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Volumn 20, Issue 13, 2000, Pages 4932-4947

Amino- and carboxy-terminal PEST domains mediate gastrin stabilization of rat L-histidine decarboxylase isoforms

Author keywords

[No Author keywords available]

Indexed keywords

CHOLECYSTOKININ B RECEPTOR; GASTRIN; HISTAMINE; HISTIDINE DECARBOXYLASE; HYBRID PROTEIN; MESSENGER RNA; ORNITHINE DECARBOXYLASE;

EID: 0034043406     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.13.4932-4947.2000     Document Type: Article
Times cited : (38)

References (50)
  • 1
    • 0030666729 scopus 로고    scopus 로고
    • Rule of Cuelp in ubiquitination and degradation at the ER surface
    • Biederer, T., C. Volkwein, and T. Sommer. 1997. Rule of Cuelp in ubiquitination and degradation at the ER surface. Science 278:1806-1809.
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 2
    • 0033974063 scopus 로고    scopus 로고
    • Posttranslational modifications of bcl-2 facilitate its proteasome-dependent degradation: Molecular characterization of the involved signaling pathway
    • Breitschopf, K., J. Haendeler, P. Malchow, A. M. Zeiher, and S. Dimmeler. 2000. Posttranslational modifications of bcl-2 facilitate its proteasome-dependent degradation: molecular characterization of the involved signaling pathway. Mol. Cell. Biol. 20:1886-1896.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1886-1896
    • Breitschopf, K.1    Haendeler, J.2    Malchow, P.3    Zeiher, A.M.4    Dimmeler, S.5
  • 3
    • 0028291492 scopus 로고
    • Acute responses of rat stomach enterochromaffin like cells to gastrin: Secretory activation and adaption
    • Chen, D., H.-J. Monstein, A. G. Nylander, C.-M. Zhao, F. Sundler, and R. Hakanson. 1994. Acute responses of rat stomach enterochromaffin like cells to gastrin: secretory activation and adaption. Gastroenterology 107:18-27.
    • (1994) Gastroenterology , vol.107 , pp. 18-27
    • Chen, D.1    Monstein, H.-J.2    Nylander, A.G.3    Zhao, C.-M.4    Sundler, F.5    Hakanson, R.6
  • 4
    • 0032538298 scopus 로고    scopus 로고
    • Novel aspects of gastrin induced activation of histidine decarboxylase in rat stomach ECL cells
    • Chen, D., C.-M. Zhao, H. Yamada, P. Norlen, and R. Hakanson. 1998. Novel aspects of gastrin induced activation of histidine decarboxylase in rat stomach ECL cells. Regulatory Peptides 77:169-175.
    • (1998) Regulatory Peptides , vol.77 , pp. 169-175
    • Chen, D.1    Zhao, C.-M.2    Yamada, H.3    Norlen, P.4    Hakanson, R.5
  • 5
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 6
    • 0029828536 scopus 로고    scopus 로고
    • Mechanism of polypeptide translocalion into the endoplasmic reticulum
    • Corsi, A. K., and R. Schekman. 1996, Mechanism of polypeptide translocalion into the endoplasmic reticulum. J. Biol. Chem. 271:30299-30302.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30299-30302
    • Corsi, A.K.1    Schekman, R.2
  • 7
    • 0032502709 scopus 로고    scopus 로고
    • Enzymes catalyzing ubiquitination and proteolytic processing of the p105 precursor of nuclear factor κB1
    • Coux, O., and A. L. Goldberg. 1998. Enzymes catalyzing ubiquitination and proteolytic processing of the p105 precursor of nuclear factor κB1. J. Biol. Chem. 273:8820-8828.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8820-8828
    • Coux, O.1    Goldberg, A.L.2
  • 8
    • 0032538322 scopus 로고    scopus 로고
    • Multiple forms of rat histidine decarhoxylase may reflect posttranslational activation of the enzyme
    • Dartsch, C., D. Chen, and L. Persson. 1998. Multiple forms of rat histidine decarhoxylase may reflect posttranslational activation of the enzyme. Regulatory Peptides 77:33-41.
    • (1998) Regulatory Peptides , vol.77 , pp. 33-41
    • Dartsch, C.1    Chen, D.2    Persson, L.3
  • 9
    • 0033036614 scopus 로고    scopus 로고
    • Histidine decarboxylase in rat stomach ECL cells: Relationship between enzyme activity and different molecular forms
    • Dartsch, C., D. Chen, R. Hakanson, and L. Persson. 1999. Histidine decarboxylase in rat stomach ECL cells: relationship between enzyme activity and different molecular forms. Regulatory Peptides 81:41-48.
