메뉴 건너뛰기




Volumn 63, Issue , 2013, Pages 391-446

Microbial eukaryote globins

Author keywords

Evolution; Fungi; Haemoglobin; Phylogeny; Protist

Indexed keywords

GLOBIN; HEMOGLOBIN; MYOGLOBIN; NEUROGLOBIN; TRANSCRIPTOME;

EID: 84884191621     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-407693-8.00009-1     Document Type: Chapter
Times cited : (36)

References (196)
  • 5
    • 77949515028 scopus 로고    scopus 로고
    • Cerebral and peripheral changes occurring in nitric oxide (NO) synthesis in a rat model of sleeping sickness: Identification of brain iNOS expressing cells
    • Amrouni D., Gautier-Sauvigne S., Meiller A., Vincendeau P., Bouteille B., Buguet A., et al. Cerebral and peripheral changes occurring in nitric oxide (NO) synthesis in a rat model of sleeping sickness: Identification of brain iNOS expressing cells. PLoS One 2010, 5:e9211.
    • (2010) PLoS One , vol.5
    • Amrouni, D.1    Gautier-Sauvigne, S.2    Meiller, A.3    Vincendeau, P.4    Bouteille, B.5    Buguet, A.6
  • 8
    • 49449115439 scopus 로고    scopus 로고
    • Contributions of experimental mouse models to the understanding of African trypanosomiasis
    • Antoine-Moussiaux N., Magez S., Desmecht D. Contributions of experimental mouse models to the understanding of African trypanosomiasis. Trends in Parasitology 2008, 24:411-418.
    • (2008) Trends in Parasitology , vol.24 , pp. 411-418
    • Antoine-Moussiaux, N.1    Magez, S.2    Desmecht, D.3
  • 9
    • 0347622945 scopus 로고    scopus 로고
    • The anti-parasitic effects of nitric oxide
    • Ascenzi P., Bocedi A., Gradoni L. The anti-parasitic effects of nitric oxide. IUBMB Life 2003, 55:573-578.
    • (2003) IUBMB Life , vol.55 , pp. 573-578
    • Ascenzi, P.1    Bocedi, A.2    Gradoni, L.3
  • 10
    • 33750858684 scopus 로고    scopus 로고
    • Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia
    • Aury J.M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., et al. Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia. Nature 2006, 444:171-178.
    • (2006) Nature , vol.444 , pp. 171-178
    • Aury, J.M.1    Jaillon, O.2    Duret, L.3    Noel, B.4    Jubin, C.5    Porcel, B.M.6
  • 11
    • 79961076133 scopus 로고    scopus 로고
    • Role of nitric oxide and flavohemoglobin homolog genes in Aspergillus nidulans sexual development and mycotoxin production
    • Baidya S., Cary J.W., Grayburn W.S., Calvo A.M. Role of nitric oxide and flavohemoglobin homolog genes in Aspergillus nidulans sexual development and mycotoxin production. Applied and Environmental Microbiology 2011, 77:5524-5528.
    • (2011) Applied and Environmental Microbiology , vol.77 , pp. 5524-5528
    • Baidya, S.1    Cary, J.W.2    Grayburn, W.S.3    Calvo, A.M.4
  • 12
    • 0031277625 scopus 로고    scopus 로고
    • Isolation of a nitric oxide synthase from the protozoan parasite, Leishmania donovani
    • Basu N.K., Kole L., Ghosh A., Das P.K. Isolation of a nitric oxide synthase from the protozoan parasite, Leishmania donovani. FEMS Microbiology Letters 1997, 156:43-47.
    • (1997) FEMS Microbiology Letters , vol.156 , pp. 43-47
    • Basu, N.K.1    Kole, L.2    Ghosh, A.3    Das, P.K.4
  • 13
    • 84859996524 scopus 로고    scopus 로고
    • Symbiodinium transcriptomes: Genome insights into the dinoflagellate symbionts of reef-building corals
    • Bayer T., Aranda M., Sunagawa S., Yum L.K., DeSalvo M.K., Lindquist E., et al. Symbiodinium transcriptomes: Genome insights into the dinoflagellate symbionts of reef-building corals. PLoS One 2012, 7:e35269.
    • (2012) PLoS One , vol.7
    • Bayer, T.1    Aranda, M.2    Sunagawa, S.3    Yum, L.K.4    DeSalvo, M.K.5    Lindquist, E.6
  • 15
    • 84867830765 scopus 로고    scopus 로고
    • Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor
    • Blank M., Burmester T. Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor. Molecular Biology and Evolution 2012, 29:3553-3561.
    • (2012) Molecular Biology and Evolution , vol.29 , pp. 3553-3561
    • Blank, M.1    Burmester, T.2
  • 16
    • 22544481774 scopus 로고    scopus 로고
    • Flavohaemoglobin HmpX from Erwinia chrysanthemi confers nitrosative stress tolerance and affects the plant hypersensitive reaction by intercepting nitric oxide produced by the host
    • Boccara M., Mills C.E., Zeier J., Anzi C., Lamb C., Poole R.K., et al. Flavohaemoglobin HmpX from Erwinia chrysanthemi confers nitrosative stress tolerance and affects the plant hypersensitive reaction by intercepting nitric oxide produced by the host. The Plant Journal 2005, 43:226-237.
    • (2005) The Plant Journal , vol.43 , pp. 226-237
    • Boccara, M.1    Mills, C.E.2    Zeier, J.3    Anzi, C.4    Lamb, C.5    Poole, R.K.6
  • 18
    • 81855175401 scopus 로고    scopus 로고
    • The diversity of microbial responses to nitric oxide and agents of nitrosative stress close cousins but not identical twins
    • Bowman L.A., McLean S., Poole R.K., Fukuto J.M. The diversity of microbial responses to nitric oxide and agents of nitrosative stress close cousins but not identical twins. Advances in Microbial Physiology 2011, 59:135-219.
    • (2011) Advances in Microbial Physiology , vol.59 , pp. 135-219
    • Bowman, L.A.1    McLean, S.2    Poole, R.K.3    Fukuto, J.M.4
  • 19
    • 68049143143 scopus 로고    scopus 로고
    • Nitrosative and oxidative stress responses in fungal pathogenicity
    • Brown A.J., Haynes K., Quinn J. Nitrosative and oxidative stress responses in fungal pathogenicity. Current Opinion in Microbiology 2009, 12:384-391.
