메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages

An intein with genetically selectable markers provides a new approach to internally label proteins with GFP

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDES; BIOCHEMICAL ACTIVITY; DNA ENCODING; E. COLI; ENDONUCLEASES; EXTEINS; FOLDED STRUCTURES; GENETIC BACKGROUNDS; GENETIC MARKERS; GENETIC SELECTION; HIGH EFFICIENCY; HYGROMYCIN; HYGROMYCIN RESISTANCE; IN-VIVO; INTEINS; N-TERMINALS; NUCLEASE ACTIVITY; PENICILLIUM CHRYSOGENUM; PHOSPHOTRANSFERASES; PRECURSOR PROTEINS; PROTEIN SEQUENCES; PROTOTROPY; S.CEREVISIAE; SELECTABLE MARKERS; TARGET PROTEINS; TRANSCRIPTIONAL ACTIVATORS;

EID: 79959544267     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-11-71     Document Type: Article
Times cited : (12)

References (62)
  • 1
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • 10.1146/annurev.biochem.69.1.447, 10966466
    • Paulus H. Protein splicing and related forms of protein autoprocessing. Annu Rev Biochem 2000, 69:447-496. 10.1146/annurev.biochem.69.1.447, 10966466.
    • (2000) Annu Rev Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 2
    • 23444433268 scopus 로고    scopus 로고
    • Protein splicing mechanisms and applications
    • 10.1080/15216540500163343, 16081367
    • Perler FB. Protein splicing mechanisms and applications. IUBMB Life 2005, 57(7):469-476. 10.1080/15216540500163343, 16081367.
    • (2005) IUBMB Life , vol.57 , Issue.7 , pp. 469-476
    • Perler, F.B.1
  • 3
    • 0025240361 scopus 로고
    • Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
    • Hirata R, Ohsumk Y, Nakano A, Kawasaki H, Suzuki K, Anraku Y. Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J Biol Chem 1990, 265(12):6726-6733.
    • (1990) J Biol Chem , vol.265 , Issue.12 , pp. 6726-6733
    • Hirata, R.1    Ohsumk, Y.2    Nakano, A.3    Kawasaki, H.4    Suzuki, K.5    Anraku, Y.6
  • 4
    • 0025226104 scopus 로고
    • Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase
    • 10.1126/science.2146742, 2146742
    • Kane PM, Yamashiro CT, Wolczyk DF, Neff N, Goebl M, Stevens TH. Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase. Science 1990, 250(4981):651-657. 10.1126/science.2146742, 2146742.
    • (1990) Science , vol.250 , Issue.4981 , pp. 651-657
    • Kane, P.M.1    Yamashiro, C.T.2    Wolczyk, D.F.3    Neff, N.4    Goebl, M.5    Stevens, T.H.6
  • 5
    • 0036084146 scopus 로고    scopus 로고
    • InBase: the Intein Database
    • 10.1093/nar/30.1.383, 99080, 11752343
    • Perler FB. InBase: the Intein Database. Nucleic Acids Res 2002, 30(1):383-384. 10.1093/nar/30.1.383, 99080, 11752343.
    • (2002) Nucleic Acids Res , vol.30 , Issue.1 , pp. 383-384
    • Perler, F.B.1
  • 6
    • 0030611387 scopus 로고    scopus 로고
    • Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity
    • 10.1016/S0092-8674(00)80237-8, 9160747
    • Duan X, Gimble FS, Quiocho FA. Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Cell 1997, 89(4):555-564. 10.1016/S0092-8674(00)80237-8, 9160747.
    • (1997) Cell , vol.89 , Issue.4 , pp. 555-564
    • Duan, X.1    Gimble, F.S.2    Quiocho, F.A.3
  • 7
    • 0029834656 scopus 로고    scopus 로고
    • Protein splicing involving the Saccharomyces cerevisiae VMA intein. The steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system
    • 10.1074/jbc.271.36.22159, 8703028
    • Chong S, Shao Y, Paulus H, Benner J, Perler FB, Xu MQ. Protein splicing involving the Saccharomyces cerevisiae VMA intein. The steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system. J Biol Chem 1996, 271(36):22159-22168. 10.1074/jbc.271.36.22159, 8703028.
