메뉴 건너뛰기




Volumn 388, Issue 11, 2007, Pages 1123-1130

Two decades of thyroglobulin type-1 domain research

Author keywords

Cysteine protease; Equistatin; IGFBP; Invariant chain; p41 fragment; Thyropin

Indexed keywords

ASPARTIC PROTEINASE; CATHEPSIN D; CATHEPSIN S; CYSTATIN; CYSTEINE PROTEINASE; EQUISTATIN; INHIBITOR PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; METALLOPROTEINASE; PAPAIN; POLYPEPTIDE; PROTEIN P41; PROTEINASE INHIBITOR; PROTEOGLYCAN; SOMATOMEDIN BINDING PROTEIN; TESTICAN; THYROGLOBULIN; THYROGLOBULIN TYPE 1; THYROPIN; UNCLASSIFIED DRUG;

EID: 35848936917     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2007.155     Document Type: Conference Paper
Times cited : (44)

References (60)
  • 1
    • 0028108215 scopus 로고
    • Production, inhibitory activity, folding and conformational analysis of an N-terminal and an internal deletion variant of chicken cystatin
    • Auerswald, E.A., Nägler, D.K., Schulze, A.J., Engh, R.A., Geneger, G., Machleidt, W., and Fritz, H. (1994). Production, inhibitory activity, folding and conformational analysis of an N-terminal and an internal deletion variant of chicken cystatin. Eur. J. Biochem. 224, 407-415.
    • (1994) Eur. J. Biochem , vol.224 , pp. 407-415
    • Auerswald, E.A.1    Nägler, D.K.2    Schulze, A.J.3    Engh, R.A.4    Geneger, G.5    Machleidt, W.6    Fritz, H.7
  • 2
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • Bakke, O. and Dobberstein, B. (1990). MHC class II-associated invariant chain contains a sorting signal for endosomal compartments. Cell 63, 707-716.
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 3
    • 77957034551 scopus 로고
    • Cystatin, the egg white inhibitor of cysteine proteinases
    • Barrett, A.J. (1981). Cystatin, the egg white inhibitor of cysteine proteinases. Methods Enzymol. 80, 771-778.
    • (1981) Methods Enzymol , vol.80 , pp. 771-778
    • Barrett, A.J.1
  • 5
    • 0029924123 scopus 로고    scopus 로고
    • Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L
    • Bevec, T., Stoka, V., Pungercic, G., Dolenc, I., and Turk, V. (1996). Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L. J. Exp. Med. 183, 1331-1338.
    • (1996) J. Exp. Med , vol.183 , pp. 1331-1338
    • Bevec, T.1    Stoka, V.2    Pungercic, G.3    Dolenc, I.4    Turk, V.5
  • 6
    • 0031019416 scopus 로고    scopus 로고
    • A fragment of the major histocompatibility complex class II-associated p41 invariant chain inhibits cruzipain, the major cysteine proteinase from Trypanosoma cruzi
    • Bevec, T., Stoka, V., Pungercic, G., Cazzulo, J.J., and Turk, V. (1997). A fragment of the major histocompatibility complex class II-associated p41 invariant chain inhibits cruzipain, the major cysteine proteinase from Trypanosoma cruzi. FEBS Lett. 401, 259-261.
    • (1997) FEBS Lett , vol.401 , pp. 259-261
    • Bevec, T.1    Stoka, V.2    Pungercic, G.3    Cazzulo, J.J.4    Turk, V.5
  • 7
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class II HLA antigens
    • Blum, J.S. and Cresswell, P. (1988). Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc. Natl. Acad. Sci. USA 185, 3975-3979.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.185 , pp. 3975-3979
    • Blum, J.S.1    Cresswell, P.2
  • 8
    • 0141815490 scopus 로고    scopus 로고
    • Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin L
    • Bocock, J.P., Edgell, C.J., Marr, H.S., and Erickson, A.H. (2003). Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin L. Eur. J. Biochem. 270, 4008-4015.
