메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

An angiotensin I-converting enzyme mutation (Y465D) causes a dramatic increase in blood ACE via accelerated ACE shedding

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARTIC ACID; DIMER; DIPEPTIDYL CARBOXYPEPTIDASE; EPITOPE; MONOMER; MUTANT PROTEIN; SERINE; ANGIOTENSIN CONVERTING ENZYME SECRETASE; PROTEINASE;

EID: 80053589501     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025952     Document Type: Article
Times cited : (43)

References (65)
  • 1
    • 0024347759 scopus 로고
    • Angiotensin-converting enzyme: new concepts concerning its biological role
    • Ehlers MWR, Riordan JF, (1989) Angiotensin-converting enzyme: new concepts concerning its biological role. Biochemistry 8: 5311-5318.
    • (1989) Biochemistry , vol.8 , pp. 5311-5318
    • Ehlers, M.W.R.1    Riordan, J.F.2
  • 2
    • 0000401180 scopus 로고
    • Biochemistry of angiotensin I- converting enzyme
    • In: Robertson JIS, Nichols MG, editors, Glower Medical Publishing, New York
    • Skidgel RA, Erdos EG, (1993) Biochemistry of angiotensin I- converting enzyme. In: Robertson JIS, Nichols MG, editors. The Renin-Angiotensin System Glower Medical Publishing, New York pp. 10.1-10.10.
    • (1993) The Renin-Angiotensin System , pp. 1-10
    • Skidgel, R.A.1    Erdos, E.G.2
  • 3
    • 84944073735 scopus 로고    scopus 로고
    • Peptidyl-dipeptidase A/Angiotensin I-converting enzyme
    • In: Barret A, Rawlings N, Woessner J, editors, Elsevier Academic Press. New York
    • Corvol P, Eyries M, Soubrier F, (2004) Peptidyl-dipeptidase A/Angiotensin I-converting enzyme. In: Barret A, Rawlings N, Woessner J, editors. Handbook of Proteolytic Enzymes Elsevier Academic Press. New York pp. 332-349.
    • (2004) Handbook of Proteolytic Enzymes , pp. 332-349
    • Corvol, P.1    Eyries, M.2    Soubrier, F.3
  • 4
    • 20444439901 scopus 로고    scopus 로고
    • Six truisms concerning ACE and the renin-angiotensin system educed from the genetic analysis of mice
    • Bernstein KE, Xiao HD, Frenzel K, Li P, Shen XZ, et al. (2005) Six truisms concerning ACE and the renin-angiotensin system educed from the genetic analysis of mice. Circ Res 96: 1135-1144.
    • (2005) Circ Res , vol.96 , pp. 1135-1144
    • Bernstein, K.E.1    Xiao, H.D.2    Frenzel, K.3    Li, P.4    Shen, X.Z.5
  • 5
    • 0017287389 scopus 로고
    • Angiotensin-converting enztme: vascular endothelial localization
    • Caldwell PR, Seegal BC, Hsu KC, Das H, Soffer RL, (1976) Angiotensin-converting enztme: vascular endothelial localization. Science 191: 1050-1051.
    • (1976) Science , vol.191 , pp. 1050-1051
    • Caldwell, P.R.1    Seegal, B.C.2    Hsu, K.C.3    Das, H.4    Soffer, R.L.5
  • 6
    • 0017234204 scopus 로고
    • Localization of angiotensin converting enzyme (kininase II). II. Immunocytochemistry and immunofluorescence
    • Ryan US, Ryan JW, Whitaker C, Chiu A, (1976) Localization of angiotensin converting enzyme (kininase II). II. Immunocytochemistry and immunofluorescence. Tissue Cell 8: 124-145.
    • (1976) Tissue Cell , vol.8 , pp. 124-145
    • Ryan, U.S.1    Ryan, J.W.2    Whitaker, C.3    Chiu, A.4
  • 8
    • 0022464749 scopus 로고
    • Angiotensin I converting enzyme in human intestine and kidney. Ultrastructural immunohistochemical localization
    • Bruneval P, Hinglais N, Alhenc-Gelas F, Tricottet V, Corvol P, et al. (1986) Angiotensin I converting enzyme in human intestine and kidney. Ultrastructural immunohistochemical localization. Histochemistry 85: 73-80.
