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Volumn 46, Issue 46, 2007, Pages 13254-13268

Spectroscopic and functional characterization of nitrophorin 7 from the blood-feeding insect Rhodnius prolixus reveals an important role of its isoform-specific N-terminus for proper protein function

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION CONSTANTS; NITROPHORIN 7; RHODNIUS PROLIXUS; SALIVA;

EID: 36349019705     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7014986     Document Type: Article
Times cited : (32)

References (75)
  • 1
    • 0000064601 scopus 로고    scopus 로고
    • Mauk, A. G, and Sykes, A. G, Eds, Academic Press, San Diego
    • Walker, F. A., and Montfort, W. R. (2001) in Advances in Inorganic Chemistry (Mauk, A. G., and Sykes, A. G., Eds.) Vol. 51, pp 295-358, Academic Press, San Diego.
    • (2001) Advances in Inorganic Chemistry , vol.51 , pp. 295-358
    • Walker, F.A.1    Montfort, W.R.2
  • 2
  • 3
    • 0019348816 scopus 로고
    • Chagas' disease: An ecological appraisal with special emphasis on its insect vectors
    • Zeledón, R., and Rabinovich, J. E. (1981) Chagas' disease: An ecological appraisal with special emphasis on its insect vectors, Annu. Rev. Entomol. 26, 101-133.
    • (1981) Annu. Rev. Entomol , vol.26 , pp. 101-133
    • Zeledón, R.1    Rabinovich, J.E.2
  • 4
    • 0027924584 scopus 로고
    • American trypanosomiasis (Chagas' disease): A tropical disease now in the United States
    • Kirchhoff, L. V. (1993) American trypanosomiasis (Chagas' disease): A tropical disease now in the United States, N. Engl. J. Med. 329, 639-644.
    • (1993) N. Engl. J. Med , vol.329 , pp. 639-644
    • Kirchhoff, L.V.1
  • 5
    • 0346876345 scopus 로고
    • Observations on vectors of Chagas' disease in the United States. I. California
    • Wood, S. F. (1942) Observations on vectors of Chagas' disease in the United States. I. California, Bull. Calif. Acad. Sci. 41, 61-69.
    • (1942) Bull. Calif. Acad. Sci , vol.41 , pp. 61-69
    • Wood, S.F.1
  • 6
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropode saliva in blood feeding: Sialome and post-sialome perspectives
    • Ribeiro, J. M. C., and Francischetti, I. M. B. (2003) Role of arthropode saliva in blood feeding: Sialome and post-sialome perspectives, Annu. Rev. Entomol. 48, 73-88.
    • (2003) Annu. Rev. Entomol , vol.48 , pp. 73-88
    • Ribeiro, J.M.C.1    Francischetti, I.M.B.2
  • 7
    • 0028947447 scopus 로고
    • Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus
    • Champagne, D. E., Nussenzveig, R. H., and Ribeiro, J. M. C. (1995) Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus, J. Biol. Chem. 270, 8691-8695.
    • (1995) J. Biol. Chem , vol.270 , pp. 8691-8695
    • Champagne, D.E.1    Nussenzveig, R.H.2    Ribeiro, J.M.C.3
  • 8
    • 0037211411 scopus 로고    scopus 로고
    • Changes in salivary nitrophorin profile during the life cycle of the blood-sucking bug Rhodnius prolixus
    • Moreira, M. F., Coelho, H. S. L., Zingali, R. B., Oliveira, P. L., and Masuda, H. (2003) Changes in salivary nitrophorin profile during the life cycle of the blood-sucking bug Rhodnius prolixus, Insect Biochem. Mol. Biol. 33, 23-28.
    • (2003) Insect Biochem. Mol. Biol , vol.33 , pp. 23-28
    • Moreira, M.F.1    Coelho, H.S.L.2    Zingali, R.B.3    Oliveira, P.L.4    Masuda, H.5
  • 9
    • 0027178971 scopus 로고
    • Nitric oxide synthase activity from a hematophagous insect salivary gland
    • Ribeiro, J. M. C., and Nussenzveig, R. H. (1993) Nitric oxide synthase activity from a hematophagous insect salivary gland, FEBS Lett. 330, 165-168.