    • (2003) Eur. J. Biochem , vol.270 , pp. 4008-4015
    • Bocock, J.P.1    Edgell, C.J.2    Marr, H.S.3    Erickson, A.H.4
  • 9
    • 0024066065 scopus 로고
    • The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J., and Turk, V. (1988). The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7, 2593-2599.
    • (1988) EMBO J , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 10
    • 0029927851 scopus 로고    scopus 로고
    • Structure and cellular distribution of mouse brain testican. Association with the postsynaptic area of hippocampus pyramidal cells
    • Bonnet, F., Perin, J.P., Charbonnier, F., Camuzat, A., Roussel, G., Nussbaum, J.L., and Alliel, P.M. (1996). Structure and cellular distribution of mouse brain testican. Association with the postsynaptic area of hippocampus pyramidal cells. J. Biol. Chem. 271, 4373-4380.
    • (1996) J. Biol. Chem , vol.271 , pp. 4373-4380
    • Bonnet, F.1    Perin, J.P.2    Charbonnier, F.3    Camuzat, A.4    Roussel, G.5    Nussbaum, J.L.6    Alliel, P.M.7
  • 11
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • Brix, K., Lemansky, P., and Herzog, V. (1996). Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137, 1963-1974.
    • (1996) Endocrinology , vol.137 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 12
    • 0021053487 scopus 로고
    • Protein inhibitors of cysteine proteinases. I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes
    • Brzin, J., Kopitar, M., Turk, V., and Machleidt, W. (1983). Protein inhibitors of cysteine proteinases. I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe-Seyler's Z. Physiol. Chem. 364, 1475-1480.
    • (1983) Hoppe-Seyler's Z. Physiol. Chem , vol.364 , pp. 1475-1480
    • Brzin, J.1    Kopitar, M.2    Turk, V.3    Machleidt, W.4
  • 14
    • 0032516003 scopus 로고    scopus 로고
    • Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
    • Deussing, J., Roth, W., Saftig, P., Peters, C., Ploegh, H.L., and Villadangos, J.A. (1998). Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc. Natl. Acad. Sci. USA 95, 4516-4521.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4516-4521
    • Deussing, J.1    Roth, W.2    Saftig, P.3    Peters, C.4    Ploegh, H.L.5    Villadangos, J.A.6
  • 15
    • 0033151771 scopus 로고    scopus 로고
    • The contribution of N-terminal region residues of cystatin A (stefin A) to the affinity and kinetics of inhibition of papain. Cathepsin B and cathepsin L
    • Estrada, S., Pavlova, A., and Björk, I. (1999). The contribution of N-terminal region residues of cystatin A (stefin A) to the affinity and kinetics of inhibition of papain. Cathepsin B and cathepsin L. Biochemistry 38, 7339-7345.
    • (1999) Biochemistry , vol.38 , pp. 7339-7345
    • Estrada, S.1    Pavlova, A.2    Björk, I.3
  • 17
    • 0028809769 scopus 로고
    • Proteolysis of major histocompatibility complex class II-associated invariant chain is regulated by the alternatively spliced gene product, p41
    • Fineschi, B., Arneson, L.S., Naujokas, M.F., and Miller, J. (1995). Proteolysis of major histocompatibility complex class II-associated invariant chain is regulated by the alternatively spliced gene product, p41. Proc. Natl. Acad. Sci. USA 92, 10257-10261.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10257-10261
    • Fineschi, B.1    Arneson, L.S.2    Naujokas, M.F.3    Miller, J.4
  • 18
    • 0030587884 scopus 로고    scopus 로고
    • The proteolytic environment involved in MHC class II-restricted antigen presentation can be modulated by the p41 form of invariant chain
    • Fineschi, B., Sakaguchi, K., Appella, E., and Miller, J. (1996). The proteolytic environment involved in MHC class II-restricted antigen presentation can be modulated by the p41 form of invariant chain. J. Immunol. 157, 3211-3215.
