Zonulin, a regulator of epithelial and endothelial barrier functions, and its involvement in chronic inflammatory diseases

Hay fever, hygiene, and household size.

Strachan, D. P. (1989) · BMJ · doi:10.1136/bmj.299.6710.1259 · Cited by 5,054

The Acute Respiratory Distress Syndrome

Matthay, M. A. (1996) · New England Journal of Medicine · doi:10.1056/nejm199605303342209 · Cited by 4,924

The Acute Respiratory Distress Syndrome

Ware, L. B., & Matthay, M. A. (2000) · New England Journal of Medicine · doi:10.1056/nejm200005043421806 · Cited by 4,666

The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors

Ridley, A. J., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90163-7 · Cited by 4,469

Intestinal mucosal barrier function in health and disease

Turner, J. R. (2009) · Nature reviews. Immunology · doi:10.1038/nri2653 · Cited by 3,952

JUNCTIONAL COMPLEXES IN VARIOUS EPITHELIA

Farquhar, M. G., & Palade, G. E. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.375 · Cited by 3,637

The small GTP-binding protein rac regulates growth factor-induced membrane ruffling

Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90164-8 · Cited by 3,616

The Effect of Infections on Susceptibility to Autoimmune and Allergic Diseases

Bach, J. (2002) · New England Journal of Medicine · doi:10.1056/nejmra020100 · Cited by 2,723

Occludin: a novel integral membrane protein localizing at tight junctions.

Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.123.6.1777 · Cited by 2,580

Claudin-1 and -2: Novel Integral Membrane Proteins Localizing at Tight Junctions with No Sequence Similarity to Occludin

Furuse, M., Fujita, K., Hiiragi, T., Fujimoto, K., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.7.1539 · Cited by 2,100

Junctional Adhesion Molecule, a Novel Member of the Immunoglobulin Superfamily That Distributes at Intercellular Junctions and Modulates Monocyte Transmigration

Martín-Padura, I., Lostaglio, S., Schneemann, M., Williams, L., Romano, M., Fruscella, P., Panzeri, C., Stoppacciaro, A., Ruco, L., Villa, A., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.117 · Cited by 1,387

. Plasma levels of soluble CD14 independently predict mortality in HIV infection.

Sandler, N. G., Wand, H., Roque, A., Law, M., Nason, M. C., Nixon, D. E., Pedersen, C., Ruxrungtham, K., Lewin, S. R., Emery, S., et al. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiq118 · Cited by 1,106

Zonulin and Its Regulation of Intestinal Barrier Function: The Biological Door to Inflammation, Autoimmunity, and Cancer

Fasano, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00003.2008 · Cited by 1,063

Systemic Effects of Inflammation on Health during Chronic HIV Infection

Deeks, S. G., Tracy, R. P., & Douek, D. C. (2013) · Immunity · doi:10.1016/j.immuni.2013.10.001 · Cited by 910

Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells

Ikenouchi, J., Furuse, M., Furuse, K., Sasaki, H., Tsukita, S., & Tsukita, S. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200510043 · Cited by 787

The small GTP-binding protein rac regulates growth factor-induced membrane ruffling

Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Trends in Cell Biology · doi:10.1016/0962-8924(92)90174-l · Cited by 756

Lipopolysaccharide Activates Distinct Signaling Pathways in Intestinal Epithelial Cell Lines Expressing Toll-Like Receptors

Cario, E., Rosenberg, I. M., Brandwein, S. L., Beck, P. L., Reinecker, H., & Podolsky, D. K. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.2.966 · Cited by 751

Toll-like receptor 2 controls mucosal inflammation by regulating epithelial barrier function

Cario, E., Gerken, G., & Podolsky, D. K. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.02.056 · Cited by 697

Inflammatory Bowel Disease and Adenomas in Mice Expressing a Dominant Negative N-Cadherin

Hermiston, M. L., & Gordon, J. I. (1995) · Science · doi:10.1126/science.270.5239.1203 · Cited by 669

Zonulin, a newly discovered modulator of intestinal permeability, and its expression in coeliac disease

Fasano, A., Not, T., Wang, W., Uzzau, S., Berti, I., Tommasini, A., & Goldblum, S. E. (2000) · The Lancet · doi:10.1016/s0140-6736(00)02169-3 · Cited by 668

Disorders of gastrointestinal motility associated with diabetes mellitus

FELDMAN, M., & SCHILLER, L. R. (1983) · Annals of Internal Medicine · doi:10.7326/0003-4819-98-3-378 · Cited by 653

Intestinal permeability and the prediction of relapse in Crohn's disease

Wyatt, J., Vogelsang, H., Hübl, W., Waldhoer, T., & Lochs, H. (1993) · The Lancet · doi:10.1016/0140-6736(93)90882-h · Cited by 626

Alterations in intestinal permeability

Arrieta, M., Bistritz, L., & Meddings, J. (2006) · Gut · doi:10.1136/gut.2005.085373 · Cited by 609

Vibrio cholerae produces a second enterotoxin, which affects intestinal tight junctions.

Fasano, A., Baudry, B., Pumplin, D. W., Wasserman, S. S., Tall, B. D., Ketley, J. M., & Kaper, J. B. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.12.5242 · Cited by 579

Soluble Markers of Inflammation and Coagulation but Not T-Cell Activation Predict Non–AIDS-Defining Morbid Events During Suppressive Antiretroviral Treatment

Tenorio, A. R., Zheng, Y., Bosch, R. J., Krishnan, S., Rodriguez, B. A., Hunt, P. W., Plants, J., Seth, A., Wilson, C. C., Deeks, S. G., et al. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu254 · Cited by 551

Zonulin Upregulation Is Associated With Increased Gut Permeability in Subjects With Type 1 Diabetes and Their Relatives

Sapone, A., de Magistris, L., Pietzak, M. M., Clemente, M. G., Tripathi, A. K., Cucca, F., Lampis, R., Kryszak, D., Cartenı̀, M., Generoso, M., et al. (2006) · Diabetes · doi:10.2337/db05-1593 · Cited by 550

Gliadin Induces an Increase in Intestinal Permeability and Zonulin Release by Binding to the Chemokine Receptor CXCR3