    • (1993) FEBS Lett , vol.330 , pp. 165-168
    • Ribeiro, J.M.C.1    Nussenzveig, R.H.2
  • 10
    • 0029294689 scopus 로고
    • Nitric oxide loading of the salivary nitric-oxide-carrying nemoproteins (nitrophorins) in the blood-sucking bug Rhodnius prolixus
    • Nussenzveig, R. H., Bentley, D. L., and Ribeiro, J. M. C. (1995) Nitric oxide loading of the salivary nitric-oxide-carrying nemoproteins (nitrophorins) in the blood-sucking bug Rhodnius prolixus, J. Exp. Biol. 198, 1093-1098.
    • (1995) J. Exp. Biol , vol.198 , pp. 1093-1098
    • Nussenzveig, R.H.1    Bentley, D.L.2    Ribeiro, J.M.C.3
  • 11
    • 0030433173 scopus 로고    scopus 로고
    • cDNA cloning, expression and characterization of nitric-oxide synthase from the salivary glands of the blood-sucking insect Rhodnius prolixus
    • Yuda, M., Hirai, M., Miura, K., Matsumura, H., Ando, K., and Chinzei, Y. (1996) cDNA cloning, expression and characterization of nitric-oxide synthase from the salivary glands of the blood-sucking insect Rhodnius prolixus, Eur. J. Biochem. 242, 807-812.
    • (1996) Eur. J. Biochem , vol.242 , pp. 807-812
    • Yuda, M.1    Hirai, M.2    Miura, K.3    Matsumura, H.4    Ando, K.5    Chinzei, Y.6
  • 13
    • 0027213409 scopus 로고
    • Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect
    • Ribeiro, J. M. C., Hazzard, J. M., Nussenzveig, R. H., Champagne, D. E., and Walker, F. A. (1993) Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect, Science 260, 539-541.
    • (1993) Science , vol.260 , pp. 539-541
    • Ribeiro, J.M.C.1    Hazzard, J.M.2    Nussenzveig, R.H.3    Champagne, D.E.4    Walker, F.A.5
  • 14
    • 0030036756 scopus 로고    scopus 로고
    • Studies on the reaction mechanism for reductive nitrosylation for ferrihemoproteins in buffer solutions
    • Hoshino, M., Maeda, M., Konishi, R., Seki, H., and Ford, P. C. (1996) Studies on the reaction mechanism for reductive nitrosylation for ferrihemoproteins in buffer solutions, J. Am. Chem. Soc. 118, 5702-5707.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 5702-5707
    • Hoshino, M.1    Maeda, M.2    Konishi, R.3    Seki, H.4    Ford, P.C.5
  • 15
    • 0037389596 scopus 로고    scopus 로고
    • Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: Stability, structure, and dynamics of axial ligand complexes
    • Shokhireva, T. Kh., Berry, R. E., Uno, E., Balfour, C. A., Zhang, H., and Walker, F. A. (2003) Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: Stability, structure, and dynamics of axial ligand complexes, Proc. Natl. Acad. Sci. U.S.A. 100, 3778-3783.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 3778-3783
    • Shokhireva, T.K.1    Berry, R.E.2    Uno, E.3    Balfour, C.A.4    Zhang, H.5    Walker, F.A.6
  • 18
    • 31344449504 scopus 로고    scopus 로고
    • Characterization of histamine release by mast cells, basophils, and monocytes
    • Falus, A, Grosman, N, and Darvas, Z, Eds, pp, SpringMed Publishing Ltd, Budapest
    • Watt, A. P., and Ennis, M. (2004) Characterization of histamine release by mast cells, basophils, and monocytes, in Histamine: Biology and Medical Aspects (Falus, A., Grosman, N., and Darvas, Z., Eds.) pp 99-111, SpringMed Publishing Ltd., Budapest.
    • (2004) Histamine: Biology and Medical Aspects , pp. 99-111
    • Watt, A.P.1    Ennis, M.2
  • 19
    • 0028029463 scopus 로고
    • High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus
    • Ribeiro, J. M. C., and Walker, F. A. (1994) High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus, J. Exp. Med. 180, 2251-2257.