    • (1996) J. Immunol , vol.157 , pp. 3211-3215
    • Fineschi, B.1    Sakaguchi, K.2    Appella, E.3    Miller, J.4
  • 19
    • 0004570729 scopus 로고
    • Intracellular distribution of proteolytic enzymes in rat liver tissue
    • Finkenstaedt, J.T. (1957). Intracellular distribution of proteolytic enzymes in rat liver tissue. Proc. Soc. Exp. Biol. Med. 95, 302-304.
    • (1957) Proc. Soc. Exp. Biol. Med , vol.95 , pp. 302-304
    • Finkenstaedt, J.T.1
  • 20
    • 0030998472 scopus 로고    scopus 로고
    • Heparin-binding, highly basic regions within the thyroglobulin type-1 repeat of insulin-like growth factor (IGF)-binding proteins (IGFBPs) -3, -5, and -6 inhibit IGFBP-4 degradation
    • Fowlkes, J.L., Thrailkill, K.M., George-Nascimento, C., Rosenberg, C.K., and Serra, D.M. (1997). Heparin-binding, highly basic regions within the thyroglobulin type-1 repeat of insulin-like growth factor (IGF)-binding proteins (IGFBPs) -3, -5, and -6 inhibit IGFBP-4 degradation. Endocrinology 138, 2280-2285.
    • (1997) Endocrinology , vol.138 , pp. 2280-2285
    • Fowlkes, J.L.1    Thrailkill, K.M.2    George-Nascimento, C.3    Rosenberg, C.K.4    Serra, D.M.5
  • 21
    • 0039547996 scopus 로고    scopus 로고
    • Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S
    • Guncar, G., Pungercic, G., Klemencic, I., Turk, V., and Turk, D. (1999). Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. EMBO J. 18, 793-803.
    • (1999) EMBO J , vol.18 , pp. 793-803
    • Guncar, G.1    Pungercic, G.2    Klemencic, I.3    Turk, V.4    Turk, D.5
  • 22
    • 7244259088 scopus 로고    scopus 로고
    • Contributions of the N- and C-terminal domains of IGF binding protein-6 to IGF binding
    • Headey, S.J., Leeding, K.S., Norton, R.S., and Bach, L.A. (2004). Contributions of the N- and C-terminal domains of IGF binding protein-6 to IGF binding. J. Mol. Endocrinol. 33, 377-386.
    • (2004) J. Mol. Endocrinol , vol.33 , pp. 377-386
    • Headey, S.J.1    Leeding, K.S.2    Norton, R.S.3    Bach, L.A.4
  • 23
    • 0037459045 scopus 로고    scopus 로고
    • Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
    • Jenko, S., Dolenc, I., Guncar, G., Dobersek, A., Podobnik, M., and Turk, D. (2003). Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases. J. Mol. Biol. 326, 875-885.
    • (2003) J. Mol. Biol , vol.326 , pp. 875-885
    • Jenko, S.1    Dolenc, I.2    Guncar, G.3    Dobersek, A.4    Podobnik, M.5    Turk, D.6
  • 24
    • 0028958031 scopus 로고
    • Insulin-like growth factors and their binding proteins: Biological actions
    • Jones, J.I. and Clemmons, D.R. (1995). Insulin-like growth factors and their binding proteins: biological actions. Endocr. Rev. 16, 33-34.
    • (1995) Endocr. Rev , vol.16 , pp. 33-34
    • Jones, J.I.1    Clemmons, D.R.2
  • 25
    • 0016611551 scopus 로고
    • Inhibition of cathepsin C by papain inhibitor from chicken egg white and by complex of this inhibitor with cathepsin B1
    • Keilova, H. and Tomasek, V. (1975). Inhibition of cathepsin C by papain inhibitor from chicken egg white and by complex of this inhibitor with cathepsin B1. Coll. Czech. Chem. Commun. 40, 218-224.
