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Volumn 26, Issue 9, 2012, Pages 3691-3702

Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production

Author keywords

Chaperones; Endocrine growth control; Glucose homeostasis; Glucose regulated protein 94; IGFs

Indexed keywords

GLUCOSE REGULATED PROTEIN 94; GROWTH HORMONE; RECOMBINANT SOMATOMEDIN C; SOMATOMEDIN; SOMATOMEDIN B; SOMATOMEDIN C;

EID: 84865788752     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-203026     Document Type: Article
Times cited : (67)

References (55)
  • 1
    • 0029040848 scopus 로고
    • Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice
    • Coleman, M. E., DeMayo, F., Yin, K. C., Lee, H. M., Geske, R., Montgomery, C., and Schwartz, R. J. (1995) Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice. J. Biol. Chem. 270, 12109-12116
    • (1995) J. Biol. Chem. , vol.270 , pp. 12109-12116
    • Coleman, M.E.1    DeMayo, F.2    Yin, K.C.3    Lee, H.M.4    Geske, R.5    Montgomery, C.6    Schwartz, R.J.7
  • 3
    • 33744938902 scopus 로고    scopus 로고
    • Viral expression of insulin-like growth factor-I isoforms promotes different responses in skeletal muscle
    • Barton, E. R. (2006) Viral expression of insulin-like growth factor-I isoforms promotes different responses in skeletal muscle. J. Appl. Physiol. 100, 1778-1784
    • (2006) J. Appl. Physiol. , vol.100 , pp. 1778-1784
    • Barton, E.R.1
  • 4
    • 0031965872 scopus 로고    scopus 로고
    • Localized infusion of IGF-I results in skeletal muscle hypertrophy in rats
    • Adams, G. R., and McCue, S. A. (1998) Localized infusion of IGF-I results in skeletal muscle hypertrophy in rats. J. Appl. Physiol. 84, 1716-1722
    • (1998) J. Appl. Physiol. , vol.84 , pp. 1716-1722
    • Adams, G.R.1    McCue, S.A.2
  • 8
    • 0023759296 scopus 로고
    • Induction of mRNA for IGF-I and -II during growth hormone-stimulated muscle hypertrophy
    • Turner, J. D., Rotwein, P., Novakofski, J., and Bechtel, P. J. (1988) Induction of mRNA for IGF-I and -II during growth hormone-stimulated muscle hypertrophy. Am. J. Physiol. 255, E513-E517
    • (1988) Am. J. Physiol. , vol.255
    • Turner, J.D.1    Rotwein, P.2    Novakofski, J.3    Bechtel, P.J.4
  • 10
    • 0030013467 scopus 로고    scopus 로고
    • The expression and characterization of human recombinant proinsulin-like growth factor II and a mutant that is defective in the O-glycosylation of its E domain
    • Yang, C. Q., Zhan, X., Hu, X., Kondepudi, A., and Perdue, J. F. (1996) The expression and characterization of human recombinant proinsulin-like growth factor II and a mutant that is defective in the O-glycosylation of its E domain. Endocrinology 137, 2766-2773
    • (1996) Endocrinology , vol.137 , pp. 2766-2773
    • Yang, C.Q.1    Zhan, X.2    Hu, X.3    Kondepudi, A.4    Perdue, J.F.5
  • 11
    • 65249092612 scopus 로고    scopus 로고
    • The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation
    • Ostrovsky, O., Ahmed, N. T., and Argon, Y. (2009) The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation. Mol. Biol. Cell 20, 1855-1864
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1855-1864
    • Ostrovsky, O.1    Ahmed, N.T.2    Argon, Y.3
  • 12
    • 77649272715 scopus 로고    scopus 로고
    • Glucose regulated protein 94 is required for muscle differentiation through its control of the autocrine production of insulin-like growth factors
    • Ostrovsky, O., Eletto, D., Makarewich, C., Barton, E. R., and Argon, Y. (2010) Glucose regulated protein 94 is required for muscle differentiation through its control of the autocrine production of insulin-like growth factors. Biochim. Biophys. Acta 1803, 333-341
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 333-341
    • Ostrovsky, O.1    Eletto, D.2    Makarewich, C.3    Barton, E.R.4    Argon, Y.5
  • 13
    • 0027958873 scopus 로고
    • The glucose-regulated proteins (GRP78 and GRP94): Functions, gene regulation, and applications
    • Little, E., Ramakrishnan, M., Roy, B., Gazit, G., and Lee, A. S. (1994) The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. Crit. Rev. Eukaryot. Gene Expr. 4, 1-18
    • (1994) Crit. Rev. Eukaryot. Gene Expr. , vol.4 , pp. 1-18
    • Little, E.1    Ramakrishnan, M.2    Roy, B.3    Gazit, G.4    Lee, A.S.5
  • 14
    • 33645239012 scopus 로고    scopus 로고
    • Roles of heat shock protein gp96 in the ER quality control: Redundant or unique function?
