Dynamic changes in protein concentrations of keratins in crop milk and related gene expression in pigeon crops during different incubation and chick rearing stages

References

• Anderson, T. R., G. L. Mayer, N. Hebert, and C. S. Nicoll. 1987. “Interactions among Prolactin, Epidermal Growth Factor, and Proinsulin on the Growth and Morphology of the Pigeon Crop-sac Mucosal Epithelium in Vivo.” Endocrinology 120 (4): 1258–1264. doi:10.1210/endo-120-4-1258.
   PubMed Web of Science ®Google Scholar
• Anderson, T. R., D. S. Pitts, and C. S. Nicoll. 1984. “Prolactin’s Mitogenic Action on the Pigeon Prop-sac Mucosal Epithelium Involves Direct and Indirect Mechanisms.” General and Comparative Endocrinology 54 (2): 236–246. doi:10.1016/0016-6480(84)90177-1.
   PubMed Web of Science ®Google Scholar
• Bader, B. L., T. M. Magin, M. Hatzfeld, and W. W. Franke. 1986. “Amino Acid Sequence and Gene Organization of Cytokeratin No. 19, an Exceptional Tail-less Intermediate Filament Protein.” EMBO Journal 5 (8): 1865–1875. doi:10.1002/j.1460-2075.1986.tb04438.x.
   PubMed Web of Science ®Google Scholar
• Batta, K., E. L. Rugg, N. J. Wilson, N. West, H. Goodyear, E. B. Lane, M. Gratian, P. Dopping-Hepenstal, C. Moss, and R. A. Eady. 2000. “A Keratin 14 ‘Knockout’ Mutation in Recessive Epidermolysis Bullosa Simplex Resulting in Less Severe Disease.” British Journal of Dermatology 143 (3): 621–627. doi:10.1111/j.1365-2133.2000.03722.x.
   PubMed Web of Science ®Google Scholar
• Beams, H. W., and R. K. Meyer. 1931. “The Formation of Pigeon “Milk”.” Physiological Zoology 4 (3): 486–500. doi:10.1086/physzool.4.3.30151154.
   Google Scholar
• Bharathi, L., K. B. Shenoy, and S. N. Hegde. 1997. “Biochemical Differences between Crop Tissue and Crop Milk of Pigeons (Columba Livia).” Comparative Biochemistry & Physiology Part A Physiology 116 (1): 51–55. doi:10.1016/S0300-9629(96)00116-8.
   PubMed Web of Science ®Google Scholar
• Birkenkamp-Demtroder, K., S. A. Hahn, F. Mansilla, K. Thorsen, A. Maghnouj, R. Christensen, B. Oster, and T. F. Orntoft. 2013. “Keratin 23 (KRT23) Knockdown Decreases Proliferation and Affects the DNA Damage Response of Colon Cancer Cells.” Plos One 8 (9): e73593. doi:10.1371/journal.pone.0073593.
   PubMed Web of Science ®Google Scholar
• Birkenkamp-Demtroder, K., F. Mansilla, F. B. Sorensen, M. Kruhoffer, T. Cabezón, L. L. Christensen, L. A. Aaltonen, H. W. Verspaget, and T. F. Orntoft. 2007. “Phosphoprotein Keratin 23 Accumulates in MSS but Not MSI Colon Cancers in Vivo and Impacts Viability and Proliferation in Vitro.” Molecular Oncology 1 (2): 181–195. doi:10.1016/j.molonc.2007.05.005.
   PubMed Web of Science ®Google Scholar
• Caulin, C., C. F. Ware, T. M. Magin, and R. G. Oshima. 2000. “Keratin-dependent, Epithelial Resistance to Tumor Necrosis Factor-induced Apoptosis.” Journal of Cell Biology 149 (1): 17–22. doi:10.1083/jcb.149.1.17.
   PubMed Web of Science ®Google Scholar
• Chen, M. J., N. X. Pan, X. Q. Wang, H. C. Yan, and C. Q. Gao. 2020. “Methionine Promotes Crop Milk Protein Synthesis through the JAK2-STAT5 Signaling during Lactation of Domestic Pigeons (Columba Livia).” Food Function 11 (12): 10786–10798. doi:10.1039/D0FO02257H.
   PubMed Web of Science ®Google Scholar
• Chou, Y. H., and R. D. Goldman. 2000. “Intermediate Filaments on the Move.” Journal of Cell Biology 150 (3): F101–F106.