    • (1999) Regulatory Peptides , vol.81 , pp. 41-48
    • Dartsch, C.1    Chen, D.2    Hakanson, R.3    Persson, L.4
  • 10
    • 0026036122 scopus 로고
    • Histidine decarhoxylase gene expression in rat fundus is regulated by gastrin
    • Dimaline, R., and A. K. Sandvik. 1991. Histidine decarhoxylase gene expression in rat fundus is regulated by gastrin. FEBS Lett. 281:20-22.
    • (1991) FEBS Lett. , vol.281 , pp. 20-22
    • Dimaline, R.1    Sandvik, A.K.2
  • 11
    • 0027287877 scopus 로고
    • Food stimulation of histidine decarboxylase messanger RNA in rat gastric fundus
    • Dimaline, R., A. K. Sandvik, D. Evans, E. R. Forster, and G. J. Dockray. 1993. Food stimulation of histidine decarboxylase messanger RNA in rat gastric fundus. J. Physiol. (Lond.) 465:449-458.
    • (1993) J. Physiol. (Lond.) , vol.465 , pp. 449-458
    • Dimaline, R.1    Sandvik, A.K.2    Evans, D.3    Forster, E.R.4    Dockray, G.J.5
  • 12
    • 0029981175 scopus 로고    scopus 로고
    • Comparison between activation of ornithine decarboxylase and histidine decarboxylase in rat stomach
    • Ding, X.-Q., D. Chen, E. Rosengren, L. Persson, and R. Hakanson. 1996. Comparison between activation of ornithine decarboxylase and histidine decarboxylase in rat stomach. Am. J. Physiol. 270:G476-G486.
    • (1996) Am. J. Physiol. , vol.270
    • Ding, X.-Q.1    Chen, D.2    Rosengren, E.3    Persson, L.4    Hakanson, R.5
  • 13
    • 0028102743 scopus 로고
    • A direct inhibitory effect of insulin on a cytosolic proteolytic complex containing insulin-degrading enzyme and multicatalytic proteinase
    • Duckworth, W. C., R. G. Bennet, and F. G. Hamel. 1994. A direct inhibitory effect of insulin on a cytosolic proteolytic complex containing insulin-degrading enzyme and multicatalytic proteinase. J. Biol. Chem. 269:24575-24580.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24575-24580
    • Duckworth, W.C.1    Bennet, R.G.2    Hamel, F.G.3
  • 14
    • 0028936760 scopus 로고
    • Degradation of ornithine decarboxylase by the mammalian and yeast 26s proteasome complexes requires all the components of the protease
    • Elias, S., B. Berchovich, C. Kahana, P. Coffino, M. Fischer, W. Hilt, D. H. Wolf, and A. Ciechanover. 1995. Degradation of ornithine decarboxylase by the mammalian and yeast 26S proteasome complexes requires all the components of the protease. Eur. J. Biochem. 229:276-283.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 276-283
    • Elias, S.1    Berchovich, B.2    Kahana, C.3    Coffino, P.4    Fischer, M.5    Hilt, W.6    Wolf, D.H.7    Ciechanover, A.8
  • 15
    • 0029954598 scopus 로고    scopus 로고
    • Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase
    • Engel, N., M. T. Olmo, C. S. Coleman, M. A. Medina, A. E. Pegg, and F. Sanchez-Jimenez. 1996. Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase. Biochem. J. 320:365-368.
    • (1996) Biochem. J. , vol.320 , pp. 365-368
    • Engel, N.1    Olmo, M.T.2    Coleman, C.S.3    Medina, M.A.4    Pegg, A.E.5    Sanchez-Jimenez, F.6
  • 16
    • 0032961877 scopus 로고    scopus 로고
    • Ovine arylalkylamine N-acetyltransferase in the pineal and pituitary glands: Differences in function and regulation
    • Fleming, J. V., P. Barrett, S. L. Coon, D. C. Klein, and P. J. Morgan. 1999. Ovine arylalkylamine N-acetyltransferase in the pineal and pituitary glands: Differences in function and regulation. Endocrinology 140:972-978.
