메뉴 건너뛰기




Volumn 19, Issue 3, 1996, Pages 149-160

Insulin-degrading enzyme

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; INSULINASE; METALLOPROTEINASE;

EID: 0030002245     PISSN: 0147958X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (153)

References (56)
  • 1
    • 0022473263 scopus 로고
    • Purification and characterization of insulin-degrading enzyme from human erythrocytes
    • Shii K, Yokono K, Baba S et al: Purification and characterization of insulin-degrading enzyme from human erythrocytes. Diabetes 1986; 35: 675-683
    • (1986) Diabetes , vol.35 , pp. 675-683
    • Shii, K.1    Yokono, K.2    Baba, S.3
  • 2
    • 0026527618 scopus 로고
    • Affinity purification of insulin-degrading enzyme and its endogenous inhibitor from rat liver
    • Ogawa W, Shii K, Yonezawa K et al: Affinity purification of insulin-degrading enzyme and its endogenous inhibitor from rat liver. J Biol Chem 1992; 267: 1310-1316
    • (1992) J Biol Chem , vol.267 , pp. 1310-1316
    • Ogawa, W.1    Shii, K.2    Yonezawa, K.3
  • 3
    • 0024215473 scopus 로고
    • Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III
    • Affholter JA, Fried VA, Roth RA: Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science 1988; 242: 1415-1418
    • (1988) Science , vol.242 , pp. 1415-1418
    • Affholter, J.A.1    Fried, V.A.2    Roth, R.A.3
  • 4
    • 0025119656 scopus 로고
    • Insulin-degrading enzyme: Stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes
    • Affholter JA, Hsieh CL, Francke U et al: Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes. Mol Endocrinol 1990; 4: 1125-1135
    • (1990) Mol Endocrinol , vol.4 , pp. 1125-1135
    • Affholter, J.A.1    Hsieh, C.L.2    Francke, U.3
  • 5
    • 0023046298 scopus 로고
    • Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III
    • Finch PW, Wilson RE, Brown K et al: Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III. Nucleic Acids Res 1986; 14: 7695-7703
    • (1986) Nucleic Acids Res , vol.14 , pp. 7695-7703
    • Finch, P.W.1    Wilson, R.E.2    Brown, K.3
  • 6
    • 0026800773 scopus 로고
    • Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III
    • Ding L, Becker AB, Suzuki A et al: Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III. J Biol Chem 1992; 267: 2414-2420
    • (1992) J Biol Chem , vol.267 , pp. 2414-2420
    • Ding, L.1    Becker, A.B.2    Suzuki, A.3
  • 7
    • 0028024153 scopus 로고
    • Identification and isolation of a cytosolic proteolytic complex containing insulin degrading enzyme and the multicatalytic proteinase
    • Bennett RG, Hamel FG, Duckworth WC: Identification and isolation of a cytosolic proteolytic complex containing insulin degrading enzyme and the multicatalytic proteinase. Biochem Biophys Res Commun 1994; 202: 1047-1053
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 1047-1053
    • Bennett, R.G.1    Hamel, F.G.2    Duckworth, W.C.3
  • 8
    • 0027983795 scopus 로고
    • Androgen and glucocorticoid receptors interact with insulin degrading enzyme
    • Kupfer SR, Wilson EM, French FS: Androgen and glucocorticoid receptors interact with insulin degrading enzyme. J Biol Chem 1994; 269: 20622-20628
    • (1994) J Biol Chem , vol.269 , pp. 20622-20628
    • Kupfer, S.R.1    Wilson, E.M.2    French, F.S.3
  • 9
    • 0028040778 scopus 로고
    • Endosomal proteolysis of insulin by an acidic thiol metalloprotease unrelated to insulin-degrading enzyme