    • (1986) Histochemistry , vol.85 , pp. 73-80
    • Bruneval, P.1    Hinglais, N.2    Alhenc-Gelas, F.3    Tricottet, V.4    Corvol, P.5
  • 9
    • 0023094566 scopus 로고
    • Isolation of two differentially glycosylated forms of peptidyl-dipeptidase A (angiotensin-converting enzyme) from pig brain: a re-evaluation of their role in neuropeptide metabolism
    • Hooper NM, Turner AJ, (1987) Isolation of two differentially glycosylated forms of peptidyl-dipeptidase A (angiotensin-converting enzyme) from pig brain: a re-evaluation of their role in neuropeptide metabolism. Biochem J 241: 625-633.
    • (1987) Biochem J , vol.241 , pp. 625-633
    • Hooper, N.M.1    Turner, A.J.2
  • 10
    • 0027241828 scopus 로고
    • Gene expression and tissue localization of the two isoforms of angiotensin I-converting enzyme
    • Sibony M, Gasc JM, Soubrier F, Alhenc-Gelas F, Corvol P, (1993) Gene expression and tissue localization of the two isoforms of angiotensin I-converting enzyme. Hypertension 21: 827-835.
    • (1993) Hypertension , vol.21 , pp. 827-835
    • Sibony, M.1    Gasc, J.M.2    Soubrier, F.3    Alhenc-Gelas, F.4    Corvol, P.5
  • 11
    • 0001722753 scopus 로고    scopus 로고
    • Angiotensin I-Converting Enzyme (CD 143) on endothelial cells in normal and in pathological conditions
    • In: Kishimoto T, editors, Garland Publishing Inc. New York
    • Franke FE, Metzger R, Bohle R-M, Kerkman L, Alhenc-Gelas F, et al. (1997) Angiotensin I-Converting Enzyme (CD 143) on endothelial cells in normal and in pathological conditions. In: Kishimoto T, editors. Leucocyte Typing VI: White Cell Differentiation Antigens Garland Publishing Inc. New York pp. 749-751.
    • (1997) Leucocyte Typing VI: White Cell Differentiation Antigens , pp. 749-751
    • Franke, F.E.1    Metzger, R.2    Bohle, R.-M.3    Kerkman, L.4    Alhenc-Gelas, F.5
  • 13
    • 79651473319 scopus 로고    scopus 로고
    • Heterogeneous distribution of Angiotensin I-converting enzyme (CD143) in the human and rat vascular systems: vessels, organs and species specificity
    • Metzger R, Franke FF, Bohle R-M, Alhenc-Gelas F, Danilov SM, (2011) Heterogeneous distribution of Angiotensin I-converting enzyme (CD143) in the human and rat vascular systems: vessels, organs and species specificity. Microvasc Res 81: 206-215.
    • (2011) Microvasc Res , vol.81 , pp. 206-215
    • Metzger, R.1    Franke, F.F.2    Bohle, R.-M.3    Alhenc-Gelas, F.4    Danilov, S.M.5
  • 14
    • 0017943633 scopus 로고
    • Angiotensin-converting enzyme in macrophages and Freund's adjuvant granuloma
    • Silverstein E, Friedland J, Setton C, (1978) Angiotensin-converting enzyme in macrophages and Freund's adjuvant granuloma. Isr J Med Sci 14: 314-318.
    • (1978) Isr J Med Sci , vol.14 , pp. 314-318
    • Silverstein, E.1    Friedland, J.2    Setton, C.3
  • 15
    • 0027419508 scopus 로고
    • Angiotensin I-converting enzyme in human circulating mononuclear cells: genetic polymorphism of expression in T-lymphocytes
    • Costerousse O, Allegrini J, Lopez M, Alhenc-Gelas F, (1993) Angiotensin I-converting enzyme in human circulating mononuclear cells: genetic polymorphism of expression in T-lymphocytes. Biochem J 290: 33-40.
    • (1993) Biochem J , vol.290 , pp. 33-40
    • Costerousse, O.1    Allegrini, J.2    Lopez, M.3    Alhenc-Gelas, F.4
  • 16
    • 0344235131 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme (CD143) is abundantly expressed by dendritic cells and discriminates human monocytes-derived dendritic cells from acute myeloid leukemia-derived dendritic cells
    • Danilov SM, Sadovnikova E, Scharenbourg N, Balysnikova IV, Svinareva DA, et al. (2003) Angiotensin-converting enzyme (CD143) is abundantly expressed by dendritic cells and discriminates human monocytes-derived dendritic cells from acute myeloid leukemia-derived dendritic cells. Exp Hem 31: 1301-1309.
