Zeitschriftenartikel zum Thema „HSP27 extracellulaire“
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Gabai, Vladimir L., und Michael Y. Sherman. „Invited Review: Interplay between molecular chaperones and signaling pathways in survival of heat shock“. Journal of Applied Physiology 92, Nr. 4 (01.04.2002): 1743–48. http://dx.doi.org/10.1152/japplphysiol.01101.2001.
Der volle Inhalt der QuelleStope, Matthias B., Gerd Klinkmann, Karoline Diesing, Dominique Koensgen, Martin Burchardt und Alexander Mustea. „Heat Shock Protein HSP27 Secretion by Ovarian Cancer Cells Is Linked to Intracellular Expression Levels, Occurs Independently of the Endoplasmic Reticulum Pathway and HSP27’s Phosphorylation Status, and Is Mediated by Exosome Liberation“. Disease Markers 2017 (2017): 1–12. http://dx.doi.org/10.1155/2017/1575374.
Der volle Inhalt der QuelleWinter, Julia, Elke Hammer, Jacqueline Heger, Heinz-Peter Schultheiss, Ursula Rauch, Ulf Landmesser und Andrea Dörner. „Adenine Nucleotide Translocase 1 Expression Is Coupled to the HSP27-Mediated TLR4 Signaling in Cardiomyocytes“. Cells 8, Nr. 12 (06.12.2019): 1588. http://dx.doi.org/10.3390/cells8121588.
Der volle Inhalt der QuelleSinger, Debora, Can Pascal Wulff, Matthias B. Stope und Sander Bekeschus. „Extracellular Heat Shock Protein 27 Is Released by Plasma-Treated Ovarian Cancer Cells and Affects THP-1 Monocyte Activity“. Plasma 5, Nr. 4 (06.12.2022): 569–78. http://dx.doi.org/10.3390/plasma5040040.
Der volle Inhalt der QuelleGrotegut, Pia, Sandra Kuehn, H. Burkhard Dick und Stephanie C. Joachim. „Destructive Effect of Intravitreal Heat Shock Protein 27 Application on Retinal Ganglion Cells and Neurofilament“. International Journal of Molecular Sciences 21, Nr. 2 (15.01.2020): 549. http://dx.doi.org/10.3390/ijms21020549.
Der volle Inhalt der QuelleJohnson, John D., Jay Campisi, Craig M. Sharkey, Sarah L. Kennedy, Molly Nickerson und Monika Fleshner. „Adrenergic receptors mediate stress-induced elevations in extracellular Hsp72“. Journal of Applied Physiology 99, Nr. 5 (November 2005): 1789–95. http://dx.doi.org/10.1152/japplphysiol.00390.2005.
Der volle Inhalt der QuelleGrotegut, Pia, Philipp Johannes Hoerdemann, Sabrina Reinehr, Nupur Gupta, H. Burkhard Dick und Stephanie C. Joachim. „Heat Shock Protein 27 Injection Leads to Caspase Activation in the Visual Pathway and Retinal T-Cell Response“. International Journal of Molecular Sciences 22, Nr. 2 (06.01.2021): 513. http://dx.doi.org/10.3390/ijms22020513.
Der volle Inhalt der QuelleBitar, K. N., A. Ibitayo und S. B. Patil. „HSP27 modulates agonist-induced association of translocated RhoA and PKC-α in muscle cells of the colon“. Journal of Applied Physiology 92, Nr. 1 (01.01.2002): 41–49. http://dx.doi.org/10.1152/jappl.2002.92.1.41.
Der volle Inhalt der QuelleSevin, Margaux, Nicolas Pernet, Franck Vitte, Selim Ramla, Paul Sagot, Laurent Martin, Jean Luc Villeval et al. „HSP27: A Therapeutic Target in Myelofibrosis“. Blood 128, Nr. 22 (02.12.2016): 1963. http://dx.doi.org/10.1182/blood.v128.22.1963.1963.
Der volle Inhalt der QuelleHatakeyama, Daijiro, Osamu Kozawa, Masayuki Niwa, Hiroyuki Matsuno, Kanefusa Kato, Norichika Tatematsu, Toshiyuki Shibata und Toshihiko Uematsu. „Inhibition by adenylyl cyclase-cAMP system of ET-1-induced HSP27 in osteoblasts“. American Journal of Physiology-Endocrinology and Metabolism 281, Nr. 6 (01.12.2001): E1260—E1266. http://dx.doi.org/10.1152/ajpendo.2001.281.6.e1260.
