Relevant bibliographies by topics / Claudin-11

Academic literature on the topic 'Claudin-11'

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Published: 4 June 2021
Last updated: 2 February 2022

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Journal articles on the topic "Claudin-11"

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Sedwick, Caitlin. "Claudin 11 stops the leaks." Journal of Cell Biology 183, no. 5 (December 1, 2008): 752. http://dx.doi.org/10.1083/jcb.1835iti1.

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Kaitu’u-Lino, Tu’uhevaha J., Pavel Sluka, Caroline F. H. Foo, and Peter G. Stanton. "Claudin-11 expression and localisation is regulated by androgens in rat Sertoli cells in vitro." Reproduction 133, no. 6 (June 2007): 1169–79. http://dx.doi.org/10.1530/rep-06-0385.

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Claudin-11 and occludin are protein components in tight junctions (TJs) between Sertoli cells which are important for the maintenance of the blood–testis barrier. Barrier formation occurs during puberty, with evidence suggesting hormonal regulation of both claudin-11 and occludin. This study aimed to investigate the regulation of claudin-11 and occludin mRNA expression by testosterone (T) and FSH and their immunolocalisation at rat Sertoli cell TJsin vitro, and to correlate any steroid regulation with the functional capacity of TJs. Sertoli cells formed functional TJs within 3 days as assessed by transepithelial electrical resistance (TER). Both T and dihydrotestosterone significantly (P< 0.01) increased TER twofold and claudin-11 mRNA two- to threefold within 3 days. FSH partially stimulated TER and claudin-11 mRNA, but estradiol had no effect. T also promoted claudin-11 localisation into extensive intercellular contacts. In contrast to claudin-11, Tand FSH did not change occludin mRNA expression, however, T promoted localisation of occludin at cell contacts in a similar manner to claudin-11. Addition of flutamide to T-stimulated cells caused a twofold decrease in both TER and claudin-11 mRNA expression, and resulted in the loss of both proteins from cell contacts. This effect was reversible following flutamide removal. It is concluded that androgens i) co-regulate claudin-11 mRNA expression and TER, implicating claudin-11 in TJ formation and ii) promote the localisation of claudin-11 and occludin at Sertoli cell contacts. Hence, the ability of androgens to maintain spermatogenesisin vivois partly via their effects on TJ proteins and regulation of the blood–testis barrier.
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Horné, Fabian, Raimund Dietze, Eniko Berkes, Frank Oehmke, Hans-Rudolf Tinneberg, Ivo Meinhold-Heerlein, and Lutz Konrad. "Impaired Localization of Claudin-11 in Endometriotic Epithelial Cells Compared to Endometrial Cells." Reproductive Sciences 26, no. 9 (December 4, 2018): 1181–92. http://dx.doi.org/10.1177/1933719118811643.

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Claudins are the major components of tight junctions and are often deregulated in human cancer, permitting escape of cancer cells along with the acquisition of invasive properties. Similarly, endometrial cells also show invasive capabilities; however, the role of tight junctions in endometriosis has only rarely been examined. In this study, we analyzed the protein expression and localization of claudin-7 and claudin-11 in human eutopic and ectopic endometrium and endometrial cell lines. We identified claudin-7 primarily at the basolateral junctions of the glandular epithelial cells in eutopic endometrium as well as in the ectopic lesions in nearly all glands and cysts. Quantification of claudin-7 localization by HSCORE showed a slight increase in peritoneal and deep infiltrating endometriosis (DIE) compared to eutopic endometrium. In contrast, claudin-11 was localized mainly in the apicolateral junctions in nearly all glandular epithelial cells of the eutopic endometrium. Interestingly, we observed a deregulation of claudin-11 localization to a basal or basolateral localization in ovarian ( P < .001), peritoneal ( P < .01), and DIE ( P < .05) and a moderately decreased abundance in ovarian endometriosis. In endometrial cell lines, claudin-7 was only present in epithelial Ishikawa cells, and silencing by small-interfering RNA increased cell invasiveness. In contrast, claudin-11 could be demonstrated in Ishikawa and endometriotic 12Z and 49Z cells. Silencing of claudin-11 decreased invasiveness of 12Z slightly but significantly in 49Z. We suggest that although claudin-7 and claudin-11 can be found in nearly all eutopic and ectopic epithelial cells, the impaired localization of claudin-11 in ectopic endometrium might contribute to the pathogenesis of endometriosis.
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Bronstein, J. M., K. Chen, S. Tiwari-Woodruff, and H. I. Kornblum. "Developmental expression of OSP/claudin-11." Journal of Neuroscience Research 60, no. 3 (May 1, 2000): 284–90. http://dx.doi.org/10.1002/(sici)1097-4547(20000501)60:3<284::aid-jnr2>3.0.co;2-t.

