메뉴 건너뛰기




Volumn 6, Issue 1, 1999, Pages 7-16

Role of the 37 kDa laminin receptor precursor in the life cycle of prions

Author keywords

37 kDa laminin receptor precursor; Prion protein; Transmissible spongiform encephalopathy

Indexed keywords

CHAPERONE; LAMININ RECEPTOR; PRION PROTEIN; PROTEIN PRECURSOR;

EID: 0033082870     PISSN: 12467820     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1246-7820(99)80006-8     Document Type: Article
Times cited : (38)

References (65)
  • 1
    • 0020321767 scopus 로고
    • Novel protcinacetms infectious particles cause si-rapie
    • Prusiner SB. Novel protcinacetms infectious particles cause si-rapie. Science 1982 ; 216 : 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 4
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • I 'rusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE. Purification and structural studies of a major scrapie prion protein. Cell 1984; 38: 127-34.
    • (1984) Cell , vol.38 , pp. 127-134
    • I'Rusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3    Kent, S.B.4    Hood, L.E.5
  • 5
    • 85030356143 scopus 로고    scopus 로고
    • Molecular Biology of Prion Diseases
    • Cary JW, Linz JE, Stern MA, Bhatnagar D, eds. Microbial food-borne diseases: mechanisms of pathogenesis and toxin synthesis. in press.
    • Lasmézas CI, Weiss S. Molecular Biology of Prion Diseases. In: Cary JW, Linz JE, Stern MA, Bhatnagar D, eds. Microbial food-borne diseases: mechanisms of pathogenesis and toxin synthesis. Lancaster: Technomic Publishing Company; 1999. (in press).
    • (1999) Lancaster: Technomic Publishing Company
    • Lasmézas, C.I.1    Weiss, S.2
  • 8
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS. Self-replication and scrapie. Nature 1967 ; 215 : 1043-4.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 9
    • 0344030333 scopus 로고    scopus 로고
    • Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein
    • Lasmézas CI, Deslys JP, Robain O, Jaegly A, Beringue V, Peyrin JM, et al. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 1997 ; 275 : 402-5.
    • (1997) Science , vol.275 , pp. 402-405
    • Lasmézas, C.I.1    Deslys, J.P.2    Robain, O.3    Jaegly, A.4    Beringue, V.5    Peyrin, J.M.6
  • 10
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B, Raymond GJ, Ernst D, Race RE. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state. J Virol 1991 ; 65 : 6597-603.
    • (1991) J Virol , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 13
    • 0027332116 scopus 로고
    • Conversion of a-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan K-M, Baldwin M, Nguyen ], Gasset M, Serban A, Groth D, et al. Conversion of a-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sei USA 1993; 90: 10962-6.
    • (1993) Proc Natl Acad Sei USA , vol.90 , pp. 10962-10966
    • Pan, K.-M.1    Baldwin, M.2    Nguyen3    Gasset, M.4    Serban, A.5    Groth, D.6
  • 14
    • 0024545093 scopus 로고
    • Prion protein biosynthesis in scrapie-infected and unintected neuroblastoma cells
    • Caughey B, Race RE, Ernst D, Buchmeier M], Chesebro B. Prion protein biosynthesis in scrapie-infected and unintected neuroblastoma cells. J Virol 1989 ; 63 : 175-81.
    • (1989) J Virol , vol.63 , pp. 175-181
    • Caughey, B.1    Race, R.E.2    Ernst, D.3    Buchmeier, M.4    Chesebro, B.5
  • 16
    • 0029110883 scopus 로고
    • The chemistry of scrapie infection: Implications of the 'ice 9' metaphor
    • Lansbury PTJ. The chemistry of scrapie infection: implications of the 'ice 9' metaphor. Chem Biol 1995 ; 2 : 1-5.
    • (1995) Chem Biol , vol.2 , pp. 1-5
    • Ptj, L.1
  • 17
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler H, Fischer M, Lang Y, Bluethman H, Lipp HP, DeArmond SJ, et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992 ; 356 : 577-82.
