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Volumn 255, Issue 1, 1996, Pages 1-11

Biotinidase and its roles in biotin metabolism

Author keywords

Biocytin; Biotin; Biotinidase; Histones; Neuronal cells; Nucleus; Transferase

Indexed keywords

BIOTIN; BIOTINIDASE;

EID: 0030588933     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/0009-8981(96)06396-6     Document Type: Review
Times cited : (109)

References (64)
  • 1
    • 0011819659 scopus 로고
    • Vitamin-dependent metabolic diseases
    • Kelley VC, editor. Philadelphia, PA: Harper and Row
    • [1] Wolf B. Vitamin-dependent metabolic diseases. In: Kelley VC, editor. Practice of pediatrics. Philadelphia, PA: Harper and Row, 1982;1-9.
    • (1982) Practice of Pediatrics , pp. 1-9
    • Wolf, B.1
  • 2
    • 0003114965 scopus 로고
    • Disorders of biotin metabolism
    • Scriver CR, Beaudet AL, Sly WS, Valle D, editors. New York: McGraw-Hill Inc.
    • [2] Wolf B. Disorders of biotin metabolism. In: Scriver CR, Beaudet AL, Sly WS, Valle D, editors. The metabolic and molecular bases of inherited disease, 7th edn. New York: McGraw-Hill Inc., 1995;3151-3180.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease, 7th Edn. , pp. 3151-3180
    • Wolf, B.1
  • 3
    • 0019607020 scopus 로고
    • Defective biotin absorption in multiple carboxylase deficiency
    • [3] Munnich A, Saudubray JM, Carre G et al. Defective biotin absorption in multiple carboxylase deficiency. Lancet 1981;2:263.
    • (1981) Lancet , vol.2 , pp. 263
    • Munnich, A.1    Saudubray, J.M.2    Carre, G.3
  • 4
    • 0020525812 scopus 로고
    • Biotinidase deficiency: The enzymatic defect in late-onset multiple carboxylase deficiency
    • [4] Wolf B, Grier RE, Allen RJ, Goodman SI, Kien CL. Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency. Clin Chim Acta 1983;131:273-281.
    • (1983) Clin Chim Acta , vol.131 , pp. 273-281
    • Wolf, B.1    Grier, R.E.2    Allen, R.J.3    Goodman, S.I.4    Kien, C.L.5
  • 5
    • 0011859364 scopus 로고
    • The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and ( + )-biotin. I. Purification of apoenzyme and synthetase: Characteristics of the reaction
    • [5] Lane MD, Young DL, Lynen F. The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and ( + )-biotin. I. Purification of apoenzyme and synthetase: characteristics of the reaction. J Biol Chem 1964;239:2858-2864.
    • (1964) J Biol Chem , vol.239 , pp. 2858-2864
    • Lane, M.D.1    Young, D.L.2    Lynen, F.3
  • 6
    • 0011825784 scopus 로고
    • Synthesis of biotin-dependent carboxylases from their apoproteins and biotin
    • [6] Achuta Murthy PN, Mistry SP. Synthesis of biotin-dependent carboxylases from their apoproteins and biotin. Biochem Rev (India) 1972;43:1-12.
    • (1972) Biochem Rev (India) , vol.43 , pp. 1-12
    • Achuta Murthy, P.N.1    Mistry, S.P.2
  • 7
    • 0011865933 scopus 로고
    • Pancreatic biotinidase activity: The potential for intestinal processing of dietary protein-bound biotin
    • [7] Heard GS, Wolf B, Reddy JK. Pancreatic biotinidase activity: the potential for intestinal processing of dietary protein-bound biotin. Pediatr Res 1984;18:198A.
    • (1984) Pediatr Res , vol.18
    • Heard, G.S.1    Wolf, B.2    Reddy, J.K.3
  • 8
    • 0022262194 scopus 로고
    • Biotinidase deficiency: A novel vitamin recycling defect
    • [8] Wolf B, Grier RE, Secor McVoy Jr, Heard GS. Biotinidase deficiency: a novel vitamin recycling defect. J Inherit Metab Dis 1985;8 (Suppl 1):53-58.