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Tiwari-Woodruff, Seema K., Alex G. Buznikov, Trung Q. Vu, Paul E. Micevych, Kendall Chen, Harley I. Kornblum, and Jeff M. Bronstein. "Osp/Claudin-11 Forms a Complex with a Novel Member of the Tetraspanin Super Family and β1 Integrin and Regulates Proliferation and Migration of Oligodendrocytes." Journal of Cell Biology 153, no. 2 (April 16, 2001): 295–306. http://dx.doi.org/10.1083/jcb.153.2.295.

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Oligodendrocyte-specific protein (OSP)/claudin-11 is a major component of central nervous system myelin and forms tight junctions (TJs) within myelin sheaths. TJs are essential for forming a paracellular barrier and have been implicated in the regulation of growth and differentiation via signal transduction pathways. We have identified an OSP/claudin-11–associated protein (OAP)1, using a yeast two-hybrid screen. OAP-1 is a novel member of the tetraspanin superfamily, and it is widely expressed in several cell types, including oligodendrocytes. OAP-1, OSP/claudin-11, and β1 integrin form a complex as indicated by coimmunoprecipitation and confocal immunocytochemistry. Overexpression of OSP/claudin-11 or OAP-1 induced proliferation in an oligodendrocyte cell line. Anti–OAP-1, anti–OSP/claudin-11, and anti–β1 integrin antibodies inhibited migration of primary oligodendrocytes, and migration was impaired in OSP/claudin-11–deficient primary oligodendrocytes. These data suggest a role for OSP/claudin-11, OAP-1, and β1 integrin complex in regulating proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair.
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Morita, Kazumasa, Hiroyuki Sasaki, Kazushi Fujimoto, Mikio Furuse, and Shoichiro Tsukita. "Claudin-11/OSP-based Tight Junctions of Myelin Sheaths in Brain and Sertoli Cells in Testis." Journal of Cell Biology 145, no. 3 (May 3, 1999): 579–88. http://dx.doi.org/10.1083/jcb.145.3.579.

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Members of the newly identified claudin gene family constitute tight junction (TJ) strands, which play a pivotal role in compartmentalization in multicellular organisms. We identified oligodendrocyte-specific protein (OSP) as claudin-11, a new claudin family member, due to its sequence similarity to claudins as well as its ability to form TJ strands in transfected fibroblasts. Claudin-11/OSP mRNA was expressed in the brain and testis. Immunofluorescence microscopy with anti–claudin-11/OSP polyclonal antibody (pAb) and anti-neurofilament mAb revealed that in the brain claudin-11/OSP-positive linear structures run in a gentle spiral around neurofilament-positive axons. At the electron microscopic level, these linear structures were identified as the so-called interlamellar strands in myelin sheaths of oligodendrocytes. In testis, well-developed TJ strands of Sertoli cells were specifically labeled with anti–claudin-11/OSP pAb both at immunofluorescence and electron microscopic levels. These findings indicated that the interlamellar strands of oligodendrocyte myelin sheaths can be regarded as a variant of TJ strands found in many other epithelial cells, and that these strands share a specific claudin species, claudin-11/OSP, with those in Sertoli cells to create and maintain the repeated compartments around axons by oligodendrocytes.
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Florin, Anne, Magali Maire, Aline Bozec, Ali Hellani, Sonia Chater, Remi Bars, Franck Chuzel, and Mohamed Benahmed. "Androgens and Postmeiotic Germ Cells Regulate Claudin-11 Expression in Rat Sertoli Cells." Endocrinology 146, no. 3 (March 1, 2005): 1532–40. http://dx.doi.org/10.1210/en.2004-0834.

