메뉴 건너뛰기




Volumn 6, Issue JUN, 2015, Pages

Why study moonlighting proteins?

Author keywords

Enzyme function; Moonlighting proteins; Multifunctional; Protein evolution; Protein structure and function

Indexed keywords

ACONITATE HYDRATASE; ALDEHYDE DEHYDROGENASE; DELTA CRYSTALLIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLYCERALDEHYDE 3 PHOSPHATE; MOONLIGHTING PROTEIN; PROTEIN; THYMIDYLATE SYNTHASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RFAH; UNCLASSIFIED DRUG;

EID: 84940104582     PISSN: None     EISSN: 16648021     Source Type: Journal    
DOI: 10.3389/fgene.2015.00211     Document Type: Note
Times cited : (91)

References (58)
  • 1
    • 52449135569 scopus 로고    scopus 로고
    • Alpha-enolase binds to human plasminogen on the surface of Bacillus anthracis
    • Agarwal, S., Kulshreshtha, P., Bambah Mukku, D., and Bhatnagar, R. (2008). Alpha-enolase binds to human plasminogen on the surface of Bacillus anthracis. Biochim. Biophys. Acta 1784, 986-994. doi: 10.1016/j.bbapap.2008.03.017.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 986-994
    • Agarwal, S.1    Kulshreshtha, P.2    Bambah Mukku, D.3    Bhatnagar, R.4
  • 2
    • 34249815828 scopus 로고    scopus 로고
    • Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase
    • Banerjee, S., Nandyala, A. K., Raviprasad, P., Ahmed, N., and Hasnain, S. E. (2007). Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase. J. Bacteriol. 189, 4046-4052. doi: 10.1128/JB.00026-07.
    • (2007) J. Bacteriol , vol.189 , pp. 4046-4052
    • Banerjee, S.1    Nandyala, A.K.2    Raviprasad, P.3    Ahmed, N.4    Hasnain, S.E.5
  • 3
    • 29644437769 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein, involved in fungal adhesion to extracellular matrix proteins and interaction with cells
    • Barbosa, M. S., Bao, S. N., Andreotti, P. F., de Faria, F. P., Felipe, M. S., dos Santos Feitosa, L., et al. (2006). Glyceraldehyde 3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein, involved in fungal adhesion to extracellular matrix proteins and interaction with cells. Infect. Immun. 74, 382-389. doi: 10.1128/IAI.74.1.382-389.2006.
    • (2006) Infect. Immun , vol.74 , pp. 382-389
    • Barbosa, M.S.1    Bao, S.N.2    Andreotti, P.F.3    de Faria, F.P.4    Felipe, M.S.5    dos Santos Feitosa, L.6
  • 4
    • 0025720599 scopus 로고
    • Expression of duck lens delta-crystallin cDNAs in yeast and bacterial host. Delta 2-crystallin is an active argininosuccinate lyase
    • Barbosa, P., Wistow, G. J., Cialkowski, M., Piatigorsky, J., and O'Brien, W. E. (1991). Expression of duck lens delta-crystallin cDNAs in yeast and bacterial hosts. Delta 2-crystallin is an active argininosuccinate lyase. J. Biol. Chem. 266, 22319-22322.
    • (1991) J. Biol. Chem , vol.266 , pp. 22319-22322
    • Barbosa, P.1    Wistow, G.J.2    Cialkowski, M.3    Piatigorsky, J.4    O'Brien, W.E.5
  • 5
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S., Rohde, M., and Hammerschmidt, S. (2004). Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect. Immun. 72, 2416-2419. doi: 10.1128/IAI.72.4.2416-2419.2004.
    • (2004) Infect. Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 6
    • 79960929092 scopus 로고    scopus 로고
    • Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin
    • Boone, T. J., Burnham, C. A., and Tyrrell, G. J. (2011). Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin. Microb. Pathog. 51, 255-261. doi: 10.1016/j.micpath.2011.06.005.
    • (2011) Microb. Pathog , vol.51 , pp. 255-261
    • Boone, T.J.1    Burnham, C.A.2    Tyrrell, G.J.3
  • 7
    • 62749196670 scopus 로고    scopus 로고
    • Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein
    • Castaldo, C., Vastano, V., Siciliano, R. A., Candela, M., Vici, M., Muscariello, L., et al. (2009). Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein. Microb. Cell Fact. 8, 14-38. doi: 10.1186/1475-2859-8-14.