    • (1985) J Inherit Metab Dis , vol.8 , Issue.SUPPL. 1 , pp. 53-58
    • Wolf, B.1    Grier, R.E.2    McVoy S., Jr.3    Heard, G.S.4
  • 9
    • 0000537899 scopus 로고
    • The enzymatic degradation of soluble bound biotin
    • [9] Thoma RW, Peterson WH. The enzymatic degradation of soluble bound biotin. J Biol Chem 1954;210:569-579.
    • (1954) J Biol Chem , vol.210 , pp. 569-579
    • Thoma, R.W.1    Peterson, W.H.2
  • 10
    • 0011865934 scopus 로고
    • Biocytinase, an enzyme concerned with hydrolytic cleavage of biocytin
    • [10] Wright LD, Driscoll CA, Boger WP. Biocytinase, an enzyme concerned with hydrolytic cleavage of biocytin. Proc Soc Exp Biol Med 1954;86:335-337.
    • (1954) Proc Soc Exp Biol Med , vol.86 , pp. 335-337
    • Wright, L.D.1    Driscoll, C.A.2    Boger, W.P.3
  • 11
    • 0022348264 scopus 로고
    • Distribution and degradation of biotin-containing carboxylases in human cell lines
    • [11] Chandler CS, Ballard FJ. Distribution and degradation of biotin-containing carboxylases in human cell lines. Biochem J 1985;232:385-393.
    • (1985) Biochem J , vol.232 , pp. 385-393
    • Chandler, C.S.1    Ballard, F.J.2
  • 12
    • 0021111993 scopus 로고
    • Regulation of the synthesis and degradation of pyruvate carboxylase in 3T3-L1 cells
    • [12] Freytag SO, Utter MF. Regulation of the synthesis and degradation of pyruvate carboxylase in 3T3-L1 cells. J Biol Chem 1983;258:6307-6312.
    • (1983) J Biol Chem , vol.258 , pp. 6307-6312
    • Freytag, S.O.1    Utter, M.F.2
  • 13
    • 0013823849 scopus 로고
    • Animal biotinidase
    • [13] Pispa J. Animal biotinidase. Ann Med Exp Biol Fenn 1965;43 (Suppl 5):1-39.
    • (1965) Ann Med Exp Biol Fenn , vol.43 , Issue.SUPPL. 5 , pp. 1-39
    • Pispa, J.1
  • 14
    • 0000178171 scopus 로고
    • Reinigung und eigenschaften der biotinidase aus schweinenieren und Lactobacillus casei
    • [14] Knappe J, Brommer W, Biederbick K. Reinigung und Eigenschaften der Biotinidase aus Schweinenieren und Lactobacillus casei. Biochem Z 1963;228:599-613.
    • (1963) Biochem Z , vol.228 , pp. 599-613
    • Knappe, J.1    Brommer, W.2    Biederbick, K.3
  • 15
    • 0023220954 scopus 로고
    • Immunological comparison of biotinidase in serum from normal and biotinidase-deficient individuals
    • [15] Wolf B, Miller JB, Hymes J, Secor McVoy J, Ishikana Y, Shapira E. Immunological comparison of biotinidase in serum from normal and biotinidase-deficient individuals. Clin Chim Acta 1987;164:27-32.
    • (1987) Clin Chim Acta , vol.164 , pp. 27-32
    • Wolf, B.1    Miller, J.B.2    Hymes, J.3    McVoy J, S.4    Ishikana, Y.5    Shapira, E.6
  • 16
    • 0021875453 scopus 로고
    • Purification of biotinidase from human plasma and its activity on biotinyl peptides
    • [16] Craft DV, Goss NH, Chandramouli N, Wood HG. Purification of biotinidase from human plasma and its activity on biotinyl peptides. Biochem 1985;24:2471-2476.
    • (1985) Biochem , vol.24 , pp. 2471-2476
    • Craft, D.V.1    Goss, N.H.2    Chandramouli, N.3    Wood, H.G.4
  • 17
    • 0023000875 scopus 로고
    • Purification and characterization of human serum biotinidase
    • [17] Chauhan J, Dakshinamurti J. Purification and characterization of human serum biotinidase. J Biol Chem 1986;261:4268-4274.