    • (2009) Current Opinion in Microbiology , vol.12 , pp. 384-391
    • Brown, A.J.1    Haynes, K.2    Quinn, J.3
  • 22
    • 0032540362 scopus 로고    scopus 로고
    • Flavohemoglobin expression and function in Saccharomyces cerevisiae. No relationship with respiration and complex response to oxidative stress
    • Buisson N., Labbe-Bois R. Flavohemoglobin expression and function in Saccharomyces cerevisiae. No relationship with respiration and complex response to oxidative stress. The Journal of Biological Chemistry 1998, 273:9527-9533.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 9527-9533
    • Buisson, N.1    Labbe-Bois, R.2
  • 26
    • 14844316642 scopus 로고    scopus 로고
    • Yeast flavohemoglobin, a nitric oxide oxidoreductase, is located in both the cytosol and the mitochondrial matrix: Effects of respiration, anoxia, and the mitochondrial genome on its intracellular level and distribution
    • Cassanova N., O'Brien K.M., Stahl B.T., McClure T., Poyton R.O. Yeast flavohemoglobin, a nitric oxide oxidoreductase, is located in both the cytosol and the mitochondrial matrix: Effects of respiration, anoxia, and the mitochondrial genome on its intracellular level and distribution. The Journal of Biological Chemistry 2005, 280:7645-7653.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 7645-7653
    • Cassanova, N.1    O'Brien, K.M.2    Stahl, B.T.3    McClure, T.4    Poyton, R.O.5
  • 27
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J. Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Molecular Biology and Evolution 2000, 17:540-552.
    • (2000) Molecular Biology and Evolution , vol.17 , pp. 540-552
    • Castresana, J.1
  • 29
    • 0344432210 scopus 로고
    • Pansporella perplexa, amoebiens à spores protégées parasite de daphnies. Réflections sur la biologie et la phylogénie des protozoaires
    • Chatton É. Pansporella perplexa, amoebiens à spores protégées parasite de daphnies. Réflections sur la biologie et la phylogénie des protozoaires. Annales Des Sciences Naturelles Zoologie 1925, 8:5-84.
    • (1925) Annales Des Sciences Naturelles Zoologie , vol.8 , pp. 5-84
    • Chatton, É.1
  • 33
    • 0033576249 scopus 로고    scopus 로고
    • Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme
    • Das T.K., Couture M., Lee H.C., Peisach J., Rousseau D.L., Wittenberg B.A., et al. Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: Evidence for ligation of tyrosine-63 (B10) to the heme. Biochemistry 1999, 38:15360-15368.
    • (1999) Biochemistry , vol.38 , pp. 15360-15368
    • Das, T.K.1    Couture, M.2    Lee, H.C.3    Peisach, J.4    Rousseau, D.L.5    Wittenberg, B.A.6
  • 36
    • 84875609542 scopus 로고    scopus 로고
    • Environmental survey meta-analysis reveals hidden diversity among unicellular opisthokonts
    • Del Campo J., Ruiz-Trillo I. Environmental survey meta-analysis reveals hidden diversity among unicellular opisthokonts. Molecular Biology and Evolution 2013, 30:802-805.
    • (2013) Molecular Biology and Evolution , vol.30 , pp. 802-805
    • Del Campo, J.1    Ruiz-Trillo, I.2
  • 38
    • 0024421175 scopus 로고
    • Human neutrophils activated by interferon-gamma and tumour necrosis factor-alpha kill Entamoeba histolytica trophozoites in vitro
    • Denis M., Chadee K. Human neutrophils activated by interferon-gamma and tumour necrosis factor-alpha kill Entamoeba histolytica trophozoites in vitro. Journal of Leukocyte Biology 1989, 46:270-274.
    • (1989) Journal of Leukocyte Biology , vol.46 , pp. 270-274
    • Denis, M.1    Chadee, K.2
  • 39
    • 0024467251 scopus 로고
    • Oxygen inhibition of globin gene transcription and bacterial haemoglobin synthesis in Vitreoscilla
    • Dikshit K.L., Spaulding D., Braun A., Webster D.A. Oxygen inhibition of globin gene transcription and bacterial haemoglobin synthesis in Vitreoscilla. Journal of General Microbiology 1989, 135:2601-2609.
    • (1989) Journal of General Microbiology , vol.135 , pp. 2601-2609
    • Dikshit, K.L.1    Spaulding, D.2    Braun, A.3    Webster, D.A.4
  • 40
    • 79959959356 scopus 로고    scopus 로고
    • T-Coffee: A web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension
    • Di Tommaso P., Moretti S., Xenarios I., Orobitg M., Montanyola A., Chang J.M., et al. T-Coffee: A web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension. Nucleic Acids Research 2011, 39:W13-W17.
    • (2011) Nucleic Acids Research , vol.39
    • Di Tommaso, P.1    Moretti, S.2    Xenarios, I.3    Orobitg, M.4    Montanyola, A.5    Chang, J.M.6
  • 41
    • 14644430471 scopus 로고    scopus 로고
    • ProbCons: Probabilistic consistency-based multiple sequence alignment
    • Do C.B., Mahabhashyam M.S., Brudno M., Batzoglou S. ProbCons: Probabilistic consistency-based multiple sequence alignment. Genome Research 2005, 15:330-340.
    • (2005) Genome Research , vol.15 , pp. 330-340
    • Do, C.B.1    Mahabhashyam, M.S.2    Brudno, M.3    Batzoglou, S.4
  • 43
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Research 2004, 32:1792-1797.
    • (2004) Nucleic Acids Research , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 45
    • 84867017278 scopus 로고    scopus 로고
    • New insights into the mechanism of electron transfer within flavohemoglobins: Tunnelling pathways, packing density, thermodynamic and kinetic analyses
    • El Hammi E., Houee-Levin C., Rezac J., Levy B., Demachy I., Baciou L., et al. New insights into the mechanism of electron transfer within flavohemoglobins: Tunnelling pathways, packing density, thermodynamic and kinetic analyses. Physical Chemistry Chemical Physics 2012, 14:13872-13880.
    • (2012) Physical Chemistry Chemical Physics , vol.14 , pp. 13872-13880
    • El Hammi, E.1    Houee-Levin, C.2    Rezac, J.3    Levy, B.4    Demachy, I.5    Baciou, L.6
  • 46
    • 79951598801 scopus 로고    scopus 로고
    • Structure of Ralstonia eutropha flavohemoglobin in complex with three antibiotic azole compounds
    • El Hammi E., Warkentin E., Demmer U., Limam F., Marzouki N.M., Ermler U., et al. Structure of Ralstonia eutropha flavohemoglobin in complex with three antibiotic azole compounds. Biochemistry 2011, 50:1255-1264.
    • (2011) Biochemistry , vol.50 , pp. 1255-1264
    • El Hammi, E.1    Warkentin, E.2    Demmer, U.3    Limam, F.4    Marzouki, N.M.5    Ermler, U.6
  • 47
    • 84870536044 scopus 로고    scopus 로고
    • Active site analysis of yeast flavohemoglobin based on its structure with a small ligand or econazole
    • El Hammi E., Warkentin E., Demmer U., Marzouki N.M., Ermler U., Baciou L. Active site analysis of yeast flavohemoglobin based on its structure with a small ligand or econazole. The FEBS Journal 2012, 279:4565-4575.
    • (2012) The FEBS Journal , vol.279 , pp. 4565-4575
    • El Hammi, E.1    Warkentin, E.2    Demmer, U.3    Marzouki, N.M.4    Ermler, U.5    Baciou, L.6
  • 48
    • 0029610660 scopus 로고
    • Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75Å resolution
    • Ermler U., Siddiqui R.A., Cramm R., Friedrich B. Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75Å resolution. The EMBO Journal 1995, 14:6067-6077.