    • (2009) Microb. Cell Fact , vol.8 , pp. 14-38
    • Castaldo, C.1    Vastano, V.2    Siciliano, R.A.3    Candela, M.4    Vici, M.5    Muscariello, L.6
  • 8
    • 84938237638 scopus 로고    scopus 로고
    • PrOnto database: GO term functional dissimilarity inferred from biological data
    • Chapple, C. E., Herrmann, C., and Brun, C. (2015). PrOnto database: GO term functional dissimilarity inferred from biological data. Front. Genet. 6:200. doi: 10.3389/fgene.2015.00200.
    • (2015) Front. Genet , vol.6 , pp. 200
    • Chapple, C.E.1    Herrmann, C.2    Brun, C.3
  • 9
    • 13244277441 scopus 로고    scopus 로고
    • Aconitase couples metabolic regulation to mitochondrial DNA maintenance
    • Chen, X. J., Wang, X., Kaufman, B. A., and Butow, R. A. (2005). Aconitase couples metabolic regulation to mitochondrial DNA maintenance. Nature 307, 714-717. doi: 10.1126/science.1106391.
    • (2005) Nature , vol.307 , pp. 714-717
    • Chen, X.J.1    Wang, X.2    Kaufman, B.A.3    Butow, R.A.4
  • 10
    • 0026059624 scopus 로고
    • Ostrich crystallins. Structural characterization of delta-crystallin with enzymic activity
    • Chiou, S. H., Lo, C. H., Chang, C. Y., Itoh, T., Kaji, H., and Samejima, T. (1991). Ostrich crystallins. Structural characterization of delta-crystallin with enzymic activity. Biochem. J. 273, 295-300.
    • (1991) Biochem. J , vol.273 , pp. 295-300
    • Chiou, S.H.1    Lo, C.H.2    Chang, C.Y.3    Itoh, T.4    Kaji, H.5    Samejima, T.6
  • 11
    • 0025990937 scopus 로고
    • Autoregulation of human thymidylate synthase messenger RNA translation by thymidylate synthase
    • Chu, E., Koeller, D. M., Casey, J. L., Drake, J. C., Chabner, B. A., Elwood, P. C., et al. (1991). Autoregulation of human thymidylate synthase messenger RNA translation by thymidylate synthase. Proc. Natl. Acad. Sci. U.S.A. 88, 8977-8981. doi: 10.1073/pnas.88.20.8977.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 8977-8981
    • Chu, E.1    Koeller, D.M.2    Casey, J.L.3    Drake, J.C.4    Chabner, B.A.5    Elwood, P.C.6
  • 12
    • 38449095243 scopus 로고    scopus 로고
    • Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression
    • Commichau, F. M., and Stulke, J. (2008). Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression. Mol. Microbiol. 67, 692-702. doi: 10.1111/j.1365-2958.2007.06071.x.
    • (2008) Mol. Microbiol , vol.67 , pp. 692-702
    • Commichau, F.M.1    Stulke, J.2
  • 13
    • 80054998427 scopus 로고    scopus 로고
    • Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase
    • Du, J., Say, R. F., Lü, W., Fuchs, G., and Einsle, O. (2011). Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase. Nature 478, 534-537. doi: 10.1038/nature10458.
    • (2011) Nature , vol.478 , pp. 534-537
    • Du, J.1    Say, R.F.2    Lü, W.3    Fuchs, G.4    Einsle, O.5
  • 16
    • 84897038608 scopus 로고    scopus 로고
    • Pneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activator
    • Fulde, M., Bernardo-García, N., Rohde, M., Nachtigall, N., Frank, R., Preissner, K. T., et al. (2013). Pneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activator. Thromb. Haemost. 111, 401-416. doi: 10.1160/TH13-05-0421.