    • (1975) Coll. Czech. Chem. Commun , vol.40 , pp. 218-224
    • Keilova, H.1    Tomasek, V.2
  • 26
    • 0018192880 scopus 로고
    • Inhibition studies of an intracellular inhibitor on thiol proteinases
    • Kopitar, M., Brzin, J., Zvonar, T., Locnikar, P., Kregar, I., and Turk V. (1978). Inhibition studies of an intracellular inhibitor on thiol proteinases. FEBS Lett. 91, 355-359.
    • (1978) FEBS Lett , vol.91 , pp. 355-359
    • Kopitar, M.1    Brzin, J.2    Zvonar, T.3    Locnikar, P.4    Kregar, I.5    Turk, V.6
  • 27
    • 0038835365 scopus 로고    scopus 로고
    • Thyropins - new structurally related proteinase inhibitors
    • Lenarcic, B. and Bevec, T. (1998). Thyropins - new structurally related proteinase inhibitors. Biol. Chem. 379, 105-111.
    • (1998) Biol. Chem , vol.379 , pp. 105-111
    • Lenarcic, B.1    Bevec, T.2
  • 28
    • 0040736139 scopus 로고    scopus 로고
    • Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D
    • Lenarcic, B. and Turk, V. (1999). Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D. J. Biol. Chem. 274, 563-566.
    • (1999) J. Biol. Chem , vol.274 , pp. 563-566
    • Lenarcic, B.1    Turk, V.2
  • 29
    • 0040020321 scopus 로고    scopus 로고
    • Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain
    • Lenarcic, B., Ritonja, A., Strukelj, B., Turk, B., and Turk, V. (1997). Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain. J. Biol. Chem. 272, 13899-13903.
    • (1997) J. Biol. Chem , vol.272 , pp. 13899-13903
    • Lenarcic, B.1    Ritonja, A.2    Strukelj, B.3    Turk, B.4    Turk, V.5
  • 30
    • 0034686047 scopus 로고    scopus 로고
    • Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases
    • Lenarcic, B., Krishnan, G., Borukhovich, R., Ruck, B., Turk, V., and Moczydlowski, E. (2000). Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases. J. Biol. Chem. 275, 15572-15577.
    • (2000) J. Biol. Chem , vol.275 , pp. 15572-15577
    • Lenarcic, B.1    Krishnan, G.2    Borukhovich, R.3    Ruck, B.4    Turk, V.5    Moczydlowski, E.6
  • 33
    • 0021080396 scopus 로고
    • Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes
    • Machleidt, W., Borchart, U., Fritz, H., Brzin, J., Ritonja, A., and Turk, V. (1983). Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe-Seyler's Z. Physiol. Chem. 364, 1481-1486.
    • (1983) Hoppe-Seyler's Z. Physiol. Chem , vol.364 , pp. 1481-1486
    • Machleidt, W.1    Borchart, U.2    Fritz, H.3    Brzin, J.4    Ritonja, A.5    Turk, V.6
  • 35
    • 0037396716 scopus 로고    scopus 로고
    • Asparagine endopeptidase can initiate the removal of the MHC class II invariant chain chaperone
    • Manoury, B., Mazzeo, D., Li, D.N., Billson, J., Loak, K., Benaroch, P., and Watts, C. (2003). Asparagine endopeptidase can initiate the removal of the MHC class II invariant chain chaperone. Immunity 18, 489-498.
    • (2003) Immunity , vol.18 , pp. 489-498
    • Manoury, B.1    Mazzeo, D.2    Li, D.N.3    Billson, J.4    Loak, K.5    Benaroch, P.6    Watts, C.7
  • 37
    • 14944357255 scopus 로고    scopus 로고
    • Dual concentration-dependent activity of thyroglobulin type-1 domain of testican: Specific inhibitor and substrate of cathepsin L
    • Meh, P., Pavsic, M., Turk, V., Baici, A., and Lenarcic, B. (2005). Dual concentration-dependent activity of thyroglobulin type-1 domain of testican: specific inhibitor and substrate of cathepsin L. Biol. Chem. 386, 75-83.