    • (1994) J. Exp. Med , vol.180 , pp. 2251-2257
    • Ribeiro, J.M.C.1    Walker, F.A.2
  • 20
    • 0035965691 scopus 로고    scopus 로고
    • Resonance Raman spectroscopic study of nitrophorin 1, a nitric oxide-binding heme protein from Rhodnius prolixus, and its nitrosyl and cyano adducts
    • Maes, E. M., Walker, F. A., Montfort, W. R., and Czernuszewicz, R. S. (2001) Resonance Raman spectroscopic study of nitrophorin 1, a nitric oxide-binding heme protein from Rhodnius prolixus, and its nitrosyl and cyano adducts, J. Am. Chem. Soc. 123, 1164-1172.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 1164-1172
    • Maes, E.M.1    Walker, F.A.2    Montfort, W.R.3    Czernuszewicz, R.S.4
  • 21
    • 1542358099 scopus 로고    scopus 로고
    • Axial ligand complexes of the Rhodnius nitrophorins: Reduction potentials, binding constants, EPR spectra, and structures of the 4-iodopyrazole and imidazole complexes of NP4
    • Berry, R. E., Ding, X. D., Shokhireva, T. Kh., Weichsel, A., Montfort, W. R., and Walker, F. A. (2004) Axial ligand complexes of the Rhodnius nitrophorins: Reduction potentials, binding constants, EPR spectra, and structures of the 4-iodopyrazole and imidazole complexes of NP4, J. Biol. Inorg. Chem. 9, 135-144.
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 135-144
    • Berry, R.E.1    Ding, X.D.2    Shokhireva, T.K.3    Weichsel, A.4    Montfort, W.R.5    Walker, F.A.6
  • 24
    • 0037469131 scopus 로고    scopus 로고
    • 13C NMR spectroscopy: An explanation of the order of heme methyl resonances in high-spin ferriheme proteins
    • 13C NMR spectroscopy: An explanation of the order of heme methyl resonances in high-spin ferriheme proteins, Biochemistry 42, 679-693.
    • (2003) Biochemistry , vol.42 , pp. 679-693
    • Shokhireva, T.K.1    Shokhirev, N.V.2    Walker, F.A.3
  • 25
    • 34250169012 scopus 로고    scopus 로고
    • Insect bites on a molecular basis. How does the blood-sucking bug Rhodnius prolixus get its meal? The ferriheme proteins nitrophorin 2 and 4 studied by Mössbauer spectroscopy
    • Wegner, P., Benda, R., Schünemann, V., Trautwein, A. X., Berry, R. E., Balfour, C. A., Wert, D., and Walker, F. A. (2002) Insect bites on a molecular basis. How does the blood-sucking bug Rhodnius prolixus get its meal? The ferriheme proteins nitrophorin 2 and 4 studied by Mössbauer spectroscopy, Hyperfine Interact. C5, 253-256.
    • (2002) Hyperfine Interact , vol.C5 , pp. 253-256
    • Wegner, P.1    Benda, R.2    Schünemann, V.3    Trautwein, A.X.4    Berry, R.E.5    Balfour, C.A.6    Wert, D.7    Walker, F.A.8
  • 26
    • 0002159495 scopus 로고    scopus 로고
    • Two- and four-pulse ESEEM studies of the heme binding center of a low-spin ferriheme protein: The importance of a multi-frequency approach
    • Astashkin, A. V., Raitsimring, A. M., and Walker, F. A. (1999) Two- and four-pulse ESEEM studies of the heme binding center of a low-spin ferriheme protein: The importance of a multi-frequency approach, Chem. Phys. Lett. 306, 9-17.
    • (1999) Chem. Phys. Lett , vol.306 , pp. 9-17
    • Astashkin, A.V.1    Raitsimring, A.M.2    Walker, F.A.3
  • 28
    • 0034702817 scopus 로고    scopus 로고
    • Kinetics and equilibria in ligand binding by nitrophorins 1-4: Evidence for stabilization of a nitric oxide-ferriheme complex through a ligand-induced conformational trap
    • Andersen, J. F., Ding, X. D., Balfour, C., Shokhireva, T. Kh., Champagne, D. E., Walker, F. A., and Montfort, W. R. (2000) Kinetics and equilibria in ligand binding by nitrophorins 1-4: Evidence for stabilization of a nitric oxide-ferriheme complex through a ligand-induced conformational trap, Biochemistry 39, 10118-10131.
    • (2000) Biochemistry , vol.39 , pp. 10118-10131
    • Andersen, J.F.1    Ding, X.D.2    Balfour, C.3    Shokhireva, T.K.4    Champagne, D.E.5    Walker, F.A.6    Montfort, W.R.7
  • 29
    • 0030993345 scopus 로고    scopus 로고
    • Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus
    • Andersen, J. F., Champagne, D. E., Weichsel, A., Ribeiro, J. M. C., Balfour, C. A., Dress, V., and Montfort, W. R. (1997) Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus, Biochemistry 36, 4423-4428.