    • (2013) Thromb. Haemost , vol.111 , pp. 401-416
    • Fulde, M.1    Bernardo-García, N.2    Rohde, M.3    Nachtigall, N.4    Frank, R.5    Preissner, K.T.6
  • 17
    • 80055018027 scopus 로고    scopus 로고
    • Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase
    • Fushinobu, S., Nishimasu, H., Hattori, D., Song, H. J., and Wakagi, T. (2011). Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase. Nature 478, 538-541. doi: 10.1038/nature10457.
    • (2011) Nature , vol.478 , pp. 538-541
    • Fushinobu, S.1    Nishimasu, H.2    Hattori, D.3    Song, H.J.4    Wakagi, T.5
  • 18
    • 40849118252 scopus 로고    scopus 로고
    • Moonlighting proteins in yeasts
    • Gancedo, C., and Flores, C. L. (2008). Moonlighting proteins in yeasts. Microbiol. Mol. Biol. Rev. 72, 197-210. doi: 10.1128/MMBR.00036-07.
    • (2008) Microbiol. Mol. Biol. Rev , vol.72 , pp. 197-210
    • Gancedo, C.1    Flores, C.L.2
  • 19
    • 0029984181 scopus 로고    scopus 로고
    • A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin
    • Graham, C., Hodin, J., and Wistow, G. (1996). A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin. J. Biol. Chem. 271, 15623-15628. doi: 10.1074/jbc.271.26.15623.
    • (1996) J. Biol. Chem , vol.271 , pp. 15623-15628
    • Graham, C.1    Hodin, J.2    Wistow, G.3
  • 20
    • 84874028131 scopus 로고    scopus 로고
    • Essential nontranslational functions of tRNA synthetases
    • Guo, M., and Schimmel, P. (2013). Essential nontranslational functions of tRNA synthetases. Nat. Chem. Biol. 9, 145-153. doi: 10.1038/nchembio.1158.
    • (2013) Nat. Chem. Biol , vol.9 , pp. 145-153
    • Guo, M.1    Schimmel, P.2
  • 21
    • 84940117732 scopus 로고    scopus 로고
    • Moonlighting bacterial virulence factors are novel therapeutic targets for bacterial infections
    • (in press)
    • Henderson, B., and Kaiser, F. (in press). Moonlighting bacterial virulence factors are novel therapeutic targets for bacterial infections. Front. Bioeng. Biotech. Res. Top.
    • Front. Bioeng. Biotech. Res. Top
    • Henderson, B.1    Kaiser, F.2
  • 22
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • Henderson, B., and Martin, A. (2011). Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect. Immun. 79, 3476-3491. doi: 10.1128/IAI.00179-11.
    • (2011) Infect. Immun , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 23
    • 84880153102 scopus 로고    scopus 로고
    • Bacterial moonlighting proteins and bacterial virulence
    • Henderson, B., and Martin, A. (2013). Bacterial moonlighting proteins and bacterial virulence. Curr. Top. Microbiol. Immunol. 358, 155-213. doi: 10.1007/82_2011_188.
    • (2013) Curr. Top. Microbiol. Immunol , vol.358 , pp. 155-213
    • Henderson, B.1    Martin, A.2
  • 25
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: an intriguing mode of multitasking
    • Huberts, D. H., and van der Klei, I. J. (2010). Moonlighting proteins: an intriguing mode of multitasking. Biochim. Biophys. Acta 1803, 520-525. doi: 10.1016/j.bbamcr.2010.01.022.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 520-525
    • Huberts, D.H.1    van der Klei, I.J.2
  • 26
    • 34247215679 scopus 로고    scopus 로고
    • Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen
    • Hurmalainen, V., Edelman, S., Antikainen, J., Baumann, M., Lähteenmäki, K., and Korhonen, T. K. (2007). Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen. Microbiology 153, 1112-1122. doi: 10.1099/mic.0.2006/000901-0.
    • (2007) Microbiology , vol.153 , pp. 1112-1122
    • Hurmalainen, V.1    Edelman, S.2    Antikainen, J.3    Baumann, M.4    Lähteenmäki, K.5    Korhonen, T.K.6
  • 28
    • 77956359469 scopus 로고    scopus 로고
    • LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species
    • Jagadeesan, B., Koo, O. K., Kim, K. P., Burkholder, K. M., Mishra, K. K., Aroonnual, A., et al. (2010). LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species. Microbiology 156, 2782-2795. doi: 10.1099/mic.0.036509-0.
