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Volumn 174, Issue 11, 2005, Pages 7022-7032

Cathepsin-L influences the expression of extracellular matrix in lymphoid organs and plays a role in the regulation of thymic output and of peripheral T cell number

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA5 INTEGRIN; ALPHA6 INTEGRIN; BETA1 INTEGRIN; CATHEPSIN L; CD4 ANTIGEN; CD45 ANTIGEN; CD8 ANTIGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 4; COMPLEMENTARY DNA; FIBRONECTIN; FLUORESCEIN ISOTHIOCYANATE; LAMININ; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MONOCLONAL ANTIBODY;

EID: 21044450326     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.174.11.7022     Document Type: Article
Times cited : (52)

References (65)
  • 1
    • 0021793969 scopus 로고
    • Extracellular matrix of the human thymus: Immunofluorescence studies on frozen sections and cultured epithelial cells
    • Berrith, S., W. Savino, and S. Cohen. 1985. Extracellular matrix of the human thymus: immunofluorescence studies on frozen sections and cultured epithelial cells. J. Histochem. Cytochem. 33: 655-664.
    • (1985) J. Histochem. Cytochem. , vol.33 , pp. 655-664
    • Berrith, S.1    Savino, W.2    Cohen, S.3
  • 2
    • 0026040167 scopus 로고
    • Extracellular matrix components of the mouse thymus microenvironment. Ontogenetic studies and modulation by glucocorticoid hormones
    • Lannes-Veira, J., M. Dardenne, and W. Savino. 1991. Extracellular matrix components of the mouse thymus microenvironment. Ontogenetic studies and modulation by glucocorticoid hormones. J. Histochem. Cytochem. 39: 1539-1546.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1539-1546
    • Lannes-Veira, J.1    Dardenne, M.2    Savino, W.3
  • 3
    • 0028832421 scopus 로고
    • Extracellular matrix proteins and integrin receptors in reactive and non-reactive lymph nodes
    • Castaños-Velez, E., P. Biberfeld, and M. Patarroyo. 1995. Extracellular matrix proteins and integrin receptors in reactive and non-reactive lymph nodes. Immunology 86: 270-278.
    • (1995) Immunology , vol.86 , pp. 270-278
    • Castaños-Velez, E.1    Biberfeld, P.2    Patarroyo, M.3
  • 4
    • 0026077561 scopus 로고
    • Adhesion of immature thymocytes to thymic stromal cells through fibronectin molecule and its significance for the induction of thymocyte differentiation
    • Utsumi K., M. Sawada, S. Narumiya, J. Nagamine, T. Sakata, S. Iwagami, Y. Kita, H. Teraoka, H. Hirano, M. Ogata, et al. 1991. Adhesion of immature thymocytes to thymic stromal cells through fibronectin molecule and its significance for the induction of thymocyte differentiation. Proc. Natl. Acad. Sci. USA 88: 5685-5689.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5685-5689
    • Utsumi, K.1    Sawada, M.2    Narumiya, S.3    Nagamine, J.4    Sakata, T.5    Iwagami, S.6    Kita, Y.7    Teraoka, H.8    Hirano, H.9    Ogata, M.10
  • 7
    • 0024447275 scopus 로고
    • Activation of CD4 cells by fibronectin and anti-CD3 antibodies: A synergistic effect mediated by the VLA-5 fibronectin receptor complex
    • Matsuyama, T., A. Yamada, J. Kay, K. M. Yamada, S. K. Akiyama, S. F. Schlossman, and C. Morimoto. 1989. Activation of CD4 cells by fibronectin and anti-CD3 antibodies: a synergistic effect mediated by the VLA-5 fibronectin receptor complex. J. Exp. Med. 170: 1133-1148.
    • (1989) J. Exp. Med. , vol.170 , pp. 1133-1148
    • Matsuyama, T.1    Yamada, A.2    Kay, J.3    Yamada, K.M.4    Akiyama, S.K.5    Schlossman, S.F.6    Morimoto, C.7
  • 8
    • 0035946844 scopus 로고    scopus 로고
    • Costimulation by extracellular matrix proteins determines the response to TCR ligation
    • Adler, B., S. Ashkar, H. Cantor, and G. F. Weber. 2001. Costimulation by extracellular matrix proteins determines the response to TCR ligation. Cell. Immunol. 210: 30-40.