    • (1992) Nature , vol.356 , pp. 577-582
    • Bueler, H.1    Fischer, M.2    Lang, Y.3    Bluethman, H.4    Lipp, H.P.5    Dearmond, S.J.6
  • 18
    • 0027997387 scopus 로고
    • Smith CJ, Palmer MS, C'larke AR, et al Prion protein is necessary for normal synaptic function
    • Collinge J, Whittington MA, Sidle KCL. Smith CJ, Palmer MS, C'larke AR, et al Prion protein is necessary for normal synaptic function. Nature 1994 ; 370 : 295-7.
    • (1994) Nature , vol.370 , pp. 295-297
    • Collinge, J.1    Whittington, M.A.2    Sidle, K.C.L.3
  • 19
    • 0029916617 scopus 로고    scopus 로고
    • Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus
    • IJedo PM, P T, SJ D, SB P, RA N. Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc Natl Acad Sei USA 1996 ; 93 : 2403-7.
    • (1996) Proc Natl Acad Sei USA , vol.93 , pp. 2403-2407
    • Ijedo, P.M.1    Sj, D.2    Sb, P.3    Ra, N.4
  • 21
    • 85048352656 scopus 로고    scopus 로고
    • PrP effects clarified
    • Weissmann C. PrP effects clarified. Curr Biol 1996 ; 6 : 11.
    • (1996) Curr Biol , vol.6 , pp. 11
    • Weissmann, C.1
  • 22
    • 0001552281 scopus 로고    scopus 로고
    • Expression of aminoterminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
    • Shmerling D, Hegyi I, Fischer M, et al. Expression of aminoterminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 1998 ; 93 : 203-14.
    • (1998) Cell , vol.93 , pp. 203-214
    • Shmerling, D.1    Hegyi, I.2    Fischer, M.3
  • 23
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993 ; 73 : 1339-47.
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3
  • 24
    • 0030054010 scopus 로고    scopus 로고
    • Normal host prion protein necessary for scrapie-induced neurotoxicity
    • Brandner S, Isenmann S, Raeber A, et al. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 1996; 379: 339-43.
    • (1996) Nature , vol.379 , pp. 339-343
    • Brandner, S.1    Isenmann, S.2    Raeber, A.3
  • 25
    • 0029825830 scopus 로고    scopus 로고
    • Normal host prion protein (PrPC) is required for scrapie spread within the central nervous system
    • Brandner S, Raeber A, Sailer A, et al. Normal host prion protein (PrPC) is required for scrapie spread within the central nervous system. Proc Natl Acad Sei USA 1996 ; 93 :13148-51.
    • (1996) Proc Natl Acad Sei USA , vol.93 , pp. 13148-13151
    • Brandner, S.1    Raeber, A.2    Sailer, A.3
  • 26
    • 0032488777 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein in neurodegenerative disease
    • Hegde RS, Mastrianni JA, Scott MR, et al. A transmembrane form of the prion protein in neurodegenerative disease. Science 1998 ; 279 : 827-34.
    • (1998) Science , vol.279 , pp. 827-834
    • Hegde, R.S.1    Mastrianni, J.A.2    Scott, M.R.3
  • 27
    • 0028874320 scopus 로고
    • A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP
    • Priola SA, Caughey B, Wehrly K, Chesebro B. A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP. J Biol Chem 1995 ; 270 : 3299-305.
    • (1995) J Biol Chem , vol.270 , pp. 3299-3305
    • Priola, S.A.1    Caughey, B.2    Wehrly, K.3    Chesebro, B.4
  • 28
    • 0032496218 scopus 로고    scopus 로고
    • Abnormal properties of prion protein with insertional mutations in different cell types.
    • Priola SA, Chesebro B. Abnormal properties of prion protein with insertional mutations in different cell types. ] Biol Chem 1998; 273 : 11980-5.
    • (1998) Biol Chem , vol.273 , pp. 11980-11985
    • Priola, S.A.1    Chesebro, B.2
  • 30
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease and phospholipase-sensitive
    • Caughey B, Raymond GJ. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease and phospholipase-sensitive. J Biol Chem 1991 ; 266 : 1821723.
    • (1991) J Biol Chem , vol.266 , pp. 1821723
    • Caughey, B.1    Raymond, G.J.2
  • 31
    • 0031436335 scopus 로고    scopus 로고
    • The human 37kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • Rieger R, Edenhofer F, Lasmézas Cl, Weiss S. The human 37kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat Med 1997 ; 3 : 1383-8.
