Статті в журналах з теми "Homocysteinylation"
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Bełtowski, Jerzy, Grażyna Wójcicka, and Hieronim Jakubowski. "Modulation of paraoxonase 1 and protein N-homocysteinylation by leptin and the synthetic liver X receptor agonist T0901317 in the rat." Journal of Endocrinology 204, no. 2 (November 2, 2009): 191–98. http://dx.doi.org/10.1677/joe-09-0298.
Повний текст джерелаChen, Nan, Zeyu Qiao, and Chu Wang. "A chemoselective reaction between protein N-homocysteinylation and azides catalyzed by heme(ii)." Chemical Communications 55, no. 25 (2019): 3654–57. http://dx.doi.org/10.1039/c9cc00055k.
Повний текст джерелаChen, Nan, Jinmin Liu, Zeyu Qiao, Yuan Liu, Yue Yang, Changtao Jiang, Xian Wang, and Chu Wang. "Chemical proteomic profiling of proteinN-homocysteinylation with a thioester probe." Chemical Science 9, no. 10 (2018): 2826–30. http://dx.doi.org/10.1039/c8sc00221e.
Повний текст джерелаXu, Leilei, Jiajia Chen, Jun Gao, Hongxiu Yu, and Pengyuan Yang. "Crosstalk of homocysteinylation, methylation and acetylation on histone H3." Analyst 140, no. 9 (2015): 3057–63. http://dx.doi.org/10.1039/c4an02355b.
Повний текст джерелаJakubowski, H. "Protein N-homocysteinylation: implications for atherosclerosis." Biomedicine & Pharmacotherapy 55, no. 8 (October 2001): 443–47. http://dx.doi.org/10.1016/s0753-3322(01)00085-3.
Повний текст джерелаJakubowski, Hieronim. "Protein N-Homocysteinylation and Colorectal Cancer." Trends in Cancer 5, no. 1 (January 2019): 7–10. http://dx.doi.org/10.1016/j.trecan.2018.10.006.
Повний текст джерелаPerna, A. F., E. Satta, F. Acanfora, C. Lombardi, D. Ingrosso, and N. G. De Santo. "Increased plasma protein homocysteinylation in hemodialysis patients." Kidney International 69, no. 5 (March 2006): 869–76. http://dx.doi.org/10.1038/sj.ki.5000070.
Повний текст джерелаColgan, Stephen M., and Richard C. Austin. "Homocysteinylation of Metallothionein Impairs Intracellular Redox Homeostasis." Arteriosclerosis, Thrombosis, and Vascular Biology 27, no. 1 (January 2007): 8–11. http://dx.doi.org/10.1161/01.atv.0000254151.00086.26.
Повний текст джерелаBalint, Brittany, Sébastien Hergalant, Jean-Michel Camadro, Sébastien Blaise, Laetitia Vanalderwiert, Laurent Lignières, Rosa-Maria Guéant-Rodriguez, and Jean-Louis Guéant. "Fetal Programming by Methyl Donor Deficiency Produces Pathological Remodeling of the Ascending Aorta." Arteriosclerosis, Thrombosis, and Vascular Biology 41, no. 6 (June 2021): 1928–41. http://dx.doi.org/10.1161/atvbaha.120.315587.
Повний текст джерелаJamroz-Wiśniewska, A., J. Bełtowski, H. Bartosik-Psujek, G. Wójcicka, and K. Rejdak. "Processes of plasma proteinN-homocysteinylation in multiple sclerosis." International Journal of Neuroscience 127, no. 8 (October 14, 2016): 709–15. http://dx.doi.org/10.1080/00207454.2016.1241782.
Повний текст джерелаZinellu, Angelo, Elisabetta Zinellu, Salvatore Sotgia, Marilena Formato, Gian Mario Cherchi, Luca Deiana, and Ciriaco Carru. "Factors Affecting S-Homocysteinylation of LDL Apoprotein B." Clinical Chemistry 52, no. 11 (November 1, 2006): 2054–59. http://dx.doi.org/10.1373/clinchem.2006.071142.