    • (2001) Cell. Immunol. , vol.210 , pp. 30-40
    • Adler, B.1    Ashkar, S.2    Cantor, H.3    Weber, G.F.4
  • 9
    • 0031051950 scopus 로고    scopus 로고
    • Modulation of proliferation and lymphokine secretion of murine CD4F T cells and cloned Th1 cells by proteins of the extracellular matrix
    • Tschoetschel, U., J. Schwing, S. Frosch, E. Schmitt, D. Schuppan, and A. K. Reske-Kunz. 1997. Modulation of proliferation and lymphokine secretion of murine CD4F T cells and cloned Th1 cells by proteins of the extracellular matrix. Int. Immunol. 9: 147-159.
    • (1997) Int. Immunol. , vol.9 , pp. 147-159
    • Tschoetschel, U.1    Schwing, J.2    Frosch, S.3    Schmitt, E.4    Schuppan, D.5    Reske-Kunz, A.K.6
  • 10
    • 0027160032 scopus 로고
    • Extracellular matrix contains insulin-like growth factor binding protein-5: Potentiation of the effects of IGF-I
    • Jones, J. I., A. Gockerman, W. H. Jr. Busby, C. Camacho-Hubner, and D. R. Clemmons. 1993. Extracellular matrix contains insulin-like growth factor binding protein-5: potentiation of the effects of IGF-I. J. Cell Biol. 121: 679-687.
    • (1993) J. Cell Biol. , vol.121 , pp. 679-687
    • Jones, J.I.1    Gockerman, A.2    Busby Jr., W.H.3    Camacho-Hubner, C.4    Clemmons, D.R.5
  • 11
    • 0027976521 scopus 로고
    • Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein
    • Taipale, J., K. Miyazono, C. H. Heldin, and J. Keski-Oja. 1994. Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein. J. Cell Biol. 124: 171-181.
    • (1994) J. Cell Biol. , vol.124 , pp. 171-181
    • Taipale, J.1    Miyazono, K.2    Heldin, C.H.3    Keski-Oja, J.4
  • 14
    • 0034786862 scopus 로고    scopus 로고
    • Enhancement of stromal cell-derived factor-1 α-induced chemotaxis for CD4/8 double-positive thymocytes by fibronectin and laminin in mice
    • Yanagawa, Y., K. Iwabuchi, and K. Onoé. 2001. Enhancement of stromal cell-derived factor-1 α-induced chemotaxis for CD4/8 double-positive thymocytes by fibronectin and laminin in mice. Immunology 104: 43-49.
    • (2001) Immunology , vol.104 , pp. 43-49
    • Yanagawa, Y.1    Iwabuchi, K.2    Onoé, K.3
  • 16
    • 0031932089 scopus 로고    scopus 로고
    • Cysteine proteinases in cancer progression and their clinical relevance for prognosis
    • Lah, T. T., and J. Kos. 1998. Cysteine proteinases in cancer progression and their clinical relevance for prognosis. Biol. Chem. 379: 125-130.
    • (1998) Biol. Chem. , vol.379 , pp. 125-130
    • Lah, T.T.1    Kos, J.2
  • 17
    • 0030850648 scopus 로고    scopus 로고
    • The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation
    • Afonso, S., L. Romagnano, and B. Babiarz. 1997. The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation. Development 124: 3415-3425.
    • (1997) Development , vol.124 , pp. 3415-3425
    • Afonso, S.1    Romagnano, L.2    Babiarz, B.3
  • 19
    • 0038002071 scopus 로고    scopus 로고
    • Cathepsin L play an active role in involution of the mouse mammary gland
    • Burke, M. A., D. Hutter, R. P. Reshamwala, and J. E. Knepper. 2003. Cathepsin L play an active role in involution of the mouse mammary gland. Dev. Dyn. 227: 315-322.