    • (1999) Endocrinology , vol.140 , pp. 972-978
    • Fleming, J.V.1    Barrett, P.2    Coon, S.L.3    Klein, D.C.4    Morgan, P.J.5
  • 17
    • 0032941751 scopus 로고    scopus 로고
    • Ubiquitination and degradation of ATF2 are dimerization dependent
    • Fuchs, S. Y., and Z. Ronai. 1999. Ubiquitination and degradation of ATF2 are dimerization dependent. Mol. Cell. Biol. 19:3289-3298.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3289-3298
    • Fuchs, S.Y.1    Ronai, Z.2
  • 18
    • 0014075204 scopus 로고
    • Concomitant histochemical demonstration of histamine and catecholamines in enterochromaffin-like cells of gastric mucosa
    • Hakanson, R., and C. Owman. 1967. Concomitant histochemical demonstration of histamine and catecholamines in enterochromaffin-like cells of gastric mucosa. Life Sci. 6:759-766.
    • (1967) Life Sci. , vol.6 , pp. 759-766
    • Hakanson, R.1    Owman, C.2
  • 19
    • 0031763979 scopus 로고    scopus 로고
    • Regulation of multicatalytic enzyme activity by insulin and the insulin-degrading enzyme
    • Hamel, F. G., R. G. Bennett, and W. C. Duckworth. 1998. Regulation of multicatalytic enzyme activity by insulin and the insulin-degrading enzyme. Endocrinology 139:4061-4066.
    • (1998) Endocrinology , vol.139 , pp. 4061-4066
    • Hamel, F.G.1    Bennett, R.G.2    Duckworth, W.C.3
  • 20
    • 0028799607 scopus 로고
    • Rapid and regulated degradation of ornithine decarboxylase
    • Hayashi, S., and Y. Murakami. 1995. Rapid and regulated degradation of ornithine decarboxylase. Biochem. J. 306:1-10.
    • (1995) Biochem. J. , vol.306 , pp. 1-10
    • Hayashi, S.1    Murakami, Y.2
  • 21
    • 0030002888 scopus 로고    scopus 로고
    • Gastrin stimulation of histamine synthesis in enterochromaffin-like cells from the rabbit fundic mucosa
    • Hollande, F., S. Combettes, J.-P. Bali, and R. Magous. 1996. Gastrin stimulation of histamine synthesis in enterochromaffin-like cells from the rabbit fundic mucosa. Am. J. Physiol. 270:G463-G469.
    • (1996) Am. J. Physiol. , vol.270
    • Hollande, F.1    Combettes, S.2    Bali, J.-P.3    Magous, R.4
  • 22
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26S proteasome
    • Jariel-Encontre, I., M. Pariat, F. Martin, S. Carillo, C. Salvat, and M. Piechaczyk. 1995. Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26S proteasome. J. Biol. Chem. 270:11623-11627.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 24
    • 0033989986 scopus 로고    scopus 로고
    • Modes of regulation of ubiquitin-mediated protein degradation
    • Kornitzer, D., and A. Ciechanover. 2000. Modes of regulation of ubiquitin-mediated protein degradation. J. Cell. Physiol. 182:1-11.
    • (2000) J. Cell. Physiol. , vol.182 , pp. 1-11
    • Kornitzer, D.1    Ciechanover, A.2
  • 25
    • 0029850997 scopus 로고    scopus 로고
    • Different mechanisms control signal-induced degradation and basal turnover of the NF-κB inhibitor IκBα in vivo
    • Krappmann, D., F. G. Wulczyn, and C. Scheidereit. 1996. Different mechanisms control signal-induced degradation and basal turnover of the NF-κB inhibitor IκBα in vivo. EMBO J. 15:6716-6726.
    • (1996) EMBO J. , vol.15 , pp. 6716-6726
    • Krappmann, D.1    Wulczyn, F.G.2    Scheidereit, C.3
  • 26
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable tools for cell biologists
    • Lee, D. H., and A. L. Goldberg. 1998. Proteasome inhibitors: valuable tools for cell biologists. Trends Cell Biol. 8:397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 27
    • 0026667106 scopus 로고
    • Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme
    • Li, X., and P. Coffino. 1992. Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme. Mol. Cell. Biol. 12:3556-3562.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3556-3562
    • Li, X.1    Coffino, P.2
  • 28
    • 0027512650 scopus 로고
    • Degradation of ornithine decarboxylase: Exposure of the C-terminal target by a polyamine-inducible inhibitory protein
    • Li, X., and P. Coffino. 1993. Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein. Mol. Cell. Biol. 13:2377-2383.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2377-2383
    • Li, X.1    Coffino, P.2
  • 29
    • 0345712325 scopus 로고    scopus 로고
    • The PEST regions containing C-termini of mammalian ornithine decarboxylase and histidine decarboxylase play different roles inn protein degradation
    • Olmo, M. T., D. Rodriguez-Agudo, M. A. Medina, and F. Sanchez-Jimenez. 1999. The PEST regions containing C-termini of mammalian ornithine decarboxylase and histidine decarboxylase play different roles inn protein degradation. Biochem. Biophys. Res. Commun. 257:269-272.