    • (2003) Exp Hem , vol.31 , pp. 1301-1309
    • Danilov, S.M.1    Sadovnikova, E.2    Scharenbourg, N.3    Balysnikova, I.V.4    Svinareva, D.A.5
  • 17
    • 0000110931 scopus 로고
    • Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning
    • Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, et al. (1988) Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci USA 85: 9386-9390.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9386-9390
    • Soubrier, F.1    Alhenc-Gelas, F.2    Hubert, C.3    Allegrini, J.4    John, M.5
  • 19
    • 0021021599 scopus 로고
    • Angiotensin-converting enzyme in cultured endothelial cells. Synthesis, degradation and transfer to culture medium
    • Ching SF, Hayes LW, Slakey LL, (1983) Angiotensin-converting enzyme in cultured endothelial cells. Synthesis, degradation and transfer to culture medium. Arteriosclerosis 3: 581-588.
    • (1983) Arteriosclerosis , vol.3 , pp. 581-588
    • Ching, S.F.1    Hayes, L.W.2    Slakey, L.L.3
  • 21
    • 0023431536 scopus 로고
    • Pig kidney angiotensin converting enzyme. Purification and characterization of amphipatic and hydrophilic forms of the enzyme establishes C-terminal anchorage to the plasma membrane
    • Hooper NM, Keen J, Pappin DJC, Turner AJ, (1987) Pig kidney angiotensin converting enzyme. Purification and characterization of amphipatic and hydrophilic forms of the enzyme establishes C-terminal anchorage to the plasma membrane. Biochem J 247: 85-93.
    • (1987) Biochem J , vol.247 , pp. 85-93
    • Hooper, N.M.1    Keen, J.2    Pappin, D.J.C.3    Turner, A.J.4
  • 22
    • 0026052933 scopus 로고
    • Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes
    • Wei L, Alhenc-Gelas F, Soubrier F, Michaud A, Corvol P, et al. (1991) Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes. J Biol Chem 266: 5540-5546.
    • (1991) J Biol Chem , vol.266 , pp. 5540-5546
    • Wei, L.1    Alhenc-Gelas, F.2    Soubrier, F.3    Michaud, A.4    Corvol, P.5
  • 23
    • 0034194191 scopus 로고    scopus 로고
    • Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites
    • Woodman ZL, Oppong SY, Cook S, Hooper NM, Schwager SL, et al. (2000) Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites. Biochem J 347: 711-718.
    • (2000) Biochem J , vol.347 , pp. 711-718
    • Woodman, Z.L.1    Oppong, S.Y.2    Cook, S.3    Hooper, N.M.4    Schwager, S.L.5
  • 24
    • 4444287211 scopus 로고    scopus 로고
    • Secretase-mediated cell surface shedding of the angiotensin-converting enzyme
    • Parkin ET, Turner AJ, Hooper NM, (2004) Secretase-mediated cell surface shedding of the angiotensin-converting enzyme. Protein Pept Lett 11: 423-432.
    • (2004) Protein Pept Lett , vol.11 , pp. 423-432
    • Parkin, E.T.1    Turner, A.J.2    Hooper, N.M.3
  • 25
    • 0025864720 scopus 로고
    • Distribution of plasma angiotensin I-converting enzyme levels in healthy men: Relationship to environmental and hormonal parameters
    • Alhenc-Gelas F, Richard J, Courbon D, Warnet JM, Corvol P, (1991) Distribution of plasma angiotensin I-converting enzyme levels in healthy men: Relationship to environmental and hormonal parameters. J Lab Clin Med 117: 33-39.
    • (1991) J Lab Clin Med , vol.117 , pp. 33-39
    • Alhenc-Gelas, F.1    Richard, J.2    Courbon, D.3    Warnet, J.M.4    Corvol, P.5
  • 26
    • 0016593854 scopus 로고
    • Elevation of serum angiotensin-converting enzyme level in sarcoidosis
    • Lieberman J, (1975) Elevation of serum angiotensin-converting enzyme level in sarcoidosis. Am J Med 59: 365-372.