    • (1997) Biochemistry , vol.36 , pp. 4423-4428
    • Andersen, J.F.1    Champagne, D.E.2    Weichsel, A.3    Ribeiro, J.M.C.4    Balfour, C.A.5    Dress, V.6    Montfort, W.R.7
  • 30
    • 2542528641 scopus 로고    scopus 로고
    • Role of binding site loops in controlling nitric oxide release: Structure and kinetics of mutant forms of nitrophorin 4
    • Maes, E. M., Weichsel, A., Andersen, J. F., Shepley, D., and Montfort, W. R. (2004) Role of binding site loops in controlling nitric oxide release: Structure and kinetics of mutant forms of nitrophorin 4, Biochemistry 43, 6679-6690.
    • (2004) Biochemistry , vol.43 , pp. 6679-6690
    • Maes, E.M.1    Weichsel, A.2    Andersen, J.F.3    Shepley, D.4    Montfort, W.R.5
  • 32
    • 0034730723 scopus 로고    scopus 로고
    • The crystal structure of nitrophorin 2. A trifunctional antihemostatic protein from the saliva of Rhodnius prolixus
    • Andersen, J. F., and Montfort, W. R. (2000) The crystal structure of nitrophorin 2. A trifunctional antihemostatic protein from the saliva of Rhodnius prolixus, J. Biol. Chem. 275, 30496-30503.
    • (2000) J. Biol. Chem , vol.275 , pp. 30496-30503
    • Andersen, J.F.1    Montfort, W.R.2
  • 33
    • 0032532483 scopus 로고    scopus 로고
    • The crystal structure of nitrophorin 4 at 1.5 Å resolution: Transport of nitric oxide by a lipocalin-based heme protein
    • Andersen, J. F., Weichsel, A., Balfour, C. A., Champagne, D. E., and Montfort, W. R. (1998) The crystal structure of nitrophorin 4 at 1.5 Å resolution: Transport of nitric oxide by a lipocalin-based heme protein, Structure 6, 1315-1327.
    • (1998) Structure , vol.6 , pp. 1315-1327
    • Andersen, J.F.1    Weichsel, A.2    Balfour, C.A.3    Champagne, D.E.4    Montfort, W.R.5
  • 34
    • 0033918403 scopus 로고    scopus 로고
    • Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial
    • Weichsel, A., Andersen, J. F., Roberts, S. A., and Montfort, W. R. (2000) Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial, Nat. Struct. Biol. 7, 551-554.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 551-554
    • Weichsel, A.1    Andersen, J.F.2    Roberts, S.A.3    Montfort, W.R.4
  • 35
    • 0035949448 scopus 로고    scopus 로고
    • Ligand-induced heme ruffling and bent NO geometry in ultra-high-resolution structures of nitrophorin 4
    • Roberts, S. A., Weichsel, A., Qiu, Y., Shelnutt, J. A., Walker, F. A., and Montfort, W. R. (2001) Ligand-induced heme ruffling and bent NO geometry in ultra-high-resolution structures of nitrophorin 4, Biochemistry 40, 11327-11337.
    • (2001) Biochemistry , vol.40 , pp. 11327-11337
    • Roberts, S.A.1    Weichsel, A.2    Qiu, Y.3    Shelnutt, J.A.4    Walker, F.A.5    Montfort, W.R.6
  • 36
    • 0034684238 scopus 로고    scopus 로고
    • Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods
    • Montfort, W. R., Weichsel, A., and Andersen, J. F. (2000) Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods, Biochim. Biophys. Acta 1482, 110-118.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 110-118
    • Montfort, W.R.1    Weichsel, A.2    Andersen, J.F.3
  • 38
    • 2642565286 scopus 로고    scopus 로고
    • Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect
    • Andersen, J. F., Gudderra, N. P., Francischetti, I. M. B., Valenzuela, J. G., and Ribeiro, J. M. C. (2004) Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect, Biochemistry 43, 6987-6994.