    • (1995) The EMBO Journal , vol.14 , pp. 6067-6077
    • Ermler, U.1    Siddiqui, R.A.2    Cramm, R.3    Friedrich, B.4
  • 49
    • 3543070252 scopus 로고
    • First steps in experimental microscopy, Leeuwenhoek as practical scientist
    • Ford B.J. First steps in experimental microscopy, Leeuwenhoek as practical scientist. Microscope 1995, 43:47-57.
    • (1995) Microscope , vol.43 , pp. 47-57
    • Ford, B.J.1
  • 50
    • 84865477384 scopus 로고    scopus 로고
    • Response to: "Is flavohemoglobin a nitric oxide dioxygenase?"
    • Forrester M.T., Foster M.W. Response to: "Is flavohemoglobin a nitric oxide dioxygenase?". Free Radical Biology & Medicine 2012, 53:1211-1212.
    • (2012) Free Radical Biology & Medicine , vol.53 , pp. 1211-1212
    • Forrester, M.T.1    Foster, M.W.2
  • 51
    • 84858964958 scopus 로고    scopus 로고
    • Protection from nitrosative stress: A central role for microbial flavohemoglobin
    • Forrester M.T., Foster M.W. Protection from nitrosative stress: A central role for microbial flavohemoglobin. Free Radical Biology & Medicine 2012, 52:1620-1633.
    • (2012) Free Radical Biology & Medicine , vol.52 , pp. 1620-1633
    • Forrester, M.T.1    Foster, M.W.2
  • 52
    • 10444268100 scopus 로고    scopus 로고
    • Globin-coupled sensors, protoglobins, and the last universal common ancestor
    • Freitas T.A., Saito J.A., Hou S., Alam M. Globin-coupled sensors, protoglobins, and the last universal common ancestor. Journal of Inorganic Biochemistry 2005, 99:23-33.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , pp. 23-33
    • Freitas, T.A.1    Saito, J.A.2    Hou, S.3    Alam, M.4
  • 53
    • 79959696175 scopus 로고    scopus 로고
    • The single-domain globin of Vitreoscilla: Augmentation of aerobic metabolism for biotechnological applications
    • Frey A.D., Shepherd M., Jokipii-Lukkari S., Haggman H., Kallio P.T. The single-domain globin of Vitreoscilla: Augmentation of aerobic metabolism for biotechnological applications. Advances in Microbial Physiology 2011, 58:81-139.
    • (2011) Advances in Microbial Physiology , vol.58 , pp. 81-139
    • Frey, A.D.1    Shepherd, M.2    Jokipii-Lukkari, S.3    Haggman, H.4    Kallio, P.T.5
  • 54
    • 79960009200 scopus 로고    scopus 로고
    • The Naegleria genome: A free-living microbial eukaryote lends unique insights into core eukaryotic cell biology
    • Fritz-Laylin L.K., Ginger M.L., Walsh C., Dawson S.C., Fulton C. The Naegleria genome: A free-living microbial eukaryote lends unique insights into core eukaryotic cell biology. Research in Microbiology 2011, 162:607-618.
    • (2011) Research in Microbiology , vol.162 , pp. 607-618
    • Fritz-Laylin, L.K.1    Ginger, M.L.2    Walsh, C.3    Dawson, S.C.4    Fulton, C.5
  • 55
    • 67649117771 scopus 로고    scopus 로고
    • Genome-wide identification and characterization of cytochrome P450 monooxygenase genes in the ciliate Tetrahymena thermophila
    • Fu C., Xiong J., Miao W. Genome-wide identification and characterization of cytochrome P450 monooxygenase genes in the ciliate Tetrahymena thermophila. BMC Genomics 2009, 10:208.
    • (2009) BMC Genomics , vol.10 , pp. 208
    • Fu, C.1    Xiong, J.2    Miao, W.3
  • 56
    • 10644291828 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • Gardner P.R. Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases. Journal of Inorganic Biochemistry 2005, 99:247-266.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , pp. 247-266
    • Gardner, P.R.1
  • 57
    • 84877806490 scopus 로고    scopus 로고
    • Hemoglobin, a nitric oxide dioxygenase
    • Gardner P.R. Hemoglobin, a nitric oxide dioxygenase. Scientifica 2012, 2012:1-34.
    • (2012) Scientifica , vol.2012 , pp. 1-34
    • Gardner, P.R.1
  • 58
    • 0037040980 scopus 로고    scopus 로고
    • Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity
    • Gardner A.M., Gardner P.R. Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity. The Journal of Biological Chemistry 2002, 277:8166-8171.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 8166-8171
    • Gardner, A.M.1    Gardner, P.R.2
  • 60
    • 34250745705 scopus 로고    scopus 로고
    • NsrR: A key regulator circumventing Salmonella enterica serovar Typhimurium oxidative and nitrosative stress in vitro and in IFN-gamma-stimulated J774.2 macrophages
    • Gilberthorpe N.J., Lee M.E., Stevanin T.M., Read R.C., Poole R.K. NsrR: A key regulator circumventing Salmonella enterica serovar Typhimurium oxidative and nitrosative stress in vitro and in IFN-gamma-stimulated J774.2 macrophages. Microbiology 2007, 153:1756-1771.
    • (2007) Microbiology , vol.153 , pp. 1756-1771
    • Gilberthorpe, N.J.1    Lee, M.E.2    Stevanin, T.M.3    Read, R.C.4    Poole, R.K.5
  • 61
    • 33847778041 scopus 로고    scopus 로고
    • Resistance of Leishmania (Leishmania) amazonensis and Leishmania (Viannia) braziliensis to nitric oxide correlates with disease severity in Tegumentary Leishmaniasis
    • Giudice A., Camada I., Leopoldo P.T., Pereira J.M., Riley L.W., Wilson M.E., et al. Resistance of Leishmania (Leishmania) amazonensis and Leishmania (Viannia) braziliensis to nitric oxide correlates with disease severity in Tegumentary Leishmaniasis. BMC Infectious Diseases 2007, 7:7.
    • (2007) BMC Infectious Diseases , vol.7 , pp. 7
    • Giudice, A.1    Camada, I.2    Leopoldo, P.T.3    Pereira, J.M.4    Riley, L.W.5    Wilson, M.E.6
  • 62
    • 0033915318 scopus 로고    scopus 로고
    • L-Arginine availability modulates local nitric oxide production and parasite killing in experimental trypanosomiasis
    • Gobert A.P., Daulouede S., Lepoivre M., Boucher J.L., Bouteille B., Buguet A., et al. l-Arginine availability modulates local nitric oxide production and parasite killing in experimental trypanosomiasis. Infection and Immunity 2000, 68:4653-4657.
    • (2000) Infection and Immunity , vol.68 , pp. 4653-4657
    • Gobert, A.P.1    Daulouede, S.2    Lepoivre, M.3    Boucher, J.L.4    Bouteille, B.5    Buguet, A.6
  • 63
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • Gough J., Karplus K., Hughey R., Chothia C. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. Journal of Molecular Biology 2001, 313:903-919.