Der volle Inhalt der QuelleArslan, Badel, Nurcan Aras, Selma Yaman und Ulku Comelekoglu. „Investigation of genetic stress parameters in brain tissues of rats exposed to 1.8 GHz cell phone radiofrequency electromagnetic field“. Medicine Science | International Medical Journal 13, Nr. 1 (2024): 78. http://dx.doi.org/10.5455/medscience.2023.06.094.
Der volle Inhalt der QuelleShi, Chunhua, Daiana Alvarez-Olmedo, Yuan Zhang, Badal S. B. Pattar und Edward R. O’Brien. „The Heat Shock Protein 27 Immune Complex Enhances Exosomal Cholesterol Efflux“. Biomedicines 8, Nr. 8 (17.08.2020): 290. http://dx.doi.org/10.3390/biomedicines8080290.
Der volle Inhalt der QuelleSinger, Debora, Verena Ressel, Matthias B. Stope und Sander Bekeschus. „Heat Shock Protein 27 Affects Myeloid Cell Activation and Interaction with Prostate Cancer Cells“. Biomedicines 10, Nr. 9 (05.09.2022): 2192. http://dx.doi.org/10.3390/biomedicines10092192.
Der volle Inhalt der QuelleYamboliev, Ilia A., Jason C. Hedges, Jack L. M. Mutnick, Leonard P. Adam und William T. Gerthoffer. „Evidence for modulation of smooth muscle force by the p38 MAP kinase/HSP27 pathway“. American Journal of Physiology-Heart and Circulatory Physiology 278, Nr. 6 (01.06.2000): H1899—H1907. http://dx.doi.org/10.1152/ajpheart.2000.278.6.h1899.
Der volle Inhalt der QuelleMusiał, Kinga, und Danuta Zwolińska. „Extracellular Hsp27 in patients with chronic kidney disease“. Kidney International 83, Nr. 5 (Mai 2013): 971. http://dx.doi.org/10.1038/ki.2013.33.
Der volle Inhalt der QuelleHyväri, Laura, Sari Vanhatupa, Miina Ojansivu, Minna Kelloniemi, Toni-Karri Pakarinen, Leena Hupa und Susanna Miettinen. „Heat Shock Protein 27 Is Involved in the Bioactive Glass Induced Osteogenic Response of Human Mesenchymal Stem Cells“. Cells 12, Nr. 2 (05.01.2023): 224. http://dx.doi.org/10.3390/cells12020224.
Der volle Inhalt der QuelleGuay, J., H. Lambert, G. Gingras-Breton, J. N. Lavoie, J. Huot und J. Landry. „Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27“. Journal of Cell Science 110, Nr. 3 (01.02.1997): 357–68. http://dx.doi.org/10.1242/jcs.110.3.357.
Der volle Inhalt der QuelleIshida, Yoshihito, Hiroshi Kubota, Akitsugu Yamamoto, Akira Kitamura, Hans Peter Bächinger und Kazuhiro Nagata. „Type I Collagen in Hsp47-null Cells Is Aggregated in Endoplasmic Reticulum and Deficient in N-Propeptide Processing and Fibrillogenesis“. Molecular Biology of the Cell 17, Nr. 5 (Mai 2006): 2346–55. http://dx.doi.org/10.1091/mbc.e05-11-1065.
Der volle Inhalt der QuelleThuringer, Dominique, Gaetan Jego, Guillaume Wettstein, Olivier Terrier, Laurent Cronier, Nadhir Yousfi, Sophie Hébrard et al. „Extracellular HSP27 mediates angiogenesis through Toll‐like receptor 3“. FASEB Journal 27, Nr. 10 (26.06.2013): 4169–83. http://dx.doi.org/10.1096/fj.12-226977.
Der volle Inhalt der QuelleOsorio, Luis A., Mauricio Lozano, Paola Soto, Viviana Moreno-Hidalgo, Angely Arévalo-Gil, Angie Ramírez-Balaguera, Daniel Hevia et al. „Levels of Small Extracellular Vesicles Containing hERG-1 and Hsp47 as Potential Biomarkers for Cardiovascular Diseases“. International Journal of Molecular Sciences 25, Nr. 9 (30.04.2024): 4913. http://dx.doi.org/10.3390/ijms25094913.