   PubMed Web of Science ®Google Scholar
• Cooper, D., A. Schermer, and T. T. Sun. 1985. “Classification of Human Epithelia and Their Neoplasms Using Monoclonal Antibodies to Keratins: Strategies, Applications, and Limitations.” Laboratory Investigation 52 (3): 243–256.
   PubMed Web of Science ®Google Scholar
• Dong, X. Y., Y. M. Wang, L. Dai, M. M. Azzam, C. Wang, and X. T. Zou. 2012. “Post Hatch Development of Intestinal Morphology and Digestive Enzyme Activities in Domestic Pigeons (Columba Livia).” Poultry Science 91 (8): 1886–1892. doi:10.3382/ps.2011-02091.
   PubMed Web of Science ®Google Scholar
• Dumont, J. N. 1965. “Prolactin-induced Cytologic Changes in the Mucosa of the Pigeon Crop during Crop Milk Formation.” Z Zellforsch Mikrosk Anat 68 (6): 755–782. doi:10.1007/BF00343930.
   PubMedGoogle Scholar
• Ferrando, R., R. Wolter, C. Fourlon, and M. Morice. 1971. “Pigeon Milk.” Annales de la Nutrition et de l’alimentation 25 (3): 241–251.
   PubMedGoogle Scholar
• Friedl, P., and S. Alexander. 2011. “Cancer Invasion and the Microenvironment: Plasticity and Reciprocity.” Cell 147 (5): 992–1009. doi:10.1016/j.cell.2011.11.016.
   PubMed Web of Science ®Google Scholar
• Fuchs, E., and D. W. Cleveland. 1998. “A Structural Scaffolding of Intermediate Filaments in Health and Disease.” Science 279 (5350): 514–519. doi:10.1126/science.279.5350.514.
   PubMed Web of Science ®Google Scholar
• Fuchs, E., and H. Green. 1980. “Changes in Keratin Gene Expression during Terminal Differentiation of the Keratinocyte.” Cell 19 (4): 1033–1042.
   PubMed Web of Science ®Google Scholar
• Gillespie, M. J., T. M. Crowley, V. R. Haring, S. L. Wilson, J. A. Harper, J. S. Payne, and R. J. Moore. 2013. “Transcriptome Analysis of Pigeon Milk Production-role of Cornification and Triglyceride Synthesis Genes.” BMC Genomics 14 (1): 169–179. doi:10.1186/1471-2164-14-169.
   PubMed Web of Science ®Google Scholar
• Gillespie, M. J., V. R. Haring, K. A. Mccoll, P. Monaghan, J. A. Donald, K. R. Nicholas, R. J. Moore, and T. M. Crowley. 2011. “Histological and Global Gene Expression Analysis of the ‘Lactating’ Pigeon Crop.” BMC Genomics 12 : 452–461. doi:10.1186/1471-2164-12-452.
   PubMed Web of Science ®Google Scholar
• Horseman, N. D., and J. D. Buntin. 1995. “Regulation of Pigeon Crop Milk Secretion and Parental Behaviors by Prolactin.” Annual Review of Nutrition 15 : 213–238. doi:10.1146/annurev.nu.15.070195.001241.
   PubMed Web of Science ®Google Scholar
• Hu, X. C., C. Q. Gao, X. H. Wang, H. C. Yan, Z. S. Chen, and X. Q. Wang. 2016. ““Crop Milk Protein Is Synthesised following Activation of the IRS1/Akt/TOR Signalling Pathway in the Domestic Pigeon (Columba Livia)”. British Poultry Science 57 (6): 855–862. doi:10.1080/00071668.2016.1219694.
   PubMed Web of Science ®Google Scholar
• Kao, W. W., C. Y. Liu, R. L. Converse, A. Shiraishi, C. W. Kao, M. Ishizaki, T. Doetschman, and J. DuVy. 1996. “Keratin 12-deficient Mice Have Fragile Corneal Epithelia.” Investigative Ophthalmology and Visual Science 37 (13): 2572–2584.
   PubMed Web of Science ®Google Scholar
• Karsten, U., G. Papsdorf, G. Roloff, P. Stolley, H. Abel, I. Walther, and H. Weiss. 1985. “Monoclonal Anti-cytokeratin Antibody from A Hybridoma Clone Generated by Electrofusion.” European Journal of Cancer and Clinical Oncology 21 (6): 733–740. doi:10.1016/0277-5379(85)90271-8.