    • Yang, Y., and Li, Z. (2005) Roles of heat shock protein gp96 in the ER quality control: redundant or unique function? Mol. Cells 20, 173-182
    • (2005) Mol. Cells , vol.20 , pp. 173-182
    • Yang, Y.1    Li, Z.2
  • 15
    • 0027931855 scopus 로고
    • GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II
    • Cala, S. E., and Jones, L. R. (1994) GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II. J. Biol. Chem. 269, 5926-5931
    • (1994) J. Biol. Chem. , vol.269 , pp. 5926-5931
    • Cala, S.E.1    Jones, L.R.2
  • 16
    • 0032102443 scopus 로고    scopus 로고
    • Rabbit cardiac and skeletal myocytes differ in constitutive and inducible expression of the glucose-regulated protein GRP94
    • Vitadello, M., Colpo, P., and Gorza, L. (1998) Rabbit cardiac and skeletal myocytes differ in constitutive and inducible expression of the glucose-regulated protein GRP94. Biochem. J. 332, 351-359
    • (1998) Biochem. J. , vol.332 , pp. 351-359
    • Vitadello, M.1    Colpo, P.2    Gorza, L.3
  • 17
    • 0037646962 scopus 로고    scopus 로고
    • Overexpression of the stress protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia
    • Vitadello, M., Penzo, D., Petronilli, V., Michieli, G., Gomirato, S., Menabo, R., Di Lisa, F., and Gorza, L. (2003) Overexpression of the stress protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia. FASEB J. 17, 923-925
    • (2003) FASEB J. , vol.17 , pp. 923-925
    • Vitadello, M.1    Penzo, D.2    Petronilli, V.3    Michieli, G.4    Gomirato, S.5    Menabo, R.6    Di Lisa, F.7    Gorza, L.8
  • 18
    • 34948853214 scopus 로고    scopus 로고
    • GRP94 is essential for mesoderm induction and muscle development because it regulates IGF secretion
    • Wanderling, S., Simen, B. B., Ostrovsky, O., Ahmed, N. T., Vogen, S., Gidalevitz, T., and Argon, Y. (2007) GRP94 is essential for mesoderm induction and muscle development because it regulates IGF secretion. Mol. Biol. Cell 18, 3764-3775
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3764-3775
    • Wanderling, S.1    Simen, B.B.2    Ostrovsky, O.3    Ahmed, N.T.4    Vogen, S.5    Gidalevitz, T.6    Argon, Y.7
  • 19
    • 33847260278 scopus 로고    scopus 로고
    • Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages
    • Yang, Y., Liu, B., Dai, J., Srivastava, P. K., Zammit, D. J., Lefrancois, L., and Li, Z. (2007) Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages. Immunity 26, 215-226
    • (2007) Immunity , vol.26 , pp. 215-226
    • Yang, Y.1    Liu, B.2    Dai, J.3    Srivastava, P.K.4    Zammit, D.J.5    Lefrancois, L.6    Li, Z.7
  • 20
    • 0022573858 scopus 로고
    • Proliferation of muscle satellite cells on intact myofibers in culture
    • Bischoff, R. (1986) Proliferation of muscle satellite cells on intact myofibers in culture. Dev. Biol. 115, 129-139
    • (1986) Dev. Biol. , vol.115 , pp. 129-139
    • Bischoff, R.1
  • 21
    • 16644397560 scopus 로고    scopus 로고
    • Isolation and culture of skeletal muscle myofibers as a means to analyze satellite cells
    • Shefer, G., and Yablonka-Reuveni, Z. (2005) Isolation and culture of skeletal muscle myofibers as a means to analyze satellite cells. Methods Mol. Biol. 290, 281-304
    • (2005) Methods Mol. Biol. , vol.290 , pp. 281-304
    • Shefer, G.1    Yablonka-Reuveni, Z.2
  • 22
    • 70349310424 scopus 로고    scopus 로고
    • The insulin-like growth factor (IGF)-I E-peptides modulate cell entry of the mature IGF-I protein
    • Pfeffer, L. A., Brisson, B. K., Lei, H., and Barton, E. R. (2009) The insulin-like growth factor (IGF)-I E-peptides modulate cell entry of the mature IGF-I protein. Mol. Biol. Cell 20, 3810-3817
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3810-3817
    • Pfeffer, L.A.1    Brisson, B.K.2    Lei, H.3    Barton, E.R.4