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In the present study we investigated whether fetal exposure to flutamide affected messenger and protein levels of claudin-11, a key Sertoli cell factor in the establishment of the hemotesticular barrier, at the time of two key events of postnatal testis development: 1) before puberty (postnatal d 14) during the establishment of the hemotesticular barrier, and 2) at the adult age (postnatal d 90) at the time of full spermatogenesis. The data obtained show that claudin-11 expression was inhibited in prepubertal rat testes exposed in utero to 2 and 10 mg/kg·d flutamide. However, in adult testes, the inhibition was observed only with 2, and not with 10, mg/kg·d of the antiandrogen. It is shown here that these differences between prepubertal and adult testes could be related to dual and opposed regulation of claudin-11 expression resulting from positive control by androgens and an inhibitory effect of postmeiotic germ cells. Indeed, testosterone is shown to stimulate claudin-11 expression in cultured Sertoli cells in a dose- and time-dependent manner (maximum effect with 0.06 μm after 72 h of treatment). In contrast, postmeiotic germ cells potentially exert a negative effect on claudin-11 expression, because adult rat testes depleted in spermatids (after local irradiation) displayed increased claudin-11 expression, whereas in a model of cocultured Sertoli and germ cells, spermatids, but not spermatocytes, inhibited claudin-11 expression. The apparent absence of claudin-11 expression changes in adult rat testes exposed to 10 mg/kg·d flutamide therefore could result from the antagonistic effects of 1) the inhibitory action of the antiandrogen and 2) the stimulatory effect of the apoptotic germ cells on claudin-11 expression. Together, due to the key role of claudin-11 in the hemotesticular barrier, the present findings suggest that such regulatory mechanisms may potentially affect this barrier (re)modeling during spermatogenesis.
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McCabe, M. J., and P. G. Stanton. "116. Contribution of claudin-11 to the inter-Sertoli cell tight junction, in vitro." Reproduction, Fertility and Development 17, no. 9 (2005): 72. http://dx.doi.org/10.1071/srb05abs116.

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The inter-Sertoli cell tight junction (TJ) forms the blood testis barrier (BTB) between Sertoli cells and is composed of three major transmembrane proteins: claudin-11, occludin and junctional adhesion molecule. Formation of the BTB occurs during puberty associating with an increase in circulating gonadotrophins. Claudin-11 and occludin are hormonally regulated in vitro although their importance to the function of the TJ is unknown. The aim of this study was to investigate the contribution of claudin-11 to the inter-Sertoli cell TJ in vitro by blocking gene expression using RNA interference. Two claudin-11-specific siRNA fragments were designed for this purpose. Sertoli cells in primary culture formed stable TJs within 5 days as measured by transepithelial electrical resistance (TER). The addition of siRNA for 2 days resulted in a significant (P < 0.01) 55% (mean, SD, n = 4 cultures) decrease in TER along with a major reduction in claudin-11 localisation to the TJ as assessed by immunocytochemistry. The specificity of the siRNA was shown by the presence of extensive immunostaining of occludin and of the adherens junction protein β-catenin in the same treatments. Similarly, claudin-11 mRNA expression significantly (P < 0.01) decreased by 71% (mean, SD, n = 3 cultures) in response to both claudin-11 siRNA fragments. Occludin mRNA expression was not affected. It is concluded that claudin-11 contributes at least 55% to the function of the rat Sertoli cell TJ in vitro. It is hypothesised that the remaining 45% of TJ function can be attributed to other integral proteins, such as occludin and junctional adhesion molecule. It is expected that claudin-11 and other TJ proteins play a pivotal role in the function of the BTB in vivo with potential implications in fertility and contraception.
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Kiuchi-Saishin, Yumiko, Shimpei Gotoh, Mikio Furuse, Akiko Takasuga, Yasuo Tano, and Shoichiro Tsukita. "Differential Expression Patterns of Claudins, Tight Junction Membrane Proteins, in Mouse Nephron Segments." Journal of the American Society of Nephrology 13, no. 4 (April 2002): 875–86. http://dx.doi.org/10.1681/asn.v134875.