Lammers, K. M., Lu, R., Brownley, J., Lu, B., Gerard, C. J., Thomas, K., Rallabhandi, P., Shea‐Donohue, T., Tamiz, A. P., Alkan, Ş. Ş., et al. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.03.023 · Cited by 545

JAM-A regulates permeability and inflammation in the intestine in vivo

Laukoetter, M. G., Nava, P., Lee, W. Y., Severson, E. A., Capaldo, C., Babbin, B. A., Williams, I. R., Koval, M. H., Peatman, E., Campbell, J. A., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071416 · Cited by 512

Gliadin, zonulin and gut permeability: Effects on celiac and non-celiac intestinal mucosa and intestinal cell lines

Drago, S., Asmar, R. E., Pierro, M. D., Clemente, M. G., Sapone, A., Thakar, M., Iacono, G., Carroccio, A., DʼAgate, C., Not, T., et al. (2005) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520500235334 · Cited by 503

Mechanisms of Disease: the role of intestinal barrier function in the pathogenesis of gastrointestinal autoimmune diseases

Fasano, A., & Shea-Donohue, T. (2005) · Nature Clinical Practice Gastroenterology & Hepatology · doi:10.1038/ncpgasthep0259 · Cited by 484

Gut Epithelial Barrier Dysfunction and Innate Immune Activation Predict Mortality in Treated HIV Infection

Hunt, P. W., Sinclair, E., Rodriguez, B. A., Shive, C. L., Clagett, B. M., Funderburg, N., Robinson, J., Huang, Y., Epling, L., Martin, J. N., et al. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu238 · Cited by 481

Toll-like receptor 2 enhances ZO-1-associated intestinal epithelial barrier integrity via protein kinase C

Cario, E., Gerken, G., & Podolsky, D. K. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.04.015 · Cited by 475

Human zonulin, a potential modulator of intestinal tight junctions

Wang, W., Uzzau, S., Goldblum, S. E., & Fasano, A. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.24.4435 · Cited by 470

Myosin light chain phosphorylation regulates barrier function by remodeling tight junction structure

Shen, L., Black, E. D., Witkowski, E. D., Lencer, W. I., Guerriero, V., Schneeberger, E. E., & Turner, J. R. (2006) · Journal of Cell Science · doi:10.1242/jcs.02915 · Cited by 467

Targeted epithelial tight junction dysfunction causes immune activation and contributes to development of experimental colitis

Su, L., Shen, L., Clayburgh, D. R., Nalle, S. C., Sullivan, E. A., Meddings, J. B., Abraham, C., & Turner, J. R. (2009) · Gastroenterology · doi:10.1053/j.gastro.2008.10.081 · Cited by 455

Identification of human zonulin, a physiological modulator of tight junctions, as prehaptoglobin-2

Tripathi, A. K., Lammers, K. M., Goldblum, S. E., Shea‐Donohue, T., Netzel–Arnett, S., Buzza, M. S., Antalis, T., Vogel, S. N., Zhao, A., Yang, S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906773106 · Cited by 449

Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function

Clemente, M. G. (2003) · Gut · doi:10.1136/gut.52.2.218 · Cited by 420

Abnormal intestinal permeability in children with autism

D'Eufemia, P., Celli, M., Finocchiaro, R., Pacifico, L., Viozzi, L., Zaccagnini, M., Cardi, E., & Giardini, O. (1996) · Acta Paediatrica · doi:10.1111/j.1651-2227.1996.tb14220.x · Cited by 416

In vivo analysis of cadherin function in the mouse intestinal epithelium: essential roles in adhesion, maintenance of differentiation, and regulation of programmed cell death.

Hermiston, M. L., & Gordon, J. I. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.2.489 · Cited by 415

The ‘microflora hypothesis’ of allergic diseases

Noverr, M. C., & Huffnagle, G. B. (2005) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2005.02379.x · Cited by 394

Genetic basis for increased intestinal permeability in families with Crohn’s disease: role of CARD15 3020insC mutation?

Bühner, S., Büning, C., Genschel, J., Kling, K., Herrmann, D., Dignass, A., Kuechler, I., Krueger, S., Schmidt, H. H.-J., & Lochs, H. (2005) · Gut · doi:10.1136/gut.2005.065557 · Cited by 381

Host-dependent zonulin secretion causes the impairment of the small intestine barrier function after bacterial exposure

Asmar, R. E., Panigrahi, P., Bamford, P. D., Berti, I., Not, T., Coppa, G. V., Catassi, C., & Fasano, A. (2002) · Gastroenterology · doi:10.1053/gast.2002.36578 · Cited by 369

Interferon‐γ induces internalization of epithelial tight junction proteins via a macropinocytosis‐like process

Bruewer, M., Utech, M., Ivanov, A. I., Hopkins, A. M., Parkos, C. A., & Nusrat, A. (2005) · The FASEB Journal · doi:10.1096/fj.04-3260com · Cited by 364

Dysbiosis of Gut Microbiota [DOGMA]—A novel theory for the development of Polycystic Ovarian Syndrome

Tremellen, K., & Pearce, K. (2012) · Medical Hypotheses · doi:10.1016/j.mehy.2012.04.016 · Cited by 359

Increased circulatory levels of lipopolysaccharide (LPS) and zonulin signify novel biomarkers of proinflammation in patients with type 2 diabetes

Jayashree, B., Bibin, Y. S., Prabhu, D., Shanthirani, C. S., Gokulakrishnan, K., Lakshmi, B. S., Mohan, V., & Balasubramanyam, M. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1911-4 · Cited by 353

Intestinal epithelial cells promote colitis-protective regulatory T-cell differentiation through dendritic cell conditioning

Iliev, I. D., Mileti, E., Matteoli, G., Chieppa, M., & Rescigno, M. (2009) · Mucosal Immunology · doi:10.1038/mi.2009.13 · Cited by 352

Zonula occludens toxin modulates tight junctions through protein kinase C-dependent actin reorganization, in vitro.

