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Volumn 25, Issue 1, 1997, Pages 105-136

5 the cellular stress response to exercise

(1)  Locke, Marius a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

EID: 0030629858     PISSN: 00916331     EISSN: 15383008     Source Type: Journal    
DOI: 10.1249/00003677-199700250-00007     Document Type: Article
Times cited : (120)

References (48)
  • 1
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis, J. Proteins as molecular chaperones. Nature 328:378-379, 1987.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 2
    • 0027158545 scopus 로고
    • Structure and organization of a murine gene encoding small heat-shock protein Hsp25
    • Gaestel, M., R. Gotthardt, and T. Muller. Structure and organization of a murine gene encoding small heat-shock protein Hsp25. Gene 128:279-283, 1993.
    • (1993) Gene , vol.128 , pp. 279-283
    • Gaestel, M.1    Gotthardt, R.2    Muller, T.3
  • 3
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic HSP, 70 genes revealed by comparison with the nucleotide: Sequence of human HSP70
    • Hunt, C., and R. I. Morimoto. Conserved features of eukaryotic HSP, 70 genes revealed by comparison with the nucleotide: sequence of human HSP70; Proci Nall. Acad. Sai I. S. A 82:6455-6459, 1985.
    • (1985) Proci Nall. Acad. Sai I.S.A , vol.82 , pp. 6455-6459
    • Hunt, C.1    Morimoto, R.I.2
  • 4
    • 85026144427 scopus 로고
    • Decreased polysom.Il HSP-70 may slow polypeptide elongation during skeletal muscle atrophy
    • Ku, Z., J. Yang, V. Mehon, and D. B. Fhomason. Decreased polysom.il HSP-70 may slow polypeptide elongation during skeletal muscle atrophy. Am. J. Physiol 268:G1360-C1374. 1995.
    • (1995) Am. J. Physiol , vol.268 , pp. G1360-C1374
    • Ku, Z.1    Yang, J.2    Mehon, V.3    Fhomason, D.B.4
  • 5
    • 0025727532 scopus 로고
    • Phosphorylation of HSP27 during development anti decay of thermotolerance in Chinese hamster t ells
    • Landry, J., P. Chretien, A. Laslo, and H. Lambert. Phosphorylation of HSP27 during development anti decay of thermotolerance in Chinese hamster t ells J. Cell. Pksyiol. 147: 93-101, 1991.
    • (1991) J. Cell. Pksyiol , vol.147 , pp. 93-101
    • Landry, J.1    Chretien, P.2    Laslo, A.3    Lambert, H.4
  • 6
    • 0026570931 scopus 로고
    • Human hsp27 is phosphtirylated at serines-78 and serines-S2 by lu at shock and mitogen-activated kinases that rec ognize the same amino acid motif as SO kinase-II
    • Landry, J., I. Lambert, M. Zhou, J. X. Lavoie, F. Hickey, I. Weber, and C. W. Anderson. Human hsp27 is phosphtirylated at serines-78 and serines-S2 by lu at shock and mitogen-activated kinases that rec ognize the same amino acid motif as SO kinase-II. J. Biol. Chem. 267:794-803, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 794-803
    • Landry, J.1    Lambert, I.2    Zhou, M.3    Lavoie, J.X.4    Hickey, F.5    Weber, I.6    Anderson, C.W.7
  • 7
    • 0019833479 scopus 로고
    • The arcumulation of three spt t ific proteins related to glucose-tegulated protein in a temperature-sensitive hamster mutant cell line K12
    • Lee, A.S. The arcumulation of three spt t ific proteins related to glucose-tegulated protein in a temperature-sensitive hamster mutant cell line K12. J. Cell Physiol. 106:119-125, 1981.
    • (1981) J. Cell Physiol , vol.106 , pp. 119-125
    • Lee, A.S.1
  • 8
    • 0029079045 scopus 로고
    • Identification of a major subfamily t it lat ge hsp70-like proteins through cloning of the mammalian 110-kDa heat shock protein
    • Lee-Yoon, D., D. Easton, M. Murawski, R. Bin d, and J R. Subjet k. Identification of a major subfamily t it lat ge hsp70-like proteins through cloning of the mammalian 110-kDa heat shock protein J. Idol. Chem.170:15725-15733, 1995.
