Статті в журналах з теми "Secretory (E/S) proteins"
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Vicente, R. L., S. Marín, J. R. Valverde, C. Palomino, R. P. Mellado, and S. Gullón. "Functional identification of a Streptomyces lividans FKBP-like protein involved in the folding of overproduced secreted proteins." Open Biology 9, no. 10 (October 2019): 190201. http://dx.doi.org/10.1098/rsob.190201.
Повний текст джерелаBickel, Perry E., Philipp E. Scherer, and Harvey F. Lodish. "P-4: Identification and cloning of adipocyte-specific secretory proteins." Experimental and Clinical Endocrinology & Diabetes 104, S 02 (July 15, 2009): 68. http://dx.doi.org/10.1055/s-0029-1211547.
Повний текст джерелаAlbers, Sonja-Verena, Zalán Szabó, and Arnold J. M. Driessen. "Archaeal Homolog of Bacterial Type IV Prepilin Signal Peptidases with Broad Substrate Specificity." Journal of Bacteriology 185, no. 13 (July 1, 2003): 3918–25. http://dx.doi.org/10.1128/jb.185.13.3918-3925.2003.
Повний текст джерелаMarkwardt, Michele L., Andongfac Nkobena, Shi-Ying Ding, and Mark A. Rizzo. "Association with Nitric Oxide Synthase on Insulin Secretory Granules Regulates Glucokinase Protein Levels." Molecular Endocrinology 26, no. 9 (September 1, 2012): 1617–29. http://dx.doi.org/10.1210/me.2012-1183.
Повний текст джерелаGorr, Sven-Ulrik, Xue Fen Huang, Darrin J. Cowley, Regina Kuliawat, and Peter Arvan. "Disruption of disulfide bonds exhibits differential effects on trafficking of regulated secretory proteins." American Journal of Physiology-Cell Physiology 277, no. 1 (July 1, 1999): C121—C131. http://dx.doi.org/10.1152/ajpcell.1999.277.1.c121.
Повний текст джерелаKochanowski, Maciej, Joanna Dąbrowska, Mirosław Różycki, Jacek Sroka, Jacek Karamon, Aneta Bełcik, Weronika Korpysa-Dzirba, and Tomasz Cencek. "Proteomic Profiling and In Silico Characterization of the Secretome of Anisakis simplex Sensu Stricto L3 Larvae." Pathogens 11, no. 2 (February 14, 2022): 246. http://dx.doi.org/10.3390/pathogens11020246.
Повний текст джерелаTan, A., J. Bolscher, C. Feltkamp, and H. Ploegh. "Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S." Journal of Cell Biology 116, no. 6 (March 15, 1992): 1357–67. http://dx.doi.org/10.1083/jcb.116.6.1357.
Повний текст джерелаBlázquez, Mercedes, and Kathleen I. Shennan. "Basic mechanisms of secretion: sorting into the regulated secretory pathway." Biochemistry and Cell Biology 78, no. 3 (April 2, 2000): 181–91. http://dx.doi.org/10.1139/o00-010.
Повний текст джерелаDonovan, Kirk W., and Anthony Bretscher. "Tracking individual secretory vesicles during exocytosis reveals an ordered and regulated process." Journal of Cell Biology 210, no. 2 (July 13, 2015): 181–89. http://dx.doi.org/10.1083/jcb.201501118.
Повний текст джерелаHigh, S., S. S. Andersen, D. Görlich, E. Hartmann, S. Prehn, T. A. Rapoport, and B. Dobberstein. "Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion." Journal of Cell Biology 121, no. 4 (May 15, 1993): 743–50. http://dx.doi.org/10.1083/jcb.121.4.743.
Повний текст джерелаChaffin, W. LaJean. "Candida albicans Cell Wall Proteins." Microbiology and Molecular Biology Reviews 72, no. 3 (September 2008): 495–544. http://dx.doi.org/10.1128/mmbr.00032-07.
Повний текст джерелаGhyselinck, N. B., C. Jimenez, Y. Courty, and J. P. Dufaure. "Androgen-dependent messenger RNA(s) related to secretory proteins in the mouse epididymis." Reproduction 85, no. 2 (March 1, 1989): 631–39. http://dx.doi.org/10.1530/jrf.0.0850631.
Повний текст джерелаEwenstein, Bruce, and Yvonne Datta. "Regulated Secretion in Endothelial Cells: Biology and Clinical Implications." Thrombosis and Haemostasis 86, no. 11 (2001): 1148–55. http://dx.doi.org/10.1055/s-0037-1616043.