   PubMedGoogle Scholar
• Kim, D., C. N. Brocker, S. Takahashi, T. Yagai, T. Kim, G. Xie, H. Wang, A. Qu, and F. J. Gonzalez. 2019. “Keratin 23 Is A Peroxisome Proliferator-activated Receptor Alpha-dependent, MYC-amplified Oncogene that Promotes Hepatocyte Proliferation.” Hepatology 70 (1): 154–167. doi:10.1002/hep.30530.
   PubMed Web of Science ®Google Scholar
• Kim, S., P. Wong, and P. A. Coulombe. 2006. “A Keratin Cytoskeletal Protein Regulates Protein Synthesis and Epithelial Cell Growth.” Nature 441 (7091): 362–365. doi:10.1038/nature04659.
   PubMed Web of Science ®Google Scholar
• Ku, N. O., J. M. Darling, S. M. Krams, C. O. Esquivel, E. B. KeeVe, R. K. Sibley, Y. M. Lee, T. L. Wright, and M. B. Omary. 2003a. “Keratin 8 and 18 Mutations are Risk Factors for Developing Liver Disease of Multiple Etiologies.” Proceedings of the National Academy of Sciences of the United States of American 100 ( 10): 6063–6068.
   Google Scholar
• Ku, N. O., R. M. Soetikno, and M. B. Omary. 2003b. “Keratin Mutation in Transgenic Mice Predisposes to Fas but Not TNF-induced Apoptosis and Massive Liver Injury.” Hepatology 37 (5): 1006–1014. doi:10.1053/jhep.2003.50181.
   PubMed Web of Science ®Google Scholar
• Le, H. Q., S. Ghatak, C. Y. Yeung, F. Tellkamp, C. Günschmann, C. Dieterich, A. Yeroslaviz, et al. 2016. “Mechanical Regulation of Transcription Controls Polycomb-mediated Gene Silencing during Lineage Commitment.” Nature Cell Biology 18 (8): 864–875. doi:10.1038/ncb3387.
   PubMed Web of Science ®Google Scholar
• Li, X. L., X. Dong, Y. Xue, C. F. Li, W. L. Gou, and Q. Chen. 2014. “Increased Expression Levels of E-cadherin, Cytokeratin 18 and 19 Observed in Preeclampsia Were Not Correlated with Disease Severity.” Placenta 35 (8): 625–631. doi:10.1016/j.placenta.2014.04.010.
   PubMed Web of Science ®Google Scholar
• Lindberg, K., and J. G. Rheinwald. 1989. “Suprabasal 40 Kd Keratin (K19) Expression as an Immunohistologic Marker of Premalignancy in Oral Epithelium.” American Journal of Pathology 134 (1): 89–98.
   PubMed Web of Science ®Google Scholar
• Livak, K. J., and T. D. Schmittgen. 2001. “Analysis of Relative Gene Expression Data Using Real-time Quantitative PCR and the 2(-Delta Delta C(T)) Method.” Methods 25 (4): 402–408. doi:10.1006/meth.2001.1262.
   PubMed Web of Science ®Google Scholar
• Lu, L., P. S. Reinach, and W. W. Kao. 2001. “Corneal Epithelial Wound Healing.” Experimental Biology and Medicine 226 (7): 653–664. doi:10.1177/153537020222600711.
   Web of Science ®Google Scholar
• Magin, T. M., P. Vijayaraj, and R. E. Leube. 2007. “Structural and Regulatory Functions of Keratins.” Experimental Cell Research 313 (10): 2021–2032. doi:10.1016/j.yexcr.2007.03.005.
   PubMed Web of Science ®Google Scholar
• McLean, W. H., and E. B. Lane. 1995. “Intermediate Filaments in Disease.” Current Opinion in Cell Biology 7 (1): 118–125. doi:10.1016/0955-0674(95)80053-0.
   PubMed Web of Science ®Google Scholar
• Mikami, T., J. Cheng, S. Maruyama, T. Kobayashi, A. Funayama, M. Yamazaki, H. A. Adeola, L. Wu, S. Shingaki, and C. Saito. 2011. “Emergence of Keratin 17 Vs. Loss of Keratin 13: Their Reciprocal Immunohistochemical Profiles in Oral Carcinoma in Situ.” Oral Oncology 47 (6): 497–503. doi:10.1016/j.oraloncology.2011.03.015.