    • (1986) J Biol Chem , vol.261 , pp. 4268-4274
    • Chauhan, J.1    Dakshinamurti, J.2
  • 18
    • 0028216529 scopus 로고
    • Human serum biotinidase: cDNA cloning, sequence and characterization
    • [18] Cole H, Reynolds TR, Buck GB et al. Human serum biotinidase: cDNA cloning, sequence and characterization. J Biol Chem 1994;269:6566-6579.
    • (1994) J Biol Chem , vol.269 , pp. 6566-6579
    • Cole, H.1    Reynolds, T.R.2    Buck, G.B.3
  • 19
    • 0024793562 scopus 로고
    • Comparative study of human milk and serum biotinidase
    • [19] Oizumi J, Hayakawa K, Hosoya M. Comparative study of human milk and serum biotinidase. Biochimie 1989;71:1163-1169.
    • (1989) Biochimie , vol.71 , pp. 1163-1169
    • Oizumi, J.1    Hayakawa, K.2    Hosoya, M.3
  • 20
    • 0026033846 scopus 로고
    • Isoforms of human serum biotinidase
    • [20] Hart PS, Hymes J, Wolf B. Isoforms of human serum biotinidase. Clin Chim Acta 1991;197:257-264.
    • (1991) Clin Chim Acta , vol.197 , pp. 257-264
    • Hart, P.S.1    Hymes, J.2    Wolf, B.3
  • 21
    • 0029114718 scopus 로고
    • Mutational 'hotspot' in the human biotinidase gene as a cause of biotinidase deficiency
    • [21] Pomponio RJ, Reynolds TR, Cole H, Buck GA, Wolf B. Mutational 'hotspot' in the human biotinidase gene as a cause of biotinidase deficiency. Nat Genet 1995;11:96-98.
    • (1995) Nat Genet , vol.11 , pp. 96-98
    • Pomponio, R.J.1    Reynolds, T.R.2    Cole, H.3    Buck, G.A.4    Wolf, B.5
  • 22
    • 0021695335 scopus 로고
    • Detection of biocytin in urine of children with congenital biotinidase deficiency
    • [22] Bonjour JP, Bausch J, Suormala T, Baumgartner ER. Detection of biocytin in urine of children with congenital biotinidase deficiency. Int J Vitam Nutr Res 1984;54:223-229.
    • (1984) Int J Vitam Nutr Res , vol.54 , pp. 223-229
    • Bonjour, J.P.1    Bausch, J.2    Suormala, T.3    Baumgartner, E.R.4
  • 23
    • 0023724757 scopus 로고
    • The role of human serum biotinidase as biotin-binding protein
    • [23] Chauhan J, Dakshinamurti K. The role of human serum biotinidase as biotin-binding protein. Biochem J 1988;256:265-270.
    • (1988) Biochem J , vol.256 , pp. 265-270
    • Chauhan, J.1    Dakshinamurti, K.2
  • 24
    • 0025266372 scopus 로고
    • Studies of the reversible binding of biotin to human plasma
    • [24] Mock DM, Lankford G. Studies of the reversible binding of biotin to human plasma. J Nutr 1990;120:375-381.
    • (1990) J Nutr , vol.120 , pp. 375-381
    • Mock, D.M.1    Lankford, G.2
  • 25
    • 0028796669 scopus 로고
    • Biotinylation of biotinidase following incubation with biocytin
    • [25] Hymes J, Fleischhauer K, Wolf B. Biotinylation of biotinidase following incubation with biocytin. Clin Chim Acta 1995;233:39-45.
    • (1995) Clin Chim Acta , vol.233 , pp. 39-45
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 26
    • 0023944005 scopus 로고
    • Human serum biotinidase is a thiol-type enzyme
    • [26] Hayakawa K, Oizumi J. Human serum biotinidase is a thiol-type enzyme. J Biochem 1988;103:773-777.
    • (1988) J Biochem , vol.103 , pp. 773-777
    • Hayakawa, K.1    Oizumi, J.2
  • 27
    • 0023132456 scopus 로고
    • Isolation of a biotin receptor from hepatic plasma membranes
    • [27] Vesely DL, Kemp SF, Elders MJ. Isolation of a biotin receptor from hepatic plasma membranes. Biochem Biophys Res Comm 1987;143:913-916.