Fasano, A., Fiorentini, C., Donelli, G., Uzzau, S., Kaper, J. B., Margaretten, K., Ding, X., Guandalini, S., Comstock, L. E., & Goldblum, S. E. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118114 · Cited by 342

Reducing small intestinal permeability attenuates colitis in the IL10 gene-deficient mouse

Arrieta, M., Madsen, K. L., Doyle, J. S. G., & Meddings, J. B. (2008) · Gut · doi:10.1136/gut.2008.150888 · Cited by 324

Chemokines and receptors in HIV encephalitis

Sanders, V. J., Pittman, C. A., White, M. G., Wang, G., Wiley, C. A., & Achim, C. L. (1998) · AIDS · doi:10.1097/00002030-199809000-00009 · Cited by 319

Luminal trypsin may regulate enterocytes through proteinase-activated receptor 2

Kong, W., McConalogue, K., Khitin, L. M., Hollenberg, M. D., Payan, D. G., Böhm, S. K., & Bunnett, N. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8884 · Cited by 318

Circulating Zonulin, a Marker of Intestinal Permeability, Is Increased in Association with Obesity-Associated Insulin Resistance

Moreno‐Navarrete, J. M., Sabater, M., Ortega, F. J., Ricart, W., & Fernández‐Real, J. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037160 · Cited by 317

Role of the intestinal tight junction modulator zonulin in the pathogenesis of type I diabetes in BB diabetic-prone rats

Watts, T. L., Berti, I., Sapone, A., Gerarduzzi, T., Not, T., Zielke, R. H., & Fasano, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500178102 · Cited by 313

Increased intestinal permeability precedes the onset of Crohn's disease in a subject with familial risk

Irvine, E. J., & Marshall, J. K. (2000) · Gastroenterology · doi:10.1053/gast.2000.20231 · Cited by 286

The safety, tolerance, pharmacokinetic and pharmacodynamic effects of single doses of AT‐1001 in coeliac disease subjects: a proof of concept study

Paterson, B. M., Lammers, K. M., Arrieta, M., Fasano, A., & Meddings, J. B. (2007) · Alimentary Pharmacology & Therapeutics · doi:10.1111/j.1365-2036.2007.03413.x · Cited by 279

Bifidobacteria Stabilize Claudins at Tight Junctions and Prevent Intestinal Barrier Dysfunction in Mouse Necrotizing Enterocolitis

Bergmann, K. R., Liu, S. X. L., Tian, R., Kushnir, A., Turner, J. R., Li, H.-L., Chou, P. M., Weber, C. R., & Plaen, I. G. D. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.01.013 · Cited by 268

Larazotide Acetate for Persistent Symptoms of Celiac Disease Despite a Gluten-Free Diet: A Randomized Controlled Trial

Leffler, D. A., Kelly, C. P., Green, P. H. R., Fedorak, R. N., DiMarino, A. J., Perrow, W., Rasmussen, H. S., Wang, C., Berčík, P., Bachir, N. M., et al. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.02.008 · Cited by 264

Genetically Determined Heterogeneity in Hemoglobin Scavenging and Susceptibility to Diabetic Cardiovascular Disease

Asleh, R., Marsh, S., Shilkrut, M., Binah, O., Guetta, J., Lejbkowicz, F., Enav, B., Shehadeh, N., KANTER, Y., Lache, O., et al. (2003) · Circulation Research · doi:10.1161/01.res.0000076889.23082.f1 · Cited by 263

Clustering of increased small intestinal permeability in families with Crohn's disease

Peeters, M., Geypens, B. J., Claus, D., Nevens, H., Ghoos, Y. F., Verbeke, G. N., Baert, F., Vermeire, S., VLIETINCK, R. F., & Rutgeerts, P. (1997) · Gastroenterology · doi:10.1016/s0016-5085(97)70174-4 · Cited by 262

Intestinal barrier failure during experimental necrotizing enterocolitis: protective effect of EGF treatment

Clark, J. A., Doelle, S. M., Halpern, M. D., Saunders, T. A., Holubec, H., Dvorak, K., Boitano, S. A., & Dvořák, B. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00090.2006 · Cited by 258

Mechanisms of Intestinal Barrier Dysfunction in Sepsis

Yoseph, B. P., Klingensmith, N. J., Liang, Z., Breed, E. R., Burd, E. M., Mittal, R., Dominguez, J. A., Petrie, B., Ford, M. L., & Coopersmith, C. M. (2016) · Shock · doi:10.1097/shk.0000000000000565 · Cited by 256

Covalent structure of human haptoglobin: a serine protease homolog.

Kurosky, A., Barnett, D. R., Lee, T. H., Touchstone, B., Hay, R. E., Arnott, M. S., Bowman, B. H., & Fitch, W. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.6.3388 · Cited by 243

The role of genes and environment in the etiology of PCOS

Diamanti-Kandarakis, E., Kandarakis, H., & Legro, R. S. (2006) · Endocrine · doi:10.1385/endo:30:1:19 · Cited by 233

Zonula Occludens-1 Function in the Assembly of Tight Junctions in Madin-Darby Canine Kidney Epithelial Cells

McNeil, E. A., Capaldo, C., & Macara, I. G. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0650 · Cited by 233

Gliadin Stimulation of Murine Macrophage Inflammatory Gene Expression and Intestinal Permeability Are MyD88-Dependent: Role of the Innate Immune Response in Celiac Disease

Thomas, K. E., Sapone, A., Fasano, A., & Vogel, S. N. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.4.2512 · Cited by 232

Haptoglobin: a review of the major allele frequencies worldwide and their association with diseases

Carter, K., & Worwood, M. (2007) · International Journal of Laboratory Hematology · doi:10.1111/j.1751-553x.2007.00898.x · Cited by 222

Effect of Gliadin on Permeability of Intestinal Biopsy Explants from Celiac Disease Patients and Patients with Non-Celiac Gluten Sensitivity

Hollon, J. R., Puppa, E. L., Greenwald, B. D., Goldberg, E., Guerrerio, A. L., & Fasano, A. (2015) · Nutrients · doi:10.3390/nu7031565 · Cited by 221

Biomarkers of Environmental Enteropathy, Inflammation, Stunting, and Impaired Growth in Children in Northeast Brazil

