메뉴 건너뛰기




Volumn 11, Issue , 2010, Pages

Functional characterization of the protein C A267T mutation: Evidence for impaired secretion due to defective intracellular transport

Author keywords

[No Author keywords available]

Indexed keywords

BAFILOMYCIN; COMPLEMENTARY DNA; LACTACYSTIN; MESSENGER RNA; N ACETYL BETA GLUCOSAMINIDASE; PROTEASOME; PROTEIN C;

EID: 77956495529     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-11-67     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 18244417756 scopus 로고    scopus 로고
    • Molecular recognition in the protein C anticoagulant pathway
    • 10.1046/j.1538-7836.2003.00299.x, 12871288
    • Dahlback B, Villoutreix BO. Molecular recognition in the protein C anticoagulant pathway. J Thromb Haemost 2003, 1:1525-1534. 10.1046/j.1538-7836.2003.00299.x, 12871288.
    • (2003) J Thromb Haemost , vol.1 , pp. 1525-1534
    • Dahlback, B.1    Villoutreix, B.O.2
  • 2
    • 0019789514 scopus 로고
    • Deficiency of protein C in congenital thrombotic disease
    • 10.1172/JCI110385, 370934, 6895379
    • Griffin JH, Evatt B, Zimmerman TS, Kleiss AJ, Wideman C. Deficiency of protein C in congenital thrombotic disease. J Clin Invest 1981, 68:1370-1373. 10.1172/JCI110385, 370934, 6895379.
    • (1981) J Clin Invest , vol.68 , pp. 1370-1373
    • Griffin, J.H.1    Evatt, B.2    Zimmerman, T.S.3    Kleiss, A.J.4    Wideman, C.5
  • 3
    • 19944433631 scopus 로고    scopus 로고
    • Familial thrombophilia and lifetime risk of venous thrombosis
    • 10.1111/j.1538-7836.2004.00852.x, 15333025
    • Vossen CY, Conard J, Fontcuberta J, Makris M, Van Der Meer FJ, Pabinger I, et al. Familial thrombophilia and lifetime risk of venous thrombosis. J Thromb Haemost 2004, 2:1526-1532. 10.1111/j.1538-7836.2004.00852.x, 15333025.
    • (2004) J Thromb Haemost , vol.2 , pp. 1526-1532
    • Vossen, C.Y.1    Conard, J.2    Fontcuberta, J.3    Makris, M.4    Van Der Meer, F.J.5    Pabinger, I.6
  • 4
    • 34250711947 scopus 로고    scopus 로고
    • Activated protein C
    • 10.1111/j.1538-7836.2007.02491.x, 17635713
    • Griffin JH, Fernandez JA, Gale AJ, Mosnier LO. Activated protein C. J Thromb Haemost 2007, 5(Suppl 1):73-80. 10.1111/j.1538-7836.2007.02491.x, 17635713.
    • (2007) J Thromb Haemost , vol.5 , Issue.SUPPL 1 , pp. 73-80
    • Griffin, J.H.1    Fernandez, J.A.2    Gale, A.J.3    Mosnier, L.O.4
  • 5
    • 0025883206 scopus 로고
    • Glycosylation of human protein C affects its secretion, processing, functional activities, and activation by thrombin
    • Grinnell BW, Walls JD, Gerlitz B. Glycosylation of human protein C affects its secretion, processing, functional activities, and activation by thrombin. J Biol Chem 1991, 266:9778-9785.
    • (1991) J Biol Chem , vol.266 , pp. 9778-9785
    • Grinnell, B.W.1    Walls, J.D.2    Gerlitz, B.3
  • 6
    • 34248155630 scopus 로고    scopus 로고
    • ProCMD: a database and 3 D web resource for protein C mutants
    • 10.1186/1471-2105-8-S1-S11, 1885840, 17430555
    • D'Ursi P, Marino F, Caprera A, Milanesi L, Faioni EM, Rovida E. ProCMD: a database and 3 D web resource for protein C mutants. BMC Bioinformatics 2007, 8(Suppl 1):S11. 10.1186/1471-2105-8-S1-S11, 1885840, 17430555.