    • (1975) Am J Med , vol.59 , pp. 365-372
    • Lieberman, J.1
  • 27
    • 0017080686 scopus 로고
    • Elevation of angiotensin-converting enzyme in Gaucher's disease
    • Lieberman J, Beutler E, (1976) Elevation of angiotensin-converting enzyme in Gaucher's disease. N Engl J Med 294: 1442-1444.
    • (1976) N Engl J Med , vol.294 , pp. 1442-1444
    • Lieberman, J.1    Beutler, E.2
  • 28
    • 0017103573 scopus 로고
    • Elevation of angiotensin-converting enzyme in granulomatous lymph nodes and serum in sarcoidosis: clinical and possible pathological significance
    • Silverstein E, Friedland J, Lyons HA, Gourin A, (1976) Elevation of angiotensin-converting enzyme in granulomatous lymph nodes and serum in sarcoidosis: clinical and possible pathological significance. Ann NY Acad Sci 278: 498-513.
    • (1976) Ann NY Acad Sci , vol.278 , pp. 498-513
    • Silverstein, E.1    Friedland, J.2    Lyons, H.A.3    Gourin, A.4
  • 29
    • 0021880414 scopus 로고
    • Serum angiotensin-converting enzyme in sarcoidosis: sensitivity and specificity in diagnosis: correlation with disease activity, duration, extra-thoracic involvement, radiographic type and therapy
    • Ainslie GM, Benatar SR, (1985) Serum angiotensin-converting enzyme in sarcoidosis: sensitivity and specificity in diagnosis: correlation with disease activity, duration, extra-thoracic involvement, radiographic type and therapy. Q J Med 55: 253-270.
    • (1985) Q J Med , vol.55 , pp. 253-270
    • Ainslie, G.M.1    Benatar, S.R.2
  • 30
    • 0024787736 scopus 로고
    • Enzymes in sarcoidosis: Angiotensin-converting enzyme (ACE)
    • Lieberman J, (1989) Enzymes in sarcoidosis: Angiotensin-converting enzyme (ACE). Clin Lab Med 9: 745-755.
    • (1989) Clin Lab Med , vol.9 , pp. 745-755
    • Lieberman, J.1
  • 31
    • 0025840320 scopus 로고
    • Angiotensin-converting enzyme: clinical applications and laboratory investigation n serum and other biological fluids
    • Beneteau-Burnat B, Baudin B, (1991) Angiotensin-converting enzyme: clinical applications and laboratory investigation n serum and other biological fluids. Crit Rev Clin Lab Sci 28: 337-356.
    • (1991) Crit Rev Clin Lab Sci , vol.28 , pp. 337-356
    • Beneteau-Burnat, B.1    Baudin, B.2
  • 32
    • 0035845629 scopus 로고    scopus 로고
    • Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease
    • Kramers C, Danilov SM, Deinum J, Balyasnikova IV, Scharenborg N, et al. (2001) Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease. Circulation 104: 1236-1240.
    • (2001) Circulation , vol.104 , pp. 1236-1240
    • Kramers, C.1    Danilov, S.M.2    Deinum, J.3    Balyasnikova, I.V.4    Scharenborg, N.5
  • 33
    • 0035937185 scopus 로고    scopus 로고
    • Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region
    • Eyries M, Michaud A, Deinum J, Aagrapart M, Chomillier J, et al. (2001) Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region. J Biol Chem 276: 5525-5532.
    • (2001) J Biol Chem , vol.276 , pp. 5525-5532
    • Eyries, M.1    Michaud, A.2    Deinum, J.3    Aagrapart, M.4    Chomillier, J.5
  • 34
    • 0347364659 scopus 로고    scopus 로고
    • Hereditary elevation of angiotensin-converting enzyme suggesting neurosarcoidosis
    • Linnebank M, Kesper K, Jeub M, Urbach H, Wullner U, et al. (2003) Hereditary elevation of angiotensin-converting enzyme suggesting neurosarcoidosis. Neurology 61: 1819-1820.
    • (2003) Neurology , vol.61 , pp. 1819-1820
    • Linnebank, M.1    Kesper, K.2    Jeub, M.3    Urbach, H.4    Wullner, U.5
  • 35
    • 33748525907 scopus 로고    scopus 로고
    • Hereditary hyper-ACE-emia due to the Pro1199Leu mutation of somatic ACE as a potential pitfall in diagnosis: a first family out of Europe
    • Semmler A, Stein RW, Caplan L, Danilov SM, Klockgether T, et al. (2006) Hereditary hyper-ACE-emia due to the Pro1199Leu mutation of somatic ACE as a potential pitfall in diagnosis: a first family out of Europe. Clin Chem Lab Med 44: 1088-1089.