Der volle Inhalt der QuelleHuot, Jacques, François Houle, Simon Rousseau, Réna G. Deschesnes, Girish M. Shah und Jacques Landry. „SAPK2/p38-dependent F-Actin Reorganization Regulates Early Membrane Blebbing during Stress-induced Apoptosis“. Journal of Cell Biology 143, Nr. 5 (30.11.1998): 1361–73. http://dx.doi.org/10.1083/jcb.143.5.1361.
Der volle Inhalt der QuelleAsea, Alexzander. „Initiation of the Immune Response by Extracellular Hsp72: Chaperokine Activity of Hsp72“. Current Immunology Reviews 2, Nr. 3 (01.08.2006): 209–15. http://dx.doi.org/10.2174/157339506778018514.
Der volle Inhalt der QuelleYamada, Paulette M., Fabiano T. Amorim, Pope Moseley, Robert Robergs und Suzanne M. Schneider. „Effect of heat acclimation on heat shock protein 72 and interleukin-10 in humans“. Journal of Applied Physiology 103, Nr. 4 (Oktober 2007): 1196–204. http://dx.doi.org/10.1152/japplphysiol.00242.2007.
Der volle Inhalt der QuelleGanter, Michael T., Lorraine B. Ware, Marybeth Howard, Jérémie Roux, Brandi Gartland, Michael A. Matthay, Monika Fleshner und Jean-François Pittet. „Extracellular heat shock protein 72 is a marker of the stress protein response in acute lung injury“. American Journal of Physiology-Lung Cellular and Molecular Physiology 291, Nr. 3 (September 2006): L354—L361. http://dx.doi.org/10.1152/ajplung.00405.2005.
Der volle Inhalt der QuelleXiong, Gaofeng, Jie Chen, Guoying Zhang, Shike Wang, Kunito Kawasaki, Jieqing Zhu, Yan Zhang et al. „Hsp47 promotes cancer metastasis by enhancing collagen-dependent cancer cell-platelet interaction“. Proceedings of the National Academy of Sciences 117, Nr. 7 (03.02.2020): 3748–58. http://dx.doi.org/10.1073/pnas.1911951117.
Der volle Inhalt der QuelleBeck, Franz-X., Wolfgang Neuhofer und Eva Müller. „Molecular chaperones in the kidney: distribution, putative roles, and regulation“. American Journal of Physiology-Renal Physiology 279, Nr. 2 (01.08.2000): F203—F215. http://dx.doi.org/10.1152/ajprenal.2000.279.2.f203.
Der volle Inhalt der QuelleGabai, Vladimir L., Julia A. Yaglom, Todd Waldman und Michael Y. Sherman. „Heat Shock Protein Hsp72 Controls Oncogene-Induced Senescence Pathways in Cancer Cells“. Molecular and Cellular Biology 29, Nr. 2 (10.11.2008): 559–69. http://dx.doi.org/10.1128/mcb.01041-08.
Der volle Inhalt der QuelleEdwards, Helen V., John D. Scott und George S. Baillie. „The A-kinase-anchoring protein AKAP-Lbc facilitates cardioprotective PKA phosphorylation of Hsp20 on Ser16“. Biochemical Journal 446, Nr. 3 (28.08.2012): 437–43. http://dx.doi.org/10.1042/bj20120570.
Der volle Inhalt der QuelleXue, Jing, Jie Zhou und Janos Zempleni. „Holocarboxylase synthetase catalyzes biotinylation of heat shock protein 72, thereby inducing RANTES expression in HEK-293 cells“. American Journal of Physiology-Cell Physiology 305, Nr. 12 (15.12.2013): C1240—C1245. http://dx.doi.org/10.1152/ajpcell.00279.2013.
Der volle Inhalt der QuelleBigham, Michael T., und Hector R. Wong. „THE ROLE OF EXTRACELLULAR HSP72 IN CARDIOMYOCYTE ACTIVATION.“ Critical Care Medicine 34 (Dezember 2006): A44. http://dx.doi.org/10.1097/00003246-200612002-00153.
Der volle Inhalt der QuelleLee, W. C., H. C. Wen, C. P. Chang, M. Y. Chen und M. T. Lin. „Heat shock protein 72 overexpression protects against hyperthermia, circulatory shock, and cerebral ischemia during heatstroke“. Journal of Applied Physiology 100, Nr. 6 (Juni 2006): 2073–82. http://dx.doi.org/10.1152/japplphysiol.01433.2005.