    • (2004) Biochemistry , vol.43 , pp. 6987-6994
    • Andersen, J.F.1    Gudderra, N.P.2    Francischetti, I.M.B.3    Valenzuela, J.G.4    Ribeiro, J.M.C.5
  • 40
    • 0033937485 scopus 로고    scopus 로고
    • Surface expression of phosphatidylserine on macrophages is required for phagocytosis of apoptotic thymocytes
    • Callahan, M. K., Williamson, P., and Schlegel, R. A. (2000) Surface expression of phosphatidylserine on macrophages is required for phagocytosis of apoptotic thymocytes, Cell Death Differ. 7, 645-653.
    • (2000) Cell Death Differ , vol.7 , pp. 645-653
    • Callahan, M.K.1    Williamson, P.2    Schlegel, R.A.3
  • 41
    • 0141893347 scopus 로고    scopus 로고
    • Rapid, noninflammatory and PS-dependent phagocytic clearance of necrotic cells
    • Hirt, U. A., and Leist, M. (2003) Rapid, noninflammatory and PS-dependent phagocytic clearance of necrotic cells, Cell Death Differ. 10, 1156-1164.
    • (2003) Cell Death Differ , vol.10 , pp. 1156-1164
    • Hirt, U.A.1    Leist, M.2
  • 42
    • 0025321355 scopus 로고
    • Biosynthesis and metabolism of endothelium-derived nitric oxide
    • Ignarro, L. J. (1990) Biosynthesis and metabolism of endothelium-derived nitric oxide, Annu. Rev. Pharmacol. Toxicol. 30, 535-560.
    • (1990) Annu. Rev. Pharmacol. Toxicol , vol.30 , pp. 535-560
    • Ignarro, L.J.1
  • 44
    • 34250177977 scopus 로고    scopus 로고
    • The effect of the N-terminus on heme cavity structure, ligand equilibrium and rate constants and reduction potentials of nitrophorin 2 from Rhodnius prolixus
    • Berry, R. E., Shokhireva, T. Kh., Filippov, I., Shokhirev, M. N., Zhang, H., and Walker, F. A. (2007) The effect of the N-terminus on heme cavity structure, ligand equilibrium and rate constants and reduction potentials of nitrophorin 2 from Rhodnius prolixus, Biochemistry 46, 6830-6843.
    • (2007) Biochemistry , vol.46 , pp. 6830-6843
    • Berry, R.E.1    Shokhireva, T.K.2    Filippov, I.3    Shokhirev, M.N.4    Zhang, H.5    Walker, F.A.6
  • 45
    • 34247344940 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli and functional reconstitution of the liposome binding ferriheme protein nitrophorin 7 from the blood sucking bug Rhodnius prolixus
    • Knipp, M., Zhang, H., Berry, R. E., and Walker, F. A. (2007) Overexpression in Escherichia coli and functional reconstitution of the liposome binding ferriheme protein nitrophorin 7 from the blood sucking bug Rhodnius prolixus, Protein Expression Purif 54, 183-191.
    • (2007) Protein Expression Purif , vol.54 , pp. 183-191
    • Knipp, M.1    Zhang, H.2    Berry, R.E.3    Walker, F.A.4
  • 46
    • 0033653207 scopus 로고    scopus 로고
    • Novel calibration method for nitric oxide microsensors by stoichiometric generation of nitric oxide from SNAP
    • Zhang, X., Cardossa, L., Broderick, M., Fein, H., and Davies, I. R. (2000) Novel calibration method for nitric oxide microsensors by stoichiometric generation of nitric oxide from SNAP, Electroanalysis 12, 425-428.
    • (2000) Electroanalysis , vol.12 , pp. 425-428
    • Zhang, X.1    Cardossa, L.2    Broderick, M.3    Fein, H.4    Davies, I.R.5
  • 47
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput, Nucleic Acids Res. 32, 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 48
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: An automated protein homology-modeling server, Nucleic Acids Res. 31, 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 49
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • Peitsch, M. C. (1995) Protein modeling by E-mail, Bio/Technology 13, 658-660.
    • (1995) Bio/Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 50
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 52
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.3    Thornton, J.M.4
  • 53
    • 0029044597 scopus 로고
    • Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus
    • Ribeiro, J. M. C., Schneider, M., and Guimarães, J. A. (1995) Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus, Biochem. J. 308, 243-249.