Guerrant, R. L., Leite, Á. M., Pinkerton, R., de Medeiros, P. H. Q. S., Cavalcante, P. A., DeBoer, M. D., Kosek, M. N., Duggan, C., Gewirtz, A. T., Kagan, J. C., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158772 · Cited by 216

Proteinases and proteinase-activated receptor 2: A possible role to promote visceral hyperalgesia in rats

Coelho, A.-M., Vergnolle, N., Guiard, B. P., Fioramonti, J., & Bueno, L. P. (2002) · Gastroenterology · doi:10.1053/gast.2002.32387 · Cited by 212

Duplication within the haptoglobin Hp2 gene

Maeda, N., Yang, F., Barnett, D. R., Bowman, B. H., & Smithies, O. (1984) · Nature · doi:10.1038/309131a0 · Cited by 211

Zonula Occludens Toxin Structure-Function Analysis

Pierro, M. D., Lu, R., Uzzau, S., Wang, W., Margaretten, K., Pazzani, C., Maimone, F., & Fasano, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009674200 · Cited by 206

Intestinal Barrier Dysfunction Develops at the Onset of Experimental Autoimmune Encephalomyelitis, and Can Be Induced by Adoptive Transfer of Auto-Reactive T Cells

Nouri, M., Bredberg, A. C. A., Weström, B. R., & Lavasani, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106335 · Cited by 206

Analysis of the angulin family consisting of LSR, ILDR1 and ILDR2: tricellulin recruitment, epithelial barrier function and implication in deafness pathogenesis

Higashi, T., Tokuda, S., Kitajiri, S., Masuda, S., Nakamura, H., Oda, Y., & Furuse, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.116442 · Cited by 202

Protective Effects of Bifidobacterium on Intestinal Barrier Function in LPS-Induced Enterocyte Barrier Injury of Caco-2 Monolayers and in a Rat NEC Model

Ling, X., Peng, L., Du, W., & Wei, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161635 · Cited by 202

Larazotide acetate in patients with coeliac disease undergoing a gluten challenge: a randomised placebo‐controlled study

Kelly, C. P., Green, P. H. R., Murray, J. A., DiMarino, A. J., Colatrella, A. M., Leffler, D. A., Alexander, T., Arsenescu, R. I., León, F., Jiang, J. G., et al. (2012) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.12147 · Cited by 201

Intestinal permeability in patients with Crohn's disease and their first degree relatives.

Teahon, K., Smethurst, P., Levi, A. J., Menzies, I. S., & Bjarnason, I. (1992) · Gut · doi:10.1136/gut.33.3.320 · Cited by 195

The human haptoglobin gene promoter: interleukin‐6‐responsive elements interact with a DNA‐binding protein induced by interleukin‐6.

Oliviero, S., & Cortese, R. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03485.x · Cited by 190

A Randomized, Double-Blind Study of Larazotide Acetate to Prevent the Activation of Celiac Disease During Gluten Challenge

Leffler, D. A., Kelly, C. P., Abdallah, H., Colatrella, A. M., Harris, L. A., León, F., Arterburn, L. A., Paterson, B. M., Lan, Z. H., & Murray, J. A. (2012) · The American Journal of Gastroenterology · doi:10.1038/ajg.2012.211 · Cited by 186

Increased gastrointestinal permeability is an early lesion in the spontaneously diabetic BB rat

Meddings, J. B., Jarand, J. M., Urbanski, S. J., Hardin, J. W., & Gall, D. (1999) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1999.276.4.g951 · Cited by 185

The enterotoxic effect of zonula occludens toxin on rabbit small intestine involves the paracellular pathway

Fasano, A., Uzzau, S., Fiore, C., & Margaretten, K. (1997) · Gastroenterology · doi:10.1053/gast.1997.v112.pm9041245 · Cited by 172

Regulation of intercellular tight junctions by zonula occludens toxin and its eukaryotic analogue zonulin

FASANO, A. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05244.x · Cited by 169

Gut Microbiota, Microinflammation, Metabolic Profile, and Zonulin Concentration in Obese and Normal Weight Subjects

Żak‐Gołąb, A., Kocełak, P., Aptekorz, M., Zientara, M., Juszczyk, Ł., Martirosian, G., Chudek, J. T., & Olszanecka‐Glinianowicz, M. (2013) · International Journal of Endocrinology · doi:10.1155/2013/674106 · Cited by 159

Modulation of colonic barrier function by the composition of the commensal flora in the rat

Garcia-Lafuente, A. M., Antolı́n, M., Guarner, F., Crespo, E., & Malagelada, J. R. (2001) · Gut · doi:10.1136/gut.48.4.503 · Cited by 156

HLA-DQ Determines the Response to Exogenous Wheat Proteins: A Model of Gluten Sensitivity in Transgenic Knockout Mice

Black, K. E., Murray, J. A., & David, C. S. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.10.5595 · Cited by 152

The role of Haptoglobin and its related protein, Zonulin, in inflammatory bowel disease

Vanuytsel, T., Vermeire, S., & Cleynen, I. (2013) · Tissue Barriers · doi:10.4161/tisb.27321 · Cited by 152

Serum concentrations of TNF-α and soluble TNF-α receptors in obesity

Zahorska‐Markiewicz, B., Janowska, J., Olszanecka‐Glinianowicz, M., & Żurakowski, A. (2000) · International Journal of Obesity · doi:10.1038/sj.ijo.0801398 · Cited by 151

Proteinase-activated receptor 1 activation induces epithelial apoptosis and increases intestinal permeability

Chin, A. C., Vergnolle, N., MacNaughton, W. K., Wallace, J. L., Hollenberg, M. D., & Buret, A. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1831452100 · Cited by 149

Initiation of human colon cancer cell proliferation by trypsin acting at protease-activated receptor-2

Darmoul, D., Marie, J., Devaud, H., Gratio, V., & Laburthe, M. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2001.1976 · Cited by 149

Haptoglobin, a hemoglobin-binding plasma protein, is present in bony fish and mammals but not in frog and chicken

Wicher, K. B., & Fries, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508723103 · Cited by 148

Intestinal permeability and irritable bowel syndrome

Camilleri, M., & Gorman, H. (2007) · Neurogastroenterology and Motility · doi:10.1111/j.1365-2982.2007.00925.x · Cited by 145