Der volle Inhalt der QuelleNeuhofer, Wolfgang, Karin Lugmayr, Maria-Luisa Fraek und Franz-X. Beck. „Regulated Overexpression of Heat Shock Protein 72 Protects Madin-Darby Canine Kidney Cells from the Detrimental Effects of High Urea Concentrations“. Journal of the American Society of Nephrology 12, Nr. 12 (Dezember 2001): 2565–71. http://dx.doi.org/10.1681/asn.v12122565.
Der volle Inhalt der QuelleXiao, Hong-bo, Rui-hong Liu, Guang-hui Ling, Li Xiao, Yuan-chen Xia, Fu-you Liu, Jun Li et al. „HSP47 regulates ECM accumulation in renal proximal tubular cells induced by TGF-β1 through ERK1/2 and JNK MAPK pathways“. American Journal of Physiology-Renal Physiology 303, Nr. 5 (01.09.2012): F757—F765. http://dx.doi.org/10.1152/ajprenal.00470.2011.
Der volle Inhalt der QuelleKim, Sung O., Christopher P. Baines, Stuart D. Critz, Steven L. Pelech, Sidney Katz, James M. Downey und Michael V. Cohen. „Ischemia induced activation of heat shock protein 27 kinases and casein kinase 2 in the preconditioned rabbit heart“. Biochemistry and Cell Biology 77, Nr. 6 (01.12.1999): 559–67. http://dx.doi.org/10.1139/o99-065.
Der volle Inhalt der QuelleSakamoto, Noriho, Daisuke Okuno, Takatomo Tokito, Hirokazu Yura, Takashi Kido, Hiroshi Ishimoto, Yoshimasa Tanaka und Hiroshi Mukae. „HSP47: A Therapeutic Target in Pulmonary Fibrosis“. Biomedicines 11, Nr. 9 (25.08.2023): 2387. http://dx.doi.org/10.3390/biomedicines11092387.
Der volle Inhalt der QuelleBruchim, Yaron, Itamar Aroch, Ady Eliav, Atallah Abbas, Ilan Frank, Efrat Kelmer, Carolina Codner, Gilad Segev, Yoram Epstein und Michal Horowitz. „Two years of combined high-intensity physical training and heat acclimatization affect lymphocyte and serum HSP70 in purebred military working dogs“. Journal of Applied Physiology 117, Nr. 2 (15.07.2014): 112–18. http://dx.doi.org/10.1152/japplphysiol.00090.2014.
Der volle Inhalt der QuelleVallés, Gema, Eduardo García-Cimbrelo und Nuria Vilaboa. „Involvement of extracellular Hsp72 in wear particle-mediated osteolysis“. Acta Biomaterialia 8, Nr. 3 (März 2012): 1146–55. http://dx.doi.org/10.1016/j.actbio.2011.12.001.
Der volle Inhalt der QuelleSalari, Samira, Tara Seibert, Yong-Xiang Chen, Tieqiang Hu, Chunhua Shi, Xiaoling Zhao, Charles M. Cuerrier, Joshua E. Raizman und Edward R. O’Brien. „Extracellular HSP27 acts as a signaling molecule to activate NF-κB in macrophages“. Cell Stress and Chaperones 18, Nr. 1 (01.08.2012): 53–63. http://dx.doi.org/10.1007/s12192-012-0356-0.
Der volle Inhalt der QuelleWhitham, Martin, Gary J. Walker und Nicolette C. Bishop. „Effect of caffeine supplementation on the extracellular heat shock protein 72 response to exercise“. Journal of Applied Physiology 101, Nr. 4 (Oktober 2006): 1222–27. http://dx.doi.org/10.1152/japplphysiol.00409.2006.
Der volle Inhalt der QuelleArcher, Ashley E., Alex T. Von Schulze und Paige C. Geiger. „Exercise, heat shock proteins and insulin resistance“. Philosophical Transactions of the Royal Society B: Biological Sciences 373, Nr. 1738 (04.12.2017): 20160529. http://dx.doi.org/10.1098/rstb.2016.0529.
Der volle Inhalt der QuelleEvdonin, Anton, Alexander Kinev, Natalia Tsupkina, Vince Guerriero, Deborah A. Raynes und Natalia Medvedeva. „Extracellular HspBP1 and Hsp72 synergistically activate epidermal growth factor receptor“. Biology of the Cell 101, Nr. 6 (Juni 2009): 351–60. http://dx.doi.org/10.1042/bc20080069.