    • (1987) Biochem Biophys Res Comm , vol.143 , pp. 913-916
    • Vesely, D.L.1    Kemp, S.F.2    Elders, M.J.3
  • 28
    • 0028858269 scopus 로고
    • Biotinylation of histones by human serum biotinidase: Assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency
    • [28] Hymes J, Fleischhauer K, Wolf B. Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency. Biochem Mol Med 1995;56:76-83.
    • (1995) Biochem Mol Med , vol.56 , pp. 76-83
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 29
    • 0027525914 scopus 로고
    • Biotin-containing intranuclear inclusions in endometrial glands during gestation and puerperium
    • [29] Yokoyama S, Kashima K, Inoue S, Daa T, Nakayama I, Moriuchi A. Biotin-containing intranuclear inclusions in endometrial glands during gestation and puerperium. Am J Clin Pathol 1993;99:13-17.
    • (1993) Am J Clin Pathol , vol.99 , pp. 13-17
    • Yokoyama, S.1    Kashima, K.2    Inoue, S.3    Daa, T.4    Nakayama, I.5    Moriuchi, A.6
  • 30
    • 0020576509 scopus 로고
    • Optically clear nuclei: Alteration of endometrial epithelium in the presence of trophoblast
    • [30] Mazur MT, Hendrickson VR, Kempson RL. Optically clear nuclei: alteration of endometrial epithelium in the presence of trophoblast. Am J Surg Pathol 1993;7:415-423.
    • (1993) Am J Surg Pathol , vol.7 , pp. 415-423
    • Mazur, M.T.1    Hendrickson, V.R.2    Kempson, R.L.3
  • 31
    • 0001196361 scopus 로고
    • Immunohistochemical and electron microscopic study of the intranuclear inclusion bodies containing biotin in the ovarian endometroid carcinoma
    • [31] Tsujimoto M, Noguchi M, Taki I. Immunohistochemical and electron microscopic study of the intranuclear inclusion bodies containing biotin in the ovarian endometroid carcinoma. J Clin Electron Microsc 1991;24:783-784.
    • (1991) J Clin Electron Microsc , vol.24 , pp. 783-784
    • Tsujimoto, M.1    Noguchi, M.2    Taki, I.3
  • 32
    • 0026486397 scopus 로고
    • Peculiar nuclear clearing composed of microfilaments in papillary carcinoma of the thyroid
    • [32] Yamashita T, Hosods Y, Kameyama K, Aiba M, Ito K, Fujimoto Y. Peculiar nuclear clearing composed of microfilaments in papillary carcinoma of the thyroid. Cancer 1992;70:2923-2928.
    • (1992) Cancer , vol.70 , pp. 2923-2928
    • Yamashita, T.1    Hosods, Y.2    Kameyama, K.3    Aiba, M.4    Ito, K.5    Fujimoto, Y.6
  • 33
    • 0028221273 scopus 로고
    • Pulmonary endodermal tumor resembling fetal lung: The optically clear nucleus is rich in biotin
    • [33] Nakatani Y, Kitamura H, Inayama Y, Ogawa N. Pulmonary endodermal tumor resembling fetal lung: the optically clear nucleus is rich in biotin. Am J Surg Pathol 1994; 18:637-642.
    • (1994) Am J Surg Pathol , vol.18 , pp. 637-642
    • Nakatani, Y.1    Kitamura, H.2    Inayama, Y.3    Ogawa, N.4
  • 34
    • 0017209274 scopus 로고
    • RNA, DNA, histones and interactions between histone proteins and DNA in the liver of biotin-deficient rats
    • [34] Petrelli F, Marsili G, Moretti P. RNA, DNA, histones and interactions between histone proteins and DNA in the liver of biotin-deficient rats. Biochem Exp Biol 1976;12:461-465.
    • (1976) Biochem Exp Biol , vol.12 , pp. 461-465
    • Petrelli, F.1    Marsili, G.2    Moretti, P.3
  • 35
    • 0018270692 scopus 로고
    • Effect of biotin on phosphorylation, acetylation, methylation of rat liver histones
    • [35] Petrelli F, Coderoni S, Moretti P, Paparelli M. Effect of biotin on phosphorylation, acetylation, methylation of rat liver histones. Mol Biol Rep 1978;4:87-92.
