메뉴 건너뛰기




Volumn 171, Issue 1, 2016, Pages 208-213

Effect of Selenium Deficiency on Nitric Oxide and Heat Shock Proteins in Chicken Erythrocytes

Author keywords

Chicken erythrocytes; Heat shock protein; Nitric oxide; Selenium deficiency

Indexed keywords

BIOLOGICAL MARKER; CHAPERONIN 60; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; INDUCIBLE NITRIC OXIDE SYNTHASE; NITRIC OXIDE; SELENIUM;

EID: 84944699201     PISSN: 01634984     EISSN: 15590720     Source Type: Journal    
DOI: 10.1007/s12011-015-0527-9     Document Type: Article
Times cited : (34)

References (48)
  • 2
    • 0033010704 scopus 로고    scopus 로고
    • The effects of selenium deficiency on differentiation, degradation, and cell lysis of L8 rat skeletal muscle cells
    • COI: 1:CAS:528:DyaK1MXjvVGru78%3D, PID: 10383095
    • Ueda Y, Whanger PD, Forsberg NE (1999) The effects of selenium deficiency on differentiation, degradation, and cell lysis of L8 rat skeletal muscle cells. Biol Trace Elem Res 69:1–13
    • (1999) Biol Trace Elem Res , vol.69 , pp. 1-13
    • Ueda, Y.1    Whanger, P.D.2    Forsberg, N.E.3
  • 3
    • 0016921508 scopus 로고
    • The clinicopathological findings of mulberry heart disease in a piglet
    • COI: 1:STN:280:DyaE287jslygsA%3D%3D
    • Gudmundson J (1976) The clinicopathological findings of mulberry heart disease in a piglet. Can Vet J Rev Veterinaire Canadienne 17:45–47
    • (1976) Can Vet J Rev Veterinaire Canadienne , vol.17 , pp. 45-47
    • Gudmundson, J.1
  • 4
    • 0031953044 scopus 로고    scopus 로고
    • Influence of selenium deficiency on vital functions in rats
    • COI: 1:CAS:528:DyaK1cXitFCjsbY%3D, PID: 9533567
    • Matsuda A, Kimura M, Itokawa Y (1998) Influence of selenium deficiency on vital functions in rats. Biol Trace Elem Res 61:287–301
    • (1998) Biol Trace Elem Res , vol.61 , pp. 287-301
    • Matsuda, A.1    Kimura, M.2    Itokawa, Y.3
  • 5
    • 0034881268 scopus 로고    scopus 로고
    • Effects of Se, Cu and Se + vitamin E deficiency on the activities of CuZnSOD, GSH-Px, CAT and LPO levels in chicken erythrocytes
    • COI: 1:CAS:528:DC%2BD3MXmt1SqsLs%3D, PID: 11494304
    • Bozkaya LA, Ozturk-Urek R, Aydemir T, Tarhan L (2001) Effects of Se, Cu and Se + vitamin E deficiency on the activities of CuZnSOD, GSH-Px, CAT and LPO levels in chicken erythrocytes. Cell Biochem Funct 19:153–157
    • (2001) Cell Biochem Funct , vol.19 , pp. 153-157
    • Bozkaya, L.A.1    Ozturk-Urek, R.2    Aydemir, T.3    Tarhan, L.4
  • 6
    • 0021352750 scopus 로고
    • The effect of vitamin E or selenium on the oxidant-antioxidant balance in rats
    • COI: 1:CAS:528:DyaL2cXhvFSmtbk%3D, PID: 6421305
    • Doni MG, Falanga A, Delaini F, et al. (1984) The effect of vitamin E or selenium on the oxidant-antioxidant balance in rats. Br J Exp Pathol 65:75–80
    • (1984) Br J Exp Pathol , vol.65 , pp. 75-80
    • Doni, M.G.1    Falanga, A.2    Delaini, F.3
  • 7
    • 84892373857 scopus 로고    scopus 로고
    • p38alpha subtype is a potential target to inhibit eNOS activity and NO production in human endothelial cells