Повний текст джерелаSharma, Gurumayum Suraj, Tarun Kumar, Tanveer Ali Dar, and Laishram Rajendrakumar Singh. "Protein N-homocysteinylation: From cellular toxicity to neurodegeneration." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 11 (November 2015): 2239–45. http://dx.doi.org/10.1016/j.bbagen.2015.08.013.
Повний текст джерелаSikora, Marta, Łukasz Marczak, Jolanta Kubalska, AŁŁa Graban, and Hieronim Jakubowski. "Identification of N-homocysteinylation sites in plasma proteins." Amino Acids 46, no. 1 (November 30, 2013): 235–44. http://dx.doi.org/10.1007/s00726-013-1617-7.
Повний текст джерелаZhloba, Alexandr A., and Tatiana F. Subbotina. "Homocysteinylation score of high-molecular weight plasma proteins." Amino Acids 46, no. 4 (December 25, 2013): 893–99. http://dx.doi.org/10.1007/s00726-013-1652-4.
Повний текст джерелаDeslandes, Jordan, Jessy-Carol Ntunzwenimana, Laurane Forestier, Vincent Lacasse, Richard J. Wagner, and Klaus Klarskov. "Dehydroascorbate-Induced Peptide S-Glutathionylation and S-Homocysteinylation." Free Radical Biology and Medicine 87 (October 2015): S53. http://dx.doi.org/10.1016/j.freeradbiomed.2015.10.139.
Повний текст джерелаJakubowski, Hieronim. "Homocysteine Thiolactone: Metabolic Origin and Protein Homocysteinylation in Humans." Journal of Nutrition 130, no. 2 (February 1, 2000): 377S—381S. http://dx.doi.org/10.1093/jn/130.2.377s.
Повний текст джерелаGates, Arther T., Leonard Moore, Monica R. Sylvain, Christina M. Jones, Mark Lowry, Bilal El-Zahab, James W. Robinson, Robert M. Strongin, and Isiah M. Warner. "Mechanistic Investigation ofN-Homocysteinylation-Mediated Protein−Gold Nanoconjugate Assembly." Langmuir 25, no. 16 (August 18, 2009): 9346–51. http://dx.doi.org/10.1021/la900798q.
Повний текст джерелаPerla‐Kaján, Joanna, and Hieronim Jakubowski. "Paraoxonase 1 protects against protein N ‐homocysteinylation in humans." FASEB Journal 24, no. 3 (October 30, 2009): 931–36. http://dx.doi.org/10.1096/fj.09-144410.
Повний текст джерелаJakubowski, Hieronim, Li Zhang, Arlene Bardeguez, and Abram Aviv. "Homocysteine Thiolactone and Protein Homocysteinylation in Human Endothelial Cells." Circulation Research 87, no. 1 (July 7, 2000): 45–51. http://dx.doi.org/10.1161/01.res.87.1.45.
Повний текст джерелаLeri, Manuela, Paola Rebuzzini, Anna Caselli, Simone Luti, Antonino Natalello, Sofia Giorgetti, Loredana Marchese, et al. "S-Homocysteinylation effects on transthyretin: worsening of cardiomyopathy onset." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 1 (January 2020): 129453. http://dx.doi.org/10.1016/j.bbagen.2019.129453.
Повний текст джерелаHuang, An, John T. Pinto, Ghezal Froogh, Sharath Kandhi, Jun Qin, Michael S. Wolin, Thomas H. Hintze, and Dong Sun. "Role of homocysteinylation of ACE in endothelial dysfunction of arteries." American Journal of Physiology-Heart and Circulatory Physiology 308, no. 2 (January 15, 2015): H92—H100. http://dx.doi.org/10.1152/ajpheart.00577.2014.