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ABSTRACT. As the first step in understanding the physiologic functions of claudins (tight junction integral membrane proteins) in nephrons, the expression of claudin-1 to -16 in mouse kidneys was examined by Northern blotting. Among these claudins, only claudin-6, -9, -13, and -14 were not detectable. Claudin-5 and -15 were detected only in endothelial cells. Polyclonal antibodies specific for claudin-7 and -12 were not available. Therefore, the distributions of claudin-1, -2, -3, -4, -8, -10, -11, and -16 in nephron segments were examined with immunofluorescence microscopy. For identification of individual segments, antibodies specific for segment markers were used. Immunofluorescence microscopic analyses of serial frozen sections of mouse kidneys with polyclonal antibodies for claudins and segment markers revealed that claudins demonstrated very complicated, segment-specific, expression patterns in nephrons, i.e., claudin-1 and -2 in Bowman’s capsule, claudin-2, -10, and -11 in the proximal tubule, claudin-2 in the thin descending limb of Henle, claudin-3, -4, and -8 in the thin ascending limb of Henle, claudin-3, -10, -11, and -16 in the thick ascending limb of Henle, claudin-3 and -8 in the distal tubule, and claudin-3, -4, and -8 in the collecting duct. These segment-specific expression patterns of claudins are discussed, with special reference to the physiologic functions of tight junctions in nephrons.
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Devaux, Jerome, and Alexander Gow. "Tight junctions potentiate the insulative properties of small CNS myelinated axons." Journal of Cell Biology 183, no. 5 (December 1, 2008): 909–21. http://dx.doi.org/10.1083/jcb.200808034.

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Claudin family proteins form the physical barriers of tight junctions (TJs) and regulate paracellular diffusion across polarized epithelia. In addition to these heterotypic TJs, claudin 11 forms autotypic TJs comprising the radial component of central nervous system myelin. The exact function of these TJs has been unclear, although their location at the membrane perimeter is well sited to regulate diffusion between the interstitium and intramyelinic space. In this study, we demonstrate that claudin 11 affords rapid nerve conduction principally for small diameter myelinated axons. Claudin 11–null mice have preserved myelin and axonal architecture, but as much as a 60% decrease in conduction. They also have increased action potential thresholds and activated internodal potassium channels. These data indicate that TJs modulate the biophysical properties of myelin. Computational modeling reveals that claudin 11 reduces current flow through myelin and moderates its capacitive charging. Together, our data shed new light on myelin structural components and our understanding of the biology and pathophysiology of this membrane.
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Dissertations / Theses on the topic "Claudin-11"

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Denninger, Andrew Ryan. "Investigations into the Function of Claudin-11 Tight Junctions in CNS Myelin." Thesis, Boston College, 2016. http://hdl.handle.net/2345/bc-ir:106981.