    • COI: 1:CAS:528:DC%2BC3sXhvVagsbbM, PID: 24200868
    • Wang B, Xing F, Liu N, et al. (2014) p38alpha subtype is a potential target to inhibit eNOS activity and NO production in human endothelial cells. Microvasc Res 91:58–65
    • (2014) Microvasc Res , vol.91 , pp. 58-65
    • Wang, B.1    Xing, F.2    Liu, N.3
  • 8
    • 84880604454 scopus 로고    scopus 로고
    • Loss of Jak2 impairs endothelial function by attenuating Raf-1/MEK1/Sp-1 signaling along with altered eNOS activities
    • COI: 1:CAS:528:DC%2BC3sXhtFyntbzJ, PID: 23747947
    • Yang P, Zhang Y, Pang J, et al. (2013) Loss of Jak2 impairs endothelial function by attenuating Raf-1/MEK1/Sp-1 signaling along with altered eNOS activities. Am J Pathol 183:617–625
    • (2013) Am J Pathol , vol.183 , pp. 617-625
    • Yang, P.1    Zhang, Y.2    Pang, J.3
  • 9
    • 68149137621 scopus 로고    scopus 로고
    • eNOS, metabolic syndrome and cardiovascular disease
    • COI: 1:CAS:528:DC%2BD1MXps1Sqsrk%3D, PID: 19647446
    • Huang PL (2009) eNOS, metabolic syndrome and cardiovascular disease. Trends Endocrinol Metab: TEM 20:295–302
    • (2009) Trends Endocrinol Metab: TEM , vol.20 , pp. 295-302
    • Huang, P.L.1
  • 10
    • 33745192118 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase regulates microvascular hyperpermeability in vivo
    • COI: 1:CAS:528:DC%2BD28XnsVyisrc%3D, PID: 16675496
    • Hatakeyama T, Pappas PJ, Hobson 2nd RW, et al. (2006) Endothelial nitric oxide synthase regulates microvascular hyperpermeability in vivo. J Physiol 574:275–281
    • (2006) J Physiol , vol.574 , pp. 275-281
    • Hatakeyama, T.1    Pappas, P.J.2    Hobson, R.W.3
  • 11
    • 0141673128 scopus 로고    scopus 로고
    • Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms
    • COI: 1:CAS:528:DC%2BD3sXmslemt7w%3D, PID: 12947383
    • Mikkelsen RB, Wardman P (2003) Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms. Oncogene 22:5734–5754
    • (2003) Oncogene , vol.22 , pp. 5734-5754
    • Mikkelsen, R.B.1    Wardman, P.2
  • 12
    • 0347695994 scopus 로고    scopus 로고
    • Inactivation of NADP+-dependent isocitrate dehydrogenase by peroxynitrite. Implications for cytotoxicity and alcohol-induced liver injury
    • COI: 1:CAS:528:DC%2BD3sXpslOht7o%3D, PID: 14551203
    • Lee JH, Yang ES, Park JW (2003) Inactivation of NADP+-dependent isocitrate dehydrogenase by peroxynitrite. Implications for cytotoxicity and alcohol-induced liver injury. J Biol Chem 278:51360–51371
    • (2003) J Biol Chem , vol.278 , pp. 51360-51371
    • Lee, J.H.1    Yang, E.S.2    Park, J.W.3
  • 14
    • 34548821573 scopus 로고    scopus 로고
    • Platelet activation in patients with sickle disease, hemolysis-associated pulmonary hypertension, and nitric oxide scavenging by cell-free hemoglobin
    • COI: 1:CAS:528:DC%2BD2sXhtVGjur7L, PID: 17536019
    • Villagra J, Shiva S, Hunter LA, et al. (2007) Platelet activation in patients with sickle disease, hemolysis-associated pulmonary hypertension, and nitric oxide scavenging by cell-free hemoglobin. Blood 110:2166–2172
    • (2007) Blood , vol.110 , pp. 2166-2172