    • Authier F, Rachubinski RA, Posner BI et al: Endosomal proteolysis of insulin by an acidic thiol metalloprotease unrelated to insulin-degrading enzyme. J Biol Chem 1994; 269: 3010-3016
    • (1994) J Biol Chem , vol.269 , pp. 3010-3016
    • Authier, F.1    Rachubinski, R.A.2    Posner, B.I.3
  • 10
    • 0001918193 scopus 로고
    • Hepatic endosomes are a major physiological locus of insulin and glucagon degradation in vivo
    • Ciechanover A, Schwartz AL (eds): Wiley-Liss, New York
    • Authier F, Posner BI, Bergeron JJM: Hepatic endosomes are a major physiological locus of insulin and glucagon degradation in vivo. In Ciechanover A, Schwartz AL (eds): Cellular Proteolytic Systems, Wiley-Liss, New York, 1994: 89-113
    • (1994) Cellular Proteolytic Systems , pp. 89-113
    • Authier, F.1    Posner, B.I.2    Bergeron, J.J.M.3
  • 11
    • 0025191059 scopus 로고
    • Peroxisomal protein import is conserved between yeast, plants, insects and mammals
    • Gould SJ, Keller GA, Schneider M et al: Peroxisomal protein import is conserved between yeast, plants, insects and mammals. EMBO J 1990; 9: 85-90
    • (1990) EMBO J , vol.9 , pp. 85-90
    • Gould, S.J.1    Keller, G.A.2    Schneider, M.3
  • 12
    • 0029024878 scopus 로고
    • Degradation of the cleaved leader peptide of thiolase by a peroxisomal proteinase
    • Authier F, Bergeron JJM, Ou WJ et al: Degradation of the cleaved leader peptide of thiolase by a peroxisomal proteinase. Proc Natl Acad Sci USA 1995; 92: 3859-3863
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3859-3863
    • Authier, F.1    Bergeron, J.J.M.2    Ou, W.J.3
  • 13
    • 0027964969 scopus 로고
    • Inducible expression and cellular localization of insulin-degrading enzyme in a stably transfected cell line
    • Kuo WL, Gehm BD, Rosner MR et al: Inducible expression and cellular localization of insulin-degrading enzyme in a stably transfected cell line. J Biol Chem 1994; 269: 22599-22606
    • (1994) J Biol Chem , vol.269 , pp. 22599-22606
    • Kuo, W.L.1    Gehm, B.D.2    Rosner, M.R.3
  • 14
    • 0025160114 scopus 로고
    • Identification of residues in the insulin molecule important for binding to insulin-degrading enzyme
    • Affholter JA, Cascieri MA, Bayne ML et al: Identification of residues in the insulin molecule important for binding to insulin-degrading enzyme. Biochemistry 1990; 29: 7727-7733
    • (1990) Biochemistry , vol.29 , pp. 7727-7733
    • Affholter, J.A.1    Cascieri, M.A.2    Bayne, M.L.3
  • 15
    • 0024454036 scopus 로고
    • An evolutionarily conserved enzyme degrades transforming growth factor-alpha as well as insulin
    • Garcia JV, Gehm BD, Rosner MR: An evolutionarily conserved enzyme degrades transforming growth factor-alpha as well as insulin. J Cell Biol 1989; 109: 1301-1307
    • (1989) J Cell Biol , vol.109 , pp. 1301-1307
    • Garcia, J.V.1    Gehm, B.D.2    Rosner, M.R.3
  • 16
    • 0024525751 scopus 로고
    • An insulin epidermal growth factor-binding protein from Drosophila has insulin-degrading activity
    • Garcia JV, Stoppelli MP, Decker SJ et al: An insulin epidermal growth factor-binding protein from Drosophila has insulin-degrading activity. J Cell Biol 1989; 108: 177-182
    • (1989) J Cell Biol , vol.108 , pp. 177-182
    • Garcia, J.V.1    Stoppelli, M.P.2    Decker, S.J.3
  • 17
    • 0026471959 scopus 로고
    • Rat insulin-degrading enzyme: Cleavage pattern of the natriuretic peptide hormones ANP, BNP, and CNP revealed by HPLC and mass spectrometry
