메뉴 건너뛰기




Volumn 80, Issue , 2013, Pages 334-345

Selection for residual feed intake alters the mitochondria protein profile in pigs

Author keywords

2D DIGE; Metabolism; Mitochondria; Oxidative stress; Residual feed intake

Indexed keywords

CHAPERONIN 60; ENDOPLASMIC RETICULUM OXIDASE 1 ALPHA; HEAT SHOCK PROTEIN 70; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 84874797532     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.01.017     Document Type: Article
Times cited : (35)

References (56)
  • 1
    • 84874816411 scopus 로고    scopus 로고
    • World Population Prospects
    • United Nations, New York, Department of Economic, P.D. Social Affairs (Eds.)
    • World Population Prospects The 2010 revision, highlights and advance tables 2011, United Nations, New York. Department of Economic, P.D. Social Affairs (Eds.).
    • (2011) The 2010 revision, highlights and advance tables
  • 2
    • 80755187936 scopus 로고    scopus 로고
    • Fresh and fresh lean pork are substantial sources of key nutrients when these products are consumed by adults in the United States
    • Murphy M.M., Spungen J.H., Bi X., Barraj L.M. Fresh and fresh lean pork are substantial sources of key nutrients when these products are consumed by adults in the United States. Nutr Res 2011, 31:776-783.
    • (2011) Nutr Res , vol.31 , pp. 776-783
    • Murphy, M.M.1    Spungen, J.H.2    Bi, X.3    Barraj, L.M.4
  • 3
    • 84863096620 scopus 로고    scopus 로고
    • Red meat in global nutrition
    • McNeill S., Van Elswyk M.E. Red meat in global nutrition. Meat Sci 2012, 92:166-173.
    • (2012) Meat Sci , vol.92 , pp. 166-173
    • McNeill, S.1    Van Elswyk, M.E.2
  • 4
    • 80053121147 scopus 로고    scopus 로고
    • Effects of ad libitum and restricted feeding on early production performance and body composition of Yorkshire pigs selected for reduced residual feed intake
    • Boddicker N., Gabler N.K., Spurlock M.E., Nettleton D., Dekkers J.C.M. Effects of ad libitum and restricted feeding on early production performance and body composition of Yorkshire pigs selected for reduced residual feed intake. Animal 2011, 5:1344-1353.
    • (2011) Animal , vol.5 , pp. 1344-1353
    • Boddicker, N.1    Gabler, N.K.2    Spurlock, M.E.3    Nettleton, D.4    Dekkers, J.C.M.5
  • 5
    • 38949149635 scopus 로고    scopus 로고
    • Selection response and genetic parameters for residual feed intake in Yorkshire swine
    • Cai W., Casey D.S., Dekkers J.C.M. Selection response and genetic parameters for residual feed intake in Yorkshire swine. J Anim Sci 2008, 86:287-298.
    • (2008) J Anim Sci , vol.86 , pp. 287-298
    • Cai, W.1    Casey, D.S.2    Dekkers, J.C.M.3
  • 6
  • 7
    • 65549120041 scopus 로고    scopus 로고
    • Physiological basis for residual feed intake
    • Herd R.M., Arthur P.F. Physiological basis for residual feed intake. J Anim Sci 2009, 87:E64-E71.
    • (2009) J Anim Sci , vol.87
    • Herd, R.M.1    Arthur, P.F.2
  • 8
    • 3042786484 scopus 로고    scopus 로고
    • Biological basis for variation in residual feed intake in beef cattle. 1. Review of potential mechanisms
    • Herd R.M., Oddy V.H., Richardson E.C. Biological basis for variation in residual feed intake in beef cattle. 1. Review of potential mechanisms. Aust J Exp Agric 2004, 44:423-430.
    • (2004) Aust J Exp Agric , vol.44 , pp. 423-430
    • Herd, R.M.1    Oddy, V.H.2    Richardson, E.C.3
  • 9
    • 0015882341 scopus 로고
    • Mitochondrial generation of hydrogen-peroxide - general properties and effect of hyperbaric-oxygen
    • Boveris A., Chance B. Mitochondrial generation of hydrogen-peroxide - general properties and effect of hyperbaric-oxygen. Biochem J 1973, 134:707-716.