    • (2003) Dev. Dyn. , vol.227 , pp. 315-322
    • Burke, M.A.1    Hutter, D.2    Reshamwala, R.P.3    Knepper, J.E.4
  • 20
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V., B. Turk, and D. Turk. 2001. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 20: 4629-4633.
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 22
    • 0037141021 scopus 로고    scopus 로고
    • + T cell selection independently of its effect on invariant chain: A role in the generation of positively selecting peptide ligands
    • + T cell selection independently of its effect on invariant chain: a role in the generation of positively selecting peptide ligands. J. Exp. Med. 195: 1349-1358.
    • (2002) J. Exp. Med. , vol.195 , pp. 1349-1358
    • Honey, K.1    Nakagawa, T.2    Peters, C.3    Rudensky, A.4
  • 23
    • 0036097449 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling
    • Tobin, D. J., K. Foitzik, T. Reinheckel, L. Mecklenburg, V. A. Botchkarev, C. Peters, and R. Paus. 2002. The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling. Am. J. Pathol. 160: 1807-1821.
    • (2002) Am. J. Pathol. , vol.160 , pp. 1807-1821
    • Tobin, D.J.1    Foitzik, K.2    Reinheckel, T.3    Mecklenburg, L.4    Botchkarev, V.A.5    Peters, C.6    Paus, R.7
  • 29
    • 0028167670 scopus 로고
    • Transmission of an Mls-1a-like superantigen to BALB/c mice by foster-nursing on F1 Mls-1 bxa mothers: Sex-influenced onset of clonal deletion
    • Piazzon, I., A. Goldman, S. Torello, I. Nepomnaschy, A. Deroche, and G. Dran. 1994. Transmission of an Mls-1a-like superantigen to BALB/c mice by foster-nursing on F1 Mls-1 bxa mothers: sex-influenced onset of clonal deletion. J. Immunol. 153: 1553-1562.
    • (1994) J. Immunol. , vol.153 , pp. 1553-1562
    • Piazzon, I.1    Goldman, A.2    Torello, S.3    Nepomnaschy, I.4    Deroche, A.5    Dran, G.6
  • 30
    • 0030816323 scopus 로고    scopus 로고
    • Synaptopodin: An actin-associated protein in telencephalic dendrites and renal podocytes
    • Mundel, P., H. W. Heid, T. M. Mundel, M. Kruger, J. Reiser, and W. Kriz. 1997. Synaptopodin: an actin-associated protein in telencephalic dendrites and renal podocytes. J. Cell Biol. 139: 193-204.
    • (1997) J. Cell Biol. , vol.139 , pp. 193-204
    • Mundel, P.1    Heid, H.W.2    Mundel, T.M.3    Kruger, M.4    Reiser, J.5    Kriz, W.6
  • 34
    • 0024263314 scopus 로고    scopus 로고
    • A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen
    • Maciewicz, R. A., and D. J. Etherington. 1998. A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen. Biochem. J. 256: 433-440.
    • (1998) Biochem. J. , vol.256 , pp. 433-440
    • Maciewicz, R.A.1    Etherington, D.J.2
  • 36
    • 0027639370 scopus 로고
    • Generation of matrix-degrading proteolytic system from fibronectin by cathepsins B, G, H, and L
    • Blondeau, X., S. L. Vidmar, I. Emod, M. Pagano, V. Turk, and V. Keil-Dlouha. 1993. Generation of matrix-degrading proteolytic system from fibronectin by cathepsins B, G, H, and L. Biol. Chem. Hoppe-Seyler 374: 651-656.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 651-656
    • Blondeau, X.1    Vidmar, S.L.2    Emod, I.3    Pagano, M.4    Turk, V.5    Keil-Dlouha, V.6
  • 37
    • 0027329828 scopus 로고
    • "In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like, and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin
    • Guinec, N., V. Dalet-Fumeron, and M. Pagano. 1993. "In vitro" study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like, and L. Digestion of collagen IV, laminin, fibronectin, and release of gelatinase activities from basement membrane fibronectin. Biol. Chem. Hoppe-Seyler 374: 1135-1146.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 1135-1146
    • Guinec, N.1    Dalet-Fumeron, V.2    Pagano, M.3
  • 38
    • 0034467924 scopus 로고    scopus 로고
    • The proteolytic activity of the recombinant cryptic fibronectin type IV collagenase from E. coli expression
    • Schenepel J., and H. Tschesche. 2000. The proteolytic activity of the recombinant cryptic fibronectin type IV collagenase from E. coli expression. J. Protein Chem. 19: 685-692.