    • Villagra, J.1    Shiva, S.2    Hunter, L.A.3
  • 15
    • 84925536133 scopus 로고    scopus 로고
    • The role of nitric oxide and oxidative stress in intestinal damage induced by selenium deficiency in chickens
    • COI: 1:CAS:528:DC%2BC2cXhvFSmtrbF, PID: 25388754
    • Yu J, Yao H, Gao X, et al. (2015) The role of nitric oxide and oxidative stress in intestinal damage induced by selenium deficiency in chickens. Biol Trace Elem Res 163:144–153
    • (2015) Biol Trace Elem Res , vol.163 , pp. 144-153
    • Yu, J.1    Yao, H.2    Gao, X.3
  • 16
    • 84925506979 scopus 로고    scopus 로고
    • Effects of selenium deficiency on principal indexes of chicken kidney function
    • COI: 1:CAS:528:DC%2BC2cXitVGmu7vM, PID: 25476001
    • Sun D, Li C, Gao J, Li S, Wang H (2015) Effects of selenium deficiency on principal indexes of chicken kidney function. Biol Trace Elem Res 164:58–63
    • (2015) Biol Trace Elem Res , vol.164 , pp. 58-63
    • Sun, D.1    Li, C.2    Gao, J.3    Li, S.4    Wang, H.5
  • 17
    • 84922080112 scopus 로고    scopus 로고
    • Selenium deficiency influences nitric oxide and selenoproteins in pancreas of chickens
    • COI: 1:CAS:528:DC%2BC2cXhvVSqs7vI, PID: 25319006
    • Zhao X, Yao H, Fan R, Zhang Z, Xu S (2014) Selenium deficiency influences nitric oxide and selenoproteins in pancreas of chickens. Biol Trace Elem Res 161:341–349
    • (2014) Biol Trace Elem Res , vol.161 , pp. 341-349
    • Zhao, X.1    Yao, H.2    Fan, R.3    Zhang, Z.4    Xu, S.5
  • 18
    • 33750212109 scopus 로고    scopus 로고
    • A novel HSF1-mediated death pathway that is suppressed by heat shock proteins
    • COI: 1:CAS:528:DC%2BD28XhtVyktb%2FL, PID: 17024176
    • Hayashida N, Inouye S, Fujimoto M, et al. (2006) A novel HSF1-mediated death pathway that is suppressed by heat shock proteins. EMBO J 25:4773–4783
    • (2006) EMBO J , vol.25 , pp. 4773-4783
    • Hayashida, N.1    Inouye, S.2    Fujimoto, M.3
  • 19
    • 0034816897 scopus 로고    scopus 로고
    • Free radicals, exercise, apoptosis, and heat shock proteins
    • COI: 1:STN:280:DC%2BD3MrjtlKhsg%3D%3D, PID: 11579749
    • Fehrenbach E, Northoff H (2001) Free radicals, exercise, apoptosis, and heat shock proteins. Exerc Immunol Rev 7:66–89
    • (2001) Exerc Immunol Rev , vol.7 , pp. 66-89
    • Fehrenbach, E.1    Northoff, H.2
  • 20
    • 84890781852 scopus 로고    scopus 로고
    • The effect of manganese-induced cytotoxicity on mRNA expressions of HSP27, HSP40, HSP60, HSP70 and HSP90 in chicken spleen lymphocytes in vitro
    • COI: 1:CAS:528:DC%2BC3sXhsFeqtbjL, PID: 24081778
    • Zhu Y, Lu X, Wu D, et al. (2013) The effect of manganese-induced cytotoxicity on mRNA expressions of HSP27, HSP40, HSP60, HSP70 and HSP90 in chicken spleen lymphocytes in vitro. Biol Trace Elem Res 156:144–152
    • (2013) Biol Trace Elem Res , vol.156 , pp. 144-152
    • Zhu, Y.1    Lu, X.2    Wu, D.3
  • 21
    • 84963662329 scopus 로고    scopus 로고
    • The Co-induced effects of molybdenum and cadmium on antioxidants and heat shock proteins in duck kidneys, Biological trace element research