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 10
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979, 59:527-605.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 11
    • 65549154306 scopus 로고    scopus 로고
    • Association of mitochondrial function and feed efficiency in poultry and livestock species
    • Bottje W.G., Carstens G.E. Association of mitochondrial function and feed efficiency in poultry and livestock species. J Anim Sci 2009, 87:E48-E63.
    • (2009) J Anim Sci , vol.87
    • Bottje, W.G.1    Carstens, G.E.2
  • 12
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002, 82:47-95.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 13
    • 0036254702 scopus 로고    scopus 로고
    • Proteolytic response to oxidative stress in mammalian cells
    • Mehlhase J., Grune T. Proteolytic response to oxidative stress in mammalian cells. Biol Chem 2002, 383:559-567.
    • (2002) Biol Chem , vol.383 , pp. 559-567
    • Mehlhase, J.1    Grune, T.2
  • 14
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T., Ullrich O., Sitte N., Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 2000, 377:65-68.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 15
    • 0342810119 scopus 로고    scopus 로고
    • National Academies Press, Washington, DC
    • NRC Nutrient requirements of swine 1998, National Academies Press, Washington, DC. 10th ed.
    • (1998) NRC Nutrient requirements of swine
  • 16
    • 84882720646 scopus 로고    scopus 로고
    • Improved nutrient digestability and retention partially explains feed efficiency gains in pigs selected for low residual feed intake
    • Harris A.J., Patience J.F., Lonergan S.M., Dekkers J.C.M., Gabler N.K. Improved nutrient digestability and retention partially explains feed efficiency gains in pigs selected for low residual feed intake. J Anim Sci 2012, 90:164-166. 10.2527/jas.53855.
    • (2012) J Anim Sci , vol.90 , pp. 164-166
    • Harris, A.J.1    Patience, J.F.2    Lonergan, S.M.3    Dekkers, J.C.M.4    Gabler, N.K.5
  • 17
    • 2042440962 scopus 로고    scopus 로고
    • Low feed efficient broilers within a single genetic line exhibit higher oxidative stress and protein expression in breast muscle with lower mitochondrial complex activity
    • Iqbal M., Pumford N.R., Tang Z.X., Lassiter K., Wing T., Cooper M., et al. Low feed efficient broilers within a single genetic line exhibit higher oxidative stress and protein expression in breast muscle with lower mitochondrial complex activity. Poult Sci 2004, 83:474-484.
    • (2004) Poult Sci , vol.83 , pp. 474-484
    • Iqbal, M.1    Pumford, N.R.2    Tang, Z.X.3    Lassiter, K.4    Wing, T.5    Cooper, M.6
  • 18
    • 77957003097 scopus 로고
    • Preparation, properties, and conditions for assay of mitochondria: slaughterhouse material, small-scale
    • Academic Press, MEP, R.W. Estabrook (Ed.)
    • Smith A.L. Preparation, properties, and conditions for assay of mitochondria: slaughterhouse material, small-scale. Meths Enzymol 1967, 81-86. Academic Press, MEP. R.W. Estabrook (Ed.).
    • (1967) Meths Enzymol , pp. 81-86
    • Smith, A.L.1
  • 20
    • 0036528091 scopus 로고    scopus 로고
    • Association of mitochondrial function with feed efficiency within a single genetic line of male broilers
    • Bottje W., Iqbal M., Tang Z., Cawthon D., Okimoto R., Wing T., et al. Association of mitochondrial function with feed efficiency within a single genetic line of male broilers. Poult Sci 2002, 81:546-555.
    • (2002) Poult Sci , vol.81 , pp. 546-555
    • Bottje, W.1    Iqbal, M.2    Tang, Z.3    Cawthon, D.4    Okimoto, R.5    Wing, T.6
  • 21
    • 0035320648 scopus 로고    scopus 로고
    • Lung mitochondrial dysfunction in pulmonary hypertension syndrome. I. Site-specific defects in the electron transport chain
    • Iqbal M., Cawthon D., Wideman R.F., Bottje W.G. Lung mitochondrial dysfunction in pulmonary hypertension syndrome. I. Site-specific defects in the electron transport chain. Poult Sci 2001, 80:485-495.