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Thesis advisor: Daniel A. Kirschner
The myelin sheath of the central nervous system contains a network of interlamellar tight junctions known as the radial component. Ablation of claudin-11, a tight junction protein, results in the absence of the radial component and compromises the passive electrical properties of the myelin sheath. Although tight junctions are known to regulate paracellular diffusion, this barrier function has not been directly demonstrated for the radial component, and some evidence suggests that the radial component may also, or instead, mediate adhesion between myelin membranes. To investigate the physical properties of claudin-11 tight junctions, we first compared fresh, unfixed Claudin 11-null and control nerves using X-ray diffraction. In Claudin 11-null tissue, we detected no changes in myelin structure, stability, or membrane interactions, which argues against the notion that myelin tight junctions exhibit significant adhesive properties. To examine myelin permeability in the absence of the radial component, we measured the kinetics of osmotic compaction and recovery in knockout and control myelin. We found that myelin lacking claudin-11 responded more rapidly to osmotic stress, indicating an increase in permeability to water and small osmolytes. To further test this hypothesis, we explored the possibility of measuring the diffusion of water through myelin using neutron diffraction, a technique that had been pioneered in myelin decades ago but was largely unused because of previous limitations in neutron technology. After establishing that present-day neutron instruments were capable of measuring diffusion in myelin, we applied this technique to samples from mice lacking claudin-11. Consistent with our X-ray diffraction studies, we found that H2O-D2O exchange was more rapid in Claudin 11-null mice compared to controls. Thus, our data indicate that the radial component serves primarily as a diffusion barrier and elucidate the mechanism by which tight junctions govern myelin function
Thesis (PhD) — Boston College, 2016
Submitted to: Boston College. Graduate School of Arts and Sciences
Discipline: Biology
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McCabe, Mark James, and markmccabe02@hotmail com. "Hormonal regulation of the testicular Sertoli cell tight junction." RMIT University. Applied Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081212.100348.

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The Sertoli cell tight junction (TJ) of the seminiferous epithelium is important for the developmental process of spermatogenesis as it separates germ cells in the seminiferous tubules from the general circulation in the testicular interstitium. Absence of the TJ leads to spermatogenic arrest and infertility. TJs form at puberty as circulating gonadotrophins luteinising hormone/testosterone and follicle stimulating hormone increase. Several studies have demonstrated hormonal regulation of the two major TJ proteins, claudin-11 and occludin, and also of TJ function in vitro and in vivo. Men with low levels of circulating gonadotrophins exhibit an immature and dysfunctional TJ phenotype, which is reversed upon the exogenous application of gonadotrophins. This thesis hypothesises that claudin-11 and occludin are the major contributors to TJ function, and that gonadotrophins regulate TJ function and structure via these two proteins in several species including humans. This PhD was divided into four separate studies to address these hypotheses. The first study selectively silenced the genetic expression of claudin-11 and occludin with small interfering RNA (siRNA) in cultured immature rat Sertoli cells to determine their contribution to Sertoli cell TJ function in vitro. siRNA treatment against either protein significantly (p less than 0.01) reduced TJ function by ~50% as assessed by transepithelial electrical resistance. Immunocytochemistry displayed marked reductions in the localisation of these proteins to the TJ after siRNA treatment. It was concluded that both proteins significantly contributed to TJ function in vitro. The second and third studies then aimed to study hormonal regulation of the TJ in vivo. Weekly injections of the gonadotrophin releasing hormone antagonist acyline were used to suppress circulating gonadotrophins and spermatogenesis in adult rats. Acyline treatment disrupted i) the localisation of occludin to the TJ and ii) TJ function as shown by permeability to a biotin tracer, which was impermeable to TJs in controls. Short-term hormone replacement partially restored the effects of gonadotrophin suppression. It was concluded that gonadotrophins regulate the maintenance of the TJ in rats in vivo. The third study used the hypogonadal (hpg) mouse, which is a naturally occurring model of gonadotrophin deficiency with inactive spermatogenesis. Claudin-11 in hpg mice was not localised at the TJs, and these were dysfunctional as shown by permeability to biotin. Following hormone treatment, TJs were structurally and functionally competent, demonstrating that gonadotrophins also regulate the formation of TJs in vivo. The fourth study subsequently analysed TJs in gonadotrophin suppressed men, and it was found that claudin-11 staining was reduced from continuous bands in control men, to punctate staining in gonadotrophin-suppressed men, demonstrating that gonadotrophins also regulate the localisation of claudin-11 to the TJ in men in vivo. In summary, it is concluded that the Sertoli cell TJ is hormonally regulated, and that the major contributors to TJ function in vivo and in vitro are claudin-11 and occludin. It is hypothesised that the reduction of claudin-11 localisation to the TJ in men may also result in a loss of human Sertoli cell TJ function, suggesting that the TJ may be a potential target of hormonal contraception in men.
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Röhrs, Lena [Verfasser]. "Untersuchungen der Blut-Hoden-Schranke während der Rekrudeszenz der Spermatogenese nach Downregulation mittels eines slow release GnRH-Implantates beim Rüden : Expression von Connexin 43, Occludin, Claudin-3, -5 und -11 / Lena Röhrs." Gießen : Universitätsbibliothek, 2014. http://d-nb.info/1068275855/34.