    • Muller D, Schulze C, Baumeister H et al: Rat insulin-degrading enzyme: cleavage pattern of the natriuretic peptide hormones ANP, BNP, and CNP revealed by HPLC and mass spectrometry. Biochemistry 1992; 31: 11138-11143
    • (1992) Biochemistry , vol.31 , pp. 11138-11143
    • Muller, D.1    Schulze, C.2    Baumeister, H.3
  • 18
    • 0028176821 scopus 로고
    • Alzheimer's ß-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • Kurochkin IV, Goto S: Alzheimer's ß-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett 1994; 345: 33-37
    • (1994) FEBS Lett , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 19
    • 0028095388 scopus 로고
    • Preparation and characterization of novel substrates of insulin protease (EC 3.4.99.45)
    • Werlen RC, Offord RE, Rose K: Preparation and characterization of novel substrates of insulin protease (EC 3.4.99.45). Biochem J 1994; 302: 907-911
    • (1994) Biochem J , vol.302 , pp. 907-911
    • Werlen, R.C.1    Offord, R.E.2    Rose, K.3
  • 20
    • 0025916307 scopus 로고
    • Purification of a protease in red blood cells that degrades oxidatively damaged haemoglobin
    • Fagan JM, Waxman L: Purification of a protease in red blood cells that degrades oxidatively damaged haemoglobin. Biochem J 1991; 277: 779-786
    • (1991) Biochem J , vol.277 , pp. 779-786
    • Fagan, J.M.1    Waxman, L.2
  • 21
    • 0025987157 scopus 로고
    • Atrial natriuretic peptide (ANP) is a high-affinity substrate for rat insulin-degrading enzyme
    • Muller D, Baumeister H, Buck F et al: Atrial natriuretic peptide (ANP) is a high-affinity substrate for rat insulin-degrading enzyme. Eur J Biochem 1991; 202: 285-292
    • (1991) Eur J Biochem , vol.202 , pp. 285-292
    • Muller, D.1    Baumeister, H.2    Buck, F.3
  • 22
    • 0023906369 scopus 로고
    • Degradation products of insulin generated by hepatocytes and by insulin protease
    • Duck worth WC, Hamel FG, Peavy DE et al: Degradation products of insulin generated by hepatocytes and by insulin protease. J Biol Chem 1988; 263: 1826-1833
    • (1988) J Biol Chem , vol.263 , pp. 1826-1833
    • Duck Worth, W.C.1    Hamel, F.G.2    Peavy, D.E.3
  • 23
    • 0024212708 scopus 로고
    • Insulin proteinase liberates from glucagon a fragment known to have enhanced activity against Ca2+-Mg2+-dependent ATPase
    • Rose K, Savoy LA, Muir AV et al: Insulin proteinase liberates from glucagon a fragment known to have enhanced activity against Ca2+-Mg2+-dependent ATPase. Biochem J 1988; 256: 847-851
    • (1988) Biochem J , vol.256 , pp. 847-851
    • Rose, K.1    Savoy, L.A.2    Muir, A.V.3
  • 24
    • 0021894454 scopus 로고
    • Uptake of insulin and other ligands into receptor-rich endocytic components of target cells: The endosomal apparatus
    • Bergeron JJM, Cruz J, Khan MN et al: Uptake of insulin and other ligands into receptor-rich endocytic components of target cells: the endosomal apparatus. Annu Rev Physiol 1985; 47: 383-403
    • (1985) Annu Rev Physiol , vol.47 , pp. 383-403
    • Bergeron, J.J.M.1    Cruz, J.2    Khan, M.N.3
  • 25
    • 0027333416 scopus 로고
    • Protein import into peroxisomes and biogenesis of the organelle
    • Subramani S: Protein import into peroxisomes and biogenesis of the organelle. Annu Rev Cell Biol 1993; 9: 445-478
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 445-478
    • Subramani, S.1
  • 26
    • 0015424741 scopus 로고
    • Degradation of insulin and proinsulin by various organ homogenates of rat
    • Kitabchi AE, Stentz FB: Degradation of insulin and proinsulin by various organ homogenates of rat. Diabetes 1912; 21: 1091-1101