    • (2007) BMC Bioinformatics , vol.8 , Issue.SUPPL 1
    • D'Ursi, P.1    Marino, F.2    Caprera, A.3    Milanesi, L.4    Faioni, E.M.5    Rovida, E.6
  • 7
    • 0029947353 scopus 로고    scopus 로고
    • Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94
    • Katsumi A, Senda T, Yamashita Y, Yamazaki T, Hamaguchi M, Kojima T, et al. Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94. Blood 1996, 87:4164-4175.
    • (1996) Blood , vol.87 , pp. 4164-4175
    • Katsumi, A.1    Senda, T.2    Yamashita, Y.3    Yamazaki, T.4    Hamaguchi, M.5    Kojima, T.6
  • 8
    • 0034994095 scopus 로고    scopus 로고
    • Symptomatic type 1 protein C deficiency caused by a de novo Ser270Leu mutation in the catalytic domain
    • 10.1046/j.1365-2141.2001.02809.x, 11380450
    • Lind B, Koefoed P, Thorsen S. Symptomatic type 1 protein C deficiency caused by a de novo Ser270Leu mutation in the catalytic domain. Br J Haematol 2001, 113:642-648. 10.1046/j.1365-2141.2001.02809.x, 11380450.
    • (2001) Br J Haematol , vol.113 , pp. 642-648
    • Lind, B.1    Koefoed, P.2    Thorsen, S.3
  • 9
    • 0036799853 scopus 로고    scopus 로고
    • Protein C deficiency caused by homozygosity for a novel PROC D180G mutation--in vitro expression and structural analysis of the mutation
    • Lind B, Gedde-Dahl T, Tjonnfjord G, Villoutreix BO, Brosstad F. Protein C deficiency caused by homozygosity for a novel PROC D180G mutation--in vitro expression and structural analysis of the mutation. Thromb Haemost 2002, 88:632-638.
    • (2002) Thromb Haemost , vol.88 , pp. 632-638
    • Lind, B.1    Gedde-Dahl, T.2    Tjonnfjord, G.3    Villoutreix, B.O.4    Brosstad, F.5
  • 10
    • 0037630008 scopus 로고    scopus 로고
    • Defective sorting to secretory vesicles in trans-Golgi network is partly responsible for protein C deficiency: molecular mechanisms of impaired secretion of abnormal protein C R169W, R352W, and G376D
    • 10.1161/01.RES.0000069020.87627.7D, 12663483
    • Naito M, Mimuro J, Endo H, Madoiwa S, Ogata K, Kikuchi J, et al. Defective sorting to secretory vesicles in trans-Golgi network is partly responsible for protein C deficiency: molecular mechanisms of impaired secretion of abnormal protein C R169W, R352W, and G376D. Circ Res 2003, 92:865-872. 10.1161/01.RES.0000069020.87627.7D, 12663483.
    • (2003) Circ Res , vol.92 , pp. 865-872
    • Naito, M.1    Mimuro, J.2    Endo, H.3    Madoiwa, S.4    Ogata, K.5    Kikuchi, J.6
  • 11
    • 0026645428 scopus 로고
    • Protein C deficiency Hong Kong 1 and 2:hereditary protein C deficiency caused by two mutant alleles, a 5-nucleotide deletion and a missense mutation
    • Sugahara Y, Miura O, Yuen P, Aoki N. Protein C deficiency Hong Kong 1 and 2:hereditary protein C deficiency caused by two mutant alleles, a 5-nucleotide deletion and a missense mutation. Blood 1992, 80:126-133.
    • (1992) Blood , vol.80 , pp. 126-133
    • Sugahara, Y.1    Miura, O.2    Yuen, P.3    Aoki, N.4
  • 12
    • 0028609488 scopus 로고
    • Compound heterozygous protein C deficiency caused by two mutations, Arg-178 to Gln and Cys-331 to Arg, leading to impaired secretion of mutant protein C
    • Sugahara Y, Miura O, Hirosawa S, Aoki N. Compound heterozygous protein C deficiency caused by two mutations, Arg-178 to Gln and Cys-331 to Arg, leading to impaired secretion of mutant protein C. Thromb Haemost 1994, 72:814-818.
