메뉴 건너뛰기




Volumn 13, Issue 11, 1999, Pages 1435-1443

Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism

Author keywords

Actin; Calpain; Muscle catabolism; Myosin; Proteasome; Ubiquitin

Indexed keywords

ACTIN; CALCIUM; CALPAIN; DANTROLENE; MUSCLE PROTEIN; MYOSIN; PROTEASOME; UBIQUITIN;

EID: 0032797384     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.13.11.1435     Document Type: Article
Times cited : (155)

References (56)
  • 2
    • 0031018516 scopus 로고    scopus 로고
    • Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle
    • Tiao, G., Hobler, S., Wang, J. J, Meyer, T. A., Luchette, F. A., Fischer, J. E., and Hasselgren, P. O. (1997) Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle. J. Clin. Invest. 99, 163-168
    • (1997) J. Clin. Invest. , vol.99 , pp. 163-168
    • Tiao, G.1    Hobler, S.2    Wang, J.J.3    Meyer, T.A.4    Luchette, F.A.5    Fischer, J.E.6    Hasselgren, P.O.7
  • 3
    • 0024238419 scopus 로고
    • Histological investigations of muscle atrophy and end plates in two critically ill patients with generalized weakness
    • Wokke, J. H. J., Jennekens, F. G. I., van den Oord, C. J. M., Veldman, H., and Van Gijn, J. (1988) Histological investigations of muscle atrophy and end plates in two critically ill patients with generalized weakness. J. Neurol. Sci. 88, 95-106
    • (1988) J. Neurol. Sci. , vol.88 , pp. 95-106
    • Wokke, J.H.J.1    Jennekens, F.G.I.2    Van Den Oord, C.J.M.3    Veldman, H.4    Van Gijn, J.5
  • 5
    • 6844258832 scopus 로고    scopus 로고
    • Respiratory muscle injury in animal models and humans
    • Reid, W. D., and MacGowan, N. A. (1998) Respiratory muscle injury in animal models and humans. Mol. Cell. Biochem. 179, 63-80
    • (1998) Mol. Cell. Biochem. , vol.179 , pp. 63-80
    • Reid, W.D.1    MacGowan, N.A.2
  • 6
    • 0024386017 scopus 로고
    • Total and myofibrillar protein breakdown in different types of rat skeletal muscle: Effects of sepsis and regulation by insulin
    • Hasselgren, P. O., James, J. H., Benson, D. W., Hall-Angerås, M., Angerås, U., Hiyama, D. T., Li, S., and Fischer, J. E. (1989) Total and myofibrillar protein breakdown in different types of rat skeletal muscle: effects of sepsis and regulation by insulin. Metabolism 38, 634-640
    • (1989) Metabolism , vol.38 , pp. 634-640
    • Hasselgren, P.O.1    James, J.H.2    Benson, D.W.3    Hall-Angerås, M.4    Angerås, U.5    Hiyama, D.T.6    Li, S.7    Fischer, J.E.8
  • 7
    • 0027973469 scopus 로고
    • Sepsis stimulates nonlysosomal energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle
    • Tiao, G., Fagan, J. M., Samuels, N., James, J. H., Hudson, K., Lieberman, M., Fischer, J. E., and Hasselgren, P. O. (1994) Sepsis stimulates nonlysosomal energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94, 2255-2264
    • (1994) J. Clin. Invest. , vol.94 , pp. 2255-2264
    • Tiao, G.1    Fagan, J.M.2    Samuels, N.3    James, J.H.4    Hudson, K.5    Lieberman, M.6    Fischer, J.E.7    Hasselgren, P.O.8
  • 8
    • 0030951073 scopus 로고    scopus 로고
    • Intracellular regulation of protein degradation during sepsis is different in fast- and slow-twitch muscle
    • Tiao, G., Lieberman, M., Fischer, J. E., and Hasselgren, P. O. (1997) Intracellular regulation of protein degradation during sepsis is different in fast- and slow-twitch muscle. Am. J. Physiol. 272, R849-R856
    • (1997) Am. J. Physiol. , vol.272
    • Tiao, G.1    Lieberman, M.2    Fischer, J.E.3    Hasselgren, P.O.4