    • (1912) Diabetes , vol.21 , pp. 1091-1101
    • Kitabchi, A.E.1    Stentz, F.B.2
  • 27
    • 0024990132 scopus 로고
    • Natural regulatory mechanisms of insulin degradation by insulin degrading enzyme
    • Akiyama H, Yokono K, Shii K et al: Natural regulatory mechanisms of insulin degradation by insulin degrading enzyme. Biochem Biophys Res Commun 1990; 170: 1325-1330
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 1325-1330
    • Akiyama, H.1    Yokono, K.2    Shii, K.3
  • 29
    • 0027410472 scopus 로고
    • The rat insulin-degrading enzyme: Molecular cloning and characterization of tissue-specific transcripts
    • Baumeister H, Muller D, Rehbein M et al: The rat insulin-degrading enzyme: molecular cloning and characterization of tissue-specific transcripts. FEBS Lett 1993; 317: 250-254
    • (1993) FEBS Lett , vol.317 , pp. 250-254
    • Baumeister, H.1    Muller, D.2    Rehbein, M.3
  • 30
    • 0027452730 scopus 로고
    • Insulin-degrading enzyme is differentially expressed and developmentally regulated in various rat tissues
    • Kuo WL, Montag AG, Rosner MR: Insulin-degrading enzyme is differentially expressed and developmentally regulated in various rat tissues. Endocrinology 1993; 132: 604-611
    • (1993) Endocrinology , vol.132 , pp. 604-611
    • Kuo, W.L.1    Montag, A.G.2    Rosner, M.R.3
  • 31
    • 0025080986 scopus 로고
    • Cloning and expression of the cDNA for a Drosophila insulin-degrading enzyme
    • Kuo WL, Gehm BD, Rosner MR: Cloning and expression of the cDNA for a Drosophila insulin-degrading enzyme. Mol Endocrinol 1990; 4: 1580-1591
    • (1990) Mol Endocrinol , vol.4 , pp. 1580-1591
    • Kuo, W.L.1    Gehm, B.D.2    Rosner, M.R.3
  • 32
    • 0028216847 scopus 로고
    • Cellular distribution of insulin-degrading enzyme gene expression
    • Bondy CA, Zhou J, Chin E et al: Cellular distribution of insulin-degrading enzyme gene expression. J Clin Invest 1994; 93: 966-973
    • (1994) J Clin Invest , vol.93 , pp. 966-973
    • Bondy, C.A.1    Zhou, J.2    Chin, E.3
  • 34
    • 0023749140 scopus 로고
    • Developmental regulation of an insulin-degrading enzyme from Drosophila melanogaster
    • Stoppelli MP, Garcia JV, Decker SJ: Developmental regulation of an insulin-degrading enzyme from Drosophila melanogaster. Proc Natl Acad Sci USA 1988; 85: 3469-3473
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3469-3473
    • Stoppelli, M.P.1    Garcia, J.V.2    Decker, S.J.3
  • 35
    • 0024062933 scopus 로고
    • Insulin degradation: Mechanisms, products, and significance
    • Duckworth WC: Insulin degradation: mechanisms, products, and significance. Endocr Rev 1988; 9: 319-345
    • (1988) Endocr Rev , vol.9 , pp. 319-345
    • Duckworth, W.C.1
  • 36
    • 0021248620 scopus 로고
    • Insulin degrading enzyme activity and insulin binding of erythrocytes in normal subjects and Type 2 (non-insulin-dependent) diabetic patients
    • Standl E, Kolb HJ: Insulin degrading enzyme activity and insulin binding of erythrocytes in normal subjects and Type 2 (non-insulin-dependent) diabetic patients. Diahetologia 1984; 27: 17-22
    • (1984) Diahetologia , vol.27 , pp. 17-22
    • Standl, E.1    Kolb, H.J.2
  • 37
    • 0026516458 scopus 로고
    • An unusual active site identified in a family of zinc metalloendopeptidases
    • Becker AB, Roth RA: An unusual active site identified in a family of zinc metalloendopeptidases. Proc Natl Acad Sci USA 1992; 89: 3835-3839
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3835-3839
