Hum Genet 2006; 79:949 - 57; http://dx.doi.org/10.1086/508617; PMID: 17033971
   PubMed Web of Science ®Google Scholar
• Hou J, Renigunta A, Gomes AS, Hou M, Paul DL, Waldegger S, et al. Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium. Proc Natl Acad Sci U S A 2009; 106:15350 - 5; http://dx.doi.org/10.1073/pnas.0907724106; PMID: 19706394
   PubMed Web of Science ®Google Scholar
• Angelow S, Yu AS. Claudins and paracellular transport: an update. Curr Opin Nephrol Hypertens 2007; 16:459 - 64; http://dx.doi.org/10.1097/MNH.0b013e32820ac97d; PMID: 17693762
   PubMed Web of Science ®Google Scholar
• Hou J, Renigunta A, Konrad M, Gomes AS, Schneeberger EE, Paul DL, et al. Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex. J Clin Invest 2008; 118:619 - 28; PMID: 18188451
   PubMed Web of Science ®Google Scholar
• Kausalya PJ, Amasheh S, Günzel D, Wurps H, Müller D, Fromm M, et al. Disease-associated mutations affect intracellular traffic and paracellular Mg2+ transport function of Claudin-16. J Clin Invest 2006; 116:878 - 91; http://dx.doi.org/10.1172/JCI26323; PMID: 16528408
   PubMed Web of Science ®Google Scholar
• Koval M. Claudin Heterogeneity and Control of Lung Tight Junctions. Annu Rev Physiol 2013; 75:551 - 67; http://dx.doi.org/10.1146/annurev-physiol-030212-183809; PMID: 23072447
   PubMed Web of Science ®Google Scholar
• Hou J, Renigunta A, Yang J, Waldegger S. Claudin-4 forms paracellular chloride channel in the kidney and requires claudin-8 for tight junction localization. Proc Natl Acad Sci U S A 2010; 107:18010 - 5; http://dx.doi.org/10.1073/pnas.1009399107; PMID: 20921420
   PubMed Web of Science ®Google Scholar
• Surma MA, Klose C, Simons K. Lipid-dependent protein sorting at the trans-Golgi network. Biochim Biophys Acta 2012; 1821:1059 - 67; http://dx.doi.org/10.1016/j.bbalip.2011.12.008; PMID: 22230596
   PubMed Web of Science ®Google Scholar
• Santos AX, Riezman H. Yeast as a model system for studying lipid homeostasis and function. FEBS Lett 2012; 586:2858 - 67; http://dx.doi.org/10.1016/j.febslet.2012.07.033; PMID: 22824640
   PubMed Web of Science ®Google Scholar
• Raleigh DR, Marchiando AM, Zhang Y, Shen L, Sasaki H, Wang Y, et al. Tight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functions. Mol Biol Cell 2010; 21:1200 - 13; http://dx.doi.org/10.1091/mbc.E09-08-0734; PMID: 20164257
   PubMed Web of Science ®Google Scholar
• Steed E, Rodrigues NT, Balda MS, Matter K. Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family. BMC Cell Biol 2009; 10:95; http://dx.doi.org/10.1186/1471-2121-10-95; PMID: 20028514
   PubMed Web of Science ®Google Scholar
• McCarthy KM, Skare IB, Stankewich MC, Furuse M, Tsukita S, Rogers RA, et al. Occludin is a functional component of the tight junction. J Cell Sci 1996; 109:2287 - 98; PMID: 8886979
   PubMed Web of Science ®Google Scholar
• Singh U, Van Itallie CM, Mitic LL, Anderson JM, McClane BA. CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin. J Biol Chem 2000; 275:18407 - 17; http://dx.doi.org/10.1074/jbc.M001530200; PMID: 10749869
   PubMed Web of Science ®Google Scholar
• Robertson SL, Smedley JG 3rd, Singh U, Chakrabarti G, Van Itallie CM, Anderson JM, et al. Compositional and stoichiometric analysis of Clostridium perfringens enterotoxin complexes in Caco-2 cells and claudin 4 fibroblast transfectants. Cell Microbiol 2007; 9:2734 - 55; http://dx.doi.org/10.1111/j.1462-5822.2007.00994.x; PMID: 17587331
   PubMed Web of Science ®Google Scholar
• Van Itallie CM, Betts L, Smedley JG 3rd, McClane BA, Anderson JM. Structure of the claudin-binding domain of Clostridium perfringens enterotoxin. J Biol Chem 2008; 283:268 - 74; http://dx.doi.org/10.1074/jbc.M708066200; PMID: 17977833
   PubMed Web of Science ®Google Scholar
• Winkler L, Gehring C, Wenzel A, Müller SL, Piehl C, Krause G, et al. Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3. J Biol Chem 2009; 284:18863 - 72; http://dx.doi.org/10.1074/jbc.M109.008623; PMID: 19429681
   PubMed Web of Science ®Google Scholar
• Mitchell LA, Koval M. Specificity of interaction between clostridium perfringens enterotoxin and claudin-family tight junction proteins. Toxins (Basel) 2010; 2:1595 - 611; http://dx.doi.org/10.3390/toxins2071595; PMID: 22069652
   PubMed Web of Science ®Google Scholar
• Mrsny RJ, Brown GT, Gerner-Smidt K, Buret AG, Meddings JB, Quan C, et al. A key claudin extracellular loop domain is critical for epithelial barrier integrity. Am J Pathol 2008; 172:905 - 15; http://dx.doi.org/10.2353/ajpath.2008.070698; PMID: 18349130
   PubMed Web of Science ®Google Scholar