    • (2010) Microbiology , vol.156 , pp. 2782-2795
    • Jagadeesan, B.1    Koo, O.K.2    Kim, K.P.3    Burkholder, K.M.4    Mishra, K.K.5    Aroonnual, A.6
  • 29
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • Jeffery, C. J. (1999). Moonlighting proteins. Trends Biochem. Sci. 24, 8-11. doi: 10.1016/S0968-0004(98)01335-8.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 30
    • 0042706146 scopus 로고    scopus 로고
    • Moonlighting proteins: old proteins learning new tricks
    • Jeffery, C. J. (2003a). Moonlighting proteins: old proteins learning new tricks. Trends. Genet. 19, 415-417. doi: 10.1016/S0168-9525(03)00167-7.
    • (2003) Trends. Genet , vol.19 , pp. 415-417
    • Jeffery, C.J.1
  • 31
    • 0037235543 scopus 로고    scopus 로고
    • Multifunctional proteins: examples of gene sharing
    • Jeffery, C. J. (2003b). Multifunctional proteins: examples of gene sharing. Ann. Med. 35, 28-35. doi: 10.1080/07853890310004101.
    • (2003) Ann. Med , vol.35 , pp. 28-35
    • Jeffery, C.J.1
  • 32
    • 9944225262 scopus 로고    scopus 로고
    • Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins
    • Jeffery, C. J. (2004a). Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins. Curr. Opin. Struct. Biol. 14, 663-668. doi: 10.1016/j.sbi.2004.10.001.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 663-668
    • Jeffery, C.J.1
  • 33
    • 12344285199 scopus 로고    scopus 로고
    • Moonlighting proteins: complications and implications for proteomics research
    • Jeffery, C. J. (2004b). Moonlighting proteins: complications and implications for proteomics research. Drug Discov. Today Targets 3, 71-78. doi: 10.1016/S1741-8372(04)02405-3.
    • (2004) Drug Discov. Today Targets , vol.3 , pp. 71-78
    • Jeffery, C.J.1
  • 34
    • 62949096122 scopus 로고    scopus 로고
    • Moonlighting proteins-an update
    • Jeffery, C. J. (2009). Moonlighting proteins-an update. Mol. Biosyst. 5, 345-350. doi: 10.1039/b900658n.
    • (2009) Mol. Biosyst , vol.5 , pp. 345-350
    • Jeffery, C.J.1
  • 35
    • 84911874292 scopus 로고    scopus 로고
    • An introduction to moonlighting proteins
    • Jeffery, C. J. (2014). An introduction to moonlighting proteins. Biochem. Soc. Trans. 42, 1679-1683. doi: 10.1042/BST20140226.
    • (2014) Biochem. Soc. Trans , vol.42 , pp. 1679-1683
    • Jeffery, C.J.1
  • 36
    • 0348141889 scopus 로고    scopus 로고
    • Acquisition of host plasmin activity by the Swine pathogen Streptococcus suis serotype 2
    • Jobin, M. C., Brassard, J., Quessy, S., Gottschalk, M., and Grenier, D. (2004). Acquisition of host plasmin activity by the Swine pathogen Streptococcus suis serotype 2. Infect. Immun. 72, 606-610. doi: 10.1128/IAI.72.1.606-610.2004.
    • (2004) Infect. Immun , vol.72 , pp. 606-610
    • Jobin, M.C.1    Brassard, J.2    Quessy, S.3    Gottschalk, M.4    Grenier, D.5
  • 37
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy, M. C., Mende-Mueller, L., Blondin, G. A., and Beinert, H. (1992). Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc. Natl. Acad. Sci. U.S.A. 89, 11730-11734. doi: 10.1073/pnas.89.24.11730.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 38
    • 85027926417 scopus 로고    scopus 로고
    • Genome-scale identification and characterization of moonlighting proteins
    • Khan, I., Chen, Y., Dong, T., Hong, X., Takeuchi, R., Mori, H., et al. (2014). Genome-scale identification and characterization of moonlighting proteins. Biol. Direct. 9:30. doi: 10.1186/s13062-014-0030-9.