  • 9
    • 0031913331 scopus 로고    scopus 로고
    • The sepsis-induced increase in muscle proteolysis is blocked by specific proteasome inhibitors
    • Hobler, S. C., Tiao, G., Fischer, J. E., Monaco, J., and Hasselgren, P. O. (1998) The sepsis-induced increase in muscle proteolysis is blocked by specific proteasome inhibitors. Am. J. Physiol. 274, R30-R37
    • (1998) Am. J. Physiol. , vol.274
    • Hobler, S.C.1    Tiao, G.2    Fischer, J.E.3    Monaco, J.4    Hasselgren, P.O.5
  • 10
    • 0027026199 scopus 로고
    • Ovine skeletal muscle multicatalytic proteinase complex (proteasome): Purification, characterization, and comparison of its effects on myofibrils with μ-calpains
    • Koohmaraie, M. (1992) Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization, and comparison of its effects on myofibrils with μ-calpains. J. Anim. Sci. 70, 3697-3708
    • (1992) J. Anim. Sci. , vol.70 , pp. 3697-3708
    • Koohmaraie, M.1
  • 11
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • Solomon, V., and Goldberg, A. L. (1996) Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J. Biol. Chem. 271, 26690-26697
    • (1996) J. Biol. Chem. , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 12
    • 0022550946 scopus 로고
    • Effect of starvation or treatment with corticosterone on the amount of easily releasable myofilaments in rat skeletal muscles
    • Dahlmann, B., Rutschmann, M., and Reinauer, H. (1986) Effect of starvation or treatment with corticosterone on the amount of easily releasable myofilaments in rat skeletal muscles. Biochem. J. 234, 659-664
    • (1986) Biochem. J. , vol.234 , pp. 659-664
    • Dahlmann, B.1    Rutschmann, M.2    Reinauer, H.3
  • 13
    • 0023198858 scopus 로고
    • Role of calcium in triggering rapid ultrastructural change in muscle: A study with chemically skinned fibers
    • Duncan, C. J. (1987) Role of calcium in triggering rapid ultrastructural change in muscle: A study with chemically skinned fibers. J. Cell Sci. 87, 581-594
    • (1987) J. Cell Sci. , vol.87 , pp. 581-594
    • Duncan, C.J.1
  • 14
    • 0027939833 scopus 로고
    • Calcium-supported calpain degradation rates for cardiac myofibrils in diabetes
    • Beicastro, A. N., Gilchrist, J. S., Scrubb, J. A., and Arthur, G. (1994) Calcium-supported calpain degradation rates for cardiac myofibrils in diabetes. Mol. Cell. Biochem. 135, 51-60
    • (1994) Mol. Cell. Biochem. , vol.135 , pp. 51-60
    • Beicastro, A.N.1    Gilchrist, J.S.2    Scrubb, J.A.3    Arthur, G.4
  • 15
    • 0030254273 scopus 로고    scopus 로고
    • Role of calcium-activated neutral protease (calpain) with diet and exercise
    • Belcastro, A. N., Albisser, T. A., and Littlejohn, B. (1996) Role of calcium-activated neutral protease (calpain) with diet and exercise. Can. J. Appl. Physiol. 21, 328-346
    • (1996) Can. J. Appl. Physiol. , vol.21 , pp. 328-346
    • Belcastro, A.N.1    Albisser, T.A.2    Littlejohn, B.3
  • 16
    • 0018349233 scopus 로고
    • Effect of sepsis on tissue adenine nucleotide levels
    • Chaudry, I. H., Wichterman, K. A., and Baue, A. E. (1979) Effect of sepsis on tissue adenine nucleotide levels. Surgery 85, 205-211
    • (1979) Surgery , vol.85 , pp. 205-211
    • Chaudry, I.H.1    Wichterman, K.A.2    Baue, A.E.3
  • 18
    • 0016420707 scopus 로고
    • In vitro preparation of the diaphragm and other skeletal muscles
    • Goldberg, A. L., Martel, S., and Kushmerick, M. (1975) In vitro preparation of the diaphragm and other skeletal muscles. Methods Enzymol. 39, 82-93