    • (2006) Clin Chem Lab Med , vol.44 , pp. 1088-1089
    • Semmler, A.1    Stein, R.W.2    Caplan, L.3    Danilov, S.M.4    Klockgether, T.5
  • 36
    • 0037443847 scopus 로고    scopus 로고
    • Increased serum activity of angiotensin-converting enzyme (ACE): indication of sarcoidosis? A Bayesian approach
    • Kramers C, Deinum J, (2003) Increased serum activity of angiotensin-converting enzyme (ACE): indication of sarcoidosis? A Bayesian approach. Ned Tijdschr Geneeskd 147: 473-476.
    • (2003) Ned Tijdschr Geneeskd , vol.147 , pp. 473-476
    • Kramers, C.1    Deinum, J.2
  • 37
    • 77949494087 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACE
    • doi:101371/journal.pone.0008282
    • Nesterovitch AB, Hogarth K, Adarichev VA, Vinokour EI, Schwartz D, et al. (2009) Angiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACE. PLoS One 4 (12): e8282 doi:101371/journal.pone.0008282.
    • (2009) PLoS One , vol.4 , Issue.12
    • Nesterovitch, A.B.1    Hogarth, K.2    Adarichev, V.A.3    Vinokour, E.I.4    Schwartz, D.5
  • 38
    • 78149236201 scopus 로고    scopus 로고
    • The N domain of human angiotensin I-converting enzyme: the role of N-glycosylation and the crystal structure in complex with an N domain specific phosphinic inhibitor RXP407
    • Anthony KS, Corradi HR, Schwager SL, Redelinghuys P, Georgiadis D, et al. (2010) The N domain of human angiotensin I-converting enzyme: the role of N-glycosylation and the crystal structure in complex with an N domain specific phosphinic inhibitor RXP407. J Biol Chem 285: 35685-35693.
    • (2010) J Biol Chem , vol.285 , pp. 35685-35693
    • Anthony, K.S.1    Corradi, H.R.2    Schwager, S.L.3    Redelinghuys, P.4    Georgiadis, D.5
  • 39
    • 0038808679 scopus 로고    scopus 로고
    • Epitope-dependent blocking of the angiotensin-converting enzyme dimerization by monoclonal antibodies to the N-terminal domain of ACE: possible link of ACE dimerization and shedding from the cell surface
    • Kost OA, Balyasnikova IV, Chemodanova EE, Nikolskaya II, Albrecht RF, et al. (2003) Epitope-dependent blocking of the angiotensin-converting enzyme dimerization by monoclonal antibodies to the N-terminal domain of ACE: possible link of ACE dimerization and shedding from the cell surface. Biochemistry 42: 6965-6976.
    • (2003) Biochemistry , vol.42 , pp. 6965-6976
    • Kost, O.A.1    Balyasnikova, I.V.2    Chemodanova, E.E.3    Nikolskaya, I.I.4    Albrecht, R.F.5
  • 40
    • 17444364151 scopus 로고    scopus 로고
    • Localization of an N domain region of angiotensin-converting enzyme involved in the regulation of ectodomain shedding using monoclonal antibodies
    • Balyasnikova IV, Woodman ZL, Albrecht RFII, Natesh R, Acharya KR, et al. (2005) Localization of an N domain region of angiotensin-converting enzyme involved in the regulation of ectodomain shedding using monoclonal antibodies. J Proteome Res 4: 258-267.
    • (2005) J Proteome Res , vol.4 , pp. 258-267
    • Balyasnikova, I.V.1    Woodman, Z.L.2    Albrecht II, R.F.3    Natesh, R.4    Acharya, K.R.5
  • 41
    • 0032868334 scopus 로고    scopus 로고
    • Antibody-mediated lung endothelium targeting: In vitro model using a cell line expressing angiotensin-converting enzyme
    • Balyasnikova IV, Gavriljuk VD, McDonald TD, Berkowitz R, Miletich DJ, et al. (1999) Antibody-mediated lung endothelium targeting: In vitro model using a cell line expressing angiotensin-converting enzyme. Tumor Targeting 4: 70-83.