    • (1995) J. Idol. Chem , vol.170 , pp. 15725-15733
    • Lee-Yoon, D.1    Easton, D.2    Murawski, M.3    Bind, R.4    Subjetk, J.R.5
  • 9
    • 0020639291 scopus 로고
    • Induc tion of thermotoleranc e and enhanced heat shock protein sc nthesis in (.hi-nese hamsu i fibroblasts be sodium arsenite and by ethanol
    • Li, G. C. Induc tion of thermotoleranc e and enhanced heat shock protein sc nthesis in (.hi-nese hamsu i fibroblasts be sodium arsenite and by ethanol. J. Cell. Physiol. 115:116-122. 1983.
    • (1983) J. Cell. Physiol , vol.115 , pp. 116-122
    • Li, G.C.1
  • 10
    • 0028958828 scopus 로고
    • Effects of expression human 1 lsp70 and its deletion derivatives on heat killing and R.YA and protein synthesis
    • Li, L., G. Shell, and G. C. Li. Effects of expression human 1 lsp70 and its deletion derivatives on heat killing and R.YA and protein synthesis. Exp. Cell. Res. 217:460-468, 1995
    • (1995) Exp. Cell. Res. , vol.217 , pp. 460-468
    • Li, L.1    Shell, G.2    Li, G.C.3
  • 11
    • 0023924166 scopus 로고
    • Characterization of the thermotqjgrant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression
    • Mizzen, L. A., and W. J. Welch. Characterization of the thermotqjgrant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression. J. Cell Biol. 106:1105-1116, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 1105-1116
    • Mizzen, L.A.1    Welch, W.J.2
  • 12
    • 0026114522 scopus 로고
    • The 2 mammalian mitochondrial stress proteins, grp-75 and hsp-58, transiently interact with newly synthesized mitochondrial proteins
    • Auzzen, L. A., A. N. Kabiling, and W. J. Welch. The 2 mammalian mitochondrial stress proteins, grp-75 and hsp-58, transiently interact with newly synthesized mitochondrial proteins. CellRegul 2:165-179, 1991.
    • (1991) Cellregul , vol.2 , pp. 165-179
    • Auzzen, L.A.1    Kabiling, A.N.2    Welch, W.J.3
  • 13
    • 0024542186 scopus 로고
    • Murine 86-and 84-kDa heat shock proteins. CDNA sequences, chromosome assignments, and evolutionary origins
    • Mdpre, S. K., C. Kozak, E. A Robinson, S. J. Ullrich, and E. Appella. Murine 86-and 84-kDa heat shock proteins. cDNA sequences, chromosome assignments, and evolutionary origins, J. Biol. Chem. 264:5343-5351, 1987.
    • (1987) J. Biol. Chem , vol.264 , pp. 5343-5351
    • Mdpre, S.K.1    Kozak, C.2    Robinson, E.A.3    Ullrich, S.J.4    Appella, E.5
  • 14
    • 0023052239 scopus 로고
    • An HSI’7()-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S. and H. R. B. Pelham. An HSI’7()-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 16: 291-300, 1986.
    • (1986) Cell , vol.16 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 15
    • 0027504337 scopus 로고
    • Basil mechanisms oi cardiac gene expression
    • Nadal-Ginard, B., and V. Mahdavi. Basil mechanisms oi cardiac gene expression. I nr Heart J. 14:2-11. 1993.
    • (1993) I Nr Heart J , vol.14 , pp. 2-11
    • Nadal-Ginard, B.1    Mahdavi, V.2
  • 16
    • 0022548519 scopus 로고
    • A major collagen-binding protein of chick embrvo fibroblasts is a novel heat shock protein
    • Nagata, K., S. Saga, and K. M. Yamada. A major collagen-binding protein of chick embrvo fibroblasts is a novel heat shock protein J. CelI Biol. 103:223-229, 1986.