    • (1997) Nat Med , vol.3 , pp. 1383-1388
    • Rieger, R.1    Edenhofer, F.2    Lasmézas, C.3    Weiss, S.4
  • 32
    • 33646114116 scopus 로고    scopus 로고
    • Une première étape dans l'identification de récepteurs cellulaire de la protéine du prion (Identifying cellular receptors for the prion protein)
    • Lasmézas CI, Deslys JP, Dormont D, Weiss S. Une première étape dans l'identification de récepteurs cellulaire de la protéine du prion (Identifying cellular receptors for the prion protein). Medecine Sciences 1998 ; 14 : 595-9.
    • (1998) Medecine Sciences , vol.14 , pp. 595-599
    • Lasmézas, C.I.1    Deslys, J.P.2    Dormont, D.3    Weiss, S.4
  • 35
    • 0029962468 scopus 로고    scopus 로고
    • Subcellular co-localization of the cellular and scrapie prion proteins in caveolae-like membranous domains
    • Vey M, Pilkuhn S, Wille H, Nixon R, DeArmond SJ, Smart EJ, et al. Subcellular co-localization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sei USA 1996 ; 93 : 14945-9.
    • (1996) Proc Natl Acad Sei USA , vol.93 , pp. 14945-14949
    • Vey, M.1    Pilkuhn, S.2    Wille, H.3    Nixon, R.4    Dearmond, S.J.5    Smart, E.J.6
  • 36
    • 0028305135 scopus 로고
    • A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits
    • Shyng SL, Heuser JE, Harris DA. A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits. J Cell Biol 1994; 125: 1239-50.
    • (1994) J Cell Biol , vol.125 , pp. 1239-1250
    • Shyng, S.L.1    Heuser, J.E.2    Harris, D.A.3
  • 37
    • 0002522491 scopus 로고    scopus 로고
    • Cell biological studies of the prion protein
    • Harris DA, ed. Norfolk: Horizon Scientific Press
    • Harris DA. Cell biological studies of the prion protein. In: Harris DA, ed. Prions: molecular and cellular biology. Norfolk: Horizon Scientific Press; 1999. p. 53-65.
    • (1999) Prions: Molecular and Cellular Biology. , pp. 53-65
    • Harris, D.A.1
  • 38
    • 0027639941 scopus 로고
    • Plasmalemmal caveolae and GPI-anchored membrane proteins
    • Anderson RG. Plasmalemmal caveolae and GPI-anchored membrane proteins. Curr Opin Cell Biol 1993 ; 5 : 647-52.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 647-652
    • Anderson, R.G.1
  • 39
    • 0019199611 scopus 로고
    • Pathogenesis of mouse scrapie: Evidence for neural spread of infection to the CNS
    • Kimberlin RH, Walker CA. Pathogenesis of mouse scrapie: evidence for neural spread of infection to the CNS. J Gen Virol 1980; 51 : 183-7.
    • (1980) J Gen Virol , vol.51 , pp. 183-187
    • Kimberlin, R.H.1    Walker, C.A.2
  • 40
    • 0031881510 scopus 로고    scopus 로고
    • Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie
    • Beekes M, McBride PA, Baldauf E. Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie. JGenVirol1998;79:601-7.
    • (1998) JGenVirol , vol.79 , pp. 601-607
    • Beekes, M.1    McBride, P.A.2    Baldauf, E.3
  • 42
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie priori protein
    • Tatzeit J, Prusiner SB, Welch W). Chemical chaperones interfere with the formation of scrapie priori protein. EMBO ) 1996; 15:6363-73.
    • (1996) EMBO , vol.15 , pp. 6363-6373
    • Tatzeit, J.1    Prusiner, S.B.2    Welch, W.3
  • 44
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling CC, Scott M, Mastrianni J, Cabizon R, Torchia M, Cohen Fli, et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995 ; 83 : 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, C.C.1    Scott, M.2    Mastrianni, J.3    Cabizon, R.4    Torchia, M.5    Fli, C.6
  • 45
    • 0026093621 scopus 로고
    • Receptors for laminin on mammalian cells
    • Mechnm RP. Receptors for laminin on mammalian cells. FASKBJ 1491 ; 5:2538-46.
