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1 involving increased inflammation and loss of claudin-3.
2 udin-19 mRNA was 25 times more abundant than claudin-3.
3  site at amino acid 192 in the C terminus of claudin-3.
4 nd diminished junctional immunoreactivity of claudin-3.
5 d downregulated expression of genes encoding claudin 3, 4, and 7 and the luminal marker, cytokeratin
6                                              Claudin 3, a tight junction protein, is transiently inco
7 regimen, a novel and tissue-specific role of claudin-3, a tight junction integral protein, in inhibit
8                                      Loss of claudin-3 also predicted poor patient survival.
9 5 only in junctions of acinar cells, whereas claudin 3 and 4 are in both.
10 EB1, S100A8, amyloid beta precursor protein, claudin 3 and cadherin 1 (downregulated in MDA-MB-231) w
11 whereas the expression of 194 genes, such as claudin 3 and cell adhesion molecule 1, is significantly
12 d decreased intestinal barrier marker genes (claudin 3 and claudin 15) expression, and rescued increa
13 family, and low to absent expression of both claudin 3 and E-cadherin.
14 junction (TJ) proteins in the ileum revealed claudin 3 and occludin expression to be increased overal
15                                              Claudin-3 and -4 are frequently overexpressed in ovarian
16                         Here, we showed that claudin-3 and -4 can be phosphorylated in ovarian cancer
17  presence of the high-affinity CPE receptors claudin-3 and -4 in both organs of rabbits, consistent w
18 present surface or secreted proteins such as claudin-3 and -4, HE4, mucin-1, epithelial cellular adhe
19 ptors on intestinal epithelial cells include claudin-3 and -4, members of a large family of tight jun
20 or role for dynamin-dependent endocytosis of claudin-3 and 4 during nutrient stress in intestinal epi
21          Specifically, the downregulation of claudin-3 and 4 was via a dynamin-dependent, but clathri
22 ity association of the PDZ domain of nNOS to claudin-3 and claudin-14, two tight junction tetraspan m
23                               In particular, claudin-3 and claudin-4 are frequently overexpressed in
24                                     However, claudin-3 and claudin-4 are the only family members capa
25 nterfering RNA (siRNA)-mediated knockdown of claudin-3 and claudin-4 expression in ovarian cancer cel
26 ely in breast cancer cells, correlating with claudin-3 and claudin-4 expression.
27 current ovarian tumors were found to express claudin-3 and claudin-4 genes at significantly higher le
28 profiling, we and others have recently found claudin-3 and claudin-4 genes to be highly expressed in
29 (CNS) revealed low or undetectable levels of claudin-3 and claudin-4 in all regions tested by Western
30 tudy was designed to study the expression of claudin-3 and claudin-4 in human prostate tissue as pote
31      Our previous studies have revealed that claudin-3 and claudin-4 proteins are highly overexpresse
32                   In contrast, expression of claudin-3 and claudin-4 was absent in adjacent normal br
33 issue Northern blot analysis, mRNAs for both claudin-3 and claudin-4 were expressed at high levels in
34             By immunohistochemical analysis, claudin-3 and claudin-4 were expressed frequently in met
35                       We found that although claudin-3 and claudin-4 were heteromerically compatible
36 estroy cancer cells expressing CPE receptors claudin-3 and claudin-4.
37 E) cells constitutively expressing wild-type claudin-3 and claudin-4.
38 ifference in polymerization capacity between claudin-3 and claudin-4.
39 ession of TJ proteins ZO-1, JAM-2, Occludin, Claudin-3 and Claudin-5, using in vitro cultures of the
40 y we investigated the level of expression of claudin-3 and/or claudin-4 in chemotherapy-naive and che
41                             The abundance of claudins-3 and -5 remained unchanged.
42                                       Rvp.1 (claudin-3) and CPE-R (claudin-4) are members of a larger
43 s 8, 18, and 19, CD133/1, telomerase, CD44H, claudin 3, and albumin (weakly).
44 e tight-junction molecules zona occludens-1, claudin 3, and claudin 5 and other pathways critically i
45 e able to heterotypically bind to claudin-1, claudin-3, and claudin-5.