A new model for dermatitis herpetiformis that uses HLA-DQ8 transgenic NOD mice

Marietta, E. V., Black, K. E., Camilleri, M., Krause, P. K., Rogers, R. S., David, C. S., Pittelkow, M. R., & Murray, J. A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200421055 · Cited by 144

Serum concentrations of nitric oxide, tumor necrosis factor (TNF)-α and TNF soluble receptors in women with overweight and obesity

Olszanecka‐Glinianowicz, M., Zahorska‐Markiewicz, B., Janowska, J., & Żurakowski, A. (2004) · Metabolism · doi:10.1016/j.metabol.2004.07.001 · Cited by 133

Gliadin-dependent neuromuscular and epithelial secretory responses in gluten-sensitive HLA-DQ8 transgenic mice

Verdu, E. F., Huang, X., Natividad, J. M., Lu, J., Blennerhassett, P. A., David, C. S., McKay, D. M., & Murray, J. A. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00225.2007 · Cited by 125

Altered Intestinal Permeability to Mannitol in Diabetes Mellitus Type I

Carratu, R., Secondulfo, M., de Magistris, L., Iafusco, D., Urio, A., Carbone, M. G., Pontoni, G., Carteni', M., & Prisco, F. (1999) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1097/00005176-199903000-00010 · Cited by 125

Positive regulatory effects of perioperative probiotic treatment on postoperative liver complications after colorectal liver metastases surgery: a double-center and double-blind randomized clinical trial

Liu, Z., Li, C. L., Huang, M., Tong, C., Zhang, X., Wang, L., Peng, H., Lan, P., Zhang, P., Huang, N., et al. (2015) · BMC Gastroenterology · doi:10.1186/s12876-015-0260-z · Cited by 124

Non-celiac gluten sensitivity: questions still to be answered despite increasing awareness

Volta, U., Caio, G., Tovoli, F., & GIORGIO, R. D. (2013) · Cellular and Molecular Immunology · doi:10.1038/cmi.2013.28 · Cited by 124

A new model for dermatitis herpetiformis that uses HLA-DQ8 transgenic NOD mice

Marietta, E. V., Black, K. E., Camilleri, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21055 · Cited by 120

Larazotide acetate regulates epithelial tight junctions in vitro and in vivo

Gopalakrishnan, S., Durai, M., Kitchens, K. M., Tamiz, A. P., Somerville, R. P. T., Ginski, M. J., Paterson, B. M., Murray, J. A., Verdu, E. F., Alkan, Ş. Ş., et al. (2012) · Peptides · doi:10.1016/j.peptides.2012.02.015 · Cited by 117

Multiple sclerosis patients have peripheral blood CD45RO+ B cells and increased intestinal permeability

Yacyshyn, B., Meddings, J. B., Sadowski, D. C., & Bowen-Yacyshyn, M. B. (1996) · Digestive Diseases and Sciences · doi:10.1007/bf02100148 · Cited by 116

Erythropoietin Protects Intestinal Epithelial Barrier Function and Lowers the Incidence of Experimental Neonatal Necrotizing Enterocolitis

Shiou, S., Yu, Y., Chen, S., Ciancio, M. J., Petrof, E. O., Sun, J., & Claud, E. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154625 · Cited by 116

Physiological, Pathological, and Therapeutic Implications of Zonulin-Mediated Intestinal Barrier Modulation

Fasano, A. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080192 · Cited by 110

Restoration of impaired intestinal barrier function by the hydrolysed casein diet contributes to the prevention of type 1 diabetes in the diabetes-prone BioBreeding rat

Visser, J. T. J., Lammers, K. M., Hoogendijk, A. J., Boer, M. W., Brugman, S., Beijer‐Liefers, S., Zandvoort, A., Harmsen, H. J. M., Welling, G. W., Stellaard, F., et al. (2010) · Diabetologia · doi:10.1007/s00125-010-1903-9 · Cited by 109

Resistance to Celiac Disease in Humanized HLA-DR3-DQ2-Transgenic Mice Expressing Specific Anti-Gliadin CD4+ T Cells

de Kauwe, A. L., Chen, Z., Anderson, R. P., Keech, C. L., Price, J. D., Wijburg, O. L. C., Jackson, D. C., Ladhams, J., Allison, J., & McCluskey, J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900233 · Cited by 106

Increased intestinal permeability in bronchial asthma

Benard, A., Desreumeaux, P., Huglo, D. G., Hoorelbeke, A., Tonnel, A., & Wallaert, B. (1996) · Journal of Allergy and Clinical Immunology · doi:10.1016/s0091-6749(96)70181-1 · Cited by 104

Identification of a novel immunomodulatory gliadin peptide that causes interleukin-8 release in a chemokine receptor CXCR3-dependent manner only in patients with coeliac disease

Lammers, K. M., Khandelwal, S., Chaudhry, F., Kryszak, D., Puppa, E. L., Casolaro, V., & Fasano, A. (2010) · Immunology · doi:10.1111/j.1365-2567.2010.03378.x · Cited by 102

The active Zot domain (aa 288–293) increases ZO‐1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO‐1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation

Goldblum, S. E., Rai, U., Tripathi, A. K., Thakar, M., Leo, L. D., Toro, N. D., Not, T., Ramachandran, R., Puché, A. C., Hollenberg, M. D., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-158972 · Cited by 98

Efficacy of melaleuca oral solution for the treatment of fluconazole refractory oral candidiasis in AIDS patients

Jandourek, A., Vaishampayan, J. K., & Vázquez, J. (1998) · AIDS (London) · doi:10.1097/00002030-199809000-00011 · Cited by 98

Increased plasma zonulin in patients with sepsis

Klaus, D. A., Motal, M. C., Burger-Klepp, U., Marschalek, C., Schmidt, E. M., Lebherz-Eichinger, D., Krenn, C. G., & Roth, G. A. (2013) · Biochemia Medica · doi:10.11613/bm.2013.013 · Cited by 98

Tumor necrosis factor inhibitor ameliorates murine intestinal graft-versus-host disease

Brown, G., Lindberg, G. M., Meddings, J. B., Silva, M., Beutler, B., & Thiele, D. L. (1999) · Gastroenterology · doi:10.1016/s0016-5085(99)70181-2 · Cited by 97