   PubMed Web of Science ®Google Scholar
• Moll, R., M. Divo, and L. Langbein. 2008. “The Human Keratins: Biology and Pathology.” Histochemistry and Cell Biology 129 (6): 705–733. doi:10.1007/s00418-008-0435-6.
   PubMed Web of Science ®Google Scholar
• Moll, R., W. W. Franke, D. L. Schiller, B. Geiger, and R. Krepler. 1982. “The Catalog of Human Cytokeratins: Patterns of Expression in Normal Epithelia, Tumors and Cultured Cells.” Cell 31 (1): 11–24. doi:10.1016/0092-8674(82)90400-7.
   PubMed Web of Science ®Google Scholar
• Moll, R., D. L. Schiller, and W. W. Franke. 1990. “Identification of Protein IT of the Intestinal Cytoskeleton as A Novel Type I Cytokeratin with Unusual Properties and Expression Patterns.” Journal Cell Biology 111 (2): 567–580. doi:10.1083/jcb.111.2.567.
   PubMed Web of Science ®Google Scholar
• Ness, S. L., W. Edelmann, T. D. Jenkins, W. Liedtke, A. K. Rustgi, and R. Kucherlapati. 1998. “Mouse Keratin 4 Is Necessary for Internal Epithelial Integrity.” Journal of Biological Chemistry 273 (37): 23904. doi:10.1074/jbc.273.37.23904.
   PubMed Web of Science ®Google Scholar
• Obara, S., G. Yamamoto, S. Hayashi, T. Jun-Ichi, T. Isobe, C. Hokazono, R. Yasuhara, T. Irie, and T. Tachikawa. 2013. “Expression of Keratin 75 (k6hf) in Oral Squamous Cell Carcinoma.” Dental Medicine Research 31 (1): 28–34. doi:10.7881/dentalmedres.31.28.
   Google Scholar
• Oshima, R. G. 2007. “Intermediate Flaments: A Historical Perspective.” Experimental Cell Research 313 (10): 1981–1994. doi:10.1016/j.yexcr.2007.04.007.
   PubMed Web of Science ®Google Scholar
• Owens, D. W., and E. B. Lane. 2003. “The Quest for the Function of Simple Epithelial Keratins.” Bioessays 25 (8): 748–758. doi:10.1002/bies.10316.
   PubMed Web of Science ®Google Scholar
• Perone, Y., A. J. Farrugia, A. Rodríguez-Meira, B. Győrffy, C. Ion, A. Uggetti, A. Chronopoulos, et al. 2019. “SREBP1 Drives Keratin-80-dependent Cytoskeletal Changes and Invasive Behavior in Endocrine-resistant ERα Breast Cancer.” Nature Communications 10 (1): 2115. doi:10.1038/s41467-019-09676-y.
   PubMed Web of Science ®Google Scholar
• Pitz, S., and R. Moll. 2002. “Intermediate-filament Expression in Ocular Tissue.” Progress in Retinal and Eye Research 21 (2): 241–262. doi:10.1016/S1350-9462(01)00025-8.
   PubMed Web of Science ®Google Scholar
• Pukac, L. A., and N. D. Horseman. 1984. “Regulation of Pigeon Crop Gene Expression by Prolactin.” Endocrinology 114 (5): 1718–1724. doi:10.1210/endo-114-5-1718.
   PubMed Web of Science ®Google Scholar
• Sales, J., and G. Janssens. 2003. “Nutrition of the Domestic Pigeon (Columba Livia Domestica).” World Poultry Science Journal 59 : 221–232. doi:10.1079/WPS20030014.
   Web of Science ®Google Scholar
• Schermer, A., S. Galvin, and T. T. Sun. 1986. “Differentiation-related Expression of a Major 64 K Corneal Keratin in Vivo and in Culture Suggests Limbal Location of Corneal Epithelial Stem Cells.” Journal of Cell Biology 103 (1): 49–62. doi:10.1083/jcb.103.1.49.