    • (2001) Journal of Molecular Biology , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 64
    • 0034729657 scopus 로고    scopus 로고
    • The hypersensitive response facilitates plant infection by the necrotrophic pathogen Botrytis cinerea
    • Govrin E.M., Levine A. The hypersensitive response facilitates plant infection by the necrotrophic pathogen Botrytis cinerea. Current Biology 2000, 10:751-757.
    • (2000) Current Biology , vol.10 , pp. 751-757
    • Govrin, E.M.1    Levine, A.2
  • 67
    • 0025191159 scopus 로고
    • Activated macrophages destroy intracellular Leishmania major amastigotes by an l-arginine-dependent killing mechanism
    • Green S.J., Meltzer M.S., Hibbs J.B., Nacy C.A. Activated macrophages destroy intracellular Leishmania major amastigotes by an l-arginine-dependent killing mechanism. Journal of Immunology 1990, 144:278-283.
    • (1990) Journal of Immunology , vol.144 , pp. 278-283
    • Green, S.J.1    Meltzer, M.S.2    Hibbs, J.B.3    Nacy, C.A.4
  • 68
    • 84875623291 scopus 로고    scopus 로고
    • The protist ribosomal reference database (PR2): A catalog of unicellular eukaryote small sub-unit rRNA sequences with curated taxonomy
    • Guillou L., Bachar D., Audic S., Bass D., Berney C., Bittner L., et al. The protist ribosomal reference database (PR2): A catalog of unicellular eukaryote small sub-unit rRNA sequences with curated taxonomy. Nucleic Acids Research 2013, 41:D597-D604.
    • (2013) Nucleic Acids Research , vol.41
    • Guillou, L.1    Bachar, D.2    Audic, S.3    Bass, D.4    Berney, C.5    Bittner, L.6
  • 69
    • 84867206822 scopus 로고    scopus 로고
    • How many species of algae are there?
    • Guiry M.D. How many species of algae are there?. Journal of Phycology 2012, 48:1057-1063.
    • (2012) Journal of Phycology , vol.48 , pp. 1057-1063
    • Guiry, M.D.1
  • 73
    • 33751357738 scopus 로고    scopus 로고
    • Trichomonas vaginalis and Giardia intestinalis produce nitric oxide and display NO-synthase activity
    • Harris K.M., Goldberg B., Biagini G.A., Lloyd D. Trichomonas vaginalis and Giardia intestinalis produce nitric oxide and display NO-synthase activity. Journal of Eukaryotic Microbiology 2006, 53(Suppl. 1):S182-S183.
    • (2006) Journal of Eukaryotic Microbiology , vol.53 , Issue.SUPPL. 1
    • Harris, K.M.1    Goldberg, B.2    Biagini, G.A.3    Lloyd, D.4
  • 74
    • 42149185064 scopus 로고    scopus 로고
    • Molecular physiology of bestrophins: Multifunctional membrane proteins linked to best disease and other retinopathies
    • Hartzell H.C., Qu Z., Yu K., Xiao Q., Chien L.T. Molecular physiology of bestrophins: Multifunctional membrane proteins linked to best disease and other retinopathies. Physiological Reviews 2008, 88:639-672.
    • (2008) Physiological Reviews , vol.88 , pp. 639-672
    • Hartzell, H.C.1    Qu, Z.2    Yu, K.3    Xiao, Q.4    Chien, L.T.5
  • 76
    • 2942568227 scopus 로고    scopus 로고
    • A molecular timescale of eukaryote evolution and the rise of complex multicellular life
    • Hedges S.B., Blair J.E., Venturi M.L., Shoe J.L. A molecular timescale of eukaryote evolution and the rise of complex multicellular life. BMC Evolutionary Biology 2004, 4:2.
    • (2004) BMC Evolutionary Biology , vol.4 , pp. 2
    • Hedges, S.B.1    Blair, J.E.2    Venturi, M.L.3    Shoe, J.L.4
  • 79
    • 84862220577 scopus 로고    scopus 로고
    • Non-symbiotic haemoglobins-What's happening beyond nitric oxide scavenging?
    • pls004
    • Hill R.D. Non-symbiotic haemoglobins-What's happening beyond nitric oxide scavenging?. AoB Plants 2012, 2012:pls004.
    • (2012) AoB Plants , vol.2012
    • Hill, R.D.1
  • 81
    • 84861376715 scopus 로고    scopus 로고
    • Whole-genome duplications spurred the functional diversification of the globin gene superfamily in vertebrates
    • Hoffmann F.G., Opazo J.C., Storz J.F. Whole-genome duplications spurred the functional diversification of the globin gene superfamily in vertebrates. Molecular Biology and Evolution 2012, 29:303-312.
    • (2012) Molecular Biology and Evolution , vol.29 , pp. 303-312
    • Hoffmann, F.G.1    Opazo, J.C.2    Storz, J.F.3
  • 85
    • 26244433294 scopus 로고    scopus 로고
    • Transcriptional response of Candida albicans to nitric oxide and the role of the YHB1 gene in nitrosative stress and virulence
    • Hromatka B.S., Noble S.M., Johnson A.D. Transcriptional response of Candida albicans to nitric oxide and the role of the YHB1 gene in nitrosative stress and virulence. Molecular Biology of the Cell 2005, 16:4814-4826.
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 4814-4826
    • Hromatka, B.S.1    Noble, S.M.2    Johnson, A.D.3
  • 87
    • 79955783127 scopus 로고    scopus 로고
    • A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification
    • Igarashi J., Kobayashi K., Matsuoka A. A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification. Journal of Biological Inorganic Chemistry 2011, 16:599-609.
    • (2011) Journal of Biological Inorganic Chemistry , vol.16 , pp. 599-609
    • Igarashi, J.1    Kobayashi, K.2    Matsuoka, A.3
  • 88
    • 0034069127 scopus 로고    scopus 로고
    • Identification and characterization of two flavohemoglobin genes in Dictyostelium discoideum
    • Iijima M., Shimizu H., Tanaka Y., Urushihara H. Identification and characterization of two flavohemoglobin genes in Dictyostelium discoideum. Cell Structure and Function 2000, 25:47-55.
    • (2000) Cell Structure and Function , vol.25 , pp. 47-55
    • Iijima, M.1    Shimizu, H.2    Tanaka, Y.3    Urushihara, H.4
  • 89
    • 42949128139 scopus 로고    scopus 로고
    • Structural studies on flavohemoglobins
    • Ilari A., Boffi A. Structural studies on flavohemoglobins. Methods in Enzymology 2008, 436:187-202.
    • (2008) Methods in Enzymology , vol.436 , pp. 187-202
    • Ilari, A.1    Boffi, A.2
  • 91
    • 0024974873 scopus 로고
    • Protozoan myoglobin from Paramecium caudatum. Its unusual amino acid sequence
    • Iwaasa H., Takagi T., Shikama K. Protozoan myoglobin from Paramecium caudatum. Its unusual amino acid sequence. Journal of Molecular Biology 1989, 208:355-358.
    • (1989) Journal of Molecular Biology , vol.208 , pp. 355-358
    • Iwaasa, H.1    Takagi, T.2    Shikama, K.3
  • 92
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • Katoh K., Kuma K., Toh H., Miyata T. MAFFT version 5: Improvement in accuracy of multiple sequence alignment. Nucleic Acids Research 2005, 33:511-518.