Повний текст джерелаMatsuno, Yuta, Yahia A. Amin, Kazuya Kusama, and Kazuhiko Imakawa. "Formation of fibrin at sites of conceptus adhesion in the ewe." Reproduction 161, no. 6 (June 1, 2021): 709–20. http://dx.doi.org/10.1530/rep-20-0531.
Повний текст джерелаRizzo, Mark A., та David W. Piston. "Regulation of β cell glucokinase by S-nitrosylation and association with nitric oxide synthase". Journal of Cell Biology 161, № 2 (21 квітня 2003): 243–48. http://dx.doi.org/10.1083/jcb.200301063.
Повний текст джерелаMeng, Zhen, Maria C. Edman, Pang-Yu Hsueh, Chiao-Yu Chen, Wannita Klinngam, Tanya Tolmachova, Curtis T. Okamoto, and Sarah F. Hamm-Alvarez. "Imbalanced Rab3D versus Rab27 increases cathepsin S secretion from lacrimal acini in a mouse model of Sjögren's Syndrome." American Journal of Physiology-Cell Physiology 310, no. 11 (June 1, 2016): C942—C954. http://dx.doi.org/10.1152/ajpcell.00275.2015.
Повний текст джерелаGrimes, M., and R. B. Kelly. "Intermediates in the constitutive and regulated secretory pathways released in vitro from semi-intact cells." Journal of Cell Biology 117, no. 3 (May 1, 1992): 539–49. http://dx.doi.org/10.1083/jcb.117.3.539.
Повний текст джерелаMiura, Natsuko, Aya Kirino, Satoshi Endo, Hironobu Morisaka, Kouichi Kuroda, Masahiro Takagi, and Mitsuyoshi Ueda. "Tracing Putative Trafficking of the Glycolytic Enzyme Enolase via SNARE-Driven Unconventional Secretion." Eukaryotic Cell 11, no. 8 (June 29, 2012): 1075–82. http://dx.doi.org/10.1128/ec.00075-12.
Повний текст джерелаCERVI, L., G. ROSSI, and D. T. MASIH. "Potential role for excretory–secretory forms of glutathione-S-transferase (GST) in Fasciola hepatica." Parasitology 119, no. 6 (December 1999): 627–33. http://dx.doi.org/10.1017/s003118209900517x.
Повний текст джерелаVillalón, Manuel, Dale E. Johnson, and Pedro Verdugo. "X-ray microanalysis of calcium content in secretory granules of goblet cell of the rabbit oviduct." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 2 (August 12, 1990): 178–79. http://dx.doi.org/10.1017/s042482010013448x.
Повний текст джерелаArber, S., K. H. Krause, and P. Caroni. "s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin." Journal of Cell Biology 116, no. 1 (January 1, 1992): 113–25. http://dx.doi.org/10.1083/jcb.116.1.113.
Повний текст джерелаBachhawat, A. K., and S. Pillai. "Distinct intracellular fates of membrane and secretory immunoglobulin heavy chains in a pre-B cell line." Journal of Cell Biology 115, no. 3 (November 1, 1991): 619–24. http://dx.doi.org/10.1083/jcb.115.3.619.
Повний текст джерелаGrimaldi, K. A., J. C. Hutton, and K. Siddle. "Production and characterization of monoclonal antibodies to insulin secretory granule membranes." Biochemical Journal 245, no. 2 (July 15, 1987): 557–66. http://dx.doi.org/10.1042/bj2450557.
Повний текст джерелаSampaio, Valéria da Silva, Ítalo Antônio Cotta Coutinho, Tiina Särkinen, and Maria Iracema Bezerra Loiola. "Secretory and ecological function of petiolar glands in." Australian Journal of Botany 70, no. 1 (November 23, 2021): 32–41. http://dx.doi.org/10.1071/bt21001.
Повний текст джерелаAppel, D., and C. Koch-Brandt. "Sorting of a secretory protein (gp80) to the apical surface of Caco-2 cells." Journal of Cell Science 107, no. 2 (February 1, 1994): 553–59. http://dx.doi.org/10.1242/jcs.107.2.553.
Повний текст джерелаBazer, FW. "Establishment of pregnancy in sheep and pigs." Reproduction, Fertility and Development 1, no. 3 (1989): 237. http://dx.doi.org/10.1071/rd9890237.