Der volle Inhalt der QuelleJin, Chunhua, Joseph C. Cleveland, Lihua Ao, Jilin Li, Qingchun Zeng, David A. Fullerton und Xianzhong Meng. „Human Myocardium Releases Heat Shock Protein 27 (HSP27) after Global Ischemia: The Proinflammatory Effect of Extracellular HSP27 through Toll-like Receptor (TLR)-2 and TLR4“. Molecular Medicine 20, Nr. 1 (Januar 2014): 280–89. http://dx.doi.org/10.2119/molmed.2014.00058.
Der volle Inhalt der QuelleLunge, Ajitesh, Radhika Gupta, Eira Choudhary und Nisheeth Agarwal. „The unfoldase ClpC1 of Mycobacterium tuberculosis regulates the expression of a distinct subset of proteins having intrinsically disordered termini“. Journal of Biological Chemistry 295, Nr. 28 (14.05.2020): 9455–73. http://dx.doi.org/10.1074/jbc.ra120.013456.
Der volle Inhalt der QuelleAbell, Amy N., Jaime A. Rivera-Perez, Bruce D. Cuevas, Mark T. Uhlik, Susan Sather, Nancy L. Johnson, Suzanne K. Minton et al. „Ablation of MEKK4 Kinase Activity Causes Neurulation and Skeletal Patterning Defects in the Mouse Embryo“. Molecular and Cellular Biology 25, Nr. 20 (15.10.2005): 8948–59. http://dx.doi.org/10.1128/mcb.25.20.8948-8959.2005.
Der volle Inhalt der QuelleSolly, Françoise, Pascale Flandrin-Gresta, Carmen Aanei, Jérôme Cornillon, Emmanuelle Tavernier, Denis Guyotat und Lydia Campos. „High Levels of Heat Shock Proteins 90 and 27 in CD34-Positive Cells from Myelodysplastic Syndromes (MDS) Are Associated with Higher Expression and Activation of Focal Adhesion Kinase (FAK) and with Disease Progression.“ Blood 114, Nr. 22 (20.11.2009): 289. http://dx.doi.org/10.1182/blood.v114.22.289.289.
Der volle Inhalt der QuelleAbboud, Patricia A., Patrick M. Lahni, Kristen Page, John S. Giuliano, Kelli Harmon, Katherine E. Dunsmore, Hector R. Wong und Derek S. Wheeler. „THE ROLE OF ENDOGENOUSLY PRODUCED EXTRACELLULAR HSP72 IN MONONUCLEAR CELL REPROGRAMMING“. Shock 30, Nr. 3 (September 2008): 285–92. http://dx.doi.org/10.1097/shk.0b013e318164e2c3.
Der volle Inhalt der QuelleGabai, Vladimir L., Julia A. Yaglom, Vladimir Volloch, Anatoli B. Meriin, Thomas Force, Maria Koutroumanis, Bernard Massie, Dick D. Mosser und Michael Y. Sherman. „Hsp72-Mediated Suppression of c-Jun N-Terminal Kinase Is Implicated in Development of Tolerance to Caspase-Independent Cell Death“. Molecular and Cellular Biology 20, Nr. 18 (15.09.2000): 6826–36. http://dx.doi.org/10.1128/mcb.20.18.6826-6836.2000.
Der volle Inhalt der QuelleTakamatsu, Hiroyuki, Zhirong Qi, Tomoyuki Sakurai, Luis Espinoza, Naomi Sugimori, Hirohito Yamazaki, Katsuya Okawa und Shinji Nakao. „Identification of a Novel Auto-Antibody Highly Prevalent in Patients with Hepatitis-Associated and Idiopathic Aplastic Anemia.“ Blood 114, Nr. 22 (20.11.2009): 3200. http://dx.doi.org/10.1182/blood.v114.22.3200.3200.
Der volle Inhalt der QuelleLuo, Hongyang, Taixiang Liu, Huasheng Yang, Huijing Ye und Xin Luo. „Expression of Collagen (Types I, III, and V), HSP47, MMP-2, and TIMP-1 in Retrobulbar Adipose Tissue of Patients with Thyroid-Associated Orbitopathy“. Journal of Ophthalmology 2020 (23.04.2020): 1–5. http://dx.doi.org/10.1155/2020/4929634.
Der volle Inhalt der QuelleThienel, Manuela, Johannes B. Müller-Reif, Zhe Zhang, Vincent Ehreiser, Judith Huth, Khrystyna Shchurovska, Badr Kilani et al. „Immobility-associated thromboprotection is conserved across mammalian species from bear to human“. Science 380, Nr. 6641 (14.04.2023): 178–87. http://dx.doi.org/10.1126/science.abo5044.
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