    • (1994) Thromb Haemost , vol.72 , pp. 814-818
    • Sugahara, Y.1    Miura, O.2    Hirosawa, S.3    Aoki, N.4
  • 13
    • 0029680791 scopus 로고    scopus 로고
    • Cellular basis for protein C deficiency caused by a single amino acid substitution at Arg15 in the gamma-carboxyglutamic acid domain
    • Tokunaga F, Tsukamoto T, Koide T. Cellular basis for protein C deficiency caused by a single amino acid substitution at Arg15 in the gamma-carboxyglutamic acid domain. J Biochem 1996, 120:360-368.
    • (1996) J Biochem , vol.120 , pp. 360-368
    • Tokunaga, F.1    Tsukamoto, T.2    Koide, T.3
  • 14
    • 0026683159 scopus 로고
    • Homozygous protein C deficiency: identification of a novel missense mutation that causes impaired secretion of the mutant protein C
    • Yamamoto K, Matsushita T, Sugiura I, Takamatsu J, Iwasaki E, Wada H, et al. Homozygous protein C deficiency: identification of a novel missense mutation that causes impaired secretion of the mutant protein C. J Lab Clin Med 1992, 119:682-689.
    • (1992) J Lab Clin Med , vol.119 , pp. 682-689
    • Yamamoto, K.1    Matsushita, T.2    Sugiura, I.3    Takamatsu, J.4    Iwasaki, E.5    Wada, H.6
  • 15
    • 33645647884 scopus 로고    scopus 로고
    • Molecular mechanism for hereditary protein C deficiency in two Chinese families with thrombosis
    • 10.1111/j.1538-7836.2006.01913.x, 16689777
    • Zhou RF, Cai XH, Xie S, Wang XF, Wang HL. Molecular mechanism for hereditary protein C deficiency in two Chinese families with thrombosis. J Thromb Haemost 2006, 4:1154-1156. 10.1111/j.1538-7836.2006.01913.x, 16689777.
    • (2006) J Thromb Haemost , vol.4 , pp. 1154-1156
    • Zhou, R.F.1    Cai, X.H.2    Xie, S.3    Wang, X.F.4    Wang, H.L.5
  • 16
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • 10.1016/j.semcdb.2007.09.003, 2706143, 18023214
    • Malhotra JD, Kaufman RJ. The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 2007, 18:716-731. 10.1016/j.semcdb.2007.09.003, 2706143, 18023214.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 17
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • 10.1146/annurev.cellbio.19.110701.153949, 14570585
    • Trombetta ES, Parodi AJ. Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol 2003, 19:649-676. 10.1146/annurev.cellbio.19.110701.153949, 14570585.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 18
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: protein folding, quality control, degradation, and related human diseases
    • 10.1152/physrev.00050.2006, 17928587
    • Hebert DN, Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 2007, 87:1377-1408. 10.1152/physrev.00050.2006, 17928587.
    • (2007) Physiol Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 19
    • 74249108651 scopus 로고    scopus 로고
    • Disease-associated variants of microsomal retinol dehydrogenase 12 (RDH12) are degraded at mutant-specific rates
    • 10.1016/j.febslet.2009.12.009, 20006610
    • Lee SA, Belyaeva OV, Kedishvili NY. Disease-associated variants of microsomal retinol dehydrogenase 12 (RDH12) are degraded at mutant-specific rates. FEBS Lett 2010, 584:507-510. 10.1016/j.febslet.2009.12.009, 20006610.
    • (2010) FEBS Lett , vol.584 , pp. 507-510
    • Lee, S.A.1    Belyaeva, O.V.2    Kedishvili, N.Y.3
  • 20
  • 21
    • 77951667813 scopus 로고    scopus 로고
    • Factor XII Ofunato: Lys346Asn mutation associated with blood coagulation factor XII deficiency causes impaired secretion through a proteasome-mediated degradation
    • 10.1016/j.thromres.2009.12.004, 20022356
    • Suzuki K, Murai K, Suwabe A, Ishida Y. Factor XII Ofunato: Lys346Asn mutation associated with blood coagulation factor XII deficiency causes impaired secretion through a proteasome-mediated degradation. Thromb Res 2010, 125:438-443. 10.1016/j.thromres.2009.12.004, 20022356.