    • Becker, A.B.1    Roth, R.A.2
  • 38
    • 0024008659 scopus 로고
    • MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease
    • Witte C, Jensen RE, Yaffe MP et al: MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease. EMBO J 1988; 7: 1439-1447
    • (1988) EMBO J , vol.7 , pp. 1439-1447
    • Witte, C.1    Jensen, R.E.2    Yaffe, M.P.3
  • 39
    • 0024517454 scopus 로고
    • A family of mitochondrial proteins involved in bioenergetics and biogenesis
    • Schulte U, Arretz M, Schneider H et al: A family of mitochondrial proteins involved in bioenergetics and biogenesis. Nature 1989; 339: 147-149
    • (1989) Nature , vol.339 , pp. 147-149
    • Schulte, U.1    Arretz, M.2    Schneider, H.3
  • 40
    • 0026549104 scopus 로고
    • Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon
    • Meulenberg JJM, Sellink E, Riegman NH et al: Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon. Mol Gen Genet 1992; 232: 284-294
    • (1992) Mol Gen Genet , vol.232 , pp. 284-294
    • Meulenberg, J.J.M.1    Sellink, E.2    Riegman, N.H.3
  • 41
    • 0027309277 scopus 로고
    • Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase
    • Chen NY, Jiang SQ, Klein DA et al: Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J Biol Chem 1993; 268: 9448-9465
    • (1993) J Biol Chem , vol.268 , pp. 9448-9465
    • Chen, N.Y.1    Jiang, S.Q.2    Klein, D.A.3
  • 42
    • 0028173765 scopus 로고
    • N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes
    • Pierotti AR, Prat A, Chesneau V et al: N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes. Proc Natl Acad Sci USA 1994; 91: 6078-6082
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6078-6082
    • Pierotti, A.R.1    Prat, A.2    Chesneau, V.3
  • 43
    • 0027263747 scopus 로고
    • Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes
    • Backer AB, Roth RA: Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes. Biochem J 1993; 292: 137-142
    • (1993) Biochem J , vol.292 , pp. 137-142
    • Backer, A.B.1    Roth, R.A.2
  • 44
    • 0027471458 scopus 로고
    • Mutations in a zinc-binding domain of human insulin-degrading enzyme eliminate catalytic activity but not insulin binding
    • Gehm BD, Kuo WL, Perlman RK et al: Mutations in a zinc-binding domain of human insulin-degrading enzyme eliminate catalytic activity but not insulin binding. J Biol Chem 1993; 268: 7943-7948
    • (1993) J Biol Chem , vol.268 , pp. 7943-7948
    • Gehm, B.D.1    Kuo, W.L.2    Perlman, R.K.3
  • 45
    • 0027454093 scopus 로고
    • Functional analysis of conserved residues in the active site of insulin-degrading enzyme
    • Perlman RK, Gehm BD, Kuo WL et al: Functional analysis of conserved residues in the active site of insulin-degrading enzyme. J Biol Chem 1993; 268: 21538-21544
    • (1993) J Biol Chem , vol.268 , pp. 21538-21544
    • Perlman, R.K.1    Gehm, B.D.2    Kuo, W.L.3
  • 46
    • 0028587344 scopus 로고
    • Identification of zinc ligands of the insulin-degrading enzyme
    • Perlman RK, Rosner MR: Identification of zinc ligands of the insulin-degrading enzyme. J Biol Chem 1994; 269: 33140-33145
    • (1994) J Biol Chem , vol.269 , pp. 33140-33145
    • Perlman, R.K.1    Rosner, M.R.2
  • 47
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings ND, Barrett AJ: Evolutionary families of peptidases. Biochem J 1993; 290: 205-218
    • (1993) Biochem J , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 48
    • 0029066902 scopus 로고
    • 1 complex evolutionary relics of a processing protease?