   PubMed Web of Science ®Google Scholar
• Shao, Y., W. Ma, F. Ji, X. Sun, S. Du, X. Li, Q. Li, and Z. Wang. 2021. “Exploration of Proteomics Analysis of Crop Milk in Pigeons (Columba Livia) during the Lactation Period.” ACS Omega 6 (42): 27726–27736. doi:10.1021/acsomega.1c02977.
   PubMed Web of Science ®Google Scholar
• Shetty, S., and S. N. Hegde. 1991. “Changes in Lipids of Pigeon “Milk” in the First Week of Its Secretion.” Lipids 26 (5): 930–933. doi:10.1007/BF02535979.
   Web of Science ®Google Scholar
• Starmann, J., M. Falth, W. Spindelbock, K. L. Lanz, C. Lackner, K. Zatloukal, M. Trauner, and H. Sültmann. 2012. “Gene Expression Profiling Unravels Cancer-related Hepatic Molecular Signatures in Steatohepatitis but Not in Steatosis.” Plos One 7 (10): e46584. doi:10.1371/journal.pone.0046584.
   PubMed Web of Science ®Google Scholar
• Stasiak, P. C., P. E. Purkis, I. M. Leigh, and E. B. Lane. 1989. “Keratin 19: Predicted Amino Acid Sequence and Broad Tissue Distribution Suggest It Evolved from Keratinocyte Keratins.” Journal of Investigative Dermatology 92 (5): 707–716. doi:10.1016/0022-202X(89)90186-3.
   PubMed Web of Science ®Google Scholar
• Tong, X., and P. A. Coulombe. 2006. “Keratin 17 Modulates Hair Follicle Cycling in A TNFalpha-dependent Fashion.” Genes and Development 20 (10): 1353–1364. doi:10.1101/gad.1387406.
   PubMed Web of Science ®Google Scholar
• Wang, K. J., X. Q. Xu, Y. F. Nie, L. Dai, P. Wang, and J. Zhang. 2009. “Identification of Tumor-associated Antigens by Using SEREX in Hepatocellular Carcinoma.” Cancer Letters 281 (2): 144–150. doi:10.1016/j.canlet.2009.02.037.
   PubMed Web of Science ®Google Scholar
• Wan, X. P., P. Xie, Z. Bu, X. T. Zou, and D. Q. Gong. 2019. “Prolactin Induces Lipid Synthesis of Organ-cultured Pigeon Crops.” Poultry Science 98 (4): 1842–1853. doi:10.3382/ps/pey540.
   PubMed Web of Science ®Google Scholar
• Waschke, J. 2008. “The Desmosome and Pemphigus.” Histochemistry and Cell Biology 130 (1): 21–54. doi:10.1007/s00418-008-0420-0.
   PubMed Web of Science ®Google Scholar
• Wawersik, M. J., S. Mazzalupo, D. Nguyen, and P. A. Coulombe. 2001. “Increased Levels of Keratin 16 Alter Epithelialization Potential of Mouse Skin Keratinocytes in Vivo and Ex Vivo.” Molecular Biology of the Cell 12 (11): 3439–3450. doi:10.1091/mbc.12.11.3439.
   PubMed Web of Science ®Google Scholar
• Weiss, R. A., R. Eichner, and T. T. Sun. 1984. “Monoclonal Antibody Analysis of Keratin Expression in Epidermal Diseases: A 49- and 56-Kdalton Keratin as Molecular Markers for Hyperproliferative Keratinocytes.” Journal of Cell Biology 98 (4): 1397–1406. doi:10.1083/jcb.98.4.1397.
   PubMed Web of Science ®Google Scholar
• Winter, H., L. Langbein, S. Praetzel, M. Jacobs, M. A. Rogers, I. M. Leigh, N. Tidman, and J. Schweizer. 1998. “A Novel Human Type II Cytokeratin, K6hf, Specifically Expressed in the Companion Layer of the Hair Follicle.” Journal of Investigative Dermatology 111 (6): 955–962. doi:10.1046/j.1523-1747.1998.00456.x.
   PubMed Web of Science ®Google Scholar
• Wojcik, S. M., D. S. Bundman, and D. R. Roop. 2000. “Delayed Wound Healing in Keratin 6a Knockout Mice.” Molecular Biology of the Cell 20 (14): 5248–5255. doi:10.1128/MCB.20.14.5248-5255.2000.
   Web of Science ®Google Scholar
• Wolosin, J. M., M. T. Budak, and M. A. Akinci. 2004. “Ocular Surface Epithelial and Stem Cell Development.” International Journal of Developmental Biology 48 (8–9): 981–991. doi:10.1387/ijdb.041876jw.