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 269-272
    • Olmo, M.T.1    Rodriguez-Agudo, D.2    Medina, M.A.3    Sanchez-Jimenez, F.4
  • 30
    • 0032954038 scopus 로고    scopus 로고
    • Structural motifs involved in ubiquitin-mediated processing of the NF-κB precursor p105: Roles of the glycine-rich region and a downstream ubiquitination domain
    • Orian, A., A. L. Schwartz, A. Israel, S. Whiteside, C. Kahana, and A. Ciechanover. 1999, Structural motifs involved in ubiquitin-mediated processing of the NF-κB precursor p105: roles of the glycine-rich region and a downstream ubiquitination domain. Mol. Cell. Biol. 19:3664-3673.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3664-3673
    • Orian, A.1    Schwartz, A.L.2    Israel, A.3    Whiteside, S.4    Kahana, C.5    Ciechanover, A.6
  • 31
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. 1994. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 32
    • 0028028863 scopus 로고
    • Gastrin effects on isolated rat enterochromaffin-like cells in primary cultures
    • Prinz, C., D. R. Scott, D. Hurwitz, H. F. Helander, and G. Sachs. 1994. Gastrin effects on isolated rat enterochromaffin-like cells in primary cultures. Am. J. Physiol. 267:G663-G675.
    • (1994) Am. J. Physiol. , vol.267
    • Prinz, C.1    Scott, D.R.2    Hurwitz, D.3    Helander, H.F.4    Sachs, G.5
  • 34
    • 0033597765 scopus 로고    scopus 로고
    • Activation of human histidine decarboxylase gene promoter activity by gastrin is mediated by two distinct nuclear factors
    • Raychowdhury, R., Z. Zhang, M. Hocker, and T. C. Wang. 1999. Activation of human histidine decarboxylase gene promoter activity by gastrin is mediated by two distinct nuclear factors. J. Biol. Chem. 274:20961-20969.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20961-20969
    • Raychowdhury, R.1    Zhang, Z.2    Hocker, M.3    Wang, T.C.4
  • 35
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and S. W. Rogers. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 36
    • 0029744632 scopus 로고    scopus 로고
    • Multisite phosphorylation of ornithine decarboxylase in transformed macrophages results in increased intracellular enzyme stability and catalytic efficiency
    • Reddy, S. G., S. M. McIlheran, B. J. Cochran, L. L. Worth, L. A. Bishop, P. J. Brown, V. P. Knutson, and M. K. Haddox. 1996. Multisite phosphorylation of ornithine decarboxylase in transformed macrophages results in increased intracellular enzyme stability and catalytic efficiency. J. Biol. Chem. 271: 24945-24953.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24945-24953
    • Reddy, S.G.1    McIlheran, S.M.2    Cochran, B.J.3    Worth, L.L.4    Bishop, L.A.5    Brown, P.J.6    Knutson, V.P.7    Haddox, M.K.8
  • 37
    • 0032211774 scopus 로고    scopus 로고
    • Mechanism of activation of the gastric aspartic proteinases: Pepsinogen, progastricsin and prochymosin
    • Richter, C., T. Tanaka, and R. Y. Yada. 1998. Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosin. Biochem. J. 335:481-490.
    • (1998) Biochem. J. , vol.335 , pp. 481-490
    • Richter, C.1    Tanaka, T.2    Yada, R.Y.3
  • 39
    • 0023409022 scopus 로고
    • Gastrin produces an immediate and dose-dependent histamine release preceding acid secretion in the totally isolated vascularly perfused rat stomach
    • Sandvik, A. K., H. L. Waldum, P. M. Kleveland, and B. Schulze Sognen. 1987. Gastrin produces an immediate and dose-dependent histamine release preceding acid secretion in the totally isolated vascularly perfused rat stomach. Scand. J. Gastroenterol. 22:803-808.
    • (1987) Scand. J. Gastroenterol. , vol.22 , pp. 803-808
    • Sandvik, A.K.1    Waldum, H.L.2    Kleveland, P.M.3    Schulze Sognen, B.4
  • 40
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T., and S. Jentsch. 1993. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365:176-179.
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 41
    • 0032538531 scopus 로고    scopus 로고
    • Membrane targeting and binding of the 74-kDa form of mouse L-histidine decarboxylase via its carboxyl-terminal sequence
    • Suzuki, S., S. Tanaka, K. Nemoto, and A. Ichikawa. 1998. Membrane targeting and binding of the 74-kDa form of mouse L-histidine decarboxylase via its carboxyl-terminal sequence. FEBS Lett. 437:44-48.