    • Xia B, Cao H, Luo J, et al. (2015) The Co-induced effects of molybdenum and cadmium on antioxidants and heat shock proteins in duck kidneys. Biological trace element research
    • (2015) et al
    • Xia, B.1    Cao, H.2    Luo, J.3
  • 22
    • 84925494578 scopus 로고    scopus 로고
    • The role of heat shock proteins in oxidative stress damage induced by Se deficiency in chicken livers
    • COI: 1:CAS:528:DC%2BC2cXitFCrtb3L, PID: 25503394
    • Liu CP, Fu J, Xu FP, Wang XS, Li S (2015) The role of heat shock proteins in oxidative stress damage induced by Se deficiency in chicken livers. Biometals 28:163–173
    • (2015) Biometals , vol.28 , pp. 163-173
    • Liu, C.P.1    Fu, J.2    Xu, F.P.3    Wang, X.S.4    Li, S.5
  • 23
    • 84963667727 scopus 로고    scopus 로고
    • The functions of antioxidants and heat shock proteins are altered in the immune organs of selenium-deficient broiler chickens
    • Yang Z, Liu C, Zheng W, Teng X, Li S (2015) The functions of antioxidants and heat shock proteins are altered in the immune organs of selenium-deficient broiler chickens. Biological trace element research
    • (2015) Biological trace element research
    • Yang, Z.1    Liu, C.2    Zheng, W.3    Teng, X.4    Li, S.5
  • 24
    • 84938999047 scopus 로고    scopus 로고
    • Selenium deficiency downregulates selenoproteins and suppresses immune function in chicken thymus
    • Khoso PA, Yang Z, Liu C, Li S (2015) Selenium deficiency downregulates selenoproteins and suppresses immune function in chicken thymus. Biological trace element research
    • (2015) Biological trace element research
    • Khoso, P.A.1    Yang, Z.2    Liu, C.3    Li, S.4
  • 25
    • 85027936647 scopus 로고    scopus 로고
    • Cold stress induces antioxidants and Hsps in chicken immune organs
    • COI: 1:CAS:528:DC%2BC2cXhsVOnu7%2FI, PID: 24390730
    • Zhao FQ, Zhang ZW, Qu JP, et al. (2014) Cold stress induces antioxidants and Hsps in chicken immune organs. Cell Stress Chaperones 19:635–648
    • (2014) Cell Stress Chaperones , vol.19 , pp. 635-648
    • Zhao, F.Q.1    Zhang, Z.W.2    Qu, J.P.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • COI: 1:CAS:528:DyaE28XksVehtrY%3D, PID: 942051
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 84926509341 scopus 로고    scopus 로고
    • Selenoproteins protect against avian nutritional muscular dystrophy by metabolizing peroxides and regulating redox/apoptotic signaling
    • COI: 1:CAS:528:DC%2BC2MXjvFOisL4%3D, PID: 25668720
    • Huang JQ, Ren FZ, Jiang YY, Xiao C, Lei XG (2015) Selenoproteins protect against avian nutritional muscular dystrophy by metabolizing peroxides and regulating redox/apoptotic signaling. Free Radic Biol Med 83:129–138
    • (2015) Free Radic Biol Med , vol.83 , pp. 129-138
    • Huang, J.Q.1    Ren, F.Z.2    Jiang, Y.Y.3    Xiao, C.4    Lei, X.G.5
  • 28
    • 84940006206 scopus 로고    scopus 로고
    • Roles of oxidative stress and endoplasmic reticulum stress in selenium deficiency-induced apoptosis in chicken liver
    • COI: 1:CAS:528:DC%2BC2MXksValsLg%3D
