메뉴 건너뛰기




Volumn 18, Issue 3, 2009, Pages 619-628

Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase

Author keywords

Camelid antibodies; Nitric oxide reductase; Phage display; SPR; VHH domain

Indexed keywords

ANTIBODY; ASCORBIC ACID; CAMELID ANTIBODY; CYTOCHROME C OXIDASE; EPITOPE; IMMUNOGLOBULIN HEAVY CHAIN; MEMBRANE PROTEIN; NITRIC OXIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 61449174868     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.69     Document Type: Article
Times cited : (33)

References (47)
  • 2
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single-domain antibody fragments: The superfluous luxury of paired domains
    • Muyldermans S, Cambillau C, Wyns L (2001) Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains. Trends Biochem Sci 26:230-235.
    • (2001) Trends Biochem Sci , vol.26 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 5
    • 33644512108 scopus 로고    scopus 로고
    • Neutralisation of venominduced haemorrhage by IgG from camels and llamas immunised, with viper venom and also by endogenous, non-IgG components in camelid sera
    • Harrison RA, Hasson SS, Harmsen M, Laing GD, Conrath K, Theakston RD (2005) Neutralisation of venominduced haemorrhage by IgG from camels and llamas immunised, with viper venom and also by endogenous, non-IgG components in camelid sera. Toxicon 47: 364-368.
    • (2005) Toxicon , vol.47 , pp. 364-368
    • Harrison, R.A.1    Hasson, S.S.2    Harmsen, M.3    Laing, G.D.4    Conrath, K.5    Theakston, R.D.6
  • 14
    • 0033561250 scopus 로고    scopus 로고
    • A single-domain antibody fragment in complex with RNase A: Non-canonical loop structures and nanomolar affinity using two CDR loops
    • Decanniere K, Desmyter A, Lauwereys M, Ghahroudi MA, Muyldermans S, Wyns L (1999) A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops. Structure 7:361-370.
    • (1999) Structure , vol.7 , pp. 361-370
    • Decanniere, K.1    Desmyter, A.2    Lauwereys, M.3    Ghahroudi, M.A.4    Muyldermans, S.5    Wyns, L.6
  • 16
    • 0035854724 scopus 로고    scopus 로고
    • Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody
    • Desmyter A, Decanniere K, Muyldermans S, Wyns L (2001) Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody. J Biol Chem 276:26285-26290.
    • (2001) J Biol Chem , vol.276 , pp. 26285-26290
    • Desmyter, A.1    Decanniere, K.2    Muyldermans, S.3    Wyns, L.4
  • 17
    • 0037189507 scopus 로고    scopus 로고
    • Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology
    • Desmyter A, Spinelli S, Payan F, Lauwereys M, Wyns L, Muyldermans S, Cambillau C (2002) Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology. J Biol Chem 277:23645-23650.
    • (2002) J Biol Chem , vol.277 , pp. 23645-23650
    • Desmyter, A.1    Spinelli, S.2    Payan, F.3    Lauwereys, M.4    Wyns, L.5    Muyldermans, S.6    Cambillau, C.7
  • 18
    • 0036606759 scopus 로고    scopus 로고
    • Renisio JG, Perez J, Czisch M, Guenneugues M, Bornet O, Frenken L, Cambillau C, Darbon H (2002) Solution structure and backbone dynamics of an antigen-free heavy chain variable domain (VHH) from. Llama. Proteins 47:546-555.
    • Renisio JG, Perez J, Czisch M, Guenneugues M, Bornet O, Frenken L, Cambillau C, Darbon H (2002) Solution structure and backbone dynamics of an antigen-free heavy chain variable domain (VHH) from. Llama. Proteins 47:546-555.
  • 22
    • 30044442097 scopus 로고    scopus 로고
    • Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses
    • Spinelli S, Desmyter A, Verrips CT, de Haard HJ, Moineau S, Cambillau C (2006) Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat Struct Mol Biol 13:85-89.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 85-89
    • Spinelli, S.1    Desmyter, A.2    Verrips, C.T.3    de Haard, H.J.4    Moineau, S.5    Cambillau, C.6
  • 25
    • 8344265279 scopus 로고    scopus 로고
    • Structural, basis of denitrification
    • Einsle O, Kroneck. PM (2004) Structural, basis of denitrification. Biol Chem 385:875-883.
    • (2004) Biol Chem , vol.385 , pp. 875-883
    • Einsle, O.1    Kroneck, P.M.2
  • 26
    • 0029054793 scopus 로고
    • The anatomy of a afunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1
    • Fulop V, Moir JW, Ferguson SJ, Hajdu J (1995) The anatomy of a afunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1. Cell 81:369-377.
    • (1995) Cell , vol.81 , pp. 369-377
    • Fulop, V.1    Moir, J.W.2    Ferguson, S.J.3    Hajdu, J.4
  • 27
    • 0032491207 scopus 로고    scopus 로고
    • Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa
    • Nurizzo D, Cutruzzola F, Arese M, Bourgeois D, Brunori M, Cambillau C, Tegoni M (1998) Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa. Biochemistry 37:13987-13996.
    • (1998) Biochemistry , vol.37 , pp. 13987-13996
    • Nurizzo, D.1    Cutruzzola, F.2    Arese, M.3    Bourgeois, D.4    Brunori, M.5    Cambillau, C.6    Tegoni, M.7
  • 31
    • 1642370336 scopus 로고    scopus 로고
    • Architecture of NarGH reveals a structural, classification of Mo-bisMGD enzymes
    • Jormakka M, Richardson D, Byrne B, Iwata S (2004) Architecture of NarGH reveals a structural, classification of Mo-bisMGD enzymes. Structure 12:95-104.
    • (2004) Structure , vol.12 , pp. 95-104
    • Jormakka, M.1    Richardson, D.2    Byrne, B.3    Iwata, S.4
  • 32
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H (1995) Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 33
    • 0035543035 scopus 로고    scopus 로고
    • The cytochrome cbb3 from Pseudomonas stutzen displays nitric oxide reductase activity
    • Forte E, Urbani A, Saraste M, Sarti P, Brunori M, Giuffre A (2001) The cytochrome cbb3 from Pseudomonas stutzen displays nitric oxide reductase activity. Eur J Biochem 268:6486-6491.
    • (2001) Eur J Biochem , vol.268 , pp. 6486-6491
    • Forte, E.1    Urbani, A.2    Saraste, M.3    Sarti, P.4    Brunori, M.5    Giuffre, A.6
  • 34
    • 61449103806 scopus 로고    scopus 로고
    • Rabat EA, Wu TT, Perry HM, Gottesmann KS, Foeller C (1991) in NH Publication no. 91-3242, 5th Ed., U.S. Department of Health and Human Services.
    • Rabat EA, Wu TT, Perry HM, Gottesmann KS, Foeller C (1991) in NH Publication no. 91-3242, 5th Ed., U.S. Department of Health and Human Services.
  • 35
    • 0027052342 scopus 로고
    • Three-dimensional structure of an Fv from a human IgM immunoglobulin
    • Fan. SF, Kao CY (1992) Three-dimensional structure of an Fv from a human IgM immunoglobulin. Eur J Pharmacol 229:259-263.
    • (1992) Eur J Pharmacol , vol.229 , pp. 259-263
    • Fan, S.F.1    Kao, C.Y.2
  • 36
    • 0036667741 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins mediated by antibody fragments
    • Hunte C, Michel H (2002) Crystallisation of membrane proteins mediated by antibody fragments. Curr Opin Struct Biol. 12:503-508.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 503-508
    • Hunte, C.1    Michel, H.2
  • 37
    • 1942436325 scopus 로고    scopus 로고