    • (1999) Tumor Targeting , vol.4 , pp. 70-83
    • Balyasnikova, I.V.1    Gavriljuk, V.D.2    McDonald, T.D.3    Berkowitz, R.4    Miletich, D.J.5
  • 42
    • 0028029798 scopus 로고
    • Structure-function analysis of angiotensin I-converting enzyme using monoclonal antibodies
    • Danilov S, Jaspard E, Churakova T, Towbin H, Savoie F, et al. (1994) Structure-function analysis of angiotensin I-converting enzyme using monoclonal antibodies. J Biol Chem 269: 26806-26814.
    • (1994) J Biol Chem , vol.269 , pp. 26806-26814
    • Danilov, S.1    Jaspard, E.2    Churakova, T.3    Towbin, H.4    Savoie, F.5
  • 43
    • 0014958429 scopus 로고
    • Studies on the angiotensin-converting enzyme with different substrates
    • Piquilloud Y, Reinharz A, Roth M, (1970) Studies on the angiotensin-converting enzyme with different substrates. Biochim Biophys Acta 206: 136-142.
    • (1970) Biochim Biophys Acta , vol.206 , pp. 136-142
    • Piquilloud, Y.1    Reinharz, A.2    Roth, M.3
  • 44
    • 0017194947 scopus 로고
    • A sensitive fluorometric assay for serum angiotensin-converting enzyme
    • Friedland J, Silverstein E, (1976) A sensitive fluorometric assay for serum angiotensin-converting enzyme. Am J Pathol 66: 416-424.
    • (1976) Am J Pathol , vol.66 , pp. 416-424
    • Friedland, J.1    Silverstein, E.2
  • 45
    • 0037216848 scopus 로고    scopus 로고
    • Monoclonal antibodies to denatured human ACE (CD 143), broad species specificity, reactivity on paraffin sections, and detection of subtle conformational changes in the C-terminal domain of ACE
    • Balyasnikova IV, Metzger R, Franke FE, Danilov SM, (2003) Monoclonal antibodies to denatured human ACE (CD 143), broad species specificity, reactivity on paraffin sections, and detection of subtle conformational changes in the C-terminal domain of ACE. Tissue Antigens 61: 49-62.
    • (2003) Tissue Antigens , vol.61 , pp. 49-62
    • Balyasnikova, I.V.1    Metzger, R.2    Franke, F.E.3    Danilov, S.M.4
  • 46
    • 14844282208 scopus 로고    scopus 로고
    • Monoclonal antibodies 1B3 and 5C8 as probes for monitoring the nativity of C-terminal end of soluble angiotensin-converting enzyme (ACE)
    • Balyasnikova IV, Sun Z-L, Berestetskaya YV, Albrecht RAII, Sturrock ED, et al. (2005) Monoclonal antibodies 1B3 and 5C8 as probes for monitoring the nativity of C-terminal end of soluble angiotensin-converting enzyme (ACE). Hybridoma 24: 14-26.
    • (2005) Hybridoma , vol.24 , pp. 14-26
    • Balyasnikova, I.V.1    Sun, Z.-L.2    Berestetskaya, Y.V.3    Albrecht II, R.A.4    Sturrock, E.D.5
  • 48
    • 0346195665 scopus 로고    scopus 로고
    • Crystal structure of the human angiotensin-converting enzyme-lisinopril complex
    • Natesh R, Schwager SL, Sturrock ED, Acharya KR, (2003) Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421: 551-554.
    • (2003) Nature , vol.421 , pp. 551-554
    • Natesh, R.1    Schwager, S.L.2    Sturrock, E.D.3    Acharya, K.R.4
  • 49
    • 77954367836 scopus 로고    scopus 로고
    • Porcine pulmonary angiotensin I-converting enzyme- Biochemical characterization and spatial arrangement of the N-and C-domains by three-dimensional electron microscopic reconstruction
    • Chen H-L, Lunsdorf H, Hecht H-J, Tsai H, (2010) Porcine pulmonary angiotensin I-converting enzyme- Biochemical characterization and spatial arrangement of the N-and C-domains by three-dimensional electron microscopic reconstruction. Micron 41: 674-685.