Expression of Protease-Activated Receptor 2 in Ulcerative Colitis

Kim, J.-A., Choi, S.-C., Yun, K.-J., Kim, D.-K., Han, M.-K., Seo, G.-S., Yeom, J.-J., Kim, T.-H., Nah, Y.-H., & Lee, Y.-M. (2003) · Inflammatory Bowel Diseases · doi:10.1097/00054725-200307000-00002 · Cited by 96

Human haptoglobin structure and function – a molecular modelling study

Polticelli, F., Bocedi, A., Minervini, G., & Ascenzi, P. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06690.x · Cited by 94

Circulating zonulin levels in newly diagnosed Chinese type 2 diabetes patients

Zhang, D., Zhang, L., Zheng, Y., Yue, F., Russell, R., & Zeng, Y. (2014) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2014.08.017 · Cited by 94

A Transient Breach in the Epithelial Barrier Leads to Regulatory T-Cell Generation and Resistance to Experimental Colitis

Boirivant, M., Amendola, A., Butera, A., Sanchez, M., Xu, L., Marinaro, M., Kitani, A., Giacinto, C. D., Strober, W., & Fuss, I. J. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.07.028 · Cited by 92

Haptoglobin phenotype and diabetic nephropathy

Nakhoul, F. M., Zoabi, R., KANTER, Y., Zoabi, M. M. A., Skorecki, K. L., Hochberg, I., Leibu, R., Miller, B. T., & Levy, A. P. (2001) · Diabetologia · doi:10.1007/s001250051666 · Cited by 89

Permeability, zonulin production, and enteropathy in dermatitis herpetiformis

Smecuol, E., Sugai, E., Niveloni, S. I., Vázquez, H., Pedreira, S. C., Mazure, R. M., Moreno, M. L., Label, M. G., Mauriño, E. C., Fasano, A., et al. (2005) · Clinical Gastroenterology and Hepatology · doi:10.1016/s1542-3565(04)00778-5 · Cited by 87

Zonulin Regulates Intestinal Permeability and Facilitates Enteric Bacteria Permeation in Coronary Artery Disease

Li, C., Gao, M., Zhang, W., Chen, C., Zhou, F., Hu, Z., & Zeng, C. (2016) · Scientific Reports · doi:10.1038/srep29142 · Cited by 87

Serum zonulin is elevated in women with polycystic ovary syndrome and correlates with insulin resistance and severity of anovulation

Zhang, D., Zhang, L., Yue, F., Zheng, Y., & Russell, R. (2014) · European Journal of Endocrinology · doi:10.1530/eje-14-0589 · Cited by 86

Nonmuscle Myosin IIA Regulates Intestinal Epithelial Barrier in vivo and Plays a Protective Role During Experimental Colitis

Naydenov, N. G., Feygin, A., Wang, D., Kuemmerle, J. F., Harris, G., Conti, M. A., Adelstein, R. S., & Ivanov, A. I. (2016) · Scientific Reports · doi:10.1038/srep24161 · Cited by 86

Intestinal permeability is increased in bronchial asthma

Hijazi, Z. (2004) · Archives of Disease in Childhood · doi:10.1136/adc.2003.027680 · Cited by 82

Increased small intestinal permeability in ulcerative colitis: Rather genetic than environmental and a risk factor for extensive disease?

Büning, C., Geissler, N., Prager, M., Sturm, A., Baumgart, D. C., Büttner, J., Bühner, S., Haas, V. K., & Lochs, H. H. (2012) · Inflammatory Bowel Diseases · doi:10.1002/ibd.22909 · Cited by 82

Abnormal intestinal permeability to sugars in diabetes mellitus

Mooradian, A. D., Morley, J. E., Levine, A. S., Prigge, W. F., & Gebhard, R. L. (1986) · Diabetologia · doi:10.1007/bf00454879 · Cited by 81

Intestinal zonulin: open sesame!

Fasano, A. (2001) · Gut · doi:10.1136/gut.49.2.159 · Cited by 80

TNF-α Producing Innate Lymphoid Cells (ILCs) Are Increased in Active Celiac Disease and Contribute to Promote Intestinal Atrophy in Mice

Marafini, I., Monteleone, I., Fusco, D. D., Cupi, M. L., Paoluzi, O. A., Colantoni, A., Ortenzi, A., Izzo, R., Vita, S., Luca, E. D., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126291 · Cited by 74

Larazotide acetate promotes tight junction assembly in epithelial cells

Gopalakrishnan, S., Tripathi, A. K., Tamiz, A. P., Alkan, Ş. Ş., & Pandey, N. B. (2012) · Peptides · doi:10.1016/j.peptides.2012.02.016 · Cited by 74

Zonulin as prehaptoglobin2 regulates lung permeability and activates the complement system

Rittirsch, D., Flierl, M. A., Nadeau, B. A., Day, D. E., Huber-Lang, M. S., Grailer, J. J., Zetoune, F. S., Andjelkovic, A. V., Fasano, A., & Ward, P. A. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00196.2012 · Cited by 69

Anti-TNF-α antibodies improve intestinal barrier function in Crohn's disease

Noth, R., Stüber, E., Häsler, R., Nikolaus, S., Kühbacher, T., Hampe, J., Bewig, B., Schreiber, S., & Arlt, A. (2012) · Journal of Crohn s and Colitis · doi:10.1016/j.crohns.2011.10.004 · Cited by 68

Prohaptoglobin is proteolytically cleaved in the endoplasmic reticulum by the complement C1r-like protein

Wicher, K. B., & Fries, E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405692101 · Cited by 68

Intestinal nutrient transport in genetically obese mice

Ferraris, R., & Vinnakota, R. R. (1995) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/62.3.540 · Cited by 67

Increased circulating zonulin in children with biopsy-proven nonalcoholic fatty liver disease

Pacifico, L. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i45.17107 · Cited by 67

Association of HLA-DQ gene with bowel transit, barrier function, and inflammation in irritable bowel syndrome with diarrhea