    • (1995) Biochem. J , vol.308 , pp. 243-249
    • Ribeiro, J.M.C.1    Schneider, M.2    Guimarães, J.A.3
  • 54
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites, Protein Eng. 10, 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 55
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen, J. D., Nielsen, H., von Heijne, G., and Brunak, S. (2004) Improved prediction of signal peptides: SignalP 3.0, J. Mol. Biol. 340, 783-795.
    • (2004) J. Mol. Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 57
    • 36348970615 scopus 로고    scopus 로고
    • Histamine in the cardiovascular system
    • Falus, A, Grosman, N, and Darvas, Z, Eds, pp, SpringMed Publishing Ltd, Budapest
    • Jochem, J., and Żwirska-Korczala, K. W. (2004) Histamine in the cardiovascular system, in Histamine: Biology and Medical Aspects (Falus, A., Grosman, N., and Darvas, Z., Eds.) pp 303-316, SpringMed Publishing Ltd., Budapest.
    • (2004) Histamine: Biology and Medical Aspects , pp. 303-316
    • Jochem, J.1    Żwirska-Korczala, K.W.2
  • 58
    • 0040292710 scopus 로고
    • Q-Band electron paramagnetic resonance study of nitrosylprotoheme dimethyl ester complexes with N-, O-, and S-donor ligand as model systems for nitrosylhemoproteins
    • Yoshimura, T. (1983) Q-Band electron paramagnetic resonance study of nitrosylprotoheme dimethyl ester complexes with N-, O-, and S-donor ligand as model systems for nitrosylhemoproteins, J. Inorg. Biochem. 18, 263-277.
    • (1983) J. Inorg. Biochem , vol.18 , pp. 263-277
    • Yoshimura, T.1
  • 59
    • 0345262998 scopus 로고
    • Kinetic properties and electron paramagnetic resonance spectra of the nitric oxide derivative of hemoglobin components of trout (Salmo irideus)
    • Brunori, M., Falcioni, G., and Rotilio, G. (1974) Kinetic properties and electron paramagnetic resonance spectra of the nitric oxide derivative of hemoglobin components of trout (Salmo irideus), Proc. Natl. Acad. Sci. U.S.A. 71, 2470-2472.
    • (1974) Proc. Natl. Acad. Sci. U.S.A , vol.71 , pp. 2470-2472
    • Brunori, M.1    Falcioni, G.2    Rotilio, G.3
  • 60
    • 0000122597 scopus 로고    scopus 로고
    • Binding and activation of nitric oxide by metalloporphyrins and heme
    • Kadish, K. M, Smith, K. M, and Guilard, R, Eds, Academic Press, San Diego
    • Cheng, L., and Richter-Addo, G. B. (2000) Binding and activation of nitric oxide by metalloporphyrins and heme, in The Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) Vol. 4, pp 219-291, Academic Press, San Diego.
    • (2000) The Porphyrin Handbook , vol.4 , pp. 219-291
    • Cheng, L.1    Richter-Addo, G.B.2
  • 62
    • 0033016162 scopus 로고    scopus 로고
    • Effect of redox state on unfolding energetics of heme proteins
    • Wittung-Stafshede, P. (1999) Effect of redox state on unfolding energetics of heme proteins, Biochim. Biophys. Acta 1432, 401-405.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 401-405
    • Wittung-Stafshede, P.1
  • 63
    • 0346994908 scopus 로고    scopus 로고
    • Low-spin ferriheme models of the cytochromes: Correlation of molecular structure with EPR spectral type
    • Yatsunyk, L. A., Carducci, M. D., and Walker, F. A. (2003) Low-spin ferriheme models of the cytochromes: Correlation of molecular structure with EPR spectral type, J. Am. Chem. Soc. 125, 15986-16005.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 15986-16005
    • Yatsunyk, L.A.1    Carducci, M.D.2    Walker, F.A.3
  • 66
    • 0000224627 scopus 로고
    • The pH dependence of the stereochemistry around the heme group in NO-cytochrome c (horse heart)
    • Yoshimura, T., and Suzuki, S. (1988) The pH dependence of the stereochemistry around the heme group in NO-cytochrome c (horse heart), Inorg. Chim. Acta 152, 241-249.