    • (2010) Thromb Res , vol.125 , pp. 438-443
    • Suzuki, K.1    Murai, K.2    Suwabe, A.3    Ishida, Y.4
  • 22
    • 0030858241 scopus 로고    scopus 로고
    • Intracellular degradation of secretion defect-type mutants of antithrombin is inhibited by proteasomal inhibitors
    • 10.1016/S0014-5793(97)00745-X, 9257691
    • Tokunaga F, Shirotani H, Hara K, Kozuki D, Omura S, Koide T. Intracellular degradation of secretion defect-type mutants of antithrombin is inhibited by proteasomal inhibitors. FEBS Lett 1997, 412:65-69. 10.1016/S0014-5793(97)00745-X, 9257691.
    • (1997) FEBS Lett , vol.412 , pp. 65-69
    • Tokunaga, F.1    Shirotani, H.2    Hara, K.3    Kozuki, D.4    Omura, S.5    Koide, T.6
  • 23
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M, Kaufman RJ. ER stress and the unfolded protein response. Mutat Res 2005, 569:29-63.
    • (2005) Mutat Res , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 24
    • 26444494585 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress compromises the ubiquitin-proteasome system
    • 10.1093/hmg/ddi312, 16103128
    • Menendez-Benito V, Verhoef LG, Masucci MG, Dantuma NP. Endoplasmic reticulum stress compromises the ubiquitin-proteasome system. Hum Mol Genet 2005, 14:2787-2799. 10.1093/hmg/ddi312, 16103128.
    • (2005) Hum Mol Genet , vol.14 , pp. 2787-2799
    • Menendez-Benito, V.1    Verhoef, L.G.2    Masucci, M.G.3    Dantuma, N.P.4
  • 25
    • 35448933677 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids
    • 10.1111/j.1742-4658.2007.06085.x, 17922840
    • Uchio N, Oma Y, Toriumi K, Sasagawa N, Tanida I, Fujita E, et al. Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids. FEBS J 2007, 274:5619-5627. 10.1111/j.1742-4658.2007.06085.x, 17922840.
    • (2007) FEBS J , vol.274 , pp. 5619-5627
    • Uchio, N.1    Oma, Y.2    Toriumi, K.3    Sasagawa, N.4    Tanida, I.5    Fujita, E.6
  • 26
    • 0344012515 scopus 로고    scopus 로고
    • Multiple endoplasmic reticulum-associated pathways degrade mutant yeast carboxypeptidase Y in mammalian cells
    • 10.1074/jbc.M302979200, 12954632
    • Mancini R, Aebi M, Helenius A. Multiple endoplasmic reticulum-associated pathways degrade mutant yeast carboxypeptidase Y in mammalian cells. J Biol Chem 2003, 278:46895-46905. 10.1074/jbc.M302979200, 12954632.
    • (2003) J Biol Chem , vol.278 , pp. 46895-46905
    • Mancini, R.1    Aebi, M.2    Helenius, A.3
  • 27
    • 34248997838 scopus 로고    scopus 로고
    • N-glycan structure dictates extension of protein folding or onset of disposal
    • 10.1038/nchembio880, 17510649
    • Molinari M. N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 2007, 3:313-320. 10.1038/nchembio880, 17510649.
    • (2007) Nat Chem Biol , vol.3 , pp. 313-320
    • Molinari, M.1
  • 28
    • 10444279177 scopus 로고    scopus 로고
    • Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming
    • Nakahara M, Koyama T, Nakazawa F, Nishio M, Shibamiya A, Hirosawa S. Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming. Thromb Haemost 2004, 92:1284-1290.
    • (2004) Thromb Haemost , vol.92 , pp. 1284-1290
    • Nakahara, M.1    Koyama, T.2    Nakazawa, F.3    Nishio, M.4    Shibamiya, A.5    Hirosawa, S.6
  • 29
    • 76949097939 scopus 로고    scopus 로고
    • Hereditary protein C deficiency caused by the Ala267Thr mutation in the protein C gene is associated with symptomatic and asymptomatic venous thrombosis
    • 10.1016/j.thromres.2009.05.013, 19535131
    • Tjeldhorn L, Sandset PM, Haugbro K, Skretting G. Hereditary protein C deficiency caused by the Ala267Thr mutation in the protein C gene is associated with symptomatic and asymptomatic venous thrombosis. Thromb Res 2010, 125:230-234. 10.1016/j.thromres.2009.05.013, 19535131.