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Li, Ching-Fei, and 李京霏. "Investigation of the role of Snail-induced claudin-11 in head and neck squamous cell carcinoma progression." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/kg3w3u.

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Book chapters on the topic "Claudin-11"

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Mazaud-Guittot, Séverine, Alexander Gow, and Brigitte Le Magueresse-Battistoni. "Phenotyping the Claudin 11 Deficiency in Testis: From Histology to Immunohistochemistry." In Methods in Molecular Biology, 223–36. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-191-8_15.

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Gow, Alexander. "The Claudin 11 Gene." In Myelin Biology and Disorders, 565–78. Elsevier, 2004. http://dx.doi.org/10.1016/b978-012439510-7/50075-9.

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"Claudin-11 (3q26.2-q26.3)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 370. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_3126.

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Southwood, Cherie, and Alexander Gow. "Functions of OSP/Claudin- 11-Containing Parallel Tight Junctions." In Tight Junctions. CRC Press, 2001. http://dx.doi.org/10.1201/9781420038538.ch33.

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"Functions of OSP/Claudin-11-Containing Parallel Tight Junctions: Implications from the Knockout Mouse." In Tight Junctions, 741–64. CRC Press, 2001. http://dx.doi.org/10.1201/9781420038538-35.

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Conference papers on the topic "Claudin-11"

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Lee, C. H., J. M. Baek, Y. J. Choi, W. H. Yoo, M. S. Lee, and J. Y. Kim. "OP0263 Claudin-11 regulates bone homeostasis via bidirectional ephb4-ephrinb2 signalling." In Annual European Congress of Rheumatology, EULAR 2018, Amsterdam, 13–16 June 2018. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-eular.3828.

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Agarwal, Rachana, Yuriko Mori, Yulan Cheng, Zhe Jin, Alexandru Olaru, James P. Hamilton, Stefan David, et al. "Abstract LB-89: Claudin-11 (CLDN11): A potential marker of gastric carcinogenesis." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-lb-89.

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Petty, HM, JM King, ME Cuevas, RA Sheller, and MC Todd. "Abstract P5-11-10: Effect of claudin-3 protein expression on its sub-cellular localization and cellular motility in breast cancer cell lines." In Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p5-11-10.

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Martin, Tracey Amanda, Gregory M. Harrison, Robert E. Mansel, Kefer Mokbel, Eleri Davies, and Wen G. Jiang. "Abstract PS4-44: Expression of the claudin transmembrane tight junction protein family (CLDN) and the prediction value of a claudin subset to the clinical outcome of patients with breast cancer." In Abstracts: 2020 San Antonio Breast Cancer Virtual Symposium; December 8-11, 2020; San Antonio, Texas. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.sabcs20-ps4-44.

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