    • (2000) J. Protein Chem. , vol.19 , pp. 685-692
    • Schenepel, J.1    Tschesche, H.2
  • 39
    • 0035958902 scopus 로고    scopus 로고
    • 3 integrins that elevates bcl-2 transcription
    • 3 integrins that elevates bcl-2 transcription. J. Biol. Chem. 276: 27757-27763.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27757-27763
    • Matter, M.L.1    Ruoslahti, E.2
  • 40
    • 1542467646 scopus 로고    scopus 로고
    • 1 inhibits Fas-mediated apoptosis in T lymphocytes by protein phosphatase 2A-dependent activation of the MAPK/ERK pathway
    • 1 inhibits Fas-mediated apoptosis in T lymphocytes by protein phosphatase 2A-dependent activation of the MAPK/ERK pathway. J. Biol. Chem. 278: 48633-48643.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48633-48643
    • Gendron, S.1    Couture, J.2    Aoudjit, F.3
  • 41
    • 0034284220 scopus 로고    scopus 로고
    • + T cells in the absence of self peptide: MHC complexes
    • + T cells in the absence of self peptide: MHC complexes. J. Immunol. 165: 2458-2464.
    • (2000) J. Immunol. , vol.165 , pp. 2458-2464
    • Clarke, S.R.1    Rudensky, A.Y.2
  • 42
    • 0036607859 scopus 로고    scopus 로고
    • Intrathymic T-cell migration: A combinatorial interplay of extracellular matrix and chemokines?
    • Savino W., D. A. Mendes-da-Cruz, J. S. Silva, M. Dardenne, and V. Cotta-de-Almeida. 2002. Intrathymic T-cell migration: a combinatorial interplay of extracellular matrix and chemokines? Trends Immunol. 23: 305-313.
    • (2002) Trends Immunol. , vol.23 , pp. 305-313
    • Savino, W.1    Mendes-Da-Cruz, D.A.2    Silva, J.S.3    Dardenne, M.4    Cotta-De-Almeida, V.5
  • 43
    • 0035081044 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-2 is correlated with invasiveness in thymic epithelial tumors
    • Kondo, K., H. Kinoshita, H. Ishikura, T. Miyoshi, T. Hirose, Y. Matsumori, and Y. Monden. 2001. Activation of matrix metalloproteinase-2 is correlated with invasiveness in thymic epithelial tumors. J. Surg. Oncol. 76: 169-175.
    • (2001) J. Surg. Oncol. , vol.76 , pp. 169-175
    • Kondo, K.1    Kinoshita, H.2    Ishikura, H.3    Miyoshi, T.4    Hirose, T.5    Matsumori, Y.6    Monden, Y.7
  • 44
    • 0033120062 scopus 로고    scopus 로고
    • Factor regulating stem cell recruitment to the fetal thymus
    • Wilkinson B., J. J. T. Owen, and E. J Jenkinson. 1999. Factor regulating stem cell recruitment to the fetal thymus. J. Immunol. 162: 3873-3781.
    • (1999) J. Immunol. , vol.162 , pp. 3873-3781
    • Wilkinson, B.1    Owen, J.J.T.2    Jenkinson, E.J.3
  • 45
    • 0034453056 scopus 로고    scopus 로고
    • Neuroendocrine control of thymus physiology
    • Savino W., and M. Dardenne. 2000. Neuroendocrine control of thymus physiology. Endocr. Rev. 21: 412-413.