  • 23
    • 0023779032 scopus 로고
    • The muscle creatine kinase gene is regulated by multiple upstream elements, including a musclespecific enhancer
    • Jaynes, J. B., Johnson, J. E., Buskin, J. N., Gartside, C. L., and Hauschka, S. D. (1988) The muscle creatine kinase gene is regulated by multiple upstream elements, including a musclespecific enhancer. Mol. Cell. Biol. 8, 62-70
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 62-70
    • Jaynes, J.B.1    Johnson, J.E.2    Buskin, J.N.3    Gartside, C.L.4    Hauschka, S.D.5
  • 24
    • 77951945432 scopus 로고    scopus 로고
    • The insulin-like growth factor (IGF)-I E-peptides are required for isoformspecific gene expression and muscle hypertrophy after local IGF-I production
    • Barton, E. R., DeMeo, J., and Lei, H. (2010) The insulin-like growth factor (IGF)-I E-peptides are required for isoformspecific gene expression and muscle hypertrophy after local IGF-I production. J. Appl. Physiol. 108, 1069-1076
    • (2010) J. Appl. Physiol. , vol.108 , pp. 1069-1076
    • Barton, E.R.1    DeMeo, J.2    Lei, H.3
  • 26
    • 77952589171 scopus 로고    scopus 로고
    • GRP94 in ER quality control and stress responses
    • Eletto, D., Dersh, D., and Argon, Y. (2010) GRP94 in ER quality control and stress responses. Semin. Cell Dev. Biol. 21, 479-485
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 479-485
    • Eletto, D.1    Dersh, D.2    Argon, Y.3
  • 27
    • 47249158198 scopus 로고    scopus 로고
    • Insulin-like growth factor-I protects cells from ER stress-induced apoptosis via enhancement of the adaptive capacity of endoplasmic reticulum
    • Novosyadlyy, R., Kurshan, N., Lann, D., Vijayakumar, A., Yakar, S., and LeRoith, D. (2008) Insulin-like growth factor-I protects cells from ER stress-induced apoptosis via enhancement of the adaptive capacity of endoplasmic reticulum. Cell Death Differ. 15, 1304-1317
    • (2008) Cell Death Differ. , vol.15 , pp. 1304-1317
    • Novosyadlyy, R.1    Kurshan, N.2    Lann, D.3    Vijayakumar, A.4    Yakar, S.5    LeRoith, D.6
  • 28
    • 0024326031 scopus 로고
    • Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles
    • Van, P. N., Peter, F., and Soling, H. D. (1989) Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles. J. Biol. Chem. 264, 17494-17501
    • (1989) J. Biol. Chem. , vol.264 , pp. 17494-17501
    • Van, P.N.1    Peter, F.2    Soling, H.D.3
  • 31
    • 58349090860 scopus 로고    scopus 로고
    • Calsequestrin content and SERCA determine normal and maximal Ca2+ storage levels in sarcoplasmic reticulum of fast- And slow-twitch fibres of rat
    • Murphy, R. M., Larkins, N. T., Mollica, J. P., Beard, N. A., and Lamb, G. D. (2009) Calsequestrin content and SERCA determine normal and maximal Ca2+ storage levels in sarcoplasmic reticulum of fast- and slow-twitch fibres of rat. J. Physiol. 587, 443-460
    • (2009) J. Physiol. , vol.587 , pp. 443-460
    • Murphy, R.M.1    Larkins, N.T.2    Mollica, J.P.3    Beard, N.A.4    Lamb, G.D.5
  • 32
    • 0023661249 scopus 로고
    • Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion
    • Beckerle, M. C., Burridge, K., DeMartino, G. N., and Croall, D. E. (1987) Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell 51, 569-577
    • (1987) Cell , vol.51 , pp. 569-577
    • Beckerle, M.C.1    Burridge, K.2    DeMartino, G.N.3    Croall, D.E.4
  • 33
    • 0034795208 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
    • Randow, F., and Seed, B. (2001) Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat. Cell Biol. 3, 891-896
    • (2001) Nat. Cell Biol. , vol.3 , pp. 891-896
    • Randow, F.1    Seed, B.2
  • 35
    • 77951252529 scopus 로고    scopus 로고
    • Gene regulation by growth hormone
    • Rotwein, P., and Chia, D. J. (2010) Gene regulation by growth hormone. Pediatr. Nephrol. 25, 651-618