    • (2001) Poult Sci , vol.80 , pp. 485-495
    • Iqbal, M.1    Cawthon, D.2    Wideman, R.F.3    Bottje, W.G.4
  • 22
    • 80555126736 scopus 로고    scopus 로고
    • Myosin light chain 1 release from myofibrillar fraction during postmortem aging is a potential indicator of proteolysis and tenderness of beef
    • Anderson M.J., Lonergan S.M., Huff-Lonergan E. Myosin light chain 1 release from myofibrillar fraction during postmortem aging is a potential indicator of proteolysis and tenderness of beef. Meat Sci 2012, 90:345-351.
    • (2012) Meat Sci , vol.90 , pp. 345-351
    • Anderson, M.J.1    Lonergan, S.M.2    Huff-Lonergan, E.3
  • 23
    • 84855685420 scopus 로고    scopus 로고
    • Proteomic assessment of the acute phase of dystrophin deficiency in mdx mice
    • Gardan-Salmon D., Dixon J.M., Lonergan S.M., Selsby J.T. Proteomic assessment of the acute phase of dystrophin deficiency in mdx mice. Eur J Appl Physiol 2011, 111:2763-2773.
    • (2011) Eur J Appl Physiol , vol.111 , pp. 2763-2773
    • Gardan-Salmon, D.1    Dixon, J.M.2    Lonergan, S.M.3    Selsby, J.T.4
  • 24
    • 2342576244 scopus 로고    scopus 로고
    • Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles
    • Melody J.L., Lonergan S.M., Rowe L.J., Huiatt T.W., Mayes M.S., Huff-Lonergan E. Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. J Anim Sci 2004, 82:1195-1205.
    • (2004) J Anim Sci , vol.82 , pp. 1195-1205
    • Melody, J.L.1    Lonergan, S.M.2    Rowe, L.J.3    Huiatt, T.W.4    Mayes, M.S.5    Huff-Lonergan, E.6
  • 25
    • 3042703233 scopus 로고    scopus 로고
    • Biological basis for variation in residual feed intake in beef cattle. 2. Synthesis of results following divergent selection
    • Richardson E.C., Herd R.M. Biological basis for variation in residual feed intake in beef cattle. 2. Synthesis of results following divergent selection. Aust J Exp Agric 2004, 44:431-440.
    • (2004) Aust J Exp Agric , vol.44 , pp. 431-440
    • Richardson, E.C.1    Herd, R.M.2
  • 26
    • 69549109918 scopus 로고    scopus 로고
    • Self-sufficient catalytic system of human cytochrome P450 4A11 and NADPH-P450 reductase
    • Han S., Eun C.Y., Han J.S., Chun Y.J., Kim D.H., Yun C.H., et al. Self-sufficient catalytic system of human cytochrome P450 4A11 and NADPH-P450 reductase. Biomol Ther 2009, 17:156-161.
    • (2009) Biomol Ther , vol.17 , pp. 156-161
    • Han, S.1    Eun, C.Y.2    Han, J.S.3    Chun, Y.J.4    Kim, D.H.5    Yun, C.H.6
  • 27
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., et al. Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 2009, 186:783-792.
    • (2009) J Cell Biol , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6
  • 28
    • 84859480323 scopus 로고    scopus 로고
    • Protein disulfide isomerase in redox cell signaling and homeostasis
    • Laurindo F.R.M., Pescatore L.A., Fernandes D.D. Protein disulfide isomerase in redox cell signaling and homeostasis. Free Radic Biol Med 2012, 52:1954-1969.
    • (2012) Free Radic Biol Med , vol.52 , pp. 1954-1969
    • Laurindo, F.R.M.1    Pescatore, L.A.2    Fernandes, D.D.3
  • 29
    • 33750902737 scopus 로고    scopus 로고
    • The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control
    • Goerlach A., Klappa P., Kietzmann T. The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxid. Redox Signal. 2006, 8:1391-1418.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1391-1418
    • Goerlach, A.1    Klappa, P.2    Kietzmann, T.3
  • 30
    • 70349352744 scopus 로고    scopus 로고
    • Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase
    • Santos C.X.C., Tanaka L.Y., Wosniak J., Laurindo F.R.M. Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase. Antioxid. Redox Signal. 2009, 11:2409-2427.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2409-2427
    • Santos, C.X.C.1    Tanaka, L.Y.2    Wosniak, J.3    Laurindo, F.R.M.4
  • 31
    • 41449116766 scopus 로고    scopus 로고
    • Ero1 and redox homeostasis in the endoplasmic reticulum
    • Sevier C.S., Kaiser C.A. Ero1 and redox homeostasis in the endoplasmic reticulum. BBA-Mol Cell Res 2008, 1783:549-556.