    • (2005) Nucleic Acids Research , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 94
    • 0001149591 scopus 로고
    • Haemoglobin in Protozoa
    • Keilin D., Ryley J.F. Haemoglobin in Protozoa. Nature 1953, 172:451.
    • (1953) Nature , vol.172 , pp. 451
    • Keilin, D.1    Ryley, J.F.2
  • 95
    • 0024449797 scopus 로고
    • Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli. Implications for protein function
    • Khosla C., Bailey J.E. Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli. Implications for protein function. Journal of Molecular Biology 1989, 210:79-89.
    • (1989) Journal of Molecular Biology , vol.210 , pp. 79-89
    • Khosla, C.1    Bailey, J.E.2
  • 96
    • 77955208664 scopus 로고    scopus 로고
    • The possible involvement of copper-containing nitrite reductase (NirK) and flavohemoglobin in denitrification by the fungus Cylindrocarpon tonkinense
    • Kim S.W., Fushinobu S., Zhou S., Wakagi T., Shoun H. The possible involvement of copper-containing nitrite reductase (NirK) and flavohemoglobin in denitrification by the fungus Cylindrocarpon tonkinense. Bioscience, Biotechnology, and Biochemistry 2010, 74:1403-1407.
    • (2010) Bioscience, Biotechnology, and Biochemistry , vol.74 , pp. 1403-1407
    • Kim, S.W.1    Fushinobu, S.2    Zhou, S.3    Wakagi, T.4    Shoun, H.5
  • 98
    • 0034736304 scopus 로고    scopus 로고
    • A primitive myoglobin from Tetrahymena pyriformis: Its heme environment, autoxidizability, and genomic DNA structure
    • Korenaga S., Igarashi J., Matsuoka A., Shikama K. A primitive myoglobin from Tetrahymena pyriformis: Its heme environment, autoxidizability, and genomic DNA structure. Biochimica et Biophysica Acta 2000, 1543:131-145.
    • (2000) Biochimica et Biophysica Acta , vol.1543 , pp. 131-145
    • Korenaga, S.1    Igarashi, J.2    Matsuoka, A.3    Shikama, K.4
  • 99
    • 0018949161 scopus 로고
    • Effect of growth conditions on yield and heme content of Vitreoscilla
    • Lamba P., Webster D.A. Effect of growth conditions on yield and heme content of Vitreoscilla. Journal of Bacteriology 1980, 142:169-173.
    • (1980) Journal of Bacteriology , vol.142 , pp. 169-173
    • Lamba, P.1    Webster, D.A.2
  • 100
  • 102
    • 75149137411 scopus 로고    scopus 로고
    • Bacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: A novel mechanism of bacterial pathogenesis
    • Laver J.R., Stevanin T.M., Messenger S.L., Lunn A.D., Lee M.E., Moir J.W., et al. Bacterial nitric oxide detoxification prevents host cell S-nitrosothiol formation: A novel mechanism of bacterial pathogenesis. The FASEB Journal 2010, 24:286-295.
    • (2010) The FASEB Journal , vol.24 , pp. 286-295
    • Laver, J.R.1    Stevanin, T.M.2    Messenger, S.L.3    Lunn, A.D.4    Lee, M.E.5    Moir, J.W.6
  • 103
    • 84874927587 scopus 로고    scopus 로고
    • Neuroglobins, pivotal proteins associated with emerging neural systems and precursors of metazoan globin diversity
    • Lechauve C., Jager M., Laguerre L., Kiger L., Correc G., Leroux C., et al. Neuroglobins, pivotal proteins associated with emerging neural systems and precursors of metazoan globin diversity. The Journal of Biological Chemistry 2013, 288:6957-6967.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 6957-6967
    • Lechauve, C.1    Jager, M.2    Laguerre, L.3    Kiger, L.4    Correc, G.5    Leroux, C.6
  • 104
    • 33750989372 scopus 로고    scopus 로고
    • Yeast flavohemoglobin protects against nitrosative stress and controls ferric reductase activity
    • Lewinska A., Bartosz G. Yeast flavohemoglobin protects against nitrosative stress and controls ferric reductase activity. Redox Report 2006, 11:231-239.
    • (2006) Redox Report , vol.11 , pp. 231-239
    • Lewinska, A.1    Bartosz, G.2
  • 105
    • 0025300228 scopus 로고
    • Macrophage killing of Leishmania parasite in vivo is mediated by nitric oxide from l-arginine
    • Liew F.Y., Millott S., Parkinson C., Palmer R.M., Moncada S. Macrophage killing of Leishmania parasite in vivo is mediated by nitric oxide from l-arginine. Journal of Immunology 1990, 144:4794-4797.
    • (1990) Journal of Immunology , vol.144 , pp. 4794-4797
    • Liew, F.Y.1    Millott, S.2    Parkinson, C.3    Palmer, R.M.4    Moncada, S.5
  • 106
    • 0028329018 scopus 로고
    • Tumor necrosis factor alpha augments nitric oxide-dependent macrophage cytotoxicity against Entamoeba histolytica by enhanced expression of the nitric oxide synthase gene
    • Lin J.Y., Seguin R., Keller K., Chadee K. Tumor necrosis factor alpha augments nitric oxide-dependent macrophage cytotoxicity against Entamoeba histolytica by enhanced expression of the nitric oxide synthase gene. Infection and Immunity 1994, 62:1534-1541.
    • (1994) Infection and Immunity , vol.62 , pp. 1534-1541
    • Lin, J.Y.1    Seguin, R.2    Keller, K.3    Chadee, K.4
  • 108
    • 0035252640 scopus 로고    scopus 로고
    • Unexpected diversity of small eukaryotes in deep-sea Antarctic plankton
    • Lopez-Garcia P., Rodriguez-Valera F., Pedros-Alio C., Moreira D. Unexpected diversity of small eukaryotes in deep-sea Antarctic plankton. Nature 2001, 409:603-607.
    • (2001) Nature , vol.409 , pp. 603-607
    • Lopez-Garcia, P.1    Rodriguez-Valera, F.2    Pedros-Alio, C.3    Moreira, D.4
  • 109
    • 22244479035 scopus 로고    scopus 로고
    • Nitric oxide and hydrogen peroxide in tomato resistance. Nitric oxide modulates hydrogen peroxide level in o-hydroxyethylorutin-induced resistance to Botrytis cinerea in tomato
    • Malolepsza U., Rozalska S. Nitric oxide and hydrogen peroxide in tomato resistance. Nitric oxide modulates hydrogen peroxide level in o-hydroxyethylorutin-induced resistance to Botrytis cinerea in tomato. Plant Physiology and Biochemistry 2005, 43:623-635.
    • (2005) Plant Physiology and Biochemistry , vol.43 , pp. 623-635
    • Malolepsza, U.1    Rozalska, S.2
  • 113
    • 0035863151 scopus 로고    scopus 로고
    • Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide
    • Mills C.E., Sedelnikova S., Soballe B., Hughes M.N., Poole R.K. Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide. The Biochemical Journal 2001, 353:207-213.