    • (1986) J. Celi Biol , vol.103 , pp. 223-229
    • Nagata, K.1    Saga, S.2    Yamada, K.M.3
  • 17
    • 0030049318 scopus 로고    scopus 로고
    • The iegulatorv domain of the human heal shock factor 1 is suificient to sense heat stress
    • Newton, E. M., U. Knauf, M. Green, and R. E. Kingston. The iegulatorv domain of the human heal shock factor 1 is suificient to sense heat stress. Mol. Cell Bel 16:839-846. 1996.
    • (1996) Mol. Cell Bel , vol.16 , pp. 839-846
    • Newton, E.M.1    Knauf, U.2    Green, M.3    Kingston, R.E.4
  • 18
    • 0027993188 scopus 로고
    • Diminished heal shock protein 70 niRNA induction in aged rat hearts aftei ischemia
    • Nina, Y., K. Abe, M. Aoki, I. Olmo, and S. Isoyama. Diminished heal shock protein 70 niRNA induction in aged rat hearts aftei ischemia. Am. J. Physiol 267:H1795-H1803, 1994.
    • (1994) Am. J. Physiol , vol.267 , pp. H1795-H1803
    • Nina, Y.1    Abe, K.2    Aoki, M.3    Olmo, I.4    Isoyama, S.5
  • 19
    • 0019485241 scopus 로고
    • A cellular protein that assoc iates with the transforming protein ol Rous sarcoma virus is also a heat-shock protein
    • Oppermann, H., W Levinson, and. M. Bishop. A cellular protein that assoc iates with the transforming protein ol Rous sarcoma virus is also a heat-shock protein. Pun. Mall Acad Sr J. V. S. A. 78:1067-1071, 1981.
    • (1981) Pun. Mall Acad Sr J. V. S. A. , vol.78 , pp. 1067-1071
    • Oppermann, H.1    Levinson, W.2    Bishop, M.3
  • 20
    • 0029157324 scopus 로고    scopus 로고
    • Expression of stress proteins and mito-chondria! chaperonins in chronical: Stimulated skeletal muscle
    • Ornatsky, O. I.., M. K. Connor, and D. A. Hood. Expression of stress proteins and mito-chondria! chaperonins in chronical: stimulated skeletal muscle. Biochem. J. 311:110-123.
    • Biochem. J. , vol.311 , pp. 110-123
    • Ornatsky, O.I.1    Connor, M.K.2    Hood, D.A.3
  • 21
    • 0020184673 scopus 로고
    • A regulator; upstream promoter element in Drosophila hsp 70 heat shock gene
    • Pelham, H. R. B. A regulator; upstream promoter element in Drosophila hsp 70 heat shock gene. Cell 30:517-52, 1982.
    • (1982) Cell , vol.30 , pp. 517-552
    • Pelham, H.R.B.1
  • 22
    • 0022969885 scopus 로고
    • Speculations of the functions I the major heat shock and glucose regulated proteins
    • Pelham, M. R. B. Speculations of the functions., I the major heat shock and glucose regulated proteins, Cell 46:959-961, 1936.
    • (1936) Cell , vol.46 , pp. 959-961
    • Pelham, M.1
  • 23
    • 0024755682 scopus 로고
    • Regulation' of HSP70 synthesis hv messenger RNA degradation
    • Pet Tseii, R. B., and S. Lindquist Regulation' of HSP70 synthesis hv messenger RNA degradation. CetlRegul. 1:135-149, 1939.
    • (1939) Cetlregul , vol.1 , pp. 135-149
    • Pet Tseii, R.B.1    Lindquist, S.2
  • 24
    • 0028950507 scopus 로고
    • Effect of an alkaline shift on induction of the heat shock response in human fibroblasts
    • Petronini, I., R. Alfieri, C. Campanini, and A. F. Borghetti. Effect of an alkaline shift on induction of the heat shock response in human fibroblasts. J. Cell Physiol. 162: 322-329. 1995.