Повний текст джерелаFerretti, Gianna, Tiziana Bacchetti, Simona Masciangelo, and Virginia Bicchiega. "Effect of homocysteinylation on high density lipoprotein physico-chemical properties." Chemistry and Physics of Lipids 163, no. 2 (February 2010): 228–35. http://dx.doi.org/10.1016/j.chemphyslip.2009.11.008.
Повний текст джерелаZinellu, Angelo, Giacomina Loriga, Bastianina Scanu, Elisabetta Pisanu, Manuela Sanna, Luca Deiana, Andrea Ercole Satta, and Ciriaco Carru. "Increased Low-Density Lipoprotein S-Homocysteinylation in Chronic Kidney Disease." American Journal of Nephrology 32, no. 3 (2010): 242–48. http://dx.doi.org/10.1159/000319012.
Повний текст джерелаStroylova, Yulia Y., Jean-Marc Chobert, Vladimir I. Muronetz, Hieronim Jakubowski, and Thomas Haertlé. "N-homocysteinylation of ovine prion protein induces amyloid-like transformation." Archives of Biochemistry and Biophysics 526, no. 1 (October 2012): 29–37. http://dx.doi.org/10.1016/j.abb.2012.06.008.
Повний текст джерелаMiyazaki, Akari, Nozomi Sagae, Yoko Usami, Megumi Sato, Takahiro Kameda, Akira Yoshimoto, Nau Ishimine, et al. "N-homocysteinylation of apolipoprotein A-I impairs the protein’s antioxidant ability but not its cholesterol efflux capacity." Biological Chemistry 395, no. 6 (June 1, 2014): 641–48. http://dx.doi.org/10.1515/hsz-2013-0262.
Повний текст джерелаPerl̷a-Kaján, Joanna, Agata Malinowska, Jarosl̷aw Zimny, Dominik Cysewski, Joanna Suszyńska-Zajczyk, and Hieronim Jakubowski. "Proteome-Wide Analysis of Protein Lysine N-Homocysteinylation in Saccharomyces cerevisiae." Journal of Proteome Research 20, no. 5 (April 2, 2021): 2458–76. http://dx.doi.org/10.1021/acs.jproteome.0c00937.
Повний текст джерелаJAKUBOWSKI, HIERONIM. "Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels." FASEB Journal 13, no. 15 (December 1999): 2277–83. http://dx.doi.org/10.1096/fasebj.13.15.2277.
Повний текст джерелаGenoud, Valeria, Paula G. Quintana, Silvana Gionco, Alicia Baldessari, and Irene Quintana. "Structural changes of fibrinogen molecule mediated by the N-homocysteinylation reaction." Journal of Thrombosis and Thrombolysis 45, no. 1 (October 26, 2017): 66–76. http://dx.doi.org/10.1007/s11239-017-1574-1.
Повний текст джерелаPaoli, Paolo, Francesca Sbrana, Bruno Tiribilli, Anna Caselli, Barbara Pantera, Paolo Cirri, Alina De Donatis, et al. "Protein N-Homocysteinylation Induces the Formation of Toxic Amyloid-Like Protofibrils." Journal of Molecular Biology 400, no. 4 (July 2010): 889–907. http://dx.doi.org/10.1016/j.jmb.2010.05.039.
Повний текст джерелаParada-Turska, Jolanta, Grażyna Wójcicka, and Jerzy Beltowski. "Paraoxonase 1 Phenotype and Protein N-Homocysteinylation in Patients with Rheumatoid Arthritis: Implications for Cardiovascular Disease." Antioxidants 9, no. 9 (September 21, 2020): 899. http://dx.doi.org/10.3390/antiox9090899.
Повний текст джерелаKhodadadi, Sirus, Gholam Hossein Riazi, Shahin Ahmadian, Elham Hoveizi, Oveis Karima та Hassan Aryapour. "Effect ofN-homocysteinylation on physicochemical and cytotoxic properties of amyloid β-peptide". FEBS Letters 586, № 2 (23 грудня 2011): 127–31. http://dx.doi.org/10.1016/j.febslet.2011.12.018.