    • Yao L, Du Q, Yao H, et al. (2015) Roles of oxidative stress and endoplasmic reticulum stress in selenium deficiency-induced apoptosis in chicken liver. Biometals Int J Role Metal Ions Bio Biochem Med 28:255–265
    • (2015) Biometals Int J Role Metal Ions Bio Biochem Med , vol.28 , pp. 255-265
    • Yao, L.1    Du, Q.2    Yao, H.3
  • 29
    • 84893825293 scopus 로고    scopus 로고
    • The effect of Se-deficient diet on gene expression of inflammatory cytokines in chicken brain
    • COI: 1:CAS:528:DC%2BC3sXhvFajsrjN, PID: 24318354
    • Sheng PF, Jiang Y, Zhang ZW, et al. (2014) The effect of Se-deficient diet on gene expression of inflammatory cytokines in chicken brain. Biometals 27:33–43
    • (2014) Biometals , vol.27 , pp. 33-43
    • Sheng, P.F.1    Jiang, Y.2    Zhang, Z.W.3
  • 30
    • 0030711684 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of endothelial cell dysfunction
    • COI: 1:CAS:528:DyaK2sXnt1Ggs74%3D, PID: 9410891
    • Harrison DG (1997) Cellular and molecular mechanisms of endothelial cell dysfunction. J Clin Invest 100:2153–2157
    • (1997) J Clin Invest , vol.100 , pp. 2153-2157
    • Harrison, D.G.1
  • 31
    • 0030780758 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase: what difference does it make?
    • COI: 1:CAS:528:DyaK2sXnsVymt7k%3D, PID: 9366554
    • Nathan C (1997) Inducible nitric oxide synthase: what difference does it make? J Clin Invest 100:2417–2423
    • (1997) J Clin Invest , vol.100 , pp. 2417-2423
    • Nathan, C.1
  • 32
    • 0030734267 scopus 로고    scopus 로고
    • Nitric oxide in excitable tissues: physiological roles and disease
    • COI: 1:CAS:528:DyaK2sXnsVymt7Y%3D, PID: 9366555
    • Christopherson KS, Bredt DS (1997) Nitric oxide in excitable tissues: physiological roles and disease. J Clin Invest 100:2424–2429
    • (1997) J Clin Invest , vol.100 , pp. 2424-2429
    • Christopherson, K.S.1    Bredt, D.S.2
  • 33
    • 84859487532 scopus 로고    scopus 로고
    • Nitric oxide synthases: regulation and function
    • PID: 21890489, 837a-837d
    • Forstermann U, Sessa WC (2012) Nitric oxide synthases: regulation and function. Eur Heart J 33:829–837 837a-837d
    • (2012) Eur Heart J , vol.33 , pp. 829-837
    • Forstermann, U.1    Sessa, W.C.2
  • 34
    • 33645976903 scopus 로고    scopus 로고
    • The selective inhibition of inducible nitric oxide synthase prevents intestinal ischemia-reperfusion injury in mice
    • COI: 1:CAS:528:DC%2BD28XksVWmsrw%3D, PID: 16504557
    • Barocelli E, Ballabeni V, Ghizzardi P, et al. (2006) The selective inhibition of inducible nitric oxide synthase prevents intestinal ischemia-reperfusion injury in mice. Nitric Oxide 14:212–218
    • (2006) Nitric Oxide , vol.14 , pp. 212-218
    • Barocelli, E.1    Ballabeni, V.2    Ghizzardi, P.3
  • 35
    • 0030345756 scopus 로고    scopus 로고
    • Erythrocytes may synthesize their own nitric oxide
    • COI: 1:CAS:528:DyaK2sXlvFGhtQ%3D%3D, PID: 8972893
    • Jubelin BC, Gierman JL (1996) Erythrocytes may synthesize their own nitric oxide. Am J Hypertens 9:1214–1219
    • (1996) Am J Hypertens , vol.9 , pp. 1214-1219