    • (1978) Mol Biol Rep , vol.4 , pp. 87-92
    • Petrelli, F.1    Coderoni, S.2    Moretti, P.3    Paparelli, M.4
  • 36
    • 0022453208 scopus 로고
    • Multiple biotin-containing protein in 3T3-L1 cells
    • [36] Chandler CS, Ballard FJ. Multiple biotin-containing protein in 3T3-L1 cells. Biochem J 1986;237:123-130.
    • (1986) Biochem J , vol.237 , pp. 123-130
    • Chandler, C.S.1    Ballard, F.J.2
  • 37
    • 0000100744 scopus 로고
    • Tissue and intracellular distribution of biotin-C1400H in rats and chicks
    • [37] Dakshinamurti K, Mistry SP. Tissue and intracellular distribution of biotin-C1400H in rats and chicks. J Biol Chem 1963;238:294-334.
    • (1963) J Biol Chem , vol.238 , pp. 294-334
    • Dakshinamurti, K.1    Mistry, S.P.2
  • 38
    • 0028327162 scopus 로고
    • Develpmental patterns of free and protein-bound biotin during maturation and germination of seeds of pisum sativum: Characterization of a novel seed-specific biotinylation protein
    • [38] Duval M, Job C, Alban C, Douce R, Job D. Develpmental patterns of free and protein-bound biotin during maturation and germination of seeds of pisum sativum: characterization of a novel seed-specific biotinylation protein. Biochem J 1994;299:141-150.
    • (1994) Biochem J , vol.299 , pp. 141-150
    • Duval, M.1    Job, C.2    Alban, C.3    Douce, R.4    Job, D.5
  • 39
    • 0022259865 scopus 로고
    • Preparations of homeostatic thymus hormone consist predominantly of histones 2A and 2B and suggest additional histone function
    • [39] Reichhart R, Zeppezauer M, Jornvall H. Preparations of homeostatic thymus hormone consist predominantly of histones 2A and 2B and suggest additional histone function. Proc Natl Acad Sci USA 1985;82:4871-4875.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4871-4875
    • Reichhart, R.1    Zeppezauer, M.2    Jornvall, H.3
  • 40
    • 0026552958 scopus 로고
    • Hisotne H4-related osteogenic growth peptide (OGP): A novel circulating stimulator of osteoblastic activity
    • [40] Bab I, Gazil D, Chorev RE, Muhirad A, Shteyer A, Greenberg Z. Hisotne H4-related osteogenic growth peptide (OGP): a novel circulating stimulator of osteoblastic activity. EMBO J 1992;11:1867-1873.
    • (1992) EMBO J , vol.11 , pp. 1867-1873
    • Bab, I.1    Gazil, D.2    Chorev, R.E.3    Muhirad, A.4    Shteyer, A.5    Greenberg, Z.6
  • 43
    • 0027504277 scopus 로고
    • Histone H4 stimulates glucose transport activity in rat skeletal muscle
    • [43] Louters LL, Henrikson EJ, Tipton CM. Histone H4 stimulates glucose transport activity in rat skeletal muscle. Biochem J 1993;295:549-553.
    • (1993) Biochem J , vol.295 , pp. 549-553
    • Louters, L.L.1    Henrikson, E.J.2    Tipton, C.M.3
  • 45
    • 0028945393 scopus 로고
    • Interaction of the C-terminal acidic domain of the insulin receptor with histone modulates the receptor kinase activity
    • [45] Baron V, Kaliman P, Alengrin F, Van Obberghen E. Interaction of the C-terminal acidic domain of the insulin receptor with histone modulates the receptor kinase activity. Eur J Biochem 1995;229:27-37.
    • (1995) Eur J Biochem , vol.229 , pp. 27-37
    • Baron, V.1    Kaliman, P.2    Alengrin, F.3    Van Obberghen, E.4
  • 46
    • 0021223572 scopus 로고
    • Effects of biotin upon the intracellular level of cGMP and the activity of glucokinase in cultured rat hepatocytes
    • [46] Spence JT, Koudelka AP. Effects of biotin upon the intracellular level of cGMP and the activity of glucokinase in cultured rat hepatocytes. J Biol Chem 1984;259:6393-6396.