Повний текст джерелаWang, Dan, Rui Zhao, Yuan-Yuan Qu, Xin-Yu Mei, Xuan Zhang, Qian Zhou, Yang Li, et al. "Colonic Lysine Homocysteinylation Induced by High-Fat Diet Suppresses DNA Damage Repair." Cell Reports 25, no. 2 (October 2018): 398–412. http://dx.doi.org/10.1016/j.celrep.2018.09.022.
Повний текст джерелаZinellu, Angelo, Salvatore Sotgia, Bastianina Scanu, Luca Deiana, Giuseppe Talanas, PierFranco Terrosu, and Ciriaco Carru. "Low density lipoprotein S-homocysteinylation is increased in acute myocardial infarction patients." Clinical Biochemistry 45, no. 4-5 (March 2012): 359–62. http://dx.doi.org/10.1016/j.clinbiochem.2011.12.017.
Повний текст джерелаHop, Cornelis E. C. A., and Ray Bakhtiar. "Homocysteine thiolactone and protein homocysteinylation: mechanistic studies with model peptides and proteins." Rapid Communications in Mass Spectrometry 16, no. 11 (2002): 1049–53. http://dx.doi.org/10.1002/rcm.681.
Повний текст джерелаJamroz-Wiśniewska, Anna, Jerzy Bełtowski, Grażyna Wójcicka, Halina Bartosik-Psujek, and Konrad Rejdak. "Cladribine Treatment Improved Homocysteine Metabolism and Increased Total Serum Antioxidant Activity in Secondary Progressive Multiple Sclerosis Patients." Oxidative Medicine and Cellular Longevity 2020 (March 17, 2020): 1–7. http://dx.doi.org/10.1155/2020/1654754.
Повний текст джерелаBorowczyk, Kamila, Jacek Wróblewski, Joanna Suliburska, Noriyuki Akahoshi, Isao Ishii, and Hieronim Jakubowski. "Mutations in Homocysteine Metabolism Genes Increase Keratin N-Homocysteinylation and Damage in Mice." International Journal of Genomics 2018 (September 23, 2018): 1–7. http://dx.doi.org/10.1155/2018/7570850.
Повний текст джерелаHubmacher, Dirk, Judith T. Cirulis, Ming Miao, Fred W. Keeley, and Dieter P. Reinhardt. "Functional Consequences of Homocysteinylation of the Elastic Fiber Proteins Fibrillin-1 and Tropoelastin." Journal of Biological Chemistry 285, no. 2 (November 4, 2009): 1188–98. http://dx.doi.org/10.1074/jbc.m109.021246.
Повний текст джерелаRossi, R., D. Giustarini, A. Milzani, and I. Dalle-Donne. "Cysteinylation and homocysteinylation of plasma protein thiols during ageing of healthy human beings." Journal of Cellular and Molecular Medicine 13, no. 9b (July 10, 2008): 3131–40. http://dx.doi.org/10.1111/j.1582-4934.2008.00417.x.
Повний текст джерелаFerretti, G., T. Bacchetti, E. Marotti, and G. Curatola. "Effect of homocysteinylation on human high-density lipoproteins: A correlation with paraoxonase activity." Metabolism 52, no. 2 (February 2003): 146–51. http://dx.doi.org/10.1053/meta.2003.50033.
Повний текст джерелаGłowacki, Rafał, and Hieronim Jakubowski. "Cross-talk between Cys34and Lysine Residues in Human Serum Albumin Revealed byN-Homocysteinylation." Journal of Biological Chemistry 279, no. 12 (December 29, 2003): 10864–71. http://dx.doi.org/10.1074/jbc.m313268200.
Повний текст джерелаSharma, Gurumayum Suraj, Tarun Kumar, and Laishram Rajendrakumar Singh. "N-Homocysteinylation Induces Different Structural and Functional Consequences on Acidic and Basic Proteins." PLoS ONE 9, no. 12 (December 31, 2014): e116386. http://dx.doi.org/10.1371/journal.pone.0116386.