46 pression of TJ proteins, ZO-1, Occludin, and Claudin-3, and exacerbated the bacterial endotoxin lipop
47 blots revealed that expression of Claudin-7, Claudin-3, and Occludin, critical proteins that regulate
48              Although glucose transporter 1, claudin-3, and plasmalemma vesicular-associated protein
49 helial cells, in which zonal occludens-1 and claudin-3, apical tight-junction proteins, are mislocali
50       Overall, these novel findings identify claudin-3 as a therapeutic target for inhibiting overact
51 e present the crystal structure of mammalian claudin-3 at 3.6 angstrom resolution.
52                                              Claudin-3, claudin-10, and claudin-19 were detected in R
53 ts were unexplained by effects on claudin-2, claudin-3, claudin-19, occludin, and ZO-1, but changes i
54 audins expressed by the alveolar epithelium, claudin-3, claudin-4, and claudin-18 are the most promin
55 hrough immunohistochemical analysis of ApoJ, claudin-3, claudin-4, and epithelial cellular adhesion m
56 pression of other tight junctional proteins (claudin-3, claudin-4, claudin-5, occludin, and ZO-1) and
57                                              Claudin-3 (CLDN3) and claudin-4 (CLDN4) are the major st
58                                              Claudin-3 (CLDN3) is a tight junction protein that is ov
59 ered intestinal morphology, and dysregulated claudin-3 crypt expression.
60 , which were heterotypically compatible with claudin-3, did not heterotypically bind to claudin-4.
61 tercellular junctional proteins (e.g., ZO-1, claudin-3, E-cadherin) and the subapical cytoskeletal/mi
62 nal barrier function maturation by promoting claudin 3 expression.
63 ibit impaired barrier function and decreased claudin 3 expression.
64 es intestinal barrier maturation and induces claudin 3 expression.
65 e findings however contrasted an upregulated claudin-3 expression in other cancer types and implicate
66                 The persistent high level of claudin-3 expression in prostate adenocarcinoma and func
67 ases in the distribution of occludin but not claudin-3 in the B, EF, and B+EF groups.
68 tes that introduction of these residues from claudin-3 into claudin-4 significantly enhances polymeri
69  from periportal to pericentral hepatocytes, claudin 3 is uniformly expressed, claudin 4 is absent, a
70 nstructs demonstrated that the C terminus of claudin-3 is an excellent substrate for cAMP-dependent p
71             The third transmembrane helix of claudin-3 is clearly bent compared with that of other su
72                                              Claudin-3 loss also upregulated the gp130/IL6/Stat3 sign
73 c and pharmacological studies confirmed that claudin-3 loss induces Wnt/beta-catenin activation, whic
74                                              Claudin-3-/- mice revealed dedifferentiated and leaky co
75 ndent manner, differentiated colon cancer in claudin-3-/- mice versus WT-mice.
76 nding normal glandular tissue, expression of claudin-3 mRNA remained high in the epithelium of prosta
77                     Our results suggest that claudin-3 phosphorylation by PKA, a kinase frequently ac
78 e blood-testis barrier to biotin, suggesting claudin 3 regulates the movement of small molecules acro
79 ed tight junction proteins (ZO-1, Claudin-1, Claudin-3), RPE disorganization, barrier leakage, and im
80 stinal tight junction proteins, occludin and claudin-3, showed decreases in the distribution of occlu
81            Abundance of intestinal Npt2b and claudin-3 (tight junctions protein) were reduced in Npt2
82 on in the first extracellular loop domain of claudin-3 to convert Asn(44) to the corresponding amino
83     In normal prostate tissue, expression of claudin-3 was localized exclusively within acinar epithe
84 icated by loss of the tight junction protein claudin-3 was not observed during acute infection despit
85                                              Claudin-3 was reduced in LSI animals with severe intesti
86 e first EL domain or the second EL domain of claudin-3 were able to heterotypically bind to claudin-1
87 ion in the ileum, VE-cadherin, occludin, and claudin-3, Western blot analyses were conducted.
88 n Sertoli cells, regulates the expression of claudin 3, which encodes a transient component of newly
89  caused a loss of the tight junction protein claudin-3, which was ameliorated by genetic ablation of