   PubMed Web of Science ®Google Scholar
• Xie, W. Y., Z. Fu, N. X. Pan, H. C. Yan, X. Q. Wang, and C. Q. Gao. 2019. “Leucine Promotes the Growth of Squabs by Increasing Crop Milk Protein Synthesis through the TOR Signaling Pathway in the Domestic Pigeon (Columba Livia).” Poultry Science 98 (11): 5514–5524. doi:10.3382/ps/pez296.
   PubMed Web of Science ®Google Scholar
• Xie, P., X. Y. Jiang, Z. Bu, S. Y. Fu, S. Y. Zhang, and Q. P. Tang. 2016. “Free Choice Feeding of Whole Grains in Meat-Type Pigeons: I. Effect on Performance, Carcass Traits, and Organ Development.” British Poultry Science 57 (5): 699–706. doi:10.1080/00071668.2016.1206191.
   PubMed Web of Science ®Google Scholar
• Xie, P., X. P. Wan, Z. Bu, E. J. Diao, D. Q. Gong, and X. T. Zou. 2018. “Changes in Hormone Profiles, Growth Factors and mRNA Expression of the Related Receptors in Crop Tissue, Relative Organ Weight, and Serum Biochemical Parameters in the Domestic Pigeon (Columba Livia) during Incubation and Chick-rearing Periods under Artificial Farming Conditions.” Poultry Science 97 (6): 2189–2202. doi:10.3382/ps/pey061.
   PubMed Web of Science ®Google Scholar
• Xie, P., X. P. Wang, Z. Bu, and X. T. Zou. 2017. “Differential Expression of Fatty Acid Transporters and Fatty Acid Synthesis-Related Genes in Crop Tissues of Male and Female Pigeons (Columba Livia Domestica) during Incubation and Chick Rearing.” British Poultry Science 58 (5): 594–602. doi:10.1080/00071668.2017.1357798.
   PubMed Web of Science ®Google Scholar
• Xie, P., Y. Wang, C. Wang, C. Yuan, and X. T. Zou. 2013. “Effect of Different Fat Sources in Parental Diets on Growth Performance, Villus Morphology, Digestive Enzymes and Colorectal Microbiota in Pigeon Squabs.” Archives of Animal Nutrition 67 (2): 147–160. doi:10.1080/1745039X.2013.776329.
   PubMed Web of Science ®Google Scholar
• Zatloukal, K., C. Stumptner, M. Lehner, H. Denk, H. Baribault, L. G. Eshkind, and W. W. Franke. 2000. “Cytokeratin 8 Protects from Hepatotoxicity, and Its Ratio to Cytokeratin 18 Determines the Ability of Hepatocytes to Form Mallory Bodies.” American Journal of Pathology 156 (4): 1263–1274. doi:10.1016/S0002-9440(10)64997-8.
   PubMed Web of Science ®Google Scholar
• Zhang, J. S., L. Wang, H. Huang, M. Nelson, and D. I. Smith. 2001. “Keratin 23 (K23), a Novel Acidic Keratin, Is Highly Induced by Histone Deacetylase Inhibitors during Differentiation of Pancreatic Cancer Cells.” Genes Chromosomes Cancer 30 (2): 123–135. doi:10.1002/1098-2264(2000)9999:9999<::AID-GCC1070>3.0.CO;2-W.
   PubMed Web of Science ®Google Scholar
• Zhou, Q., M. Cadrin, H. Herrmann, C. H. Chen, R. J. Chalkley, A. L. Burlingame, and M. B. Omary. 2006. “Keratin 20 Serine 13 Phosphorylation Is A Stress and Intestinal Goblet Cell Marker.” Journal of Biological Chemistry 281 (24): 16453–16461. doi:10.1074/jbc.M512284200.
   PubMed Web of Science ®Google Scholar
• Zhou, Q., D. M. Toivola, N. Feng, H. B. Greenberg, W. W. Franke, and M. B. Omary. 2003. “Keratin 20 Helps Maintain Intermediate Filament Organization in Intestinal Epithelia.” Molecular Biology of the Cell 14 (7): 2959–2971. doi:10.1091/mbc.e03-02-0059.
   PubMed Web of Science ®Google Scholar