Повний текст джерелаSchiappacasse, Agustina, Romina Eugenia Maltaneri, María Eugenia Chamorro, Alcira Beatriz Nesse, Diana Elena Wetzler, and Daniela Cecilia Vittori. "Modification of erythropoietin structure by N ‐homocysteinylation affects its antiapoptotic and proliferative functions." FEBS Journal 285, no. 20 (August 29, 2018): 3801–14. http://dx.doi.org/10.1111/febs.14632.
Повний текст джерелаSotgia, Salvatore, Ciriaco Carru, Gerard Aime Pinna, Luca Deiana, and Angelo Zinellu. "D-Penicillamine Interferes With S-Homocysteinylation and S-Cysteinylation of LDL Apolipoprotein B." Journal of Clinical Pharmacology 51, no. 12 (December 2011): 1728–32. http://dx.doi.org/10.1177/0091270010385933.
Повний текст джерелаGałczyński, Krzysztof, Jerzy Bełtowski, Łukasz Nowakowski, Danuta Vasilevska, Tomasz Rechberger, and Andrzej Semczuk. "Serum paraoxonase 1 activity and protein N-homocysteinylation in primary human endometrial cancer." Tumor Biology 40, no. 9 (August 2018): 101042831879786. http://dx.doi.org/10.1177/1010428318797869.
Повний текст джерелаZinellu, Angelo, Salvatore Sotgia, Elisabetta Pisanu, Giacomina Loriga, Luca Deiana, Andrea Ercole Satta, and Ciriaco Carru. "LDL S-homocysteinylation decrease in chronic kidney disease patients undergone lipid lowering therapy." European Journal of Pharmaceutical Sciences 47, no. 1 (August 2012): 117–23. http://dx.doi.org/10.1016/j.ejps.2012.05.006.
Повний текст джерелаStroylova, Yulia Y., Jaroslaw Zimny, Reza Yousefi, Jean-Marc Chobert, Hieronim Jakubowski, Vladimir I. Muronetz та Thomas Haertlé. "Aggregation and structural changes of αS1-, β- and κ-caseins induced by homocysteinylation". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1814, № 10 (жовтень 2011): 1234–45. http://dx.doi.org/10.1016/j.bbapap.2011.05.017.
Повний текст джерелаSharma, Gurumayum Suraj, and Laishram Rajendrakumar Singh. "Conformational status of cytochrome c upon N-homocysteinylation: Implications to cytochrome c release." Archives of Biochemistry and Biophysics 614 (January 2017): 23–27. http://dx.doi.org/10.1016/j.abb.2016.12.006.
Повний текст джерелаZinellu, Angelo, Salvatore Sotgia, Bastianina Scanu, Dionigia Arru, Annalisa Cossu, Anna Maria Posadino, Roberta Giordo, Arduino A. Mangoni, Gianfranco Pintus, and Ciriaco Carru. "N- and S-homocysteinylation reduce the binding of human serum albumin to catechins." European Journal of Nutrition 56, no. 2 (December 10, 2015): 785–91. http://dx.doi.org/10.1007/s00394-015-1125-5.
Повний текст джерелаSundaramoorthy, Elayanambi, Souvik Maiti, Samir K. Brahmachari, and Shantanu Sengupta. "Predicting protein homocysteinylation targets based on dihedral strain energy and pKa of cysteines." Proteins: Structure, Function, and Bioinformatics 71, no. 3 (December 12, 2007): 1475–83. http://dx.doi.org/10.1002/prot.21846.
Повний текст джерелаZhang, Xuan, Yuan-Yuan Qu, Lian Liu, Ya-Nan Qiao, Hao-Ran Geng, Yan Lin, Wei Xu, Jing Cao, and Jian-Yuan Zhao. "Homocysteine inhibits pro-insulin receptor cleavage and causes insulin resistance via protein cysteine-homocysteinylation." Cell Reports 37, no. 2 (October 2021): 109821. http://dx.doi.org/10.1016/j.celrep.2021.109821.
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