    • (2001) The Biochemical Journal , vol.353 , pp. 207-213
    • Mills, C.E.1    Sedelnikova, S.2    Soballe, B.3    Hughes, M.N.4    Poole, R.K.5
  • 114
    • 0035252376 scopus 로고    scopus 로고
    • Oceanic 18S rDNA sequences from picoplankton reveal unsuspected eukaryotic diversity
    • Moon-van der Staay S.Y., De Wachter R., Vaulot D. Oceanic 18S rDNA sequences from picoplankton reveal unsuspected eukaryotic diversity. Nature 2001, 409:607-610.
    • (2001) Nature , vol.409 , pp. 607-610
    • Moon-van der Staay, S.Y.1    De Wachter, R.2    Vaulot, D.3
  • 115
    • 31544432566 scopus 로고    scopus 로고
    • NO way to live; the various roles of nitric oxide in plant-pathogen interactions
    • Mur L.A.J., Carver T.L.W., Prats E. NO way to live; the various roles of nitric oxide in plant-pathogen interactions. Journal of Experimental Botany 2006, 57:489-505.
    • (2006) Journal of Experimental Botany , vol.57 , pp. 489-505
    • Mur, L.A.J.1    Carver, T.L.W.2    Prats, E.3
  • 118
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K., Horton P. PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends in Biochemical Sciences 1999, 24:34-36.
    • (1999) Trends in Biochemical Sciences , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 120
    • 84868159385 scopus 로고    scopus 로고
    • Diverse lifestyles and strategies of plant pathogenesis encoded in the genomes of eighteen Dothideomycetes fungi
    • Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W., et al. Diverse lifestyles and strategies of plant pathogenesis encoded in the genomes of eighteen Dothideomycetes fungi. PLoS Pathogens 2012, 8:e1003037.
    • (2012) PLoS Pathogens , vol.8
    • Ohm, R.A.1    Feau, N.2    Henrissat, B.3    Schoch, C.L.4    Horwitz, B.A.5    Barry, K.W.6
  • 121
    • 0036740889 scopus 로고    scopus 로고
    • Nitric oxide negatively modulates wound signaling in tomato plants
    • Orozco-Cardenas M.L., Ryan C.A. Nitric oxide negatively modulates wound signaling in tomato plants. Plant Physiology and Biochemistry 2002, 130:487-493.
    • (2002) Plant Physiology and Biochemistry , vol.130 , pp. 487-493
    • Orozco-Cardenas, M.L.1    Ryan, C.A.2
  • 124
    • 0141728071 scopus 로고
    • The oxygen equilibrium of yeast hemoglobin
    • Oshino R., Oshino N., Chance B. The oxygen equilibrium of yeast hemoglobin. FEBS Letters 1971, 19:96-100.
    • (1971) FEBS Letters , vol.19 , pp. 96-100
    • Oshino, R.1    Oshino, N.2    Chance, B.3
  • 125
    • 0015885088 scopus 로고
    • Studies on yeast hemoglobin. The properties of yeast hemoglobin and its physiological function in the cell
    • Oshino R., Oshino N., Chance B. Studies on yeast hemoglobin. The properties of yeast hemoglobin and its physiological function in the cell. European Journal of Biochemistry 1973, 35:23-33.
    • (1973) European Journal of Biochemistry , vol.35 , pp. 23-33
    • Oshino, R.1    Oshino, N.2    Chance, B.3
  • 129
    • 0034213366 scopus 로고    scopus 로고
    • A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family
    • Pesce A., Couture M., Dewilde S., Guertin M., Yamauchi K., Ascenzi P., et al. A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family. The EMBO Journal 2000, 19:2424-2434.
    • (2000) The EMBO Journal , vol.19 , pp. 2424-2434
    • Pesce, A.1    Couture, M.2    Dewilde, S.3    Guertin, M.4    Yamauchi, K.5    Ascenzi, P.6
  • 131
    • 0028324494 scopus 로고
    • Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: Evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing
    • Poole R.K., Ioannidis N., Orii Y. Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: Evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing. Proceedings of the Royal Society B: Biological Sciences 1994, 255:251-258.
    • (1994) Proceedings of the Royal Society B: Biological Sciences , vol.255 , pp. 251-258
    • Poole, R.K.1    Ioannidis, N.2    Orii, Y.3
  • 132
    • 49549097135 scopus 로고    scopus 로고
    • Pathogen-derived nitric oxide influences formation of the appressorium infection structure in the phytopathogenic fungus Blumeria graminis
    • Prats E., Carver T.L., Mur L.A. Pathogen-derived nitric oxide influences formation of the appressorium infection structure in the phytopathogenic fungus Blumeria graminis. Research in Microbiology 2008, 159:476-480.
    • (2008) Research in Microbiology , vol.159 , pp. 476-480
    • Prats, E.1    Carver, T.L.2    Mur, L.A.3
  • 133
    • 0017068536 scopus 로고
    • Respiratory components and oxidase activities in Alcaligenes eutrophus
    • Probst I., Schlegel H.G. Respiratory components and oxidase activities in Alcaligenes eutrophus. Biochimica et Biophysica Acta 1976, 440:412-428.
    • (1976) Biochimica et Biophysica Acta , vol.440 , pp. 412-428
    • Probst, I.1    Schlegel, H.G.2
  • 134
    • 0018801772 scopus 로고
    • An oxygen-binding flavohemoprotein from Alcaligenes eutrophus
    • Probst I., Wolf G., Schlegel H.G. An oxygen-binding flavohemoprotein from Alcaligenes eutrophus. Biochimica et Biophysica Acta 1979, 576:471-478.
    • (1979) Biochimica et Biophysica Acta , vol.576 , pp. 471-478
    • Probst, I.1    Wolf, G.2    Schlegel, H.G.3
  • 138
    • 19044373265 scopus 로고    scopus 로고
    • Nitric oxide generation during the interaction with Phytophthora capsici of two Capsicum annuum varieties showing different degrees of sensitivity
    • Requena M.-E., Egea-Gilabert C., Candela M.-E. Nitric oxide generation during the interaction with Phytophthora capsici of two Capsicum annuum varieties showing different degrees of sensitivity. Physiologia Plantarum 2005, 124:50-60.
    • (2005) Physiologia Plantarum , vol.124 , pp. 50-60
    • Requena, M.-E.1    Egea-Gilabert, C.2    Candela, M.-E.3
  • 140
    • 60349108359 scopus 로고    scopus 로고
    • Evolution: Revisiting the root of the eukaryote tree
    • Roger A.J., Simpson A.G. Evolution: Revisiting the root of the eukaryote tree. Current Biology 2009, 19:R165-R167.
    • (2009) Current Biology , vol.19
    • Roger, A.J.1    Simpson, A.G.2
  • 141
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F., Huelsenbeck J.P. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 2003, 19:1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 143
    • 0024679708 scopus 로고
    • Protozoa, Protista, Protoctista: What's in a name?
    • Rothschild L.J. Protozoa, Protista, Protoctista: What's in a name?. Journal of the History of Biology 1989, 22:277-305.