Повний текст джерелаWainwright, Eleanor, and Rebecca K. Shears. "Trichuris WAP and CAP proteins: Potential whipworm vaccine candidates?" PLOS Neglected Tropical Diseases 16, no. 12 (December 22, 2022): e0010933. http://dx.doi.org/10.1371/journal.pntd.0010933.
Повний текст джерелаKoul, Anil, Axel Choidas, Martin Treder, Anil K. Tyagi, Karl Drlica, Yogendra Singh, and Axel Ullrich. "Cloning and Characterization of Secretory Tyrosine Phosphatases of Mycobacterium tuberculosis." Journal of Bacteriology 182, no. 19 (October 1, 2000): 5425–32. http://dx.doi.org/10.1128/jb.182.19.5425-5432.2000.
Повний текст джерелаWatson, Patricia R., Edouard E. Galyov, Sue M. Paulin, Philip W. Jones, and Tim S. Wallis. "Mutation of invH, but Notstn, Reduces Salmonella-Induced Enteritis in Cattle." Infection and Immunity 66, no. 4 (April 1, 1998): 1432–38. http://dx.doi.org/10.1128/iai.66.4.1432-1438.1998.
Повний текст джерелаMAK, C. H., and R. C. KO. "DNA-binding activity in the excretory–secretory products ofTrichinella pseudospiralis(Nematoda: Trichinelloidea)." Parasitology 123, no. 3 (March 2001): 301–8. http://dx.doi.org/10.1017/s0031182001008459.
Повний текст джерелаKwon, Min Jin, Mark Arentshorst, Markus Fiedler, Florence L. M. de Groen, Peter J. Punt, Vera Meyer, and Arthur F. J. Ram. "Molecular genetic analysis of vesicular transport in Aspergillus niger reveals partial conservation of the molecular mechanism of exocytosis in fungi." Microbiology 160, no. 2 (February 1, 2014): 316–29. http://dx.doi.org/10.1099/mic.0.074252-0.
Повний текст джерелаPrašnikar, Erika, Jure Knez, Borut Kovačič, and Tanja Kunej. "Molecular signature of eutopic endometrium in endometriosis based on the multi-omics integrative synthesis." Journal of Assisted Reproduction and Genetics 37, no. 7 (May 30, 2020): 1593–611. http://dx.doi.org/10.1007/s10815-020-01833-3.
Повний текст джерелаZinkevičiūtė, Rūta, Raimundas Ražanskas, Algirdas Kaupinis, Neringa Macijauskaitė, Evaldas Čiplys, Gunnar Houen, and Rimantas Slibinskas. "Yeast Secretes High Amounts of Human Calreticulin without Cellular Stress." Current Issues in Molecular Biology 44, no. 5 (April 19, 2022): 1768–87. http://dx.doi.org/10.3390/cimb44050122.
Повний текст джерелаFukuda, M. "Rab27 and its effectors in secretory granule exocytosis: a novel docking machinery composed of a Rab27·effector complex." Biochemical Society Transactions 34, no. 5 (October 1, 2006): 691–95. http://dx.doi.org/10.1042/bst0340691.
Повний текст джерелаBrewer, Joseph W., and Suzanne Jackowski. "UPR-Mediated Membrane Biogenesis in B Cells." Biochemistry Research International 2012 (2012): 1–7. http://dx.doi.org/10.1155/2012/738471.
Повний текст джерелаSPINNER, W. G., F. J. THOMPSON, D. C. EMERY, and M. E. VINEY. "Characterization of genes with a putative key role in the parasitic lifestyle of the nematode Strongyloides ratti." Parasitology 139, no. 10 (May 2, 2012): 1317–28. http://dx.doi.org/10.1017/s0031182012000637.
Повний текст джерелаCantacessi, Cinzia, Jason Mulvenna, Neil D. Young, Martin Kasny, Petr Horak, Ammar Aziz, Andreas Hofmann, Alex Loukas, and Robin B. Gasser. "A Deep Exploration of the Transcriptome and “Excretory/Secretory” Proteome of Adult Fascioloides magna." Molecular & Cellular Proteomics 11, no. 11 (August 16, 2012): 1340–53. http://dx.doi.org/10.1074/mcp.m112.019844.
Повний текст джерелаShishodia, Sonia Kumari, and Jata Shankar. "Exploration of Mycelial Proteins from Aspergillus terreus Revealed Ribosome Biogenesis and Antioxidant Enzymes." Current Proteomics 17, no. 5 (July 16, 2020): 433–45. http://dx.doi.org/10.2174/1570164617666191004163734.