    • (1491) FASKBJ , vol.5 , pp. 2538-2546
    • Mechnm, R.P.1
  • 46
    • 0000596059 scopus 로고
    • Isolation of a laminin binding protein from muscle cell membranes
    • Lesot H, Kühl U, von der Mark K. Isolation of a laminin binding protein from muscle cell membranes. EMBO J 1983 ; 2 : Sol-5.
    • (1983) EMBO J , vol.2 , pp. 5
    • Lesot, H.1    Kühl, U.2    Von Der Mark, K.3
  • 47
    • 0020618286 scopus 로고
    • Isolation of a cell surface receptor for laminin from murine fibrosarcoma cells
    • Malinoff HL, Wicha MS. Isolation of a cell surface receptor for laminin from murine fibrosarcoma cells. J Cell Biol 1983; 96: 1475-9.
    • (1983) J Cell Biol , vol.96 , pp. 1475-1479
    • Malinoff, H.L.1    Wicha, M.S.2
  • 49
    • 0027279623 scopus 로고
    • Laminin receptors and laminin-binding proteins during tumor invasion and metastasis
    • Castronovo V. Laminin receptors and laminin-binding proteins during tumor invasion and metastasis. Invasion Metastasis 1493 ; 13 : 1-30.
    • (1493) Invasion Metastasis , vol.13 , pp. 1-30
    • Castronovo, V.1
  • 50
    • 0025821651 scopus 로고
    • Characterization of a putative clone for the 67-kilodalton elastin/Laminin receptor suggests that it encodes a cytoplasmic protein rather than a cell surface receptor
    • Grosso LIS, Park PW, Mecham RP. Characterization of a putative clone for the 67-kilodalton elastin/Laminin receptor suggests that it encodes a cytoplasmic protein rather than a cell surface receptor. Biochemistry 1991 ; 30 : 3346-50.
    • (1991) Biochemistry , vol.30 , pp. 3346-3350
    • Lis, G.1    Park, P.W.2    Mecham, R.P.3
  • 51
    • 0345518033 scopus 로고
    • Increased mRNA expression of a laminin-binding protein in human colon carcinoma: Complete sequence of a full-length cDNA encoding the protein
    • Yow H, Wong JM, Chen HS, Lee C, Steele GDJ, Chen LB. Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein. Proc Natl Acad Sei USA 1988 ; 85 : 6394-K
    • (1988) Proc Natl Acad Sei USA , vol.85
    • Yow, H.1    Wong, J.M.2    Chen, H.S.3    Lee, C.4    Gdj, S.5    Chen, L.B.6
  • 53
    • 0026554288 scopus 로고
    • A 33-kDa polypeptide with homology to the laminin receptor: Component of translation machinery
    • Auth D, Brawerman Ci. A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery. Proc Natl Acad Sei USA 1992 ; 89 : 4368-72.
    • (1992) Proc Natl Acad Sei USA , vol.89 , pp. 4368-4372
    • Auth, D.1    Ci, B.2
  • 54
    • 0031880124 scopus 로고    scopus 로고
    • The 67-kDa laminin receptor originated from a ribosorruil protein that acquired a dual function during evolution
    • Ardini E, Pesole G, Tagliabue E, Magnifico A, Castronovo V, Sobel ME, et al. The 67-kDa laminin receptor originated from a ribosorruil protein that acquired a dual function during evolution. Mol Biol Evol 1998 ; 15 : 1017-25.
    • (1998) Mol Biol Evol , vol.15 , pp. 1017-1025
    • Ardini, E.1    Pesole, G.2    Tagliabue, E.3    Magnifico, A.4    Castronovo, V.5    Sobel, M.E.6
  • 55
  • 56
    • 0029789977 scopus 로고    scopus 로고
    • Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p2L3
    • Jackers P, Minoletti F, Belotti D, Clausse N, Soxzi G, Sobel ME, et al. Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p2L3. Oncogene 19% ; 13 : 445-503.
    • Oncogene , vol.13 , pp. 445-503
    • Jackers, P.1    Minoletti, F.2    Belotti, D.3    Clausse, N.4    Soxzi, G.5    Sobel, M.E.6
  • 57
    • 0030020325 scopus 로고    scopus 로고
    • Seventeen copies of the human 37 kDa laminin receptor precursor/p40 ribosome-associated protein gene are processed pseudogenes arisen from retropositional events
    • Jackers P, Clausse N, Fernandez M, Berti A, Princen F, Wewer U, et al. Seventeen copies of the human 37 kDa laminin receptor precursor/p40 ribosome-associated protein gene are processed pseudogenes arisen from retropositional events. Biochim Biophys Acta 1996 ; 1305 : 98-104.