    • (1989) Journal of the History of Biology , vol.22 , pp. 277-305
    • Rothschild, L.J.1
  • 145
    • 33748607486 scopus 로고    scopus 로고
    • Insights into the evolutionary origin and genome architecture of the unicellular opisthokonts Capsaspora owczarzaki and Sphaeroforma arctica
    • Ruiz-Trillo I., Lane C.E., Archibald J.M., Roger A.J. Insights into the evolutionary origin and genome architecture of the unicellular opisthokonts Capsaspora owczarzaki and Sphaeroforma arctica. Journal of Eukaryotic Microbiology 2006, 53:379-384.
    • (2006) Journal of Eukaryotic Microbiology , vol.53 , pp. 379-384
    • Ruiz-Trillo, I.1    Lane, C.E.2    Archibald, J.M.3    Roger, A.J.4
  • 147
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler J.E. Biochemistry and genetics of von Willebrand factor. Annual Review of Biochemistry 1998, 67:395-424.
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 148
    • 84863179892 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-sensing mechanism is activated in Entamoeba histolytica upon treatment with nitric oxide
    • Santi-Rocca J., Smith S., Weber C., Pineda E., Hon C.C., Saavedra E., et al. Endoplasmic reticulum stress-sensing mechanism is activated in Entamoeba histolytica upon treatment with nitric oxide. PLoS One 2012, 7:e31777.
    • (2012) PLoS One , vol.7
    • Santi-Rocca, J.1    Smith, S.2    Weber, C.3    Pineda, E.4    Hon, C.C.5    Saavedra, E.6
  • 149
    • 1642318820 scopus 로고    scopus 로고
    • Trichomonas vaginalis degrades nitric oxide and expresses a flavorubredoxin-like protein: A new pathogenic mechanism?
    • Sarti P., Fiori P.L., Forte E., Rappelli P., Teixeira M., Mastronicola D., et al. Trichomonas vaginalis degrades nitric oxide and expresses a flavorubredoxin-like protein: A new pathogenic mechanism?. Cellular and Molecular Life Sciences 2004, 61:618-623.
    • (2004) Cellular and Molecular Life Sciences , vol.61 , pp. 618-623
    • Sarti, P.1    Fiori, P.L.2    Forte, E.3    Rappelli, P.4    Teixeira, M.5    Mastronicola, D.6
  • 150
    • 0033287214 scopus 로고    scopus 로고
    • Not plants or animals: A brief history of the origin of Kingdoms Protozoa, Protista and Protoctista
    • Scamardella J.M. Not plants or animals: A brief history of the origin of Kingdoms Protozoa, Protista and Protoctista. International Microbiology 1999, 2:207-216.
    • (1999) International Microbiology , vol.2 , pp. 207-216
    • Scamardella, J.M.1
  • 151
    • 0035878724 scopus 로고    scopus 로고
    • Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements
    • Schaffer A.A., Aravind L., Madden T.L., Shavirin S., Spouge J.L., Wolf Y.I., et al. Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements. Nucleic Acids Research 2001, 29:2994-3005.
    • (2001) Nucleic Acids Research , vol.29 , pp. 2994-3005
    • Schaffer, A.A.1    Aravind, L.2    Madden, T.L.3    Shavirin, S.4    Spouge, J.L.5    Wolf, Y.I.6
  • 153
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J., Blundell T.L., Mizuguchi K. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. Journal of Molecular Biology 2001, 310:243-257.
    • (2001) Journal of Molecular Biology , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 154
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F., Wilm A., Dineen D., Gibson T.J., Karplus K., Li W., et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Molecular Systems Biology 2011, 7:539.
    • (2011) Molecular Systems Biology , vol.7 , pp. 539
    • Sievers, F.1    Wilm, A.2    Dineen, D.3    Gibson, T.J.4    Karplus, K.5    Li, W.6
  • 155
    • 0037108318 scopus 로고    scopus 로고
    • Eukaryotic evolution: Getting to the root of the problem
    • Simpson A.G., Roger A.J. Eukaryotic evolution: Getting to the root of the problem. Current Biology 2002, 12:R691-R693.
    • (2002) Current Biology , vol.12
    • Simpson, A.G.1    Roger, A.J.2
  • 158
    • 0031893975 scopus 로고    scopus 로고
    • Evolution of the protists and protistan parasites from the perspective of molecular systematics
    • Sogin M.L., Silberman J.D. Evolution of the protists and protistan parasites from the perspective of molecular systematics. International Journal for Parasitology 1998, 28:11-20.
    • (1998) International Journal for Parasitology , vol.28 , pp. 11-20
    • Sogin, M.L.1    Silberman, J.D.2
  • 159
    • 50249100595 scopus 로고    scopus 로고
    • A rapid bootstrap algorithm for the RAxML Web servers
    • Stamatakis A., Hoover P., Rougemont J. A rapid bootstrap algorithm for the RAxML Web servers. Systematic Biology 2008, 57:758-771.
    • (2008) Systematic Biology , vol.57 , pp. 758-771
    • Stamatakis, A.1    Hoover, P.2    Rougemont, J.3
  • 161
    • 0036070723 scopus 로고    scopus 로고
    • Flavohemoglobin Hmp protects Salmonella enterica serovar typhimurium from nitric oxide-related killing by human macrophages
    • Stevanin T.M., Poole R.K., Demoncheaux E.A., Read R.C. Flavohemoglobin Hmp protects Salmonella enterica serovar typhimurium from nitric oxide-related killing by human macrophages. Infection and Immunity 2002, 70:4399-4405.
    • (2002) Infection and Immunity , vol.70 , pp. 4399-4405
    • Stevanin, T.M.1    Poole, R.K.2    Demoncheaux, E.A.3    Read, R.C.4
  • 162
    • 84855960615 scopus 로고    scopus 로고
    • Analysis of raphidophyte assimilatory nitrate reductase reveals unique domain architecture incorporating a 2/2 hemoglobin
    • Stewart J.J., Coyne K.J. Analysis of raphidophyte assimilatory nitrate reductase reveals unique domain architecture incorporating a 2/2 hemoglobin. Plant Molecular Biology 2011, 77:565-575.
    • (2011) Plant Molecular Biology , vol.77 , pp. 565-575
    • Stewart, J.J.1    Coyne, K.J.2
  • 163
    • 84873096226 scopus 로고    scopus 로고
    • Gene duplication, genome duplication, and the functional diversification of vertebrate globins
    • Storz J.F., Opazo J.C., Hoffmann F.G. Gene duplication, genome duplication, and the functional diversification of vertebrate globins. Molecular Phylogenetics and Evolution 2013, 66:469-478.
    • (2013) Molecular Phylogenetics and Evolution , vol.66 , pp. 469-478
    • Storz, J.F.1    Opazo, J.C.2    Hoffmann, F.G.3
  • 165
    • 0030799397 scopus 로고    scopus 로고
    • Purification and characterization of a flavohemoglobin from the denitrifying fungus Fusarium oxysporum
    • Takaya N., Suzuki S., Matsuo M., Shoun H. Purification and characterization of a flavohemoglobin from the denitrifying fungus Fusarium oxysporum. FEBS Letters 1997, 414:545-548.