    • (1995) J. Cell Physiol. , vol.162 , pp. 322-329
    • Petronini, I.1    Alfieri, R.2    Campanini, C.3    Borghetti, A.F.4
  • 25
    • 0017665008 scopus 로고
    • Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation
    • Pouyssegur, J., R. P. G. Shiu, and I. Pastan. Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation. Cell 11:941-947, 1977.
    • (1977) Cell , vol.11 , pp. 941-947
    • Pouyssegur, J.1    Shiu, R.P.G.2    Pastan, I.3
  • 26
    • 0023638872 scopus 로고
    • Transformation of glucocorticoid and progesterone receptors to the DNA-binding state
    • Pratt', W. B. Transformation of glucocorticoid and progesterone receptors to the DNA-binding state. J. Cell. Biochem. 35:51-68, 1987.
    • (1987) J. Cell. Biochem , vol.35 , pp. 51-68
    • Pratt', W.B.1
  • 27
    • 85026141605 scopus 로고
    • Heat shock is lethal to fibroblasts mi-croinjected with antibodies against hsp70
    • Riabowol, K. T., L. A. Mizzen, and W. J. Welch. Heat shock is lethal to fibroblasts mi-croinjected with antibodies against hsp70. Science 242:453-436, 1938.
    • (1938) Science , vol.242 , pp. 436-453
    • Riabowol, K.T.1    Mizzen, L.A.2    Welch, W.J.3
  • 28
    • 0022893717 scopus 로고
    • The synergistic effect of hyperthermia and ethanol of changing gene expression of mouse lymphocytes
    • Rodenhiser, D. I., J. H. Jung, and B. G. Atkinson. The synergistic effect of hyperthermia and ethanol of changing gene expression of mouse lymphocytes. Can.J. Cftol 28:1986.
    • (1986) Can.J. Cftol , pp. 28
    • Rodenhiser, D.I.1    Jung, J.H.2    Atkinson, B.G.3
  • 29
    • 0023661048 scopus 로고
    • The 90-kilodalton peptide of the heme-regulated eIF-2a kinase has sequence similarity with the 90-kilodalton heat sKoch protein
    • Rose, D. W., R. E. H. Wettenhall, W. kudlicki, G. Kramer, and B. Hardestv. The 90-kilodalton peptide of the heme-regulated eIF-2a kinase has sequence similarity with the 90-kilodalton heat sKoch protein. Biochemistry 26:6582-6537. 1987.
    • (1987) Biochemistry , vol.26 , pp. 6537-6582
    • Rose, D.W.1    Wettenhall, R.E.H.2    Kudlicki, W.3    Kramer, G.4    Hardestv, B.5
  • 30
    • 85026150996 scopus 로고    scopus 로고
    • A feat shock protein expression'after training in the iplantaris muscle of Fischer 344 tats
    • Samelman, T. R., and S. E. Alway, A feat shock protein expression'after training in the iplantaris muscle of Fischer 344 tats Mid Sd Sports Exerc: 28:8115, 1999.
    • (1999) Mid Sd Sports Exerc , vol.28 , pp. 8115
    • Samelman, T.R.1    Alway, S.E.2
  • 31
    • 0025290187 scopus 로고
    • The 56-59-kilodalton protein s; identified in untransformed steroid receptor complexes is a unique protein that ixists in tytospl in a complex with both the 70-and 90-kilodalton. Heat shock proteins
    • Sanchez, E. R., L. E. Fabei, W.J. Henze, and W. B. Pratt. The 56-59-kilodalton protein s; identified in untransformed steroid receptor complexes is a unique protein that ixists in tytospl in a complex with both the 70-and 90-kilodalton., heat shock proteins. BioChemisirs 29:5145-5152. 1990.
    • (1990) Biochemisirs , vol.29 , pp. 5145-5152
    • Sanchez, E.R.1    Fabei, L.E.2    Henze, W.J.3    Pratt, W.B.4
  • 32
    • 0025989349 scopus 로고
    • Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DN.-V binding ability
    • Sarge, V K. D., J. Zimarino, K. Holm, C. Wu, and R. I. Morimoto. Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DN.-V binding ability. Qenes Dm. 5:1902-1911, 1991.