    • Jubelin, B.C.1    Gierman, J.L.2
  • 36
    • 33645532445 scopus 로고    scopus 로고
    • Red blood cells express a functional endothelial nitric oxide synthase
    • COI: 1:CAS:528:DC%2BD28XjtlKks7Y%3D, PID: 16368881
    • Kleinbongard P, Schulz R, Rassaf T, et al. (2006) Red blood cells express a functional endothelial nitric oxide synthase. Blood 107:2943–2951
    • (2006) Blood , vol.107 , pp. 2943-2951
    • Kleinbongard, P.1    Schulz, R.2    Rassaf, T.3
  • 37
    • 84869786258 scopus 로고    scopus 로고
    • Human red blood cells at work: identification and visualization of erythrocytic eNOS activity in health and disease
    • COI: 1:CAS:528:DC%2BC38XhslKmu7bF, PID: 23007404
    • Cortese-Krott MM, Rodriguez-Mateos A, Sansone R, et al. (2012) Human red blood cells at work: identification and visualization of erythrocytic eNOS activity in health and disease. Blood 120:4229–4237
    • (2012) Blood , vol.120 , pp. 4229-4237
    • Cortese-Krott, M.M.1    Rodriguez-Mateos, A.2    Sansone, R.3
  • 38
    • 84873735581 scopus 로고    scopus 로고
    • RBC-NOS-dependent S-nitrosylation of cytoskeletal proteins improves RBC deformability
    • COI: 1:CAS:528:DC%2BC3sXjtFKnsLc%3D, PID: 23424675
    • Grau M, Pauly S, Ali J, et al. (2013) RBC-NOS-dependent S-nitrosylation of cytoskeletal proteins improves RBC deformability. PLoS One 8:e56759
    • (2013) PLoS One , vol.8 , pp. e56759
    • Grau, M.1    Pauly, S.2    Ali, J.3
  • 39
    • 84886948605 scopus 로고    scopus 로고
    • Association between erythrocyte n-3 polyunsaturated fatty acids and biomarkers of inflammation and oxidative stress in patients with and without depression
    • COI: 1:CAS:528:DC%2BC3sXhsF2ns7bP
    • Baek D, Park Y (2013) Association between erythrocyte n-3 polyunsaturated fatty acids and biomarkers of inflammation and oxidative stress in patients with and without depression. Prostaglandins Leukot Essent Fat Acids 89:291–296
    • (2013) Prostaglandins Leukot Essent Fat Acids , vol.89 , pp. 291-296
    • Baek, D.1    Park, Y.2
  • 40
    • 84899587101 scopus 로고    scopus 로고
    • C4d deposits on the surface of RBCs in trauma patients and interferes with their function
    • COI: 1:CAS:528:DC%2BC2cXmtFaitrw%3D, PID: 24448198
    • Muroya T, Kannan L, Ghiran IC, et al. (2014) C4d deposits on the surface of RBCs in trauma patients and interferes with their function. Crit Care Med 42:e364–e372
    • (2014) Crit Care Med , vol.42 , pp. e364-e372
    • Muroya, T.1    Kannan, L.2    Ghiran, I.C.3
  • 41
    • 0037380147 scopus 로고    scopus 로고
    • Fluoride causing abnormally elevated serum nitric oxide levels in chicks
    • COI: 1:CAS:528:DC%2BD3sXisV2rsL8%3D, PID: 21782655
    • Liu G, Chai C, Cui L (2003) Fluoride causing abnormally elevated serum nitric oxide levels in chicks. Environ Toxicol Pharmacol 13:199–204
    • (2003) Environ Toxicol Pharmacol , vol.13 , pp. 199-204
    • Liu, G.1    Chai, C.2    Cui, L.3
  • 42
    • 84885472132 scopus 로고    scopus 로고
    • The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts
    • COI: 1:CAS:528:DC%2BC3sXhsF2gsLvL, PID: 23636703