    • (1998) FEBS Lett. , vol.437 , pp. 44-48
    • Suzuki, S.1    Tanaka, S.2    Nemoto, K.3    Ichikawa, A.4
  • 42
    • 0021322926 scopus 로고
    • Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization
    • Taguchi, Y., T. Watanabe, H. Kuota, H. Havashi, and H. Wada. 1984. Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization. J. Biol. Chem. 259:5214-5221.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5214-5221
    • Taguchi, Y.1    Watanabe, T.2    Kuota, H.3    Havashi, H.4    Wada, H.5
  • 43
    • 0030778610 scopus 로고    scopus 로고
    • Degradation of the 74kDa form of L-histidine decarboxylase via the ubiquitin-proteosome pathway in a rat basophilic/mast cell line (RBL-2H3)
    • Tanaka, S., K. Nemoto, E. Yamamura, S. Ohmura, and A. Ichikawa. 1997. Degradation of the 74kDa form of L-histidine decarboxylase via the ubiquitin-proteosome pathway in a rat basophilic/mast cell line (RBL-2H3). FEBS Lett. 417:203-207.
    • (1997) FEBS Lett. , vol.417 , pp. 203-207
    • Tanaka, S.1    Nemoto, K.2    Yamamura, E.3    Ohmura, S.4    Ichikawa, A.5
  • 44
    • 0032478714 scopus 로고    scopus 로고
    • Intracellular localization of the 74-and 53-kDa forms of L-histidine decarboxylase in a rat basophilic/mast cell line, RBL-2H3
    • Tanaka, S., K. Nemoto, E. Yamamura, and A. Ichikawa. 1998. Intracellular localization of the 74-and 53-kDa forms of L-histidine decarboxylase in a rat basophilic/mast cell line, RBL-2H3. J. Biol. Chem. 273:8177-8182.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8177-8182
    • Tanaka, S.1    Nemoto, K.2    Yamamura, E.3    Ichikawa, A.4
  • 45
    • 0025739155 scopus 로고
    • Gastrinhistamine sequence in the regulation of gastric acid secretion
    • Waldum, H. L., A. K. Sandvik, E. Brenna, and H. Petersen. 1991. Gastrinhistamine sequence in the regulation of gastric acid secretion. Gut 32:698-701.
    • (1991) Gut , vol.32 , pp. 698-701
    • Waldum, H.L.1    Sandvik, A.K.2    Brenna, E.3    Petersen, H.4
  • 46
    • 0026543951 scopus 로고
    • Purification and properties of L-histidine decarboxylase from mouse stomach
    • Watabe, A., T. Fukui, E. Ohmori, and A. Ichikawa. 1992. Purification and properties of L-histidine decarboxylase from mouse stomach. Biochem. Pharmacol. 43:587-593.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 587-593
    • Watabe, A.1    Fukui, T.2    Ohmori, E.3    Ichikawa, A.4
  • 48
    • 0029559924 scopus 로고
    • Comparative studies of human recombinant 74-and 54-kDa L-histidine decarboxylase
    • Yatsunami, K., M. Tsuchikawa, M. Kamada, K. Hori, and T. Higuchi. 1995. Comparative studies of human recombinant 74-and 54-kDa L-histidine decarboxylase. J. Biol. Chem. 270:30813-30817.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30813-30817
    • Yatsunami, K.1    Tsuchikawa, M.2    Kamada, M.3    Hori, K.4    Higuchi, T.5
  • 49
    • 17544364954 scopus 로고    scopus 로고
    • The human histidine decarboxylase promoter is regulated by gastrin and phorbol 12-myristate 13-acetate through a downstream cis-acting element
    • Zhang, Z., M. Hocker, T. J. Koh, and T. C. Wang. 1996. The human histidine decarboxylase promoter is regulated by gastrin and phorbol 12-myristate 13-acetate through a downstream cis-acting element. J. Biol. Chem. 271: 14188-14197.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14188-14197
    • Zhang, Z.1    Hocker, M.2    Koh, T.J.3    Wang, T.C.4
  • 50
    • 0032544634 scopus 로고    scopus 로고
    • Regulated co-translation ubiquitination of apolipoprotein B100
    • Zhou, M., E. A. Fischer, and H. N. Ginsberg. 1998. Regulated co-translation ubiquitination of apolipoprotein B100. J. Biol. Chem. 273:24649-24653.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24649-24653
    • Zhou, M.1    Fischer, E.A.2    Ginsberg, H.N.3


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