    • (1984) J Biol Chem , vol.259 , pp. 6393-6396
    • Spence, J.T.1    Koudelka, A.P.2
  • 47
    • 0029002832 scopus 로고
    • Regulation of neuronal nitric oxide synthetase by histone, protamine, and myelin basic protein
    • [47] Hu J, Fridlund J, el-Fakanhany EE. Regulation of neuronal nitric oxide synthetase by histone, protamine, and myelin basic protein. Neurochem Res 1995;20:497-503.
    • (1995) Neurochem Res , vol.20 , pp. 497-503
    • Hu, J.1    Fridlund, J.2    El-Fakanhany, E.E.3
  • 48
    • 0023877407 scopus 로고
    • Biotin enrichment in oligodendrocytes in the rat brain
    • [48] LeVine SM, Macklin WB. Biotin enrichment in oligodendrocytes in the rat brain. Brain Res 1988;444:199-203.
    • (1988) Brain Res , vol.444 , pp. 199-203
    • LeVine, S.M.1    Macklin, W.B.2
  • 49
    • 0026684198 scopus 로고
    • Evidence that biocytin is taken up by axons
    • [49] Chevalier G, Deniau JM, Menetrey A. Evidence that biocytin is taken up by axons. Neurosci Lett 1992; 140:197-199.
    • (1992) Neurosci Lett , vol.140 , pp. 197-199
    • Chevalier, G.1    Deniau, J.M.2    Menetrey, A.3
  • 51
    • 0028344116 scopus 로고
    • Biotin staining in the giant fiber systems of the lobster
    • [51] Ma PK. Biotin staining in the giant fiber systems of the lobster. J Comp Neur 1994;341:567-579.
    • (1994) J Comp Neur , vol.341 , pp. 567-579
    • Ma, P.K.1
  • 52
    • 0021961541 scopus 로고
    • Neurologic symptoms of biotinidase deficiency: Possible explanation
    • [52] Suchy SF, McVoy S Jr, Wolf B. Neurologic symptoms of biotinidase deficiency: possible explanation. Neurology 1985;35:1510-1511.
    • (1985) Neurology , vol.35 , pp. 1510-1511
    • Suchy, S.F.1    McVoy S., Jr.2    Wolf, B.3
  • 53
    • 0022536656 scopus 로고
    • Biotinidase deficiency: Accumulation of lactate in the brain and response to physiologic doses of biotin
    • [53] Diamantopoulos N, Painter MJ, Wolf B, Heard GS, Roe C. Biotinidase deficiency: accumulation of lactate in the brain and response to physiologic doses of biotin. Neurology 1986;36:1107-1109.
    • (1986) Neurology , vol.36 , pp. 1107-1109
    • Diamantopoulos, N.1    Painter, M.J.2    Wolf, B.3    Heard, G.S.4    Roe, C.5
  • 54
    • 0020063419 scopus 로고
    • Brain pyruvate carboxylase and the pathophysiology of biotin-dependent diseases
    • [54] Sander JE, Packman S, Townsend JJ. Brain pyruvate carboxylase and the pathophysiology of biotin-dependent diseases. Neurology 1982;32:878-880.
    • (1982) Neurology , vol.32 , pp. 878-880
    • Sander, J.E.1    Packman, S.2    Townsend, J.J.3
  • 55
    • 0021592331 scopus 로고
    • Different organic acid patterns in urine and in cerebrospinal fluid in a patient with biotinidase deficiency
    • [55] Dirocco M, Superti-Furga A, Durand P, Cerone R, Romano C. Different organic acid patterns in urine and in cerebrospinal fluid in a patient with biotinidase deficiency. J Inherit Metab Dis 1984;2 (Suppl 7): 119-120.
    • (1984) J Inherit Metab Dis , vol.2 , Issue.SUPPL. 7 , pp. 119-120
    • Dirocco, M.1    Superti-Furga, A.2    Durand, P.3    Cerone, R.4    Romano, C.5
  • 56
    • 0023676157 scopus 로고
    • Biotin stores in rodent lungs: Localization to clara and type II alveolar cells
    • [56] Kuhn C. Biotin stores in rodent lungs: localization to clara and type II alveolar cells. Exp Lung Res 1988;14:527-536.