    • (1975) Methods Enzymol. , vol.39 , pp. 82-93
    • Goldberg, A.L.1    Martel, S.2    Kushmerick, M.3
  • 19
    • 0025366346 scopus 로고
    • Regulation of total and myofibrillar protein breakdown in rat extensor digitorum longus and soleus muscle incubated flaccid or at resting length
    • Hasselgren, P. O., Hall-Angerås, M., Angerås, U., Benson, D. W., James, J. H., and Fischer, J. E. (1990) Regulation of total and myofibrillar protein breakdown in rat extensor digitorum longus and soleus muscle incubated flaccid or at resting length. Biochem. J. 267, 33-44
    • (1990) Biochem. J. , vol.267 , pp. 33-44
    • Hasselgren, P.O.1    Hall-Angerås, M.2    Angerås, U.3    Benson, D.W.4    James, J.H.5    Fischer, J.E.6
  • 20
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi, H., Ishiura, S., and Suzuki, K. (1997) Structure and physiological function of calpains. Biochem. J. 328, 721-732
    • (1997) Biochem. J. , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 22
    • 0028202753 scopus 로고
    • Dantrolene ameliorates the metabolic hallmarks of sepsis in rats and improves survival in a mouse model of endotoxemia
    • Hotchkiss, R. S., and Karl, I. E. (1994) Dantrolene ameliorates the metabolic hallmarks of sepsis in rats and improves survival in a mouse model of endotoxemia. Proc. Natl. Acad. Sci. USA 91, 3039-3043
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3039-3043
    • Hotchkiss, R.S.1    Karl, I.E.2
  • 23
    • 0026729315 scopus 로고
    • Capillary to fiber geometry and mitochondrial density in hummingbird flight muscle
    • Mathieu-Costello, O., Suarez, R. K., and Hockachka, P. W. (1992) Capillary to fiber geometry and mitochondrial density in hummingbird flight muscle. Resp. Physiol. 89, 113-132
    • (1992) Resp. Physiol. , vol.89 , pp. 113-132
    • Mathieu-Costello, O.1    Suarez, R.K.2    Hockachka, P.W.3
  • 24
    • 0013632737 scopus 로고
    • Mosby Year Book Europe, Ltd., London
    • Stevens, A., and Lowe, J. S. (1993) Histology, p. 58, Mosby Year Book Europe, Ltd., London
    • (1993) Histology , pp. 58
    • Stevens, A.1    Lowe, J.S.2
  • 25
    • 0016771837 scopus 로고
    • Isolation of newly synthesized myosin filaments from skeletal muscle homogenates and myofibrils
    • Etlinger, J. D., Zak, R., Fischman, D. A., and Rabinowitz, M. (1975) Isolation of newly synthesized myosin filaments from skeletal muscle homogenates and myofibrils. Nature (London) 255, 259-261
    • (1975) Nature (London) , vol.255 , pp. 259-261
    • Etlinger, J.D.1    Zak, R.2    Fischman, D.A.3    Rabinowitz, M.4
  • 26
    • 0019888648 scopus 로고
    • Easily releasable myofilaments from skeletal and cardiac muscles maintained in vitro. Role in myofibrillar assembly and turnover
    • van der Westhuyzen, D. R., Matsumoto, K., and Etlinger, J. D. (1981) Easily releasable myofilaments from skeletal and cardiac muscles maintained in vitro. Role in myofibrillar assembly and turnover. J. Biol. Chem. 256, 11791-11797
    • (1981) J. Biol. Chem. , vol.256 , pp. 11791-11797
    • Van Der Westhuyzen, D.R.1    Matsumoto, K.2    Etlinger, J.D.3
  • 27
    • 0025877817 scopus 로고
    • Regulation of ATP-stimulated releasable myofilaments from cardiac and skeletal muscle myofibrils
    • Belcastro, A. N., Scrubb, J., and Gilchrist, J. S. (1991) Regulation of ATP-stimulated releasable myofilaments from cardiac and skeletal muscle myofibrils. Mol. Cell. Biochem. 103, 113-120
    • (1991) Mol. Cell. Biochem. , vol.103 , pp. 113-120