Vázquez‐Roque, M. I., Camilleri, M., Smyrk, T. C., Murray, J. A., O’Neill, J., Carlson, P., Lamsam, J. L., Eckert, D. J., Janzow, D., Burton, D. B., et al. (2012) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00294.2012 · Cited by 67

Affinity Purification and Partial Characterization of the Zonulin/Zonula Occludens Toxin (Zot) Receptor from Human Brain

Lu, R., Wang, W., Uzzau, S., Vigorito, R. D., Zielke, H. R., & Fasano, A. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740320.x · Cited by 67

Transmigration of Neural Stem Cells across the Blood Brain Barrier Induced by Glioma Cells

Díaz-Coránguez, M., Segovia, J., López-Ornelas, A., Puerta-Guardo, H. N., Ludert, J. E., Chávez, B., Meraz‐Cruz, N., & González‐Mariscal, L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060655 · Cited by 67

Enterocyte Actin Autoantibody Detection: A New Diagnostic Tool in Celiac Disease Diagnosis: Results of a Multicenter Study

Clemente, M. G., Musu, M. P., Troncone, R., Volta, U., Congia, M., Ciacci, C., Neri, E., Not, T., Maggiore, G., Strisciuglio, P., et al. (2004) · The American Journal of Gastroenterology · doi:10.1111/j.1572-0241.2004.30296.x · Cited by 66

Haptoglobin Genotype as a Risk Factor for Diabetic Retinopathy

Nakhoul, F. M., Marsh, S., Hochberg, I., Leibu, R., Miller, B. P., & Levy, A. P. (2000) · JAMA · doi:10.1001/jama.284.10.1244-a · Cited by 63

Intestinal mucosal permeability in inflammatory rheumatic diseases. II. Role of disease.

Mielants, H., Vos, M. D., Goemaere, S., Schelstraete, K., Cuvelier, C. A., Goethals, K., Maertens, M., Ackerman, C. M., & VEYS, E. M. (1991) · PubMed · Cited by 61

Intestinal alkaline phosphatase administration in newborns is protective of gut barrier function in a neonatal necrotizing enterocolitis rat model

Rentea, R. M., Liedel, J., Welak, S. R., Cassidy, L. D., Mayer, A. N., Pritchard, K. A., Oldham, K. T., & Gourlay, D. M. (2012) · Journal of Pediatric Surgery · doi:10.1016/j.jpedsurg.2012.03.018 · Cited by 58

Haptoglobin Polymorphism And Mortality In Patients With Tuberculosis

Kasvosve, I., Gomo, Z. A. R., Mvundura, E., Moyo, V. M., Saungweme, T., Khumalo, H., Gordeuk, V. R., Boelaert, J. R., Delanghe, J. R., Bacquer, D. D., et al. (2004) · Springer eBooks · doi:10.1007/978-3-642-18480-2_7 · Cited by 54

EGF receptor transactivation and MAP kinase mediate proteinase-activated receptor-2-induced chloride secretion in intestinal epithelial cells

van der Merwe, J. Q., Hollenberg, M. D., & MacNaughton, W. K. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00303.2007 · Cited by 48

Purification and preliminary characterization of the zonula occludens toxin receptor from human (CaCo2) and murine (IEC6) intestinal cell lines

Uzzau, S., Lu, R., Wang, W., Fiore, C., & Fasano, A. (2001) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2001.tb09437.x · Cited by 46

Haptoglobin polymorphism and schizophrenia: Genetic variation on chromosome 16

Maes, M. H. J., Delanghe, J., Bocchio‐Chiavetto, L., Bignotti, S., Tura, G. B., Pioli, R., Zanardini, R., & Altamura, C. A. (2001) · Psychiatry Research · doi:10.1016/s0165-1781(01)00298-0 · Cited by 46

Effects of Combined CCR5/Integrase Inhibitors-Based Regimen on Mucosal Immunity in HIV-Infected Patients Naïve to Antiretroviral Therapy: A Pilot Randomized Trial

Villar, S. S., Sainz, T., Ma, Z.-M., Utay, N. S., Chun, T., Mann, S. K., Kashuba, A. D. M., Siewe, B. T., Albanese, A. P., Troia-Cancio, P. V., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005381 · Cited by 46

Pneumococcal vaccination and risk of acute coronary syndromes in patients with pneumonia: population-based cohort study

Eurich, D. T., Johnstone, J., Minhas‐Sandhu, J. K., Marrie, T. J., & Majumdar, S. R. (2012) · Heart · doi:10.1136/heartjnl-2012-301743 · Cited by 44

Protease activated receptor 2: a new target for IBS treatment.

Bueno, L. P. (2008) · PubMed · Cited by 42

Expression of Zonulin, c-kit, and Glial Fibrillary Acidic Protein in Human Gliomas

Skardelly, M., Armbruster, F. P., Meixensberger, J., & Hilbig, H. (2009) · Translational Oncology · doi:10.1593/tlo.09115 · Cited by 38

Body fat changes and activity of tumor necrosis factor α system—a 5-year follow-up study

Olszanecka‐Glinianowicz, M., Chudek, J. T., Kocełak, P., Szromek, A. R., & Zahorska‐Markiewicz, B. (2010) · Metabolism · doi:10.1016/j.metabol.2010.04.023 · Cited by 38

Haptoglobin Polymorphism: A Novel Genetic Risk Factor for Celiac Disease Development and Its Clinical Manifestations

Papp, M., Földi, I., Nemes, É., Udvardy, M., Hársfalvi, J., Altorjay, I., Máté, I., Dinya, T., Várvölgyi, C., Barta, Z., et al. (2008) · Clinical Chemistry · doi:10.1373/clinchem.2007.098780 · Cited by 32

Helicobacter pylori infection and coronary artery disease.