    • (1996) J Biol Chem , vol.271 , Issue.36 , pp. 22159-22168
    • Chong, S.1    Shao, Y.2    Paulus, H.3    Benner, J.4    Perler, F.B.5    Xu, M.Q.6
  • 8
    • 0030803760 scopus 로고    scopus 로고
    • Genetic definition of a protein-splicing domain: functional mini-inteins support structure predictions and a model for intein evolution
    • 10.1073/pnas.94.21.11466, 23508, 9326633
    • Derbyshire V, Wood DW, Wu W, Dansereau JT, Dalgaard JZ, Belfort M. Genetic definition of a protein-splicing domain: functional mini-inteins support structure predictions and a model for intein evolution. Proc Natl Acad Sci USA 1997, 94(21):11466-11471. 10.1073/pnas.94.21.11466, 23508, 9326633.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.21 , pp. 11466-11471
    • Derbyshire, V.1    Wood, D.W.2    Wu, W.3    Dansereau, J.T.4    Dalgaard, J.Z.5    Belfort, M.6
  • 9
    • 37549063049 scopus 로고    scopus 로고
    • Minimization of a eukaryotic mini-intein
    • 10.1016/j.bbrc.2007.11.126, 18054328
    • Elleuche S, Doring K, Poggeler S. Minimization of a eukaryotic mini-intein. Biochem Biophys Res Commun 2008, 366(1):239-243. 10.1016/j.bbrc.2007.11.126, 18054328.
    • (2008) Biochem Biophys Res Commun , vol.366 , Issue.1 , pp. 239-243
    • Elleuche, S.1    Doring, K.2    Poggeler, S.3
  • 10
    • 70349446285 scopus 로고    scopus 로고
    • Protein splicing: A versatile tool for drug discovery
    • 10.1016/j.addr.2009.04.021, 19442693
    • Cheriyan M, Perler FB. Protein splicing: A versatile tool for drug discovery. Adv Drug Deliv Rev 2009, 61(11):899-907. 10.1016/j.addr.2009.04.021, 19442693.
    • (2009) Adv Drug Deliv Rev , vol.61 , Issue.11 , pp. 899-907
    • Cheriyan, M.1    Perler, F.B.2
  • 11
    • 77953043452 scopus 로고    scopus 로고
    • Inteins, valuable genetic elements in molecular biology and biotechnology
    • 10.1007/s00253-010-2628-x, 2874743, 20449740
    • Elleuche S, Poggeler S. Inteins, valuable genetic elements in molecular biology and biotechnology. Appl Microbiol Biotechnol 2010, 87(2):479-489. 10.1007/s00253-010-2628-x, 2874743, 20449740.
    • (2010) Appl Microbiol Biotechnol , vol.87 , Issue.2 , pp. 479-489
    • Elleuche, S.1    Poggeler, S.2
  • 12
    • 77957758860 scopus 로고    scopus 로고
    • Biological applications of protein splicing
    • 10.1016/j.cell.2010.09.031, 20946979
    • Vila-Perello M, Muir TW. Biological applications of protein splicing. Cell 2010, 143(2):191-200. 10.1016/j.cell.2010.09.031, 20946979.
    • (2010) Cell , vol.143 , Issue.2 , pp. 191-200
    • Vila-Perello, M.1    Muir, T.W.2
  • 13
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: an enabling technology for the biophysical analysis of proteins
    • 10.1038/nmeth886, 16721376
    • Muralidharan V, Muir TW. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nature methods 2006, 3(6):429-438. 10.1038/nmeth886, 16721376.