    • 1 complex evolutionary relics of a processing protease? TIBS 1995; 20: 171-175
    • (1995) TIBS , vol.20 , pp. 171-175
    • Braun, H.P.1    Schmitz, U.K.2
  • 49
    • 0026985165 scopus 로고
    • Characterization and partial purification of an insulinase from Neurospora crassa
    • Kole HK, Smith DR, Lenard J: Characterization and partial purification of an insulinase from Neurospora crassa. Arch Biochem Biophys 1992; 297: 199-204
    • (1992) Arch Biochem Biophys , vol.297 , pp. 199-204
    • Kole, H.K.1    Smith, D.R.2    Lenard, J.3
  • 50
    • 0026049145 scopus 로고
    • Regulation of insulin degradation: Expression of an evolutionarily conserved insulin-degrading enzyme increases degradation via an intracellular pathway
    • Kuo WL, Gehm BD, Rosner MR: Regulation of insulin degradation: expression of an evolutionarily conserved insulin-degrading enzyme increases degradation via an intracellular pathway. Mol Endocrinol 1991; 5: 1467-1476
    • (1991) Mol Endocrinol , vol.5 , pp. 1467-1476
    • Kuo, W.L.1    Gehm, B.D.2    Rosner, M.R.3
  • 51
    • 0022445076 scopus 로고
    • Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease
    • Shii K, Roth RA: Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease. Proc Natl Acad Sci USA 1986; 83: 4147-4151
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4147-4151
    • Shii, K.1    Roth, R.A.2
  • 52
    • 8944256251 scopus 로고
    • A study of insulin metabolism in an insulin tolerant strain of mice
    • Beyer RE: A study of insulin metabolism in an insulin tolerant strain of mice. Acta Endocrinol 1955; 19: 309-332
    • (1955) Acta Endocrinol , vol.19 , pp. 309-332
    • Beyer, R.E.1
  • 53
    • 0024335103 scopus 로고
    • Metalloendoprotease inhibitors which block the differentiation of L6 myoblasts inhibit insulin degradation by the endogenous insulin-degrading enzyme
    • Kayalar C, Wong WT: Metalloendoprotease inhibitors which block the differentiation of L6 myoblasts inhibit insulin degradation by the endogenous insulin-degrading enzyme. J Biol Chem 1989; 264: 8928-8934
    • (1989) J Biol Chem , vol.264 , pp. 8928-8934
    • Kayalar, C.1    Wong, W.T.2
  • 54
    • 0023164755 scopus 로고
    • 125I]-insulin with a cytosolic insulin-degrading enzyme: Detection by covalent cross-linking and immunoprecipitation with a monoclonal antibody
    • 125I]-insulin with a cytosolic insulin-degrading enzyme: detection by covalent cross-linking and immunoprecipitation with a monoclonal antibody. Endocrinology 1987; 120: 829-831
    • (1987) Endocrinology , vol.120 , pp. 829-831
    • Hari, J.1    Shii, K.2    Roth, R.A.3
  • 55
    • 0028998783 scopus 로고
    • Proteolysis of glucagon within hepatic endosomes by membrane-associated cathepsins B and D
    • Authier F, Mort JS, Bell AW et al: Proteolysis of glucagon within hepatic endosomes by membrane-associated cathepsins B and D. J Biol Chem 1995; 270: 15798-15807
    • (1995) J Biol Chem , vol.270 , pp. 15798-15807
    • Authier, F.1    Mort, J.S.2    Bell, A.W.3
  • 56
    • 0025198488 scopus 로고
    • Differentiation of BC3H1 and primary skeletal muscle cells and the activity of their endogenous insulin-degrading enzyme are inhibited by the same metalloendoprotease inhibitors
    • Kayalar C, Wong WT, Hendrickson L: Differentiation of BC3H1 and primary skeletal muscle cells and the activity of their endogenous insulin-degrading enzyme are inhibited by the same metalloendoprotease inhibitors. J Cell Biochem 1990; 44: 137-151
    • (1990) J Cell Biochem , vol.44 , pp. 137-151
    • Kayalar, C.1    Wong, W.T.2    Hendrickson, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.