Повний текст джерелаNagano, Isao, Zhiliang Wu, and Yuzo Takahashi. "Species-Specific Antibody Responses to the Recombinant 53-Kilodalton Excretory and Secretory Proteins in Mice Infected with Trichinella spp." Clinical and Vaccine Immunology 15, no. 3 (January 9, 2008): 468–73. http://dx.doi.org/10.1128/cvi.00467-07.
Повний текст джерелаLemons, Paula P., Dong Chen, Audrey M. Bernstein, Mark K. Bennett, and S. W. Whiteheart. "Regulated Secretion in Platelets: Identification of Elements of the Platelet Exocytosis Machinery." Blood 90, no. 4 (August 15, 1997): 1490–500. http://dx.doi.org/10.1182/blood.v90.4.1490.
Повний текст джерелаLemons, Paula P., Dong Chen, Audrey M. Bernstein, Mark K. Bennett, and S. W. Whiteheart. "Regulated Secretion in Platelets: Identification of Elements of the Platelet Exocytosis Machinery." Blood 90, no. 4 (August 15, 1997): 1490–500. http://dx.doi.org/10.1182/blood.v90.4.1490.1490_1490_1500.
Повний текст джерелаMARÉCHAL, Alexandre, Pierre-Luc TANGUAY, Mario CALLEJO, Renée GUÉRIN, Guy BOILEAU, and Luis A. ROKEACH. "Cell viability and secretion of active proteins in Schizosaccharomyces pombe do not require the chaperone function of calnexin." Biochemical Journal 380, no. 2 (June 1, 2004): 441–48. http://dx.doi.org/10.1042/bj20031546.
Повний текст джерелаBuerth, Christoph, Clemens J. Heilmann, Frans M. Klis, Chris G. de Koster, Joachim F. Ernst, and Denis Tielker. "Growth-dependent secretome of Candida utilis." Microbiology 157, no. 9 (September 1, 2011): 2493–503. http://dx.doi.org/10.1099/mic.0.049320-0.
Повний текст джерелаPian, M. S., and L. G. Dobbs. "Activation of G proteins may inhibit or stimulate surfactant secretion in rat alveolar type II cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 266, no. 4 (April 1, 1994): L375—L381. http://dx.doi.org/10.1152/ajplung.1994.266.4.l375.
Повний текст джерелаCao, Zhe, and Sabine Banniza. "Cross-Kingdom Gene Coexpression Analysis Using a Stemphylium botryosum–Lens ervoides System Revealed Plasticity of Intercommunication Between the Pathogen Secretome and the Host Immune Systems." Molecular Plant-Microbe Interactions® 34, no. 12 (December 2021): 1365–77. http://dx.doi.org/10.1094/mpmi-05-21-0112-r.
Повний текст джерелаKlumperman, Judith, Regina Kuliawat, Janice M. Griffith, Hans J. Geuze, and Peter Arvan. "Mannose 6–Phosphate Receptors Are Sorted from Immature Secretory Granules via Adaptor Protein AP-1, Clathrin, and Syntaxin 6–positive Vesicles." Journal of Cell Biology 141, no. 2 (April 20, 1998): 359–71. http://dx.doi.org/10.1083/jcb.141.2.359.
Повний текст джерелаBryant, Nia J., and Tom H. Stevens. "Vacuole Biogenesis in Saccharomyces cerevisiae: Protein Transport Pathways to the Yeast Vacuole." Microbiology and Molecular Biology Reviews 62, no. 1 (March 1, 1998): 230–47. http://dx.doi.org/10.1128/mmbr.62.1.230-247.1998.
Повний текст джерелаLontok, Erik, Emily Corse, and Carolyn E. Machamer. "Intracellular Targeting Signals Contribute to Localization of Coronavirus Spike Proteins near the Virus Assembly Site." Journal of Virology 78, no. 11 (June 1, 2004): 5913–22. http://dx.doi.org/10.1128/jvi.78.11.5913-5922.2004.
Повний текст джерелаNorman, J. C., L. S. Price, A. J. Ridley, and A. Koffer. "The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways." Molecular Biology of the Cell 7, no. 9 (September 1996): 1429–42. http://dx.doi.org/10.1091/mbc.7.9.1429.
Повний текст джерелаPalacín, Arantxa, Ricardo de la Fuente, Inmaculada Valle, Luis A. Rivas, and Rafael P. Mellado. "Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion." Microbiology 149, no. 9 (September 1, 2003): 2435–42. http://dx.doi.org/10.1099/mic.0.26313-0.
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