    • (1988) Exp Lung Res , vol.14 , pp. 527-536
    • Kuhn, C.1
  • 57
    • 0026686648 scopus 로고
    • Huamn herpes-virus 6 and endogenous biotin in salivary glands
    • [57] Green M, Sviland L, Taylor CE et al. Huamn herpes-virus 6 and endogenous biotin in salivary glands. J Clin Pathol 1992;45:788-790.
    • (1992) J Clin Pathol , vol.45 , pp. 788-790
    • Green, M.1    Sviland, L.2    Taylor, C.E.3
  • 58
    • 0019451604 scopus 로고
    • Suppression of endogenous avidin-binding activity in tissues and its relevance to biotin-avidin detection systems
    • [58] Wood GS, Warnke R. Suppression of endogenous avidin-binding activity in tissues and its relevance to biotin-avidin detection systems. J Histochem Cytochem 1981;29:1196-1204.
    • (1981) J Histochem Cytochem , vol.29 , pp. 1196-1204
    • Wood, G.S.1    Warnke, R.2
  • 59
    • 0021892967 scopus 로고
    • Stimulation of growth factor production in cultured cells by biotin
    • [59] Moskowitz M, Cheng DK. Stimulation of growth factor production in cultured cells by biotin. Ann NY Acad Sci 1985;447:212-221.
    • (1985) Ann NY Acad Sci , vol.447 , pp. 212-221
    • Moskowitz, M.1    Cheng, D.K.2
  • 60
    • 0025836220 scopus 로고
    • Transcriptional regulation of the glucokinase gene by biotin in starved rats
    • [60] Chauhan J, Dakshinamurti K. Transcriptional regulation of the glucokinase gene by biotin in starved rats. J Biol Chem 1991;266:10033-10038.
    • (1991) J Biol Chem , vol.266 , pp. 10033-10038
    • Chauhan, J.1    Dakshinamurti, K.2
  • 61
    • 0022518058 scopus 로고
    • Transfer of retinoic acid from its complex with cellular retinoic acid-binding protein to the nucleus
    • [61] Takase S, Ong DE, Chytil F. Transfer of retinoic acid from its complex with cellular retinoic acid-binding protein to the nucleus. Arch Biochem Biophys 1986;247:328-334.
    • (1986) Arch Biochem Biophys , vol.247 , pp. 328-334
    • Takase, S.1    Ong, D.E.2    Chytil, F.3
  • 62
    • 0029281195 scopus 로고
    • Retinoic acid and retinoic acid receptors in development
    • [62] Sucov HM, Evans RM. Retinoic acid and retinoic acid receptors in development. Mol Neurobiol 1995; 10:169-184.
    • (1995) Mol Neurobiol , vol.10 , pp. 169-184
    • Sucov, H.M.1    Evans, R.M.2
  • 63
    • 0028896171 scopus 로고
    • Differential effects of N-(4-hydoxyphenyl) retinamide and retinoic acid on neuroblastoma cells: Apoptoses versus differentiation
    • [63] Ponzoni M, Bocca P, Chiesa V et al. Differential effects of N-(4-hydoxyphenyl) retinamide and retinoic acid on neuroblastoma cells: apoptoses versus differentiation. Cancer Res 1995;55:853-861.
    • (1995) Cancer Res , vol.55 , pp. 853-861
    • Ponzoni, M.1    Bocca, P.2    Chiesa, V.3
  • 64
    • 0026564656 scopus 로고
    • Retinamides: Hydrolytic conversion of retinoylglycine to retinoic acid in pregnant mice contributes to teratogenicity
    • [64] Kochhar DM, Shealy YF, Penner JD, Jiang H. Retinamides: hydrolytic conversion of retinoylglycine to retinoic acid in pregnant mice contributes to teratogenicity. Teratol 1992;45:175-185.
    • (1992) Teratol , vol.45 , pp. 175-185
    • Kochhar, D.M.1    Shealy, Y.F.2    Penner, J.D.3    Jiang, H.4


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