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Regina S. Komsa-Penkova, Georgi M. Golemanov, Zdravka V. Radionova, Pencho T. Tonchev, Sergej D. Iliev and Veselin V. Penkov

bone tissue. Calcif Tissue Res.1978;26:155-61. 39. Termine JD, Belcourt AB, Conn KM, Kleinman HK. Mineral and collagen-binding proteins of fetal calf bone. J Biol Chem. 1981;256:10403-8. 40. Schinke T, Amendt C, Trindl A, Pöschke O, Müller-Esterl W, Jahnen-Dechent W. The serum protein α2-HS glycoprotein/fetuin inhibits apatite formation in vitro and in mineralizing calvaria cells. A possible role in mineralization and calcium homeostasis. J Biol Chem. 1996;271:20789-96. 41. Jahnen-Dechent W, Schäfer C, Ketteler M, McKee MD. Mineral chaperones: a

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Rigers Bakiu

-06. 11. Beard NA, Laver DR, Dulhunty AF. Calsequestrin and the calcium release channel of skeletal and cardiac muscle. Prog Biophys Mol Biol 2004; 85: 33-69. 12. Beard NA, Wei L, Dulhunty AF. Ca(2+) signaling in striated muscle: the elusive roles of triadin, junctin, and calsequestrin. Eur. Biophys. J. 2009; 39: 27-36. DOI: 10.1007/s00249-009-0449-6. 13. Beard NA, Casarotto MG, Wei L, Varsanyi M, Laver DR, Dulhunty AF. Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation. and phosphorylation

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Zubeyir Elmazoglu, Volkan Ergin, Ergin Sahin, Handan Kayhan and Cimen Karasu

neurodegeneration. J Neurol Sci 322: 254-62. Galehdar Z, Swan P, Fuerth B, Callaghan SM, Park DS, Cregan SP. (2010). Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA. J Neurosci 30: 16938-48. Halperin L, Jung J, Michalak M. (2014). The many functions of the endoplasmic reticulum chaperones and folding enzymes. IUBMB Life 66: 318-26. Hauser DN, Hastings TG. (2013). Mitochondrial dysfunction and oxidative stress in Parkinson’s disease and

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Grażyna Janikowska, Aleksandra Kochańska - Dziurowicz, Aleksandra Żebrowska, Aleksandra Bijak and Magdalena Kimsa

, Gusev N. Large potentials of small heat shock proteins. Physiol Rev, 2011; 91: 1123 - 1159 Périard J, Ruell P, Caillaud C, Thompson M. Plasma Hsp72 (HSPA1A) and Hsp27 (HSPB1) expression under heat stress: influence of exercise intensity. Cell Stress Chaperones, 2012; 17: 375 - 383 Schaller K, Mechau D, Scharmann H, Weiss M, Baum M, Liesen H. Increased training load and the β - adrenergic - receptor system in human lymphocytes. J Appl Physiol, 1999; 87: 317 - 324 Seissler J. Vasoregulatory peptides pro - endothelin - 1

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Małgorzata Kandefer-Gola, Marcin Nowak, Rafał Ciaputa and Janusz A. Madej

–233. 19. Lukas W., Jones K.A.: Cortical neurons containing calretinin are selectively resistant to calcium overload and exitotoxicity in vitro . Neuroscience 1994, 61, 307–316. 20. Mariotti F., Giacomo R., Subeide M.: Immunohistochemical evaluation of ovarian hormonal receptors in canine mammary tumors. Open J Vet Med 2013, 3, 104–110. 21. Masferrer J.L., Leahy K.M., Koki A.T., Zweifel B.S., Settle S.L., Woerner M., Edwards D.A., Flickinger A.G., Moore R.J., Seibert K.: Antiangiogenic and antitumor activities of cyclooxygenase-2 inhibitors. Cancer Res 2000

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Katarzyna Ognik, Ewelina Cholewińska, Anna Stępniowska, Aleksandra Drażbo, Krzysztof Kozłowski and Jan Jankowski

). Metabolic crossroads of iron and copper. Nutr. Rev., 68: 133-147. EFSA. Panel on Additives and Products or Substances used in Animal Feed (FEEDAP). (2016). Revision of the currently authorised maximum copper content in complete feed. EFSA Journal, 14: 4563. Gaetke L.M., Chow C.K. (2003). Copper toxicity, oxidative stress, and antioxidant nutrients. Toxicology, 189: 147–163. Hatori Y., Lutsenko S. (2016). The role of copper chaperone atox1 in coupling redox homeostasis to intracellular copper distribution. Antioxidants, 5: 25-41. Hellman N

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Suphannee Thanyaphoo and Jasadee Kaewsrichan

. Med. 87 (2014) 549-561. 7. J. O. Hollinger, H. Uludag and S. R. Win, Sustained release emphasizing recombinant human bone morphogenetic protein-2, Adv. Drug Deliv. Rev. 31 (1998) 303-318; DOI: 10.1016/S0169-409X(97)00126-9. 8. D. S. Keskin, A. Texcaner, P. Korkusuz, F. Korkusuz and V. Hasirci, Collagen-chondroitin sulfatebased PLLA-SAIB-coated rhBMP-2 delivery system for bone repair, Biomaterials 26 (2005) 4023-4034; DOI: 10.1016/j.biomaterials.2004.09.063. 9. M. P. Ginebra, T. Traykova and J. A. Planell, Calcium

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Zuzana Kyselova

). Calcium activated proteolysis and protein modification in the U18666A cataract. Exp Eye Res   57 : 737-745. Cheng HM. (2002). Water diffusion in the rabbit lens in vivo . Dev Ophthalmol   35 : 169-175. Chikamoto N, Chikama T, Yamada N, Nishida T, Ishimitsu T and Kamiya A. (2009). Efficacy of substance P and insulin-like growth factor-1 peptides for preventing postsurgical superficial punctate keratopathy in diabetic patients. Jpn J Ophthalmol   53 : 464-469. Churchill GC and Louis CF

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R. Rękawiecki, M. Kowalik and J. Kotwica

: form and function in brain. Front Neuroendocrinol 29: 313-339. Cadepond F, Ulmann A, Baulieu EE ( 1997 ) RU486 (mifepristone): mechanisms of action and clinical uses. Annu Rev Med 48: 129-156. Chakravarti D, LaMorte VJ, Nelson MC, Nakajima T, Schulman IG, Juguilon H, Montminy M, Evans RM ( 1996 ) Role of CBP/P300 in nuclear receptor signalling. Nature 383: 99-103. Cheung J, Smith DF ( 2000 ) Molecular Chaperone Interactions with Steroid Receptors: an Update. Mol Endocrinol 14: 939

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Małgorzata Popis

Lmx1b. Nat Neurosci. 2000;3(4):337-41; DOI:10.1038/73902. 13. Surmeier D, Guzman J, Sanchez-Padilla J, Schumacker P. The role of calcium and mitochondrial oxidant stress in the lossof substantia nigra pars compacta dopaminergic neurons in Parkinson’s disease. Neuroscience. 2011;198:221-31; DOI:10.1016/j.neuroscience.2011.08.045. 14. Surmeier D, Schumacker P, Guzman J, Ilijic E, Yang B, Zampese E. Calcium and Parkinson’s disease. Biochem Biophys Res Commun. 2017;483(4):1013-1019; DOI:10.1016/j.bbrc.2016.08.168. 15. Exner N, Lutz A, Haass C