    • (2010) Micron , vol.41 , pp. 674-685
    • Chen, H.-L.1    Lunsdorf, H.2    Hecht, H.-J.3    Tsai, H.4
  • 51
    • 33645920640 scopus 로고    scopus 로고
    • Inhibitory antibodies to human angiotensin-converting enzyme: fine epitope mapping and mechanism of action
    • Skirgello OE, Balyasnikova IV, Binevski PV, Sun Z-L, Baskin II, et al. (2006) Inhibitory antibodies to human angiotensin-converting enzyme: fine epitope mapping and mechanism of action. Biochemistry 45: 4831-4847.
    • (2006) Biochemistry , vol.45 , pp. 4831-4847
    • Skirgello, O.E.1    Balyasnikova, I.V.2    Binevski, P.V.3    Sun, Z.-L.4    Baskin, I.I.5
  • 52
    • 34248136986 scopus 로고    scopus 로고
    • Monoclonal antibodies 1G12 and 6A12 to the N-domain of human angiotensin-converting enzyme: fine epitope mapping and antibody-based method for revelation and quantification of ACE inhibitors in the human blood
    • Balyasnikova IV, Skirgello OE, Binevski PV, Nesterovitch AB, Albrecht RFII, et al. (2007) Monoclonal antibodies 1G12 and 6A12 to the N-domain of human angiotensin-converting enzyme: fine epitope mapping and antibody-based method for revelation and quantification of ACE inhibitors in the human blood. J Proteome Res 6: 1580-1594.
    • (2007) J Proteome Res , vol.6 , pp. 1580-1594
    • Balyasnikova, I.V.1    Skirgello, O.E.2    Binevski, P.V.3    Nesterovitch, A.B.4    Albrecht II, R.F.5
  • 53
    • 34547728057 scopus 로고    scopus 로고
    • Fine epitope mapping of mAb 5F1 reveals anticatalytic activity toward the N domain of human angiotensin-converting enzyme
    • Danilov SM, Watermeyer JM, Balyasnikova IB, Gordon K, Kugaevskaya EV, et al. (2007) Fine epitope mapping of mAb 5F1 reveals anticatalytic activity toward the N domain of human angiotensin-converting enzyme. Biochemistry 46: 9019-9031.
    • (2007) Biochemistry , vol.46 , pp. 9019-9031
    • Danilov, S.M.1    Watermeyer, J.M.2    Balyasnikova, I.B.3    Gordon, K.4    Kugaevskaya, E.V.5
  • 54
    • 53049083477 scopus 로고    scopus 로고
    • Mapping of conformational mAb epitopes to the C domain of human angiotensin I-converting enzyme (ACE)
    • Naperova IA, Balyasnikova IV, Schwartz DE, Watermeyer J, Sturrock DE, et al. (2008) Mapping of conformational mAb epitopes to the C domain of human angiotensin I-converting enzyme (ACE). J Proteome Res 7: 3396-3411.
    • (2008) J Proteome Res , vol.7 , pp. 3396-3411
    • Naperova, I.A.1    Balyasnikova, I.V.2    Schwartz, D.E.3    Watermeyer, J.4    Sturrock, D.E.5
  • 55
    • 73949083200 scopus 로고    scopus 로고
    • Fine epitope mapping of monoclonal antibodies 9B9 and 3G8, to the N domain of human angiotensin I-converting enzyme (ACE) defines a region involved in regulating ACE dimerization and shedding
    • Gordon K, Balyasnikova IV, Nesterovitch AB, Schwartz DE, Sturrock ED, et al. (2010) Fine epitope mapping of monoclonal antibodies 9B9 and 3G8, to the N domain of human angiotensin I-converting enzyme (ACE) defines a region involved in regulating ACE dimerization and shedding. Tissue Antigens 75: 136-150.
    • (2010) Tissue Antigens , vol.75 , pp. 136-150
    • Gordon, K.1    Balyasnikova, I.V.2    Nesterovitch, A.B.3    Schwartz, D.E.4    Sturrock, E.D.5
  • 56
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 57
    • 0037325195 scopus 로고    scopus 로고
    • Isoforms of angiotensin I-converting enzyme in the development and differentiation of human testis and epididymis
    • Pauls K, Metzger R, Steger K, Klonisch T, Danilov S, et al. (2003) Isoforms of angiotensin I-converting enzyme in the development and differentiation of human testis and epididymis. Andrologia 35: 32-43.