    • (2010) Pediatr. Nephrol. , vol.25 , pp. 651-1618
    • Rotwein, P.1    Chia, D.J.2
  • 37
    • 0021206935 scopus 로고
    • Stimulation of growth hormone (GH) and somatomedin C in idiopathic GH-deficient subjects by intermittent pulsatile administration of synthetic human pancreatic tumor GH-releasing factor
    • Borges, J. L., Blizzard, R. M., Evans, W. S., Furlanetto, R., Rogol, A. D., Kaiser, D. L., Rivier, J., Vale, W., and Thorner, M. O. (1984) Stimulation of growth hormone (GH) and somatomedin C in idiopathic GH-deficient subjects by intermittent pulsatile administration of synthetic human pancreatic tumor GH-releasing factor. J. Clin. Endocrinol. Metab. 59, 1-6
    • (1984) J. Clin. Endocrinol. Metab. , vol.59 , pp. 1-6
    • Borges, J.L.1    Blizzard, R.M.2    Evans, W.S.3    Furlanetto, R.4    Rogol, A.D.5    Kaiser, D.L.6    Rivier, J.7    Vale, W.8    Thorner, M.O.9
  • 39
    • 33745855835 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induction of insulin-like growth factor-binding protein-1 involves ATF4
    • Marchand, A., Tomkiewicz, C., Magne, L., Barouki, R., and Garlatti, M. (2006) Endoplasmic reticulum stress induction of insulin-like growth factor-binding protein-1 involves ATF4. J. Biol. Chem. 281, 19124-19133
    • (2006) J. Biol. Chem. , vol.281 , pp. 19124-19133
    • Marchand, A.1    Tomkiewicz, C.2    Magne, L.3    Barouki, R.4    Garlatti, M.5
  • 40
    • 0026052697 scopus 로고
    • Insulin inhibits transcription of the human gene for insulin-like growth factor-binding protein-1
    • Powell, D. R., Suwanichkul, A., Cubbage, M. L., DePaolis, L. A., Snuggs, M. B., and Lee, P. D. (1991) Insulin inhibits transcription of the human gene for insulin-like growth factor-binding protein-1. J. Biol. Chem. 266, 18868-18876
    • (1991) J. Biol. Chem. , vol.266 , pp. 18868-18876
    • Powell, D.R.1    Suwanichkul, A.2    Cubbage, M.L.3    DePaolis, L.A.4    Snuggs, M.B.5    Lee, P.D.6
  • 41
    • 8444243360 scopus 로고    scopus 로고
    • Regulation of muscle mass by myostatin
    • Lee, S. J. (2004) Regulation of muscle mass by myostatin. Annu. Rev. Cell Dev. Biol. 20, 61-86
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 61-86
    • Lee, S.J.1
  • 42
    • 0036170286 scopus 로고    scopus 로고
    • Muscle-specific inactivation of the IGF-I receptor induces compensatory hyperplasia in skeletal muscle
    • Fernandez, A. M., Dupont, J., Farrar, R. P., Lee, S., Stannard, B., and Le Roith, D. (2002) Muscle-specific inactivation of the IGF-I receptor induces compensatory hyperplasia in skeletal muscle. J. Clin. Invest. 109, 347-355
    • (2002) J. Clin. Invest. , vol.109 , pp. 347-355
    • Fernandez, A.M.1    Dupont, J.2    Farrar, R.P.3    Lee, S.4    Stannard, B.5    Le Roith, D.6
  • 43
    • 0028152377 scopus 로고
    • Facilitative glucose transporters
    • Mueckler, M. (1994) Facilitative glucose transporters. Eur. J. Biochem. 219, 713-725
    • (1994) Eur. J. Biochem. , vol.219 , pp. 713-725
    • Mueckler, M.1
  • 44
    • 0032588041 scopus 로고    scopus 로고
    • The α7β1 integrin in muscle development and disease
    • Burkin, D. J., and Kaufman, S. J. (1999) The α7β1 integrin in muscle development and disease. Cell Tissue Res. 296, 183-190
    • (1999) Cell Tissue Res. , vol.296 , pp. 183-190
    • Burkin, D.J.1    Kaufman, S.J.2
  • 45
    • 19644362276 scopus 로고    scopus 로고
    • Tissue-specific mRNA expression profiles of human Toll-like receptors and related genes
    • Nishimura, M., and Naito, S. (2005) Tissue-specific mRNA expression profiles of human Toll-like receptors and related genes. Biol. Pharm. Bull. 28, 886-892
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 886-892
    • Nishimura, M.1    Naito, S.2
  • 46