    • Belcastro, A.N.1    Scrubb, J.2    Gilchrist, J.S.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by guanidinium thiocyanate-phenol-chloroform extraction
    • Chomzynski, P., and Sacchi, N. (1987) Single step method of RNA isolation by guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomzynski, P.1    Sacchi, N.2
  • 31
    • 0027973469 scopus 로고
    • Sepsis stimulates nonlysosomal energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle
    • Tiao, G., Fagan, J. M., Samuels, N., James, J. H., Hudson, K., Lieberman, M., Fischer, J. E., and Hasselgren, P. O. (1994) Sepsis stimulates nonlysosomal energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94, 2255-2264
    • (1994) J. Clin. Invest. , vol.94 , pp. 2255-2264
    • Tiao, G.1    Fagan, J.M.2    Samuels, N.3    James, J.H.4    Hudson, K.5    Lieberman, M.6    Fischer, J.E.7    Hasselgren, P.O.8
  • 32
    • 0025214103 scopus 로고
    • Histologic and ultrastructural changes in nonpulmonary organs during early hyperdynamic sepsis
    • Hersch, J., Gnidec, A. A., Bersten, A. D., Troster, M., Rutledge, F. S., and Sibbald, W. J. (1990) Histologic and ultrastructural changes in nonpulmonary organs during early hyperdynamic sepsis. Surgery 107, 397-410
    • (1990) Surgery , vol.107 , pp. 397-410
    • Hersch, J.1    Gnidec, A.A.2    Bersten, A.D.3    Troster, M.4    Rutledge, F.S.5    Sibbald, W.J.6
  • 33
    • 0028030618 scopus 로고
    • Skeletal muscle oedema and muscle fibre necrosis during septic shock. Observations with a porcine septic shock model
    • Hauptmann, S., Klosterhalfen, B., Weis, J., Mittermeyer, C., and Kirkpatrick, C. J. (1994) Skeletal muscle oedema and muscle fibre necrosis during septic shock. Observations with a porcine septic shock model. Virchows Arch. 424, 653-659
    • (1994) Virchows Arch. , vol.424 , pp. 653-659
    • Hauptmann, S.1    Klosterhalfen, B.2    Weis, J.3    Mittermeyer, C.4    Kirkpatrick, C.J.5
  • 34
    • 0031984113 scopus 로고    scopus 로고
    • Histochemical and ultrastructural study of skeletal muscle in patients with sepsis and multiple organ failure syndrome (MOFS)
    • Diaz, N. L., Finol, H. J., Torres, S. H., Zambrano, C. I., and Adjounian, H. (1998) Histochemical and ultrastructural study of skeletal muscle in patients with sepsis and multiple organ failure syndrome (MOFS). Histol. Hispathol. 13, 121-128
    • (1998) Histol. Hispathol. , vol.13 , pp. 121-128
    • Diaz, N.L.1    Finol, H.J.2    Torres, S.H.3    Zambrano, C.I.4    Adjounian, H.5
  • 35
    • 0030967587 scopus 로고    scopus 로고
    • Architecture and function in the muscle sarcomere
    • Squire, J. M. (1997) Architecture and function in the muscle sarcomere. Curr. Opin. Struct. Biol. 7, 247-257
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 247-257
    • Squire, J.M.1
  • 36
    • 0028283285 scopus 로고
    • The muscle Z band: Lessons in stress management
    • Vigoreaux, J. O. (1994) The muscle Z band: lessons in stress management. J. Muscle Res. Cell Motil 15, 237-255
    • (1994) J. Muscle Res. Cell Motil , vol.15 , pp. 237-255
    • Vigoreaux, J.O.1
  • 37
    • 0031016596 scopus 로고    scopus 로고
    • The giant protein titin. Emerging roles in physiology and pathophysiology
    • Labeit, S., Kolmerer, B., and Linke, W. A. (1997) The giant protein titin. Emerging roles in physiology and pathophysiology. Circ. Res. 80, 290-294
    • (1997) Circ. Res. , vol.80 , pp. 290-294
    • Labeit, S.1    Kolmerer, B.2    Linke, W.A.3
  • 38