    • (2010) Thromb Res , vol.125 , pp. 230-234
    • Tjeldhorn, L.1    Sandset, P.M.2    Haugbro, K.3    Skretting, G.4
  • 30
    • 0032819023 scopus 로고    scopus 로고
    • Protein misfolding and degradation in genetic diseases
    • 10.1002/(SICI)1098-1004(1999)14:3<186::AID-HUMU2>3.0.CO;2-J, 10477427
    • Bross P, Corydon TJ, Andresen BS, Jorgensen MM, Bolund L, Gregersen N. Protein misfolding and degradation in genetic diseases. Hum Mutat 1999, 14:186-198. 10.1002/(SICI)1098-1004(1999)14:3<186::AID-HUMU2>3.0.CO;2-J, 10477427.
    • (1999) Hum Mutat , vol.14 , pp. 186-198
    • Bross, P.1    Corydon, T.J.2    Andresen, B.S.3    Jorgensen, M.M.4    Bolund, L.5    Gregersen, N.6
  • 31
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: towards an understanding at the molecular level
    • 10.1016/S0955-0674(00)00233-7, 11454449
    • Ellgaard L, Helenius A. ER quality control: towards an understanding at the molecular level. Curr Opin Cell Biol 2001, 13:431-437. 10.1016/S0955-0674(00)00233-7, 11454449.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 32
    • 13244271981 scopus 로고    scopus 로고
    • Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion
    • 10.1111/j.1538-7836.2004.00756.x, 15219198
    • Enjolras N, Plantier JL, Rodriguez MH, Rea M, Attali O, Vinciguerra C, et al. Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion. J Thromb Haemost 2004, 2:1143-1154. 10.1111/j.1538-7836.2004.00756.x, 15219198.
    • (2004) J Thromb Haemost , vol.2 , pp. 1143-1154
    • Enjolras, N.1    Plantier, J.L.2    Rodriguez, M.H.3    Rea, M.4    Attali, O.5    Vinciguerra, C.6
  • 33
    • 0029665491 scopus 로고    scopus 로고
    • A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule
    • Arbini AA, Mannucci M, Bauer KA. A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule. Blood 1996, 87:5085-5094.
    • (1996) Blood , vol.87 , pp. 5085-5094
    • Arbini, A.A.1    Mannucci, M.2    Bauer, K.A.3
  • 34
    • 34250737299 scopus 로고    scopus 로고
    • Transient arrest in proteasomal degradation during inhibition of translation in the unfolded protein response
    • 10.1042/BJ20061854, 1896287, 17338678
    • Shenkman M, Tolchinsky S, Kondratyev M, Lederkremer GZ. Transient arrest in proteasomal degradation during inhibition of translation in the unfolded protein response. Biochem J 2007, 404:509-516. 10.1042/BJ20061854, 1896287, 17338678.
    • (2007) Biochem J , vol.404 , pp. 509-516
    • Shenkman, M.1    Tolchinsky, S.2    Kondratyev, M.3    Lederkremer, G.Z.4
  • 35
    • 0037185014 scopus 로고    scopus 로고
    • Intracellular accumulation of antithrombin Morioka (C95R), a novel mutation causing type I antithrombin deficiency
    • 10.1074/jbc.M210231200, 12399451
    • Tanaka Y, Ueda K, Ozawa T, Sakuragawa N, Yokota S, Sato R, et al. Intracellular accumulation of antithrombin Morioka (C95R), a novel mutation causing type I antithrombin deficiency. J Biol Chem 2002, 277:51058-51067. 10.1074/jbc.M210231200, 12399451.