    • (2008) BBA-Mol Cell Res , vol.1783 , pp. 549-556
    • Sevier, C.S.1    Kaiser, C.A.2
  • 32
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 1991, 11:81-128.
    • (1991) Free Radic Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 34
    • 78650966910 scopus 로고    scopus 로고
    • Effects of selection for decreased residual feed intake on composition and quality of fresh pork
    • Smith R.M., Gabler N.K., Young J.M., Cai W., Boddicker N.J., Anderson M.J., et al. Effects of selection for decreased residual feed intake on composition and quality of fresh pork. J Anim Sci 2011, 89:192-200.
    • (2011) J Anim Sci , vol.89 , pp. 192-200
    • Smith, R.M.1    Gabler, N.K.2    Young, J.M.3    Cai, W.4    Boddicker, N.J.5    Anderson, M.J.6
  • 36
    • 0031549576 scopus 로고    scopus 로고
    • Caloric intake and aging
    • Weindruch R., Sohal R.S. Caloric intake and aging. N Engl J Med 1997, 337:986-994.
    • (1997) N Engl J Med , vol.337 , pp. 986-994
    • Weindruch, R.1    Sohal, R.S.2
  • 37
    • 0036710886 scopus 로고    scopus 로고
    • Mechanisms of aging: an appraisal of the oxidative stress hypothesis
    • Sohal R.S., Mockett R.J., Orr W.C. Mechanisms of aging: an appraisal of the oxidative stress hypothesis. Free Radic Biol Med 2002, 33:575-586.
    • (2002) Free Radic Biol Med , vol.33 , pp. 575-586
    • Sohal, R.S.1    Mockett, R.J.2    Orr, W.C.3
  • 38
    • 75449104615 scopus 로고    scopus 로고
    • Gene expression profiling of the short-term adaptive response to acute caloric restriction in liver and adipose tissues of pigs differing in feed efficiency
    • Lkhagvadorj S., Qu L., Cai W.G., Couture O.P., Barb C.R., Hausman G.J., et al. Gene expression profiling of the short-term adaptive response to acute caloric restriction in liver and adipose tissues of pigs differing in feed efficiency. Am J Physiol Regul Integr Comp Physiol 2010, 298:R494-R507.
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.298
    • Lkhagvadorj, S.1    Qu, L.2    Cai, W.G.3    Couture, O.P.4    Barb, C.R.5    Hausman, G.J.6
  • 39
    • 0035403165 scopus 로고    scopus 로고
    • Caloric restriction decreases mitochondrial free radical generation at complex I and lowers oxidative damage to mitochondrial DNA in the rat heart
    • Gredilla R., Sanz A., Lopez-Torres M., Barja G. Caloric restriction decreases mitochondrial free radical generation at complex I and lowers oxidative damage to mitochondrial DNA in the rat heart. FASEB J 2001, 15:1589.
    • (2001) FASEB J , vol.15 , pp. 1589
    • Gredilla, R.1    Sanz, A.2    Lopez-Torres, M.3    Barja, G.4
  • 41
    • 79957656816 scopus 로고    scopus 로고
    • Protein composition and function of red and white skeletal muscle mitochondria
    • Glancy B., Balaban R.S. Protein composition and function of red and white skeletal muscle mitochondria. Am J Physiol Cell Physiol 2011, 300:C1280-C1290.
    • (2011) Am J Physiol Cell Physiol , vol.300
    • Glancy, B.1    Balaban, R.S.2
  • 42
    • 11144318614 scopus 로고    scopus 로고
    • Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging
    • Kanski J., Behring A., Pelling J., Schoneich C. Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging. Am J Physiol Heart Circ Physiol 2005, 288:H371-H381.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Kanski, J.1    Behring, A.2    Pelling, J.3    Schoneich, C.4
  • 43
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota D.A., Davies K.J.A. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 2002, 4:674-680.
    • (2002) Nat Cell Biol , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.A.2
  • 44
    • 77950676470 scopus 로고    scopus 로고
    • The role of protein quality control in mitochondrial protein homeostasis under oxidative stress
    • Bender T., Leidhold C., Ruppert T., Franken S., Voos W. The role of protein quality control in mitochondrial protein homeostasis under oxidative stress. Proteomics 2010, 10:1426-1443.