    • (2000) Endocr. Rev. , vol.21 , pp. 412-413
    • Savino, W.1    Dardenne, M.2
  • 46
    • 0036184491 scopus 로고    scopus 로고
    • Functional insulin-like growth factor-1/insulin-like growth factor-1 receptor-mediated circuit in human and murine thymic epithelial cells
    • de Mello Coelho, V., D. M. Villa-Verde, D. A. Farias-de-Oliveira, J. M. Brito, M. Dardenne, and W. Savino. 2002. Functional insulin-like growth factor-1/insulin-like growth factor-1 receptor-mediated circuit in human and murine thymic epithelial cells. Neuroendocrinology 75: 139-150.
    • (2002) Neuroendocrinology , vol.75 , pp. 139-150
    • De Mello Coelho, V.1    Villa-Verde, D.M.2    Farias-De-Oliveira, D.A.3    Brito, J.M.4    Dardenne, M.5    Savino, W.6
  • 47
    • 0036953846 scopus 로고    scopus 로고
    • Triiodothyronine modulates extracellular matrix-mediated interactions between thymocytes and thymic microenvironmental cells
    • Ribeiro-Carvalho, M. M., D. A. Farias-de-Oliveira, D. M. Villa-Verde, and W. Savino. 2002-2003. Triiodothyronine modulates extracellular matrix-mediated interactions between thymocytes and thymic microenvironmental cells. Neuroimmunomodulation 10: 142-152.
    • (2002) Neuroimmunomodulation , vol.10 , pp. 142-152
    • Ribeiro-Carvalho, M.M.1    Farias-De-Oliveira, D.A.2    Villa-Verde, D.M.3    Savino, W.4
  • 48
    • 0037116601 scopus 로고    scopus 로고
    • Decreased intracellular degradation of insulin-like growth factor binding protein-3 in cathepsin L-deficient fibroblast
    • Zwad, O., B. Kubler, W. Roth, J. G. Scharf, P. Saftig, C. Peters, and T. Braulke. 2002. Decreased intracellular degradation of insulin-like growth factor binding protein-3 in cathepsin L-deficient fibroblast. FEBS Lett. 510: 211-215.
    • (2002) FEBS Lett. , vol.510 , pp. 211-215
    • Zwad, O.1    Kubler, B.2    Roth, W.3    Scharf, J.G.4    Saftig, P.5    Peters, C.6    Braulke, T.7
  • 49
    • 0031434673 scopus 로고    scopus 로고
    • The role of IGF-I in human skin and its appendages: Morphogen as well as mitogen?
    • Rudman, S. M., M. P. Philpott, G. A. Thomas, and T. Kealey. 1997. The role of IGF-I in human skin and its appendages: morphogen as well as mitogen? J. Invest. Dermatol. 109: 770-777.
    • (1997) J. Invest. Dermatol. , vol.109 , pp. 770-777
    • Rudman, S.M.1    Philpott, M.P.2    Thomas, G.A.3    Kealey, T.4
  • 51
    • 0033773605 scopus 로고    scopus 로고
    • Role of extracellular matrix-mediated interactions in thymocyte migration
    • Savino W., S. R. Dalmau, and V. C. Dealmeida. 2000. Role of extracellular matrix-mediated interactions in thymocyte migration. Dev. Immunol. 1: 279-291.
    • (2000) Dev. Immunol. , vol.1 , pp. 279-291
    • Savino, W.1    Dalmau, S.R.2    Dealmeida, V.C.3
  • 55
    • 0029988961 scopus 로고    scopus 로고
    • MHC class II-specific T cells can develop in the CD8 lineage when CD4 is absent
    • Matechak, E. O., N. Killeen, S. M. Hedrick, and B. J. Fowlkes. 1996. MHC class II-specific T cells can develop in the CD8 lineage when CD4 is absent. Immunity 4: 337-347.