    • (1997) FEBS Letters , vol.414 , pp. 545-548
    • Takaya, N.1    Suzuki, S.2    Matsuo, M.3    Shoun, H.4
  • 166
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Molecular Biology and Evolution 2011, 28:2731-2739.
    • (2011) Molecular Biology and Evolution , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 167
    • 77949328035 scopus 로고    scopus 로고
    • Phylogeny of fungal hemoglobins and expression analysis of the Aspergillus oryzae flavohemoglobin gene fhbA during hyphal growth
    • Te Biesebeke R., Levasseur A., Boussier A., Record E., van den Hondel C.A., Punt P.J. Phylogeny of fungal hemoglobins and expression analysis of the Aspergillus oryzae flavohemoglobin gene fhbA during hyphal growth. Fungal Biology 2010, 114:135-143.
    • (2010) Fungal Biology , vol.114 , pp. 135-143
    • Te Biesebeke, R.1    Levasseur, A.2    Boussier, A.3    Record, E.4    van den Hondel, C.A.5    Punt, P.J.6
  • 168
    • 84855881484 scopus 로고    scopus 로고
    • Phylogenetic relationships within the Opisthokonta based on phylogenomic analyses of conserved single-copy protein domains
    • Torruella G., Derelle R., Paps J., Lang B.F., Roger A.J., Shalchian-Tabrizi K., et al. Phylogenetic relationships within the Opisthokonta based on phylogenomic analyses of conserved single-copy protein domains. Molecular Biology and Evolution 2012, 29:531-544.
    • (2012) Molecular Biology and Evolution , vol.29 , pp. 531-544
    • Torruella, G.1    Derelle, R.2    Paps, J.3    Lang, B.F.4    Roger, A.J.5    Shalchian-Tabrizi, K.6
  • 169
    • 77950866481 scopus 로고    scopus 로고
    • The flavohemoglobin BCFHG1 is the main NO detoxification system and confers protection against nitrosative conditions but is not a virulence factor in the fungal necrotroph Botrytis cinerea
    • Turrion-Gomez J.L., Eslava A.P., Benito E.P. The flavohemoglobin BCFHG1 is the main NO detoxification system and confers protection against nitrosative conditions but is not a virulence factor in the fungal necrotroph Botrytis cinerea. Fungal Genetics and Biology 2010, 47:484-496.
    • (2010) Fungal Genetics and Biology , vol.47 , pp. 484-496
    • Turrion-Gomez, J.L.1    Eslava, A.P.2    Benito, E.P.3
  • 174
    • 42949118797 scopus 로고    scopus 로고
    • Tracing globin phylogeny using PSIBLAST searches based on groups of sequences
    • Vinogradov S.N. Tracing globin phylogeny using PSIBLAST searches based on groups of sequences. Methods in Enzymology 2008, 436:571-583.
    • (2008) Methods in Enzymology , vol.436 , pp. 571-583
    • Vinogradov, S.N.1
  • 175
    • 79551530357 scopus 로고    scopus 로고
    • Phylogenetic relationships of 3/3 and 2/2 hemoglobins in Archaeplastida genomes to bacterial and other eukaryote hemoglobins
    • Vinogradov S.N., Fernandez I., Hoogewijs D., Arredondo-Peter R. Phylogenetic relationships of 3/3 and 2/2 hemoglobins in Archaeplastida genomes to bacterial and other eukaryote hemoglobins. Molecular Plant 2011, 4:42-58.
    • (2011) Molecular Plant , vol.4 , pp. 42-58
    • Vinogradov, S.N.1    Fernandez, I.2    Hoogewijs, D.3    Arredondo-Peter, R.4
  • 181
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: Enzymatic, transport, storage, and sensing
    • Vinogradov S.N., Moens L. Diversity of globin function: Enzymatic, transport, storage, and sensing. The Journal of Biological Chemistry 2008, 283:8773-8777.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 183
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • Vuletich D.A., Lecomte J.T. A phylogenetic and structural analysis of truncated hemoglobins. Journal of Molecular Evolution 2006, 62:196-210.
    • (2006) Journal of Molecular Evolution , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.2
  • 184
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • Wittenberg J.B., Bolognesi M., Wittenberg B.A., Guertin M. Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. The Journal of Biological Chemistry 2002, 277:871-874.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 187
    • 0026498290 scopus 로고
    • The unique structure of the Paramecium caudatum hemoglobin gene: The presence of one intron in the middle of the coding region
    • Yamauchi K., Ochiai T., Usuki I. The unique structure of the Paramecium caudatum hemoglobin gene: The presence of one intron in the middle of the coding region. Biochimica et Biophysica Acta 1992, 1171:81-87.
    • (1992) Biochimica et Biophysica Acta , vol.1171 , pp. 81-87
    • Yamauchi, K.1    Ochiai, T.2    Usuki, I.3
  • 188
    • 0027192969 scopus 로고
    • Structure of the Paramecium caudatum gene encoding the B-type of the major hemoglobin component
    • Yamauchi K., Tada H., Ochiai T., Usuki I. Structure of the Paramecium caudatum gene encoding the B-type of the major hemoglobin component. Gene 1993, 126:243-246.
    • (1993) Gene , vol.126 , pp. 243-246
    • Yamauchi, K.1    Tada, H.2    Ochiai, T.3    Usuki, I.4
  • 189
  • 190
    • 0028791575 scopus 로고
    • Serum antibodies to Trichomonas vaginalis in invasive cervical cancer patients
    • Yap E.H., Ho T.H., Chan Y.C., Thong T.W., Ng G.C., Ho L.C., et al. Serum antibodies to Trichomonas vaginalis in invasive cervical cancer patients. Genitourinary Medicine 1995, 71:402-404.
    • (1995) Genitourinary Medicine , vol.71 , pp. 402-404
    • Yap, E.H.1    Ho, T.H.2    Chan, Y.C.3    Thong, T.W.4    Ng, G.C.5    Ho, L.C.6
  • 191
    • 0033759647 scopus 로고    scopus 로고
    • Dependence of Trichomonas vaginalis upon polyamine backconversion
    • Yarlett N., Martinez M.P., Goldberg B., Kramer D.L., Porter C.W. Dependence of Trichomonas vaginalis upon polyamine backconversion. Microbiology 2000, 146(Pt 10):2715-2722.
    • (2000) Microbiology , vol.146 , Issue.PART 10 , pp. 2715-2722
    • Yarlett, N.1    Martinez, M.P.2    Goldberg, B.3    Kramer, D.L.4    Porter, C.W.5
  • 192
    • 0029818837 scopus 로고    scopus 로고
    • Function and expression of flavohemoglobin in Saccharomyces cerevisiae. Evidence for a role in the oxidative stress response
    • Zhao X.J., Raitt D., Burke P.V., Clewell A.S., Kwast K.E., Poyton R.O. Function and expression of flavohemoglobin in Saccharomyces cerevisiae. Evidence for a role in the oxidative stress response. The Journal of Biological Chemistry 1996, 271:25131-25138.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 25131-25138
    • Zhao, X.J.1    Raitt, D.2    Burke, P.V.3    Clewell, A.S.4    Kwast, K.E.5    Poyton, R.O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.