    • (2010) Proteomics , vol.10 , pp. 1426-1443
    • Bender, T.1    Leidhold, C.2    Ruppert, T.3    Franken, S.4    Voos, W.5
  • 45
    • 84862264118 scopus 로고    scopus 로고
    • Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production
    • Jong C.J., Azuma J., Schaffer S. Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production. Amino Acids 2012, 42:2223-2232.
    • (2012) Amino Acids , vol.42 , pp. 2223-2232
    • Jong, C.J.1    Azuma, J.2    Schaffer, S.3
  • 47
    • 79959525266 scopus 로고    scopus 로고
    • Effect of selection for residual feed intake on feeding behavior and daily feed intake patterns in Yorkshire swine
    • Young J.M., Cai W., Dekkers J.C.M. Effect of selection for residual feed intake on feeding behavior and daily feed intake patterns in Yorkshire swine. J Anim Sci 2011, 89:639-647.
    • (2011) J Anim Sci , vol.89 , pp. 639-647
    • Young, J.M.1    Cai, W.2    Dekkers, J.C.M.3
  • 48
    • 26244465889 scopus 로고    scopus 로고
    • Explaining the phenomenon of nitrate tolerance
    • Munzel T., Daiber A., Mulsch A. Explaining the phenomenon of nitrate tolerance. Circ Res 2005, 97:618-628.
    • (2005) Circ Res , vol.97 , pp. 618-628
    • Munzel, T.1    Daiber, A.2    Mulsch, A.3
  • 49
    • 3242879188 scopus 로고    scopus 로고
    • 'The stress of ding': the role of heat shock proteins in the regulation of apoptosis
    • Beere H.M. 'The stress of ding': the role of heat shock proteins in the regulation of apoptosis. J Cell Sci 2004, 117:2641-2651.
    • (2004) J Cell Sci , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 50
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere H.M., Wolf B.B., Cain K., Mosser D.D., Mahboubi A., Kuwana T., et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2000, 2:469-475.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3    Mosser, D.D.4    Mahboubi, A.5    Kuwana, T.6
  • 51
    • 0031026233 scopus 로고    scopus 로고
    • P75, a member of the heat shock protein family, undergoes tyrosine phosphorylation in response to oxidative stress
    • Hadari Y.R., Haring H.U., Zick Y. p75, a member of the heat shock protein family, undergoes tyrosine phosphorylation in response to oxidative stress. J Biol Chem 1997, 272:657-662.
    • (1997) J Biol Chem , vol.272 , pp. 657-662
    • Hadari, Y.R.1    Haring, H.U.2    Zick, Y.3
  • 52
    • 84865142024 scopus 로고    scopus 로고
    • Impairment of cellular immunity is associated with overexpression of heat shock protein 70 in neonatal pigs with intrauterine growth retardation
    • Zhong X., Li W., Huang X.X., Zhang L.L., Yimamu M., Raiput N., et al. Impairment of cellular immunity is associated with overexpression of heat shock protein 70 in neonatal pigs with intrauterine growth retardation. Cell Stress Chaperones 2012, 17:495-505.
    • (2012) Cell Stress Chaperones , vol.17 , pp. 495-505
    • Zhong, X.1    Li, W.2    Huang, X.X.3    Zhang, L.L.4    Yimamu, M.5    Raiput, N.6
  • 53
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A., Kraeft S.K., Kurt-Jones E.A., Stevenson M.A., Chen L.B., Finberg R.W., et al. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 2000, 6:435-442.
    • (2000) Nat Med , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6
  • 55
    • 0344959625 scopus 로고    scopus 로고
    • Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis
    • Xanthoudakis S., Roy S., Rasper D., Hennessey T., Aubin Y., Cassady R., et al. Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis. EMBO J 1999, 18:2049-2056.
    • (1999) EMBO J , vol.18 , pp. 2049-2056
    • Xanthoudakis, S.1    Roy, S.2    Rasper, D.3    Hennessey, T.4    Aubin, Y.5    Cassady, R.6
  • 56
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink A.L. Chaperone-mediated protein folding. Physiol Rev 1999, 79:425-449.
    • (1999) Physiol Rev , vol.79 , pp. 425-449
    • Fink, A.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.