    • (1991) Qenes Dm. , vol.5 , pp. 1902-1911
    • Sarge, V.K.D.1    Zimarino, J.2    Holm, K.3    Wu, C.4    Morimoto, R.I.5
  • 33
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor involves oligomerization, acquisition of DMA-binding activity, and nuclear localization and can incur in the absence of stress
    • Sarge, K. D, S P Murplyy, and R. I. Morimoto. Activation of heat shock gene transcription by heat shock factor involves oligomerization, acquisition of DMA-binding activity, and nuclear localization and can incur in the absence of stress. Mol. Cell Biol. 13: 1592-1407. 1993.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 1407-1592
    • Sarge, K.D.1    Murplyy, S.P.2    Morimoto, R.I.3
  • 34
    • 0028241317 scopus 로고
    • Expression of heat shock factor 2 in mouse testis potential role as a regulator of heat-shock gene expression during spermatogenesis
    • Sarge, K. D., O.-K. Park-Sarge, J. D. Kirby, K. E. Mavo, and R. I. Morimoto. Expression of heat shock factor 2 in mouse testis potential role as a regulator of heat-shock gene expression during spermatogenesis. Biol Reprod. 50:1334-1343, 1994.
    • (1994) Biol Reprod , vol.50 , pp. 1334-1343
    • Sarge, K.D.1    Park-Sarge, O.-K.2    Kirby, J.D.3    Mavo, K.E.4    Morimoto, R.I.5
  • 35
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., A. Baici, H. Gehring, and P. Christen. Kinetics of molecular chaperone action. Science 265:971-973, 1994.
    • (1994) Science , vol.265 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 36
    • 0026643651 scopus 로고
    • The transport ol' ptoleins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. D
    • Shi, V., and J. O. Thomas. The transport ol' ptoleins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. D. Mol. Cell. Biol. 12:2186-2192, 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2186-2192
    • Shi, V.1    Thomas, J.O.2
  • 37
    • 0028835412 scopus 로고
    • HSP70 induction during exercise and heat stress in rats: Role of internal temperature
    • Skidmore, R., J. A. Gutierrez, V. Guerriero, and K. Kregel. HSP70 induction during exercise and heat stress in rats: role of internal temperature. Am. J. Physiol. 268.R92-R97, 1995.
    • (1995) Am. J. Physiol. , vol.268 , pp. R92-R97
    • Skidmore, R.1    Gutierrez, J.A.2    Guerriero, V.3    Kregel, K.4
  • 38
    • 0026346847 scopus 로고
    • Expression and cellular distribution of heat-shock and nuclear oncogene proteins in rat hearts
    • Snoeckx, I. H. E. H., F. Routard, J. L. Samuel, T. Mat one, and I. Rappaport. Expression and cellular distribution of heat-shock and nuclear oncogene proteins in rat hearts. Am. J. Physiol. 261:H1443-H1451, 1991
    • (1991) Am. J. Physiol. , vol.261 , pp. H1443-H1451
    • Snoeckx, I.H.E.H.1    Routard, F.2    Samuel, J.L.3    Mat One, T.4    Rappaport, I.5
  • 39
    • 0028135554 scopus 로고
    • Hsp70s and lysosomal proteolysis
    • Terlecky, S. R. Hsp70s and lysosomal proteolysis. Rxperientia 50:1021-1925. 1994.
    • (1994) Rxperientia , vol.50 , pp. 1021-1925
    • Terlecky, S.R.1
  • 40
    • 0016373748 scopus 로고
    • Protein synthesis in salivan glands of Drosophila melanogaster: Relation to chromosome pulís
    • Tissiéres, A., H. K. Mitchell, and U. M. Tracy. Protein synthesis in salivan glands of Drosophila melanogaster: relation to chromosome pulís. J. Mol. Biol. 81:389-398, 1974.