    • 85012650875 scopus 로고
    • An electron microscope study of denervation atrophy in red and white skeletal muscle fibers
    • Pellegrino, C., and Franzini, C. (1963) An electron microscope study of denervation atrophy in red and white skeletal muscle fibers. J. Cell Biol. 17, 327-349
    • (1963) J. Cell Biol. , vol.17 , pp. 327-349
    • Pellegrino, C.1    Franzini, C.2
  • 39
    • 0015736516 scopus 로고
    • Degeneration of different types of skeletal muscle fibers. I. Denervation
    • Tananek, R. J., and Lund, D. D. (1973) Degeneration of different types of skeletal muscle fibers. I. Denervation. J. Anat. 116, 395-407
    • (1973) J. Anat. , vol.116 , pp. 395-407
    • Tananek, R.J.1    Lund, D.D.2
  • 40
    • 0020967467 scopus 로고
    • Myofibrillar damage following intense exercise in man
    • Friden, J., Sjöström, M., and Ekblom, B. (1983) Myofibrillar damage following intense exercise in man. Int. J. Sports Med. 4, 170-176
    • (1983) Int. J. Sports Med. , vol.4 , pp. 170-176
    • Friden, J.1    Sjöström, M.2    Ekblom, B.3
  • 41
    • 0031934265 scopus 로고    scopus 로고
    • Exercise-induced muscle injury: A calpain hypothesis
    • Belcastro, A. N., Shewchuk, L. D., and Raj, D. A. (1998) Exercise-induced muscle injury: a calpain hypothesis. Mol. Cell. Biochem. 179, 135-145
    • (1998) Mol. Cell. Biochem. , vol.179 , pp. 135-145
    • Belcastro, A.N.1    Shewchuk, L.D.2    Raj, D.A.3
  • 42
    • 0022552652 scopus 로고
    • Protein dynamics in skeletal muscle after trauma: Local and systemic effects
    • Downey, R. S., Monafo, W. W., Karl, I. E., Matthews, D. E., and Bier, D. M. (1986) Protein dynamics in skeletal muscle after trauma: local and systemic effects. Surgery 99, 265-273
    • (1986) Surgery , vol.99 , pp. 265-273
    • Downey, R.S.1    Monafo, W.W.2    Karl, I.E.3    Matthews, D.E.4    Bier, D.M.5
  • 43
    • 0022969340 scopus 로고
    • Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation
    • Lowell, B. B., Rudermann, N. B., and Goodman, M. N. (1986) Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation. Metabolism 35, 1121-1127
    • (1986) Metabolism , vol.35 , pp. 1121-1127
    • Lowell, B.B.1    Rudermann, N.B.2    Goodman, M.N.3
  • 44
    • 0027469524 scopus 로고
    • Skeletal muscle calcium-activated neutral protease (calpain) with exercise
    • Belcastro, A. N. (1993) Skeletal muscle calcium-activated neutral protease (calpain) with exercise. J. Appl. Physiol. 746, 1381-1386
    • (1993) J. Appl. Physiol. , vol.746 , pp. 1381-1386
    • Belcastro, A.N.1
  • 45
    • 0025988513 scopus 로고
    • Calcium-dependent and calcium-independent protease activities in skeletal muscle during sepsis
    • Bhattacharyya, J., Thompson, K., and Sayeed, M. M. (1991) Calcium-dependent and calcium-independent protease activities in skeletal muscle during sepsis. Circ. Shock 35, 117-122
    • (1991) Circ. Shock , vol.35 , pp. 117-122
    • Bhattacharyya, J.1    Thompson, K.2    Sayeed, M.M.3
  • 46
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium-dependent protease distinct from both α- and m-types: Specific expression of the mRNA in skeletal muscle
    • Sorimachi, H., Imajoh, S., Emori, Y., Kawasaki, H., Ohno, S., Minami, Y., and Suzuki, K. (1989) Molecular cloning of a novel mammalian calcium-dependent protease distinct from both α- and m-types: specific expression of the mRNA in skeletal muscle. J. Biol. Chem. 264, 20106-20111