    • (2003) Andrologia , vol.35 , pp. 32-43
    • Pauls, K.1    Metzger, R.2    Steger, K.3    Klonisch, T.4    Danilov, S.5
  • 58
    • 0029949790 scopus 로고    scopus 로고
    • Development of enzyme-linked immunoassays for human angiotensin I converting enzyme suitable for large-scale studies
    • Danilov S, Savoie F, Lenoir B, Jeunemaitre X, Azizi M, et al. (1996) Development of enzyme-linked immunoassays for human angiotensin I converting enzyme suitable for large-scale studies. J Hypertens 14: 719-727.
    • (1996) J Hypertens , vol.14 , pp. 719-727
    • Danilov, S.1    Savoie, F.2    Lenoir, B.3    Jeunemaitre, X.4    Azizi, M.5
  • 59
    • 33645831776 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme (ACE) dimerization is the initial step in the ACE inhibitor-induced ACE signaling cascade in endothelial cells
    • Kohlstedt K, Gershome C, Friedrich M, Müller-Ester W, Alhenc-Gelas F, et al. (2006) Angiotensin-converting enzyme (ACE) dimerization is the initial step in the ACE inhibitor-induced ACE signaling cascade in endothelial cells. Mol Pharmacol 69: 1725-1732.
    • (2006) Mol Pharmacol , vol.69 , pp. 1725-1732
    • Kohlstedt, K.1    Gershome, C.2    Friedrich, M.3    Müller-Ester, W.4    Alhenc-Gelas, F.5
  • 60
    • 0037086711 scopus 로고    scopus 로고
    • Epitope-specific antibody-induced cleavage of angiotensin-converting enzyme from the cell surface
    • Balyasnikova IV, Karran EH, Albrecht RF, Danilov SM, (2002) Epitope-specific antibody-induced cleavage of angiotensin-converting enzyme from the cell surface. Biochem J 362: 585-595.
    • (2002) Biochem J , vol.362 , pp. 585-595
    • Balyasnikova, I.V.1    Karran, E.H.2    Albrecht, R.F.3    Danilov, S.M.4
  • 61
    • 78149390382 scopus 로고    scopus 로고
    • Conformational fingerprinting of the angiotensin-converting enzyme (ACE): Application in sarcoidosis
    • Danilov SM, Balyasnikova IB, Danilova AS, Naperova IA, Arablinskaya E, et al. (2010) Conformational fingerprinting of the angiotensin-converting enzyme (ACE): Application in sarcoidosis. J Proteome Res 9: 5782-5793.
    • (2010) J Proteome Res , vol.9 , pp. 5782-5793
    • Danilov, S.M.1    Balyasnikova, I.B.2    Danilova, A.S.3    Naperova, I.A.4    Arablinskaya, E.5
  • 62
    • 0028998747 scopus 로고
    • Catalytic properties of the two active sites of angiotensin I-converting enzyme on the cell surface
    • Jaspard E, Alhenc-Gelas F, (1995) Catalytic properties of the two active sites of angiotensin I-converting enzyme on the cell surface. Biochem Biophys Res Commun 211: 528-534.
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 528-534
    • Jaspard, E.1    Alhenc-Gelas, F.2
  • 63
    • 19644373766 scopus 로고    scopus 로고
    • Detection of mutated angiotensin I-converting enzyme by serum/plasma analysis using a pair of monoclonal antibodies
    • Danilov SM, Deinum J, Balyasnikova IV, Sun Z-L, Kramers C, et al. (2005) Detection of mutated angiotensin I-converting enzyme by serum/plasma analysis using a pair of monoclonal antibodies. Clin Chem 51: 1040-1043.
    • (2005) Clin Chem , vol.51 , pp. 1040-1043
    • Danilov, S.M.1    Deinum, J.2    Balyasnikova, I.V.3    Sun, Z.-L.4    Kramers, C.5
  • 64
    • 33644945546 scopus 로고    scopus 로고
    • Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design
    • Corradi HR, Schwager SL, Nchinda AT, Sturrock ED, Acharya KR, (2006) Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design. J Mol Biol 357: 964-974.
    • (2006) J Mol Biol , vol.357 , pp. 964-974
    • Corradi, H.R.1    Schwager, S.L.2    Nchinda, A.T.3    Sturrock, E.D.4    Acharya, K.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.