    • (1974) J. Mol. Biol. , vol.81 , pp. 389-398
    • Tissiéres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 41
    • 0028117097 scopus 로고
    • The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondr ia
    • Ungermann, C., W. Neupert, and D. M. Cry. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondr ia. Science 266:1250-1253, 1994.
    • (1994) Science , vol.266 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cry, D.M.3
  • 42
    • 0022427782 scopus 로고
    • The 70-krl mammalian heat slunk proteins are xinu mrallv and functionally related to the umoating protein that trlrases clathrin triskelia Irom coated vesicles
    • Ingewh kell, E. The 70-krl mammalian heat slunk proteins are xinu mrallv and functionally related to the umoating protein that trlrases clathrin triskelia Irom coated vesicles. EMBOJ. 4:3385-3391, 1985.
    • (1985) EMBOJ , vol.4 , pp. 3385-3391
    • Ingewh Kell, E.1
  • 43
    • 0018734032 scopus 로고
    • Heat shock induced proteins present in the cell nucleus of Ghironomus tentans salivary gland
    • Vincent, M., and R. M. Tanguay. Heat shock induced proteins present in the cell nucleus of Ghironomus tentans salivary gland. Nature 281:501-503, 1979.
    • (1979) Nature , vol.281 , pp. 501-503
    • Vincent, M.1    Tanguay, R.M.2
  • 44
    • 0022352547 scopus 로고
    • Differential induction of glucose-regulated and heat shock proteins: Effects of pH and sulfhydiyi-reducing agents on chicken embryo cells
    • Whelan, S. A., and L. E. Hightower. Differential induction of glucose-regulated and heat shock proteins: effects of pH and sulfhydiyi-reducing agents on chicken embryo cells. J. Cell. Physiol. 125:251-258, 1985.
    • (1985) J. Cell. Physiol. , vol.125 , pp. 251-258
    • Whelan, S.A.1    Hightower, L.E.2
  • 45
    • 0027291238 scopus 로고
    • Heat-shock protein hsp 90 governs the activity of pp60v-src kinase
    • Xu, Y., and S. Lindquist. Heat-shock protein hsp 90 governs the activity of pp60v-src kinase. Proc. Natl. Acad. Sri. I S. A. 90:7074-7078, 1993.
    • (1993) Proc. Natl. Acad. Sri. I S. A. , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 46
    • 0026011111 scopus 로고
    • Heal shock proteins affect RXA professing during the heat shock t rsponse of Sacehavomyns-Cerroisiae
    • Yost, H. J., and S. Lindquist. Heal shock proteins affect RXA professing during the heat shock t rsponse of Sacehavomyns-Cerroisiae. Mol. Cell. Biol. 11:1062-1068. 1991.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 1062-1068
    • Yost, H.J.1    Lindquist, S.2
  • 47
    • 0023921692 scopus 로고
    • Identification and sequence analysis of a new member of the mouse IISP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line
    • Zakeri, Z. f., D. J. Wolgenmth, and C. R. Hum. Identification and sequence analysis of a new member of the mouse IISP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line. Mol. Cell Biol 8: 2925-2932, 1988.
    • (1988) Mol. Cell Biol , vol.8 , pp. 2925-2932
    • Zakeri, Z.F.1    Wolgenmth, D.J.2    Hum, C.R.3
  • 48
    • 85026136034 scopus 로고
    • Thermostability-of lactate dehvflrdgena.Se I.DH-A4 isoenzv me: Effect of heal shot k protein Duals on the enzyme activity
    • Zietara, M. S., and E. F. Skorkowski. Thermostability-of lactate dehvflrdgena.se I.DH-A4 isoenzv me: effect of heal shot k protein Duals on the enzyme activity, int. f. Bior.hrm. Cell Biol. 27:1 169-1174, 1995.
    • (1995) Int. F. Bior.Hrm. Cell Biol , vol.1 , pp. 169-1174
    • Zietara, M.S.1    Skorkowski, E.F.2


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