    • (2006) Nature methods , vol.3 , Issue.6 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 14
    • 67650492166 scopus 로고    scopus 로고
    • Modulation of intein activity by its neighboring extein substrates
    • 10.1073/pnas.0904366106, 2708771, 19541659
    • Amitai G, Callahan BP, Stanger MJ, Belfort G, Belfort M. Modulation of intein activity by its neighboring extein substrates. Proc Natl Acad Sci USA 2009, 106(27):11005-11010. 10.1073/pnas.0904366106, 2708771, 19541659.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.27 , pp. 11005-11010
    • Amitai, G.1    Callahan, B.P.2    Stanger, M.J.3    Belfort, G.4    Belfort, M.5
  • 15
    • 38749100508 scopus 로고    scopus 로고
    • The structure of the gamma-tubulin small complex: implications of its architecture and flexibility for microtubule nucleation
    • 10.1091/mbc.E07-09-0879, 2174199, 17978090
    • Kollman JM, Zelter A, Muller EG, Fox B, Rice LM, Davis TN, Agard DA. The structure of the gamma-tubulin small complex: implications of its architecture and flexibility for microtubule nucleation. Mol Biol Cell 2008, 19(1):207-215. 10.1091/mbc.E07-09-0879, 2174199, 17978090.
    • (2008) Mol Biol Cell , vol.19 , Issue.1 , pp. 207-215
    • Kollman, J.M.1    Zelter, A.2    Muller, E.G.3    Fox, B.4    Rice, L.M.5    Davis, T.N.6    Agard, D.A.7
  • 16
    • 34548074957 scopus 로고    scopus 로고
    • In vivo analysis of cohesin architecture using FRET in the budding yeast Saccharomyces cerevisiae
    • 10.1038/sj.emboj.7601793, 1952217, 17660750
    • Mc Intyre J, Muller EG, Weitzer S, Snydsman BE, Davis TN, Uhlmann F. In vivo analysis of cohesin architecture using FRET in the budding yeast Saccharomyces cerevisiae. EMBO J 2007, 26(16):3783-3793. 10.1038/sj.emboj.7601793, 1952217, 17660750.
    • (2007) EMBO J , vol.26 , Issue.16 , pp. 3783-3793
    • Mc Intyre, J.1    Muller, E.G.2    Weitzer, S.3    Snydsman, B.E.4    Davis, T.N.5    Uhlmann, F.6
  • 18
    • 78149350522 scopus 로고    scopus 로고
    • Vesicle docking to the spindle pole body is necessary to recruit the exocyst during membrane formation in Saccharomyces cerevisiae
    • 10.1091/mbc.E10-07-0563, 2965686, 20826607
    • Mathieson EM, Suda Y, Nickas M, Snydsman B, Davis TN, Muller EG, Neiman AM. Vesicle docking to the spindle pole body is necessary to recruit the exocyst during membrane formation in Saccharomyces cerevisiae. Molecular biology of the cell 2010, 21(21):3693-3707. 10.1091/mbc.E10-07-0563, 2965686, 20826607.
    • (2010) Molecular biology of the cell , vol.21 , Issue.21 , pp. 3693-3707
    • Mathieson, E.M.1    Suda, Y.2    Nickas, M.3    Snydsman, B.4    Davis, T.N.5    Muller, E.G.6    Neiman, A.M.7
  • 19
    • 33749179044 scopus 로고    scopus 로고
    • Protein splicing of PRP8 mini-inteins from species of the genus Penicillium
    • 10.1007/s00253-006-0350-5, 16544141
    • Elleuche S, Nolting N, Poggeler S. Protein splicing of PRP8 mini-inteins from species of the genus Penicillium. Appl Microbiol Biotechnol 2006, 72(5):959-967. 10.1007/s00253-006-0350-5, 16544141.