    • (2014) Biol. Direct , vol.9 , pp. 30
    • Khan, I.1    Chen, Y.2    Dong, T.3    Hong, X.4    Takeuchi, R.5    Mori, H.6
  • 39
    • 84911913899 scopus 로고    scopus 로고
    • Computational characterization of moonlighting proteins
    • Khan, I. K., and Kihara, D. (2014). Computational characterization of moonlighting proteins. Biochem. Soc Trans. 42, 1780-1785. doi: 10.1042/BST20140214.
    • (2014) Biochem. Soc Trans , vol.42 , pp. 1780-1785
    • Khan, I.K.1    Kihara, D.2
  • 40
    • 34247854961 scopus 로고    scopus 로고
    • Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis
    • Knaust, A., Weber, M. V. R., Hammerschmidt, S., Bergmann, S., Frosch, M., and Kurzai, O. (2007). Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis. J. Bacteriol. 189, 3246-3255. doi: 10.1128/JB.01966-06.
    • (2007) J. Bacteriol , vol.189 , pp. 3246-3255
    • Knaust, A.1    Weber, M.V.R.2    Hammerschmidt, S.3    Bergmann, S.4    Frosch, M.5    Kurzai, O.6
  • 41
    • 84946048847 scopus 로고    scopus 로고
    • MoonProt: a database of proteins that are known to moonlight
    • Mani, M., Chen, C., Amblee, V., Liu, H., Mathur, T., Zwicke, G., et al. (2015). MoonProt: a database of proteins that are known to moonlight. Nucleic Acids Res. 43, D277-D282. doi: 10.1093/nar/gku954.
    • (2015) Nucleic Acids Res , vol.43 , pp. D277-D282
    • Mani, M.1    Chen, C.2    Amblee, V.3    Liu, H.4    Mathur, T.5    Zwicke, G.6
  • 42
    • 77956649845 scopus 로고    scopus 로고
    • Surface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding protein
    • Matta, S. K., Agarwal, S., and Bhatnagar, R. (2010). Surface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding protein. Biochim. Biophys. Acta 1804, 2111-2120. doi: 10.1016/j.bbapap.2010.08.004.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 2111-2120
    • Matta, S.K.1    Agarwal, S.2    Bhatnagar, R.3
  • 43
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • Nobeli, I., Favia, A. D., and Wool, I. G. (1996). Extraribosomal functions of ribosomal proteins. Trends Biochem. Sci. 21, 164-165. doi: 10.1016/0968-0004(96)20011-8.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 164-165
    • Nobeli, I.1    Favia, A.D.2    Wool, I.G.3
  • 44
    • 0027294788 scopus 로고
    • PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator
    • Ostrovsky de Spicer, P., and Maloy, S. (1993). PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator. Proc. Natl. Acad. Sci. U.S.A. 90, 4295-4298. doi: 10.1073/pnas.90.9.4295.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 4295-4298
    • Ostrovsky de Spicer, P.1    Maloy, S.2
  • 45
    • 0026024741 scopus 로고
    • Regulation of proline utilization in Salmonella typhimurium: a membrane-associated dehydrogenase binds DNA in vitro
    • Ostrovsky de Spicer, P., O'Brien, K., and Maloy, S. (1991). Regulation of proline utilization in Salmonella typhimurium: a membrane-associated dehydrogenase binds DNA in vitro. J. Bacteriol. 173, 211-219.
    • (1991) J. Bacteriol , vol.173 , pp. 211-219
    • Ostrovsky de Spicer, P.1    O'Brien, K.2    Maloy, S.3
  • 46
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V., and Fischetti, V., A (1992). A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J. Exp. Med. 176, 415-426. doi: 10.1084/jem.176.2.415.
    • (1992) J. Exp. Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 47
    • 0028276577 scopus 로고
    • The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation
    • Philpott, C. C., Klausner, R. D., and Rouault, T. A. (1994). The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation. Proc. Natl. Acad. Sci. U.S.A. 91, 7321-7325. doi: 10.1073/pnas.91.15.7321.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 7321-7325
    • Philpott, C.C.1    Klausner, R.D.2    Rouault, T.A.3
  • 49
    • 0030592171 scopus 로고    scopus 로고
    • Characterization and enzyme activity of argininosuccinate lyase/delta-crystallin of the embryonic duck lens
    • Piatigorsky, J., and Horwitz, J. (1996). Characterization and enzyme activity of argininosuccinate lyase/delta-crystallin of the embryonic duck lens. Biochim. Biophys. Acta 1295, 158-164. doi: 10.1016/0167-4838(96)00030-1.