    • An antibody library for stabilizing and crystallizing membrane proteins selecting binders to the citrate carrier CitS
    • Rothlisberger D, Pos KM, Pluckthun A (2004) An antibody library for stabilizing and crystallizing membrane proteins selecting binders to the citrate carrier CitS. FEBS Lett 564:340-348.
    • (2004) FEBS Lett , vol.564 , pp. 340-348
    • Rothlisberger, D.1    Pos, K.M.2    Pluckthun, A.3
  • 39
    • 0028798287 scopus 로고
    • Engineered Fv fragments as a tool for the one-step purification, of integral multisubunit membrane protein complexes
    • Kleymann G, Ostermeier C, Ludwig B, Skerra A, Michel H (1995) Engineered Fv fragments as a tool for the one-step purification, of integral multisubunit membrane protein complexes. Biotechnology (N Y) 13:155-160.
    • (1995) Biotechnology (N Y) , vol.13 , pp. 155-160
    • Kleymann, G.1    Ostermeier, C.2    Ludwig, B.3    Skerra, A.4    Michel, H.5
  • 40
    • 0032981135 scopus 로고    scopus 로고
    • MAD structure of Pseudomonas náutica dimeric cytochrome 0(552) mimicks the c(4) dihemic cytochrome domain association
    • Brown K, Nurizzo D, Besson S, Shepard W, Moura J, Moura I, Tegoni M, Cambillau C (1999) MAD structure of Pseudomonas náutica dimeric cytochrome 0(552) mimicks the c(4) dihemic cytochrome domain association. J Mol Biol 289:1017-1028.
    • (1999) J Mol Biol , vol.289 , pp. 1017-1028
    • Brown, K.1    Nurizzo, D.2    Besson, S.3    Shepard, W.4    Moura, J.5    Moura, I.6    Tegoni, M.7    Cambillau, C.8
  • 41
    • 33846270025 scopus 로고    scopus 로고
    • A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme
    • Thorndycroft FH, Butland G, Richardson DJ, Watmough NJ (2007) A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme. Biochem J 401:111-119.
    • (2007) Biochem J , vol.401 , pp. 111-119
    • Thorndycroft, F.H.1    Butland, G.2    Richardson, D.J.3    Watmough, N.J.4
  • 42
    • 0032836317 scopus 로고    scopus 로고
    • Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16
    • Gramm R, Pohlmann A, Friedrich B (1999) Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16. FEBS Lett 460: 6-10.
    • (1999) FEBS Lett , vol.460 , pp. 6-10
    • Gramm, R.1    Pohlmann, A.2    Friedrich, B.3
  • 44
    • 10644287538 scopus 로고    scopus 로고
    • Single domain antibodies derived from dromedary lymph node and peripheral blood lymphocytes sensing conformational variants of prostate-specific antigen
    • Saerens D, Kinne J, Bosnians E, Wernery U, Muyldermans S, Conrath K (2004) Single domain antibodies derived from dromedary lymph node and peripheral blood lymphocytes sensing conformational variants of prostate-specific antigen. J Biol Chem 279:51965-51972.
    • (2004) J Biol Chem , vol.279 , pp. 51965-51972
    • Saerens, D.1    Kinne, J.2    Bosnians, E.3    Wernery, U.4    Muyldermans, S.5    Conrath, K.6
  • 45
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel, heavy-chain antibodies
    • Arbabi Ghahroudi M, Desmyter A, Wyns L, Hamers R, Muyldermans S (1997) Selection and identification of single domain antibody fragments from camel, heavy-chain antibodies. FEBS Lett 414:521-526.
    • (1997) FEBS Lett , vol.414 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 47
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin. Fv fragment in Escherichia coli
    • Skerra A, Pluckthun A (1988) Assembly of a functional immunoglobulin. Fv fragment in Escherichia coli. Science 240:1038-1041.
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Pluckthun, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.