• Van Itallie CM, Mitic LL, Anderson JM. Claudin-2 forms homodimers and is a component of a high molecular weight protein complex. J Biol Chem 2011; 286:3442 - 50; http://dx.doi.org/10.1074/jbc.M110.195578; PMID: 21098027
   PubMed Web of Science ®Google Scholar
• Cording J, Berg J, Kading N, Bellmann C, Tscheik C, Westphal JK, et al. Tight junctions: Claudins regulate the interactions between occludin, tricellulin and marvelD3, which, inversely, modulate claudin oligomerization. J Cell Sci 2012; 126:554 - 64; http://dx.doi.org/10.1242/jcs.114306; PMID: 23203797
   PubMed Web of Science ®Google Scholar
• Ikenouchi J, Furuse M, Furuse K, Sasaki H, Tsukita S, Tsukita S. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J Cell Biol 2005; 171:939 - 45; http://dx.doi.org/10.1083/jcb.200510043; PMID: 16365161
   PubMed Web of Science ®Google Scholar
• Krug SM, Amasheh S, Richter JF, Milatz S, Günzel D, Westphal JK, et al. Tricellulin forms a barrier to macromolecules in tricellular tight junctions without affecting ion permeability. Mol Biol Cell 2009; 20:3713 - 24; http://dx.doi.org/10.1091/mbc.E09-01-0080; PMID: 19535456
   PubMed Web of Science ®Google Scholar
• Shen L, Weber CR, Turner JR. The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J Cell Biol 2008; 181:683 - 95; http://dx.doi.org/10.1083/jcb.200711165; PMID: 18474622
   PubMed Web of Science ®Google Scholar
• Mitic LL, Unger VM, Anderson JM. Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4. Protein Sci 2003; 12:218 - 27; http://dx.doi.org/10.1110/ps.0233903; PMID: 12538885
   PubMed Web of Science ®Google Scholar
• Ellgaard L, Helenius A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 2003; 4:181 - 91; http://dx.doi.org/10.1038/nrm1052; PMID: 12612637
   PubMed Web of Science ®Google Scholar
• Sitia R, Molteni SN. Stress, protein (mis)folding, and signaling: the redox connection. Sci STKE 2004; 2004:pe27; http://dx.doi.org/10.1126/stke.2392004pe27; PMID: 15226511
   PubMedGoogle Scholar
• Maza J, Mateescu M, Das Sarma J, Koval M. Differential oligomerization of endoplasmic reticulum-retained connexin43/connexin32 chimeras. Cell Commun Adhes 2003; 10:319 - 22; PMID: 14681035
   PubMed Web of Science ®Google Scholar
• Das S, Smith TD, Sarma JD, Ritzenthaler JD, Maza J, Kaplan BE, et al. ERp29 restricts Connexin43 oligomerization in the endoplasmic reticulum. Mol Biol Cell 2009; 20:2593 - 604; http://dx.doi.org/10.1091/mbc.E08-07-0790; PMID: 19321666
   PubMed Web of Science ®Google Scholar
• Laird DW. Life cycle of connexins in health and disease. Biochem J 2006; 394:527 - 43; http://dx.doi.org/10.1042/BJ20051922; PMID: 16492141
   PubMed Web of Science ®Google Scholar
• Koval M. Pathways and control of connexin oligomerization. Trends Cell Biol 2006; 16:159 - 66; http://dx.doi.org/10.1016/j.tcb.2006.01.006; PMID: 16490353
   PubMed Web of Science ®Google Scholar
• Das Sarma J, Wang F, Koval M. Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization. J Biol Chem 2002; 277:20911 - 8; http://dx.doi.org/10.1074/jbc.M111498200; PMID: 11929864
   PubMed Web of Science ®Google Scholar
• Gong XQ, Shao Q, Lounsbury CS, Bai D, Laird DW. Functional characterization of a GJA1 frameshift mutation causing oculodentodigital dysplasia and palmoplantar keratoderma. J Biol Chem 2006; 281:31801 - 11; http://dx.doi.org/10.1074/jbc.M605961200; PMID: 16891658
   PubMed Web of Science ®Google Scholar
• Das Sarma J, Kaplan BE, Willemsen D, Koval M. Identification of rab20 as a potential regulator of connexin 43 trafficking. Cell Commun Adhes 2008; 15:65 - 74; http://dx.doi.org/10.1080/15419060802014305; PMID: 18649179
   PubMed Web of Science ®Google Scholar
• Maeda S, Nakagawa S, Suga M, Yamashita E, Oshima A, Fujiyoshi Y, et al. Structure of the connexin 26 gap junction channel at 3.5 A resolution. Nature 2009; 458:597 - 602; http://dx.doi.org/10.1038/nature07869; PMID: 19340074
   PubMed Web of Science ®Google Scholar
• Piontek J, Fritzsche S, Cording J, Richter S, Hartwig J, Walter M, et al. Elucidating the pr. inciples of the molecular organization of heteropolymeric tight junction strands. Cell Mol Life Sci 2011;68:3903-18
   Google Scholar
• Smith TD, Mohankumar A, Minogue PJ, Beyer EC, Berthoud VM, Koval M. Cytoplasmic amino acids within the membrane interface region influence connexin oligomerization. J Membr Biol 2012; 245:221 - 30; http://dx.doi.org/10.1007/s00232-012-9443-5; PMID: 22722762
   PubMed Web of Science ®Google Scholar
• Kaufmann R, Piontek J, Grüll F, Kirchgessner M, Rossa J, Wolburg H, et al. Visualization and quantitative analysis of reconstituted tight junctions using localization microscopy. PLoS One 2012; 7:e31128; http://dx.doi.org/10.1371/journal.pone.0031128; PMID: 22319608
   PubMed Web of Science ®Google Scholar