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 158-164
    • Piatigorsky, J.1    Horwitz, J.2
  • 51
    • 0024520027 scopus 로고
    • Enzyme/crystallins: gene sharing as an evolutionary strategy
    • Piatigorsky, J., and Wistow, G. J. (1989). Enzyme/crystallins: gene sharing as an evolutionary strategy. Cell 57, 197-199. doi: 10.1016/0092-8674(89)90956-2.
    • (1989) Cell , vol.57 , pp. 197-199
    • Piatigorsky, J.1    Wistow, G.J.2
  • 52
    • 84940117734 scopus 로고    scopus 로고
    • Novel cycloheximide derivatives targeting the moonlighting protein Mip exhibit specific antimicrobial activity against Legionella pneumophila
    • Rasch, J., Theuerkorn, M., Unal, C., Heinsohn, N., Tran, S., Fischer, G., et al. (2015). Novel cycloheximide derivatives targeting the moonlighting protein Mip exhibit specific antimicrobial activity against Legionella pneumophila. Front. Bioeng. Biotech. Res. Top. 3:41. doi: 10.3389/fbioe.2015.00041.
    • (2015) Front. Bioeng. Biotech. Res. Top , vol.3 , pp. 41
    • Rasch, J.1    Theuerkorn, M.2    Unal, C.3    Heinsohn, N.4    Tran, S.5    Fischer, G.6
  • 53
    • 84864257340 scopus 로고    scopus 로고
    • An a helix to β barrel domain switch transforms the transcription factor RfaH into a translation factor
    • Schweimer, K., Mooney, R. A., Landick, R., Artsimovitch, I., and Rösch, P. (2012). An a helix to β barrel domain switch transforms the transcription factor RfaH into a translation factor. Cell 150, 291-303. doi: 10.1016/j.cell.2012.05.042.
    • (2012) Cell , vol.150 , pp. 291-303
    • Schweimer, K.1    Mooney, R.A.2    Landick, R.3    Artsimovitch, I.4    Rösch, P.5
  • 54
    • 0141834741 scopus 로고    scopus 로고
    • Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions
    • Seifert, K. N., McArthur, W. P., Bleiweis, A. S., and Brady, L. J. (2003). Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions. J. Microbiol. 49, 350-356. doi: 10.1139/w03-042.
    • (2003) J. Microbiol , vol.49 , pp. 350-356
    • Seifert, K.N.1    McArthur, W.P.2    Bleiweis, A.S.3    Brady, L.J.4
  • 55
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa, P., Szász, C., and Buday, L. (2005). Structural disorder throws new light on moonlighting. Trends Biochem. Sci. 30, 484-489. doi: 10.1016/j.tibs.2005.07.008.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szász, C.2    Buday, L.3
  • 56
    • 0025740495 scopus 로고
    • Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor
    • Watanabe, H., Carmi, P., Hogan, V., Raz, T., Silletti, S., Nabi, I. R., et al. (1991). Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor. J. Biol. Chem. 266, 13442-13448.
    • (1991) J. Biol. Chem , vol.266 , pp. 13442-13448
    • Watanabe, H.1    Carmi, P.2    Hogan, V.3    Raz, T.4    Silletti, S.5    Nabi, I.R.6
  • 57
    • 0023225865 scopus 로고
    • Recruitment of enzymes as lens structural proteins
    • Wistow, G., and Piatigorsky, J. (1987). Recruitment of enzymes as lens structural proteins. Science 236, 1554-1556. doi: 10.1126/science.3589669.
    • (1987) Science , vol.236 , pp. 1554-1556
    • Wistow, G.1    Piatigorsky, J.2
  • 58
    • 0019862229 scopus 로고
    • Genetics of L-proline utilization in Escherichia coli
    • Wood, J. M. (1981). Genetics of L-proline utilization in Escherichia coli. J. Bacteriol. 146, 895-901.
    • (1981) J. Bacteriol , vol.146 , pp. 895-901
    • Wood, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.