Včev, A., Nakić, D., Mrđen, A., Mirat, J., Balen, S., Ružić, A., Peršić, V., Soldo, I., Matijević, M., Barbić, J., et al. (2007) · PubMed · Cited by 29

Genes regulating tight junctions and cell adhesion are altered in early experimental necrotizing enterocolitis

Högberg, N., Stenbäck, A., Carlsson, P., Wanders, A., & Lilja, H. E. (2013) · Journal of Pediatric Surgery · doi:10.1016/j.jpedsurg.2013.06.027 · Cited by 27

Haptoglobin Polymorphisms Are Associated with Crohn’s Disease, Disease Behavior, and Extraintestinal Manifestations in Hungarian Patients

Papp, M., Lakatos, P. L., Hungarian IBD Study Group, Palatka, K., Földi, I., Udvardy, M., Hársfalvi, J., Tornai, I., Vitális, Z., Dinya, T., et al. (2007) · Digestive Diseases and Sciences · doi:10.1007/s10620-006-9615-1 · Cited by 27

Haptoglobin phenotype appears to affect the pathogenesis of American trypanosomiasis

Calderoni, D. R., Andrade, T. D. S., & Grotto, H. Z. W. (2006) · Annals of Tropical Medicine and Parasitology · doi:10.1179/136485906x86356 · Cited by 16

Transitioning From Descriptive to Mechanistic Understanding of the Microbiome: The Need for a Prospective Longitudinal Approach to Predicting Disease

Martin, V., Leonard, M. M., Fiechtner, L. G., & Fasano, A. (2016) · The Journal of Pediatrics · doi:10.1016/j.jpeds.2016.08.049 · Cited by 14

Correction: Effects of Combined CCR5/Integrase Inhibitors-Based Regimen on Mucosal Immunity in HIV-Infected Patients Naïve to Antiretroviral Therapy: A Pilot Randomized Trial

Villar, S. S., Sainz, T., Ma, Z.-M., Utay, N. S., Chun, T., Mann, S. K., Kashuba, A. D. M., Siewe, B. T., Albanese, A., Troia-Cancio, P. V., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005540 · Cited by 13

Genetic Polymorphism and Idiopathic Generalized Epilepsy. Evidence of Interaction between Haptoglobin and ACP1 Systems

Gloria‐Bottini, F., Lucarelli, P., Saccucci, P., Cozzoli, E., Cerminara, C., Curatolo, P., & Bottini, E. (2008) · Neuropediatrics · doi:10.1055/s-0029-1202834 · Cited by 12

Haptoglobin genotypes in Chagas' disease

Jorge, S. E., Abreu, C. F., Guariento, M. E., & Sonati, M. D. F. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2009.09.020 · Cited by 10

Altered mannitol absorption in diabetic children.

MAGISTRIS, L. D., Secondulfo, M., Iafusco, D., Ag, C., Urio, A., Pontoni, G., & Carratu, R. (1996) · PubMed · Cited by 10

SPONTANEOUS DIABETES IN A DOG

KRUMBHAAR, E. B. (1916) · The Journal of Experimental Medicine · doi:10.1084/jem.24.4.361 · Cited by 6

Haptoglobin polymorphism, iron metabolism and mortality in HIV infection

Delanghe, J. R., Langlois, M. R., Boelaert, J. R., Van Acker, J., Van Wanzeele, F., van der Groen, G., Hemmer, R., Verhofstede, C., De Buyzere, M., De Bacquer, D., et al. (1998) · AIDS · doi:10.1097/00002030-199809000-00010 · Cited by 3

Koronare Herzerkrankung bei HIV-infizierten Personen

Neumann, T., Lülsdorf, K. A., Krings, P., Reinsch, N., & Erbel, R. (2010) · Herz · doi:10.1007/s00059-010-3410-7 · Cited by 2

Chronic inflammation in the etiology of disease across the life span

Furman, D., Campisi, J., Verdin, E., Carrera-Bastos, P., Targ, S., Franceschi, C., Ferrucci, L., Gilroy, D. W., Fasano, A., Miller, G. W., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0675-0 · Cited by 4,915

Impact of Bacterial Metabolites on Gut Barrier Function and Host Immunity: A Focus on Bacterial Metabolism and Its Relevance for Intestinal Inflammation

Gasaly, N., de Vos, P., & Hermoso, M. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.658354 · Cited by 611

Increased human intestinal barrier permeability plasma biomarkers zonulin and FABP2 correlated with plasma LPS and altered gut microbiome in anxiety or depression

Stevens, B. R., Goel, R., Seungbum, K., Richards, E. M., Holbert, R. C., Pepine, C. J., & Raizada, M. K. (2018) · Gut · doi:10.1136/gutjnl-2017-314759 · Cited by 508

Targeting zonulin and intestinal epithelial barrier function to prevent onset of arthritis

Tajik, N., Frech, M., Schulz, O., Schälter, F., Lucas, S., Azizov, V., Dürholz, K., Steffen, F., Omata, Y., Rings, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15831-7 · Cited by 515

All disease begins in the (leaky) gut: role of zonulin-mediated gut permeability in the pathogenesis of some chronic inflammatory diseases

Fasano, A. (2020) · F1000Research · doi:10.12688/f1000research.20510.1 · Cited by 496

Physiopathology of intestinal barrier and the role of zonulin

Caviglia, G. P., Rosso, C., Ribaldone, D. G., Dughera, F., Fagoonee, S., Astegiano, M., & Pellicano, R. (2019) · Minerva Biotecnologica · doi:10.23736/s1120-4826.19.02554-0 · Cited by 78

Elucidating the Significance of Zonulin in the Pathogenesis of Chronic Inflammatory Disorders: Emphasis on Intestinal Barrier Function and Tight Junction Regulation

Mohammadi-Kordkhayli, M., Mousavi, M. J., Camara-Lemarroy, C. R., Noorbakhsh, F., & Saboor-Yaraghi, A. A. (2024) · Current Medicinal Chemistry · doi:10.2174/0109298673335863240829060545 · Cited by 12

Zonulin and Its Regulation of Intestinal Barrier Function: The Biological Door to Inflammation, Autoimmunity, and Cancer

Fasano, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00003.2008 · Cited by 1,063

Intestinal permeability and its regulation by zonulin: Diagnostic and therapeutic implications

Fasano, A. (2012) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2012.08.012 · Cited by 402

Intestinal permeability and the zonulin pathway: tight junctions, mucosal immunity, dietary modulators and clinical relevance

Bermejo, D. G., García-Pérez-de-Sevilla, G., & Molina-López, A. (2026) · Frontiers in Nutrition · doi:10.3389/fnut.2026.1938370