    • (1989) J. Biol. Chem. , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh, S.2    Emori, Y.3    Kawasaki, H.4    Ohno, S.5    Minami, Y.6    Suzuki, K.7
  • 47
    • 0024409591 scopus 로고
    • Effect of sepsis on calcium uptake and content in skeletal muscle and regulation in vitro by calcium of total and myofibrillar protein breakdown in control and septic muscle: Results from a preliminary study
    • Benson, D. W., Hasselgren, P. O., Hiyama, D. T., James, J. H., Li, S., Rigel, D. F., and Fischer, J. E. (1989) Effect of sepsis on calcium uptake and content in skeletal muscle and regulation in vitro by calcium of total and myofibrillar protein breakdown in control and septic muscle: results from a preliminary study. Surgery 106, 87-93
    • (1989) Surgery , vol.106 , pp. 87-93
    • Benson, D.W.1    Hasselgren, P.O.2    Hiyama, D.T.3    James, J.H.4    Li, S.5    Rigel, D.F.6    Fischer, J.E.7
  • 49
    • 0019175054 scopus 로고
    • The effects of calcium ions, ionophore A23187, and inhibition of energy metabolism on protein degradation in the rat diaphragm and epitrochlears muscles in vitro
    • Sugden, P. H. (1980) The effects of calcium ions, ionophore A23187, and inhibition of energy metabolism on protein degradation in the rat diaphragm and epitrochlears muscles in vitro. Biochem. J. 190, 593-603
    • (1980) Biochem. J. , vol.190 , pp. 593-603
    • Sugden, P.H.1
  • 50
    • 0022455294 scopus 로고
    • Influence of calcium and other divalent cations on protein turnover in rat skeletal muscle
    • Baracos, V., Greenberg, R. E., and Goldberg, A. L. (1986) Influence of calcium and other divalent cations on protein turnover in rat skeletal muscle. Am. J. Physiol. 250, E702-E710
    • (1986) Am. J. Physiol. , vol.250
    • Baracos, V.1    Greenberg, R.E.2    Goldberg, A.L.3
  • 51
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A., and Ciechanover, A. (1992) The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61, 761-807
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 52
    • 0030632048 scopus 로고    scopus 로고
    • The N-end rule pathway of protein degradation
    • Varshavsky, A. (1997) The N-end rule pathway of protein degradation. Genes to Cells 2, 13-28
    • (1997) Genes to Cells , vol.2 , pp. 13-28
    • Varshavsky, A.1
  • 53
    • 0028007982 scopus 로고
    • 14-kDa ubiquitin-conjugating enzyme: Structure of the rat gene and regulation upon fasting and by insulin
    • Wing, S. S., and Banville, D. (1994) 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. Am. J. Physiol. 267, E39-E48
    • (1994) Am. J. Physiol. , vol.267
    • Wing, S.S.1    Banville, D.2
  • 55
    • 0032566716 scopus 로고    scopus 로고
    • The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle
    • Solomon, V., Lecker, S. H., and Goldberg, A. L. (1998) The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. J. Biol. Chem. 273, 25216-25222
    • (1998) J. Biol. Chem. , vol.273 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 56
    • 0032514735 scopus 로고    scopus 로고
    • Rates of ubiquitin conjugation increases when muscles atrophy, largely through activation of the N-end rule pathway
    • Solomon, V., Baracos, V., Sarraf, P., and Goldberg, A. L. (1998) Rates of ubiquitin conjugation increases when muscles atrophy, largely through activation of the N-end rule pathway. Proc. Natl. Acad. Sci. USA 95, 12602-12607
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12602-12607
    • Solomon, V.1    Baracos, V.2    Sarraf, P.3    Goldberg, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.