    • (1988) Inorg. Chim. Acta , vol.152 , pp. 241-249
    • Yoshimura, T.1    Suzuki, S.2
  • 67
    • 0000894717 scopus 로고
    • Electronic and magnetic circular dichroism spectra of pentacoordinate nitrosulhemes in cytochromes c′ from nonphotosynthetic bacteria and their model complexes
    • Suzuki, S., Yoshimura, T., Nakahara, A., Iwasaki, H., Shidara, S., and Matsubara, T. (1987) Electronic and magnetic circular dichroism spectra of pentacoordinate nitrosulhemes in cytochromes c′ from nonphotosynthetic bacteria and their model complexes, Inorg. Chem. 26, 1006-1008.
    • (1987) Inorg. Chem , vol.26 , pp. 1006-1008
    • Suzuki, S.1    Yoshimura, T.2    Nakahara, A.3    Iwasaki, H.4    Shidara, S.5    Matsubara, T.6
  • 68
    • 0025793468 scopus 로고
    • Spectral properties of Achromobacter xylosoxidans cytochrome c and their NO complexes
    • Iwasaki, H., Yoshimura, T., Suzuki, S., and Shidara, S. (1991) Spectral properties of Achromobacter xylosoxidans cytochrome c and their NO complexes, Biochim. Biophys. Acta 1058, 79-82.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 79-82
    • Iwasaki, H.1    Yoshimura, T.2    Suzuki, S.3    Shidara, S.4
  • 69
    • 0030021582 scopus 로고    scopus 로고
    • Spectroscopic characterization of nitrosylheme in nitric oxide complexes of ferric and ferrous cytochrome c′ from photosynthetic bacteria
    • Yoshimura, T., Fujii, S., Kamada, H., Yamaguchi, K., Suzuki, S., Shidara, S., and Takakuwa, S. (1996) Spectroscopic characterization of nitrosylheme in nitric oxide complexes of ferric and ferrous cytochrome c′ from photosynthetic bacteria, Biochim. Biophys. Acta 1292, 39-46.
    • (1996) Biochim. Biophys. Acta , vol.1292 , pp. 39-46
    • Yoshimura, T.1    Fujii, S.2    Kamada, H.3    Yamaguchi, K.4    Suzuki, S.5    Shidara, S.6    Takakuwa, S.7
  • 70
    • 0033396608 scopus 로고    scopus 로고
    • Activation of soluble guanylate cyclase by carbon monoxide and nitric oxide: A mechanistic model
    • Sharma, V. S., and Madge, D. (1999) Activation of soluble guanylate cyclase by carbon monoxide and nitric oxide: A mechanistic model, Methods 19, 494-505.
    • (1999) Methods , vol.19 , pp. 494-505
    • Sharma, V.S.1    Madge, D.2
  • 71
    • 0031435306 scopus 로고    scopus 로고
    • Soluble guanylate cyclase: The forgotten sibling
    • Hobbs, A. J. (1997) Soluble guanylate cyclase: The forgotten sibling, Trends Pharmacol. Sci. 18, 484-491.
    • (1997) Trends Pharmacol. Sci , vol.18 , pp. 484-491
    • Hobbs, A.J.1
  • 72
    • 0029028563 scopus 로고
    • Studies of the heme coordination and ligand binding properties of soluble guanylate cyclase (sGC): Characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopy and failure of CO to activate the enzyme
    • Burstyn, J. N., Yu, A. E., Dierks, E. A., Hawkins, B. K., and Dawson, J. H. (1995) Studies of the heme coordination and ligand binding properties of soluble guanylate cyclase (sGC): Characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopy and failure of CO to activate the enzyme, Biochemistry 34, 5896-5903.
    • (1995) Biochemistry , vol.34 , pp. 5896-5903
    • Burstyn, J.N.1    Yu, A.E.2    Dierks, E.A.3    Hawkins, B.K.4    Dawson, J.H.5
  • 74
    • 0032030178 scopus 로고    scopus 로고
    • The deactivation of soluble guanylyl cyclase by redox-active agents
    • Dierks, E. A., and Burstyn, J. N. (1998) The deactivation of soluble guanylyl cyclase by redox-active agents, Arch. Biochem. Biophys. 351, 1-7.
    • (1998) Arch. Biochem. Biophys , vol.351 , pp. 1-7
    • Dierks, E.A.1    Burstyn, J.N.2
  • 75
    • 0031006612 scopus 로고    scopus 로고
    • Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase
    • Kharitonov, V. G., Sharma, V. S., Magde, D., and Koesling, D. (1997) Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase, Biochemistry 36, 6814-6818.
    • (1997) Biochemistry , vol.36 , pp. 6814-6818
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4


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