    • Zhao FQ, Zhang ZW, Wang C, et al. (2013) The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts. Cell Stress Chaperones 18:773–783
    • (2013) Cell Stress Chaperones , vol.18 , pp. 773-783
    • Zhao, F.Q.1    Zhang, Z.W.2    Wang, C.3
  • 43
    • 0036357322 scopus 로고    scopus 로고
    • Neuroprotection: heat shock proteins
    • PID: 12365831
    • Kelly S, Yenari MA (2002) Neuroprotection: heat shock proteins. Curr Med Res Opin 18(Suppl 2):s55–s60
    • (2002) Curr Med Res Opin , vol.18 , pp. s55-s60
    • Kelly, S.1    Yenari, M.A.2
  • 44
    • 77952107755 scopus 로고    scopus 로고
    • Protein levels of heat shock proteins 27, 32, 60, 70, 90 and thioredoxin-1 in amnestic mild cognitive impairment: an investigation on the role of cellular stress response in the progression of Alzheimer disease
    • PID: 20362559
    • Di Domenico F, Sultana R, Tiu GF, et al. (2010) Protein levels of heat shock proteins 27, 32, 60, 70, 90 and thioredoxin-1 in amnestic mild cognitive impairment: an investigation on the role of cellular stress response in the progression of Alzheimer disease. Brain Res 1333:72–81
    • (2010) Brain Res , vol.1333 , pp. 72-81
    • Di Domenico, F.1    Sultana, R.2    Tiu, G.F.3
  • 45
    • 44149104599 scopus 로고    scopus 로고
    • Heat shock proteins: essential proteins for apoptosis regulation
    • COI: 1:CAS:528:DC%2BD1cXotlCrt70%3D, PID: 18266962
    • Lanneau D, Brunet M, Frisan E, et al. (2008) Heat shock proteins: essential proteins for apoptosis regulation. J Cell Mol Med 12:743–761
    • (2008) J Cell Mol Med , vol.12 , pp. 743-761
    • Lanneau, D.1    Brunet, M.2    Frisan, E.3
  • 46
    • 0034212699 scopus 로고    scopus 로고
    • Nitric oxide synthase induction in astroglial cell cultures: effect on heat shock protein 70 synthesis and oxidant/antioxidant balance
    • COI: 1:CAS:528:DC%2BD3cXktVCqt7Y%3D, PID: 10820432
    • Calabrese V, Copani A, Testa D, et al. (2000) Nitric oxide synthase induction in astroglial cell cultures: effect on heat shock protein 70 synthesis and oxidant/antioxidant balance. J Neurosci Res 60:613–622
    • (2000) J Neurosci Res , vol.60 , pp. 613-622
    • Calabrese, V.1    Copani, A.2    Testa, D.3
  • 47
    • 84929043170 scopus 로고    scopus 로고
    • Synergistic effects of toxic elements on heat shock proteins
    • Mahmood K, Jadoon S (2014) Synergistic effects of toxic elements on heat shock proteins. 2014:564136
    • (2014) 2014:564136
    • Mahmood, K.1    Jadoon, S.2
  • 48
    • 84919950171 scopus 로고    scopus 로고
    • Selenium deficiency influences the gene expressions of heat shock proteins and nitric oxide levels in neutrophils of broilers
    • COI: 1:CAS:528:DC%2BC2cXhslGjurrP, PID: 25315471
    • Chen X, Yao H, Yao L, et al. (2014) Selenium deficiency influences the gene expressions of heat shock proteins and nitric oxide levels in neutrophils of broilers. Biol Trace Elem Res 161:334–340
    • (2014) Biol Trace Elem Res , vol.161 , pp. 334-340
    • Chen, X.1    Yao, H.2    Yao, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.