    • (2006) Appl Microbiol Biotechnol , vol.72 , Issue.5 , pp. 959-967
    • Elleuche, S.1    Nolting, N.2    Poggeler, S.3
  • 20
    • 33847249392 scopus 로고    scopus 로고
    • Trans-splicing of an artificially split fungal mini-intein
    • 10.1016/j.bbrc.2007.02.035, 17316565
    • Elleuche S, Poggeler S. Trans-splicing of an artificially split fungal mini-intein. Biochem Biophys Res Commun 2007, 355(3):830-834. 10.1016/j.bbrc.2007.02.035, 17316565.
    • (2007) Biochem Biophys Res Commun , vol.355 , Issue.3 , pp. 830-834
    • Elleuche, S.1    Poggeler, S.2
  • 21
    • 0031472251 scopus 로고    scopus 로고
    • A yeast genetic system for selecting small molecule inhibitors of protein-protein interactions in nanodroplets
    • 10.1073/pnas.94.25.13396, 28315, 9391035
    • Huang J, Schreiber SL. A yeast genetic system for selecting small molecule inhibitors of protein-protein interactions in nanodroplets. Proc Natl Acad Sci USA 1997, 94(25):13396-13401. 10.1073/pnas.94.25.13396, 28315, 9391035.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.25 , pp. 13396-13401
    • Huang, J.1    Schreiber, S.L.2
  • 22
    • 0037459248 scopus 로고    scopus 로고
    • The crystal structure of aminoglycoside-3'-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance
    • 10.1016/S0022-2836(03)00121-9, 12628253
    • Nurizzo D, Shewry SC, Perlin MH, Brown SA, Dholakia JN, Fuchs RL, Deva T, Baker EN, Smith CA. The crystal structure of aminoglycoside-3'-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance. J Mol Biol 2003, 327(2):491-506. 10.1016/S0022-2836(03)00121-9, 12628253.
    • (2003) J Mol Biol , vol.327 , Issue.2 , pp. 491-506
    • Nurizzo, D.1    Shewry, S.C.2    Perlin, M.H.3    Brown, S.A.4    Dholakia, J.N.5    Fuchs, R.L.6    Deva, T.7    Baker, E.N.8    Smith, C.A.9
  • 24
    • 78751475029 scopus 로고    scopus 로고
    • Structure and function of APH(4)-Ia, a hygromycin B resistance enzyme
    • 10.1074/jbc.M110.194266, 21084294
    • Stogios PJ, Shakya T, Evdokimova E, Savchenko A, Wright GD. Structure and function of APH(4)-Ia, a hygromycin B resistance enzyme. The Journal of biological chemistry 2011, 286(3):1966-1975. 10.1074/jbc.M110.194266, 21084294.
    • (2011) The Journal of biological chemistry , vol.286 , Issue.3 , pp. 1966-1975
    • Stogios, P.J.1    Shakya, T.2    Evdokimova, E.3    Savchenko, A.4    Wright, G.D.5
  • 25
    • 0027965510 scopus 로고
    • Solution structure of the LexA repressor DNA binding domain determined by 1 H NMR spectroscopy
    • 395313, 8076591
    • Fogh RH, Ottleben G, Ruterjans H, Schnarr M, Boelens R, Kaptein R. Solution structure of the LexA repressor DNA binding domain determined by 1 H NMR spectroscopy. The EMBO journal 1994, 13(17):3936-3944. 395313, 8076591.
    • (1994) The EMBO journal , vol.13 , Issue.17 , pp. 3936-3944
    • Fogh, R.H.1    Ottleben, G.2    Ruterjans, H.3    Schnarr, M.4    Boelens, R.5    Kaptein, R.6
  • 26
    • 0023006881 scopus 로고
    • Isolation of the yeast calmodulin gene: calmodulin is an essential protein
    • 10.1016/0092-8674(86)90599-4, 3533275
    • Davis TN, Urdea MS, Masiarz FR, Thorner J. Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 1986, 47(3):423-431. 10.1016/0092-8674(86)90599-4, 3533275.