    • (2002) J Biol Chem , vol.277 , pp. 51058-51067
    • Tanaka, Y.1    Ueda, K.2    Ozawa, T.3    Sakuragawa, N.4    Yokota, S.5    Sato, R.6
  • 36
    • 62549147038 scopus 로고    scopus 로고
    • The E693Delta mutation in amyloid precursor protein increases intracellular accumulation of amyloid beta oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells
    • 10.2353/ajpath.2009.080480, 2665755, 19164507
    • Nishitsuji K, Tomiyama T, Ishibashi K, Ito K, Teraoka R, Lambert MP, et al. The E693Delta mutation in amyloid precursor protein increases intracellular accumulation of amyloid beta oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells. Am J Pathol 2009, 174:957-969. 10.2353/ajpath.2009.080480, 2665755, 19164507.
    • (2009) Am J Pathol , vol.174 , pp. 957-969
    • Nishitsuji, K.1    Tomiyama, T.2    Ishibashi, K.3    Ito, K.4    Teraoka, R.5    Lambert, M.P.6
  • 37
    • 18844425019 scopus 로고    scopus 로고
    • Misfolded BiP is degraded by a proteasome-independent endoplasmic-reticulum-associated degradation pathway
    • 10.1042/BJ20041312, 1135023, 15610068
    • Donoso G, Herzog V, Schmitz A. Misfolded BiP is degraded by a proteasome-independent endoplasmic-reticulum-associated degradation pathway. Biochem J 2005, 387:897-903. 10.1042/BJ20041312, 1135023, 15610068.
    • (2005) Biochem J , vol.387 , pp. 897-903
    • Donoso, G.1    Herzog, V.2    Schmitz, A.3
  • 38
    • 0034717072 scopus 로고    scopus 로고
    • Degradation of human thyroperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein
    • 10.1074/jbc.M905763199, 10748076
    • Fayadat L, Siffroi-Fernandez S, Lanet J, Franc JL. Degradation of human thyroperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein. J Biol Chem 2000, 275:15948-15954. 10.1074/jbc.M905763199, 10748076.
    • (2000) J Biol Chem , vol.275 , pp. 15948-15954
    • Fayadat, L.1    Siffroi-Fernandez, S.2    Lanet, J.3    Franc, J.L.4
  • 39
    • 0033864420 scopus 로고    scopus 로고
    • Intracellular degradation of histidine-rich glycoprotein mutants: tokushima-1 and 2 mutants are degraded by different proteolytic systems
    • Wakabayashi S, Yoshida H, Shigekiyo T, Koide T. Intracellular degradation of histidine-rich glycoprotein mutants: tokushima-1 and 2 mutants are degraded by different proteolytic systems. J Biochem 2000, 128:201-206.
    • (2000) J Biochem , vol.128 , pp. 201-206
    • Wakabayashi, S.1    Yoshida, H.2    Shigekiyo, T.3    Koide, T.4
  • 40
    • 9644272423 scopus 로고    scopus 로고
    • The ubiquitin system: pathogenesis of human diseases and drug targeting
    • 10.1016/j.bbamcr.2004.09.018, 15571805
    • Ciechanover A, Schwartz AL. The ubiquitin system: pathogenesis of human diseases and drug targeting. Biochim Biophys Acta 2004, 1695:3-17. 10.1016/j.bbamcr.2004.09.018, 15571805.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 3-17
    • Ciechanover, A.1    Schwartz, A.L.2
  • 41
    • 0026760593 scopus 로고
    • Post-translational processing events in the secretion pathway of human protein C, a complex vitamin K-dependent antithrombotic factor
    • McClure DB, Walls JD, Grinnell BW. Post-translational processing events in the secretion pathway of human protein C, a complex vitamin K-dependent antithrombotic factor. J Biol Chem 1992, 267:19710-19717.
    • (1992) J Biol Chem , vol.267 , pp. 19710-19717
    • McClure, D.B.1    Walls, J.D.2    Grinnell, B.W.3
  • 42
    • 29244445116 scopus 로고    scopus 로고
    • Post-translational modifications in proteins involved in blood coagulation
    • 10.1111/j.1538-7836.2005.01478.x, 16129023
    • Hansson K, Stenflo J. Post-translational modifications in proteins involved in blood coagulation. J Thromb Haemost 2005, 3:2633-2648. 10.1111/j.1538-7836.2005.01478.x, 16129023.
    • (2005) J Thromb Haemost , vol.3 , pp. 2633-2648
    • Hansson, K.1    Stenflo, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.