    • (1996) Biochim Biophys Acta , vol.1305 , pp. 98-104
    • Jackers, P.1    Clausse, N.2    Fernandez, M.3    Berti, A.4    Princen, F.5    Wewer, U.6
  • 58
    • 0030444250 scopus 로고    scopus 로고
    • Identification of the active gene coding for the metastasisassociated 37LRP/p40 multifunctional protein
    • Clausse N, Jackers P, Jares P, Joris B, Sobel ME, Castronovo V. Identification of the active gene coding for the metastasisassociated 37LRP/p40 multifunctional protein. DNA Cell Biol 1996; 15 : 1009-23.
    • (1996) DNA Cell Biol , vol.15 , pp. 1009-1023
    • Clausse, N.1    Jackers, P.2    Jares, P.3    Joris, B.4    Sobel, M.E.5    Castronovo, V.6
  • 59
    • 0028795717 scopus 로고
    • A protein similar to the 67 kDa laminin binding protein and p40 is probably a component of the translational machinery in Urechis caupo oocytes and embryos
    • Rosenthal ET, Wordeman L. A protein similar to the 67 kDa laminin binding protein and p40 is probably a component of the translational machinery in Urechis caupo oocytes and embryos. J Cell Sei 1995 ; 108 : 245-56.
    • (1995) J Cell Sei , vol.108 , pp. 245-256
    • Rosenthal, E.T.1    Wordeman, L.2
  • 60
    • 15844364296 scopus 로고    scopus 로고
    • Yeast proteins related to the p40/Laminin receptor precursor are essential components of the 40 S ribosomal subunit
    • Demianova M, Formosa TG, Ellis SR. Yeast proteins related to the p40/Laminin receptor precursor are essential components of the 40 S ribosomal subunit. J Biol Chem 1996 ; 271 : 11383-91.
    • (1996) J Biol Chem , vol.271 , pp. 11383-11391
    • Demianova, M.1    Formosa, T.G.2    Ellis, S.R.3
  • 61
    • 0026628752 scopus 로고
    • High affinity laminin receptor is a receptor for Sindbis Virus in mammalian cells
    • Wang K-S, Kühn RJ, Strauss EG, Ou S, Strauss J High affinity laminin receptor is a receptor for Sindbis Virus in mammalian cells. J Virol 1992 ; 66 : 4992-5001.
    • (1992) J Virol , vol.66 , pp. 4992-5001
    • Wang, K.-S.1    Kühn, R.J.2    Strauss, E.G.3    Ou, S.4    Strauss, J.5
  • 62
    • 0030013729 scopus 로고    scopus 로고
    • A putative receptor for Venezuelan Equine Encephalitis virus from mosquito cells.
    • Ludwig GV, Kondig JP, Smith JE A putative receptor for Venezuelan Equine Encephalitis virus from mosquito cells. ] Virol 1996;70:5592-9.
    • (1996) Virol , vol.70 , pp. 5592-5599
    • Ludwig, G.V.1    Kondig, J.P.2    Smith, J.E.3
  • 63
    • 0029154305 scopus 로고
    • Studies of the structure of the metastasis-associated 67 kDa laminin binding protein: Fatty acid acylation and evidence supporting dimerization of the 32 kDa gene product to form the mature protein
    • Landowski TH, Dratz EA, Starkey JR. Studies of the structure of the metastasis-associated 67 kDa laminin binding protein: Fatty acid acylation and evidence supporting dimerization of the 32 kDa gene product to form the mature protein. Biochemistry 1995 ; 34 : 11276-87.
    • (1995) Biochemistry , vol.34 , pp. 11276-11287
    • Landowski, T.H.1    Dratz, E.A.2    Starkey, J.R.3
  • 65
    • 0024535958 scopus 로고
    • A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction
    • Hunter DD, Shah V, Merlie JP, Sanes JR. A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature 1989 ; 338 : 229-34.
    • (1989) Nature , vol.338 , pp. 229-234
    • Hunter, D.D.1    Shah, V.2    Merlie, J.P.3    Sanes, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.