    • (1986) Cell , vol.47 , Issue.3 , pp. 423-431
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 27
    • 0026637084 scopus 로고
    • Calmodulin concentrates at regions of cell growth in Saccharomyces cerevisiae
    • 10.1083/jcb.118.3.619, 2289548, 1639847
    • Brockerhoff SE, Davis TN. Calmodulin concentrates at regions of cell growth in Saccharomyces cerevisiae. J Cell Biol 1992, 118(3):619-629. 10.1083/jcb.118.3.619, 2289548, 1639847.
    • (1992) J Cell Biol , vol.118 , Issue.3 , pp. 619-629
    • Brockerhoff, S.E.1    Davis, T.N.2
  • 29
    • 77952298647 scopus 로고    scopus 로고
    • The Yeast Resource Center Public Image Repository: A large database of fluorescence microscopy images
    • 10.1186/1471-2105-11-263, 2882934, 20482811
    • Riffle M, Davis TN. The Yeast Resource Center Public Image Repository: A large database of fluorescence microscopy images. BMC bioinformatics 2010, 11:263. 10.1186/1471-2105-11-263, 2882934, 20482811.
    • (2010) BMC bioinformatics , vol.11 , pp. 263
    • Riffle, M.1    Davis, T.N.2
  • 30
    • 61849177109 scopus 로고    scopus 로고
    • Expressed protein ligation (EPL) in the study of signal transduction, ion conduction, and chromatin biology
    • 10.1021/ar800129c, 18939858
    • Flavell RR, Muir TW. Expressed protein ligation (EPL) in the study of signal transduction, ion conduction, and chromatin biology. Acc Chem Res 2009, 42(1):107-116. 10.1021/ar800129c, 18939858.
    • (2009) Acc Chem Res , vol.42 , Issue.1 , pp. 107-116
    • Flavell, R.R.1    Muir, T.W.2
  • 31
    • 0036753960 scopus 로고    scopus 로고
    • Development of a positive genetic selection system for inhibition of protein splicing using mycobacterial inteins in Escherichia coli DNA gyrase subunit A
    • Adam E, Perler FB. Development of a positive genetic selection system for inhibition of protein splicing using mycobacterial inteins in Escherichia coli DNA gyrase subunit A. J Mol Microbiol Biotechnol 2002, 4(5):479-487.
    • (2002) J Mol Microbiol Biotechnol , vol.4 , Issue.5 , pp. 479-487
    • Adam, E.1    Perler, F.B.2
  • 32
    • 3042742569 scopus 로고    scopus 로고
    • Temperature-sensitive control of protein activity by conditionally splicing inteins
    • 10.1038/nbt979, 15184905
    • Zeidler MP, Tan C, Bellaiche Y, Cherry S, Hader S, Gayko U, Perrimon N. Temperature-sensitive control of protein activity by conditionally splicing inteins. Nat Biotechnol 2004, 22(7):871-876. 10.1038/nbt979, 15184905.
    • (2004) Nat Biotechnol , vol.22 , Issue.7 , pp. 871-876
    • Zeidler, M.P.1    Tan, C.2    Bellaiche, Y.3    Cherry, S.4    Hader, S.5    Gayko, U.6    Perrimon, N.7
  • 33
    • 70350161834 scopus 로고    scopus 로고
    • Temperature-sensitive mutations made easy: generating conditional mutations by using temperature-sensitive inteins that function within different temperature ranges
    • 10.1534/genetics.109.104794, 2746138, 19596904
    • Tan G, Chen M, Foote C, Tan C. Temperature-sensitive mutations made easy: generating conditional mutations by using temperature-sensitive inteins that function within different temperature ranges. Genetics 2009, 183(1):13-22. 10.1534/genetics.109.104794, 2746138, 19596904.