    • (1996) Immunity , vol.4 , pp. 337-347
    • Matechak, E.O.1    Killeen, N.2    Hedrick, S.M.3    Fowlkes, B.J.4
  • 56
    • 0034544509 scopus 로고    scopus 로고
    • The quantity of TCR signal determines positive selection and lineage commitment of T cells
    • Watanabe, N., H. Arase, M. Onodera, P. S. Ohashi, and T. Saito. 2000. The quantity of TCR signal determines positive selection and lineage commitment of T cells. J. Immunol. 165: 6252-6261.
    • (2000) J. Immunol. , vol.165 , pp. 6252-6261
    • Watanabe, N.1    Arase, H.2    Onodera, M.3    Ohashi, P.S.4    Saito, T.5
  • 59
    • 0036346647 scopus 로고    scopus 로고
    • Duration of calcineurin and Erk signals regulates CD4/CD8 lineage commitment of thymocytes
    • Adachi, S., and M. Iwata. 2002. Duration of calcineurin and Erk signals regulates CD4/CD8 lineage commitment of thymocytes. Cell. Immunol. 215: 45-53.
    • (2002) Cell. Immunol. , vol.215 , pp. 45-53
    • Adachi, S.1    Iwata, M.2
  • 61
    • 0031448222 scopus 로고    scopus 로고
    • The influence of the MAPK pathway on the T cell lineage commitment
    • Sharp, L. L., D. A. Schwartz, C. M. Bott, C. J. Marshall, and S. M. Hedrick. 1997. The influence of the MAPK pathway on the T cell lineage commitment. Immunity 7: 609-618.
    • (1997) Immunity , vol.7 , pp. 609-618
    • Sharp, L.L.1    Schwartz, D.A.2    Bott, C.M.3    Marshall, C.J.4    Hedrick, S.M.5
  • 62
    • 0033565424 scopus 로고    scopus 로고
    • Activation of the extracellular signal-related kinase/mitogen-activated protein kinase pathway discriminates CD4 versus CD8 lineage
    • Bommhardt, U., M. A. Basson, U. Krummrei, and R. Zamoyska. 1999. Activation of the extracellular signal-related kinase/mitogen-activated protein kinase pathway discriminates CD4 versus CD8 lineage. J. Immunol. 163: 715-722.
    • (1999) J. Immunol. , vol.163 , pp. 715-722
    • Bommhardt, U.1    Basson, M.A.2    Krummrei, U.3    Zamoyska, R.4
  • 63
    • 0032740314 scopus 로고    scopus 로고
    • Commitment to the CD4 lineage mediated by extracellular signal-related kinase mitogen-activated protein kinase and lck signaling
    • Sharp L. L., and S. M. Hedrick. 1999. Commitment to the CD4 lineage mediated by extracellular signal-related kinase mitogen-activated protein kinase and lck signaling. J. Immunol. 163: 6598-6605.
    • (1999) J. Immunol. , vol.163 , pp. 6598-6605
    • Sharp, L.L.1    Hedrick, S.M.2
  • 64
    • 0035477991 scopus 로고    scopus 로고
    • Integrin functions play a key role in the differentiation of thymocytes in vivo
    • Schmeissner, P. J., H. Xie, L. B. Smilenov, F. Shu, and E. E. Marcantonio. 2001. Integrin functions play a key role in the differentiation of thymocytes in vivo. J. Immunol. 167: 3715-3724.
    • (2001) J. Immunol. , vol.167 , pp. 3715-3724
    • Schmeissner, P.J.1    Xie, H.2    Smilenov, L.B.3    Shu, F.4    Marcantonio, E.E.5
  • 65
    • 0032499627 scopus 로고    scopus 로고
    • Involvement of carboxy-terminal amino acids in secretion of human lysosomal protease cathepsin L
    • Chauhan, S. S., D. Ray, S. E. Kane., M. C. Willingham, and M. M. Gottesman. 1998. Involvement of carboxy-terminal amino acids in secretion of human lysosomal protease cathepsin L. Biochemistry 37: 8584-8594.
    • (1998) Biochemistry , vol.37 , pp. 8584-8594
    • Chauhan, S.S.1    Ray, D.2    Kane, S.E.3    Willingham, M.C.4    Gottesman, M.M.5


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