    • (2005) Biol. Chem , vol.386 , pp. 75-83
    • Meh, P.1    Pavsic, M.2    Turk, V.3    Baici, A.4    Lenarcic, B.5
  • 38
    • 33745827338 scopus 로고    scopus 로고
    • Mouse stefins A1 and A2 (Stfa1 and Stfa2) differentiate between papain-like endo- and exopeptidases
    • Mihelic, M., Teuscher, C., Turk, V., and Turk, D. (2006). Mouse stefins A1 and A2 (Stfa1 and Stfa2) differentiate between papain-like endo- and exopeptidases. FEBS Lett. 580, 4195-4199.
    • (2006) FEBS Lett , vol.580 , pp. 4195-4199
    • Mihelic, M.1    Teuscher, C.2    Turk, V.3    Turk, D.4
  • 39
    • 0029797002 scopus 로고    scopus 로고
    • Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families
    • Molina, F., Bouanani, M., Pau, B., and Granier, C. (1996). Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families. Eur. J. Biochem. 240, 125-133.
    • (1996) Eur. J. Biochem , vol.240 , pp. 125-133
    • Molina, F.1    Bouanani, M.2    Pau, B.3    Granier, C.4
  • 40
    • 0035893764 scopus 로고    scopus 로고
    • Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes
    • Nakada, M., Yamada, A., Takino, T., Miyamori, H., Takahashi, T., Yamashita, J., and Sato, H. (2001). Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes. Cancer Res. 61, 8896-8902.
    • (2001) Cancer Res , vol.61 , pp. 8896-8902
    • Nakada, M.1    Yamada, A.2    Takino, T.3    Miyamori, H.4    Takahashi, T.5    Yamashita, J.6    Sato, H.7
  • 42
    • 0027761288 scopus 로고
    • Purification of the complex of cathepsin L and MHC class II associated invariant chain fragment from human kidney
    • Ogrinc, T., Dolenc, I., Ritonja, A., and Turk, V. (1993). Purification of the complex of cathepsin L and MHC class II associated invariant chain fragment from human kidney. FEBS Lett. 336, 555-559.
    • (1993) FEBS Lett , vol.336 , pp. 555-559
    • Ogrinc, T.1    Dolenc, I.2    Ritonja, A.3    Turk, V.4
  • 43
    • 0034731319 scopus 로고    scopus 로고
    • Cystatin inhibition of cathepsin B requires dislocation of the proteinase occluding loop. Demonstration by release of loop anchoring through mutation of His110
    • Pavlova, A., Mort, J.S., Abrahamson, M., and Björk, I. (2000). Cystatin inhibition of cathepsin B requires dislocation of the proteinase occluding loop. Demonstration by release of loop anchoring through mutation of His110. FEBS Lett. 487, 156-160.
    • (2000) FEBS Lett , vol.487 , pp. 156-160
    • Pavlova, A.1    Mort, J.S.2    Abrahamson, M.3    Björk, I.4
  • 44
    • 0036869527 scopus 로고    scopus 로고
    • Individual recombinant thyroglobulin type-1 domains are substrates for lysosomal cysteine proteinases
    • Pungercic, G., Dolenc, I., Dolinar, M., Bevec, T., Jenko, S., Kolaric, S., and Turk, V. (2002). Individual recombinant thyroglobulin type-1 domains are substrates for lysosomal cysteine proteinases. Biol. Chem. 383, 1809-1812.
    • (2002) Biol. Chem , vol.383 , pp. 1809-1812
    • Pungercic, G.1    Dolenc, I.2    Dolinar, M.3    Bevec, T.4    Jenko, S.5    Kolaric, S.6    Turk, V.7
  • 45
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R.J., Wolf, P.R., Bromme, D., Natkin, L.R., Villadangos, J.A., Ploegh, H.L., and Chapman, H.A. (1996). Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4, 357-366.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 47
    • 0029069504 scopus 로고
    • Destructive proteolysis by cysteine proteases in antigen presentation of ovalbumin
    • Rodriguez, G.M. and Diment, S. (1995). Destructive proteolysis by cysteine proteases in antigen presentation of ovalbumin. Eur. J. Immunol. 25, 1823-1827.