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: Evidence for TLR4 as the Lps gene product
    • Hoshino, K., Takeuchi, O., Kawai, T., Sanjo, H., Ogawa, T., Takeda, Y., Takeda, K., and Akira, S. (1999) Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J. Immunol. 162, 3749-3752
    • (1999) J. Immunol. , vol.162 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3    Sanjo, H.4    Ogawa, T.5    Takeda, Y.6    Takeda, K.7    Akira, S.8
  • 48
    • 0032514704 scopus 로고    scopus 로고
    • Role of calpain in skeletal-muscle protein degradation
    • Huang, J., and Forsberg, N. E. (1998) Role of calpain in skeletal-muscle protein degradation. Proc. Natl. Acad. Sci. U. S. A. 95, 12100-12105
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12100-12105
    • Huang, J.1    Forsberg, N.E.2
  • 50
    • 34548062140 scopus 로고    scopus 로고
    • Disruption of insulin-like growth factor-I expression in type IIαI collagen-expressing cells reduces bone length and width in mice
    • Govoni, K. E., Lee, S. K., Chung, Y. S., Behringer, R. R., Wergedal, J. E., Baylink, D. J., and Mohan, S. (2007) Disruption of insulin-like growth factor-I expression in type IIαI collagen-expressing cells reduces bone length and width in mice. Physiol. Genomics 30, 354-362
    • (2007) Physiol. Genomics , vol.30 , pp. 354-362
    • Govoni, K.E.1    Lee, S.K.2    Chung, Y.S.3    Behringer, R.R.4    Wergedal, J.E.5    Baylink, D.J.6    Mohan, S.7
  • 51
    • 79955968276 scopus 로고    scopus 로고
    • Increased serum IGF-1 levels protect the musculoskeletal system but are associated with elevated oxidative stress markers and increased mortality independent of tissue igf1 gene expression
    • Elis, S., Wu, Y., Courtland, H. W., Sun, H., Rosen, C. J., Adamo, M. L., and Yakar, S. (2011) Increased serum IGF-1 levels protect the musculoskeletal system but are associated with elevated oxidative stress markers and increased mortality independent of tissue igf1 gene expression. Aging Cell 10, 547-550
    • (2011) Aging Cell , vol.10 , pp. 547-550
    • Elis, S.1    Wu, Y.2    Courtland, H.W.3    Sun, H.4    Rosen, C.J.5    Adamo, M.L.6    Yakar, S.7
  • 52
    • 0027423419 scopus 로고
    • Role of insulin-like growth factors in embryonic and postnatal growth
    • Baker, J., Liu, J. P., Robertson, E. J., and Efstratiadis, A. (1993) Role of insulin-like growth factors in embryonic and postnatal growth. Cell 75, 73-82
    • (1993) Cell , vol.75 , pp. 73-82
    • Baker, J.1    Liu, J.P.2    Robertson, E.J.3    Efstratiadis, A.4
  • 53
    • 0029826839 scopus 로고    scopus 로고
    • Biochemical diagnostic strategies in the evaluation of short stature: The diagnosis of insulin-like growth factor deficiency
    • Rosenfeld, R. G. (1996) Biochemical diagnostic strategies in the evaluation of short stature: the diagnosis of insulin-like growth factor deficiency. Horm. Res. 46, 170-173
    • (1996) Horm. Res. , vol.46 , pp. 170-173
    • Rosenfeld, R.G.1
  • 54
    • 67650882756 scopus 로고    scopus 로고
    • An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells
    • Ostrovsky, O., Makarewich, C., Snapp, E. L., and Argon, Y. (2009) An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells. Proc. Natl. Acad. Sci. U. S. A. 106, 11600-11605
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11600-11605
    • Ostrovsky, O.1    Makarewich, C.2    Snapp, E.L.3    Argon, Y.4
  • 55
    • 70350367846 scopus 로고    scopus 로고
    • NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation
    • Datta, K., Guan, T., and Gerace, L. (2009) NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation. J. Biol. Chem. 284, 29666-29676
    • (2009) J. Biol. Chem. , vol.284 , pp. 29666-29676
    • Datta, K.1    Guan, T.2    Gerace, L.3


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