    • (1995) Eur. J. Immunol , vol.25 , pp. 1823-1827
    • Rodriguez, G.M.1    Diment, S.2
  • 48
    • 0015857449 scopus 로고
    • Some properties of a ficinpapain inhibitor from avian egg white
    • Sen, L.C. and Whitaker, J.R. (1973). Some properties of a ficinpapain inhibitor from avian egg white. Arch. Biochem. Biophys. 158, 623-632.
    • (1973) Arch. Biochem. Biophys , vol.158 , pp. 623-632
    • Sen, L.C.1    Whitaker, J.R.2
  • 49
    • 33748367666 scopus 로고    scopus 로고
    • Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins
    • Sitar, T., Popowicz, G.M., Siwanowicz, I., Huber, R., and Holak, T.A. (2006). Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins. Proc. Natl. Acad. Sci. USA 103, 13028-13033.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13028-13033
    • Sitar, T.1    Popowicz, G.M.2    Siwanowicz, I.3    Huber, R.4    Holak, T.A.5
  • 50
    • 0023054136 scopus 로고
    • Alternative splicing and alternative initiation of translation explain the four forms of the Ia antigen-associated invariant chain
    • Strubin, M., Berte, C., and Mach, B. (1986). Alternative splicing and alternative initiation of translation explain the four forms of the Ia antigen-associated invariant chain. EMBO J. 5, 3483-3488.
    • (1986) EMBO J , vol.5 , pp. 3483-3488
    • Strubin, M.1    Berte, C.2    Mach, B.3
  • 51
    • 0025301658 scopus 로고
    • The refined 2.4 A° X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs, M.T., Laber, B., Bode, W., Huber, R., Jerala, R., Lenarcic, B., and Turk, V. (1990). The refined 2.4 A° X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J. 9, 1939-1947.
    • (1990) EMBO J , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 52
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel, C., Bromme, D., Herzog, V., and Brix, K. (2000). Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 24, 4487-4498.
    • (2000) J. Cell Sci , vol.24 , pp. 4487-4498
    • Tepel, C.1    Bromme, D.2    Herzog, V.3    Brix, K.4
  • 54
    • 0035986219 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators
    • Turk, B., Turk, D., and Salvesen, G.S. (2002). Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Curr. Pharm. Des. 8, 1623-1637.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 55
    • 35848932451 scopus 로고
    • Weiterentwicklung eines Programmes fur Molekulgraphik und Elektronendichte-manipulation und seine Anwendungen auf verschiedene Protein-strukturaufkläurungen. Ph.D. Thesis, Technische Universitàt Mùnchen, Germany
    • Turk, D. (1992). Weiterentwicklung eines Programmes fur Molekulgraphik und Elektronendichte-manipulation und seine Anwendungen auf verschiedene Protein-strukturaufkläurungen. Ph.D. Thesis, Technische Universitàt Mùnchen, Germany.
    • (1992)
    • Turk, D.1
  • 56
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk, V. and Bode, W. (1991). The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 285, 213-219.
    • (1991) FEBS Lett , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 59
    • 0025787834 scopus 로고
    • Cysteine protease inhibitor in egg of chum salmon
    • Yamashita, M. and Konagaya, S. (1991). Cysteine protease inhibitor in egg of chum salmon. J. Biochem. 110, 762-766.
    • (1991) J. Biochem , vol.110 , pp. 762-766
    • Yamashita, M.1    Konagaya, S.2
  • 60
    • 0030067774 scopus 로고    scopus 로고
    • A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif
    • Yamashita, M. and Konagaya, S. (1996). A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif. J. Biol. Chem. 271, 1282-1284.
    • (1996) J. Biol. Chem , vol.271 , pp. 1282-1284
    • Yamashita, M.1    Konagaya, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.