    • (2009) Genetics , vol.183 , Issue.1 , pp. 13-22
    • Tan, G.1    Chen, M.2    Foote, C.3    Tan, C.4
  • 34
    • 41449091908 scopus 로고    scopus 로고
    • Activation of protein splicing with light in yeast
    • Tyszkiewicz AB, Muir TW. Activation of protein splicing with light in yeast. Nat Methods 2008, 5(4):303-305.
    • (2008) Nat Methods , vol.5 , Issue.4 , pp. 303-305
    • Tyszkiewicz, A.B.1    Muir, T.W.2
  • 35
    • 3242694003 scopus 로고    scopus 로고
    • Directed evolution of ligand dependence: small-molecule-activated protein splicing
    • 10.1073/pnas.0402762101, 489967, 15247421
    • Buskirk AR, Ong YC, Gartner ZJ, Liu DR. Directed evolution of ligand dependence: small-molecule-activated protein splicing. Proc Natl Acad Sci USA 2004, 101(29):10505-10510. 10.1073/pnas.0402762101, 489967, 15247421.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.29 , pp. 10505-10510
    • Buskirk, A.R.1    Ong, Y.C.2    Gartner, Z.J.3    Liu, D.R.4
  • 36
    • 0041854719 scopus 로고    scopus 로고
    • Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo
    • 10.1021/ja0362813, 12940738
    • Mootz HD, Blum ES, Tyszkiewicz AB, Muir TW. Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo. J Am Chem Soc 2003, 125(35):10561-10569. 10.1021/ja0362813, 12940738.
    • (2003) J Am Chem Soc , vol.125 , Issue.35 , pp. 10561-10569
    • Mootz, H.D.1    Blum, E.S.2    Tyszkiewicz, A.B.3    Muir, T.W.4
  • 37
    • 0037036791 scopus 로고    scopus 로고
    • Protein splicing triggered by a small molecule
    • 10.1021/ja026769o, 12148996
    • Mootz HD, Muir TW. Protein splicing triggered by a small molecule. J Am Chem Soc 2002, 124(31):9044-9045. 10.1021/ja026769o, 12148996.
    • (2002) J Am Chem Soc , vol.124 , Issue.31 , pp. 9044-9045
    • Mootz, H.D.1    Muir, T.W.2
  • 38
    • 79960645285 scopus 로고    scopus 로고
    • PRP8 intein in Ajellomycetaceae family pathogens: Sequence analysis, splicing evaluation and homing endonuclease activity
    • Theodoro RC, Volkmann G, Liu XQ, Bagagli E. PRP8 intein in Ajellomycetaceae family pathogens: Sequence analysis, splicing evaluation and homing endonuclease activity. Fungal Genet Biol 2010,
    • (2010) Fungal Genet Biol
    • Theodoro, R.C.1    Volkmann, G.2    Liu, X.Q.3    Bagagli, E.4
  • 39
    • 62449227975 scopus 로고    scopus 로고
    • Inteins and introns within the prp8 -gene of four Eupenicillium species
    • 10.1002/jobm.200800168, 19253333
    • Elleuche S, Pelikan C, Nolting N, Poggeler S. Inteins and introns within the prp8 -gene of four Eupenicillium species. J Basic Microbiol 2009, 49(1):52-57. 10.1002/jobm.200800168, 19253333.
    • (2009) J Basic Microbiol , vol.49 , Issue.1 , pp. 52-57
    • Elleuche, S.1    Pelikan, C.2    Nolting, N.3    Poggeler, S.4
  • 40
    • 33745979535 scopus 로고    scopus 로고
    • The distribution and evolutionary history of the PRP8 intein
    • 10.1186/1471-2148-6-42, 1508164, 16737526
    • Butler MI, Gray J, Goodwin TJ, Poulter RT. The distribution and evolutionary history of the PRP8 intein. BMC Evol Biol 2006, 6:42. 10.1186/1471-2148-6-42, 1508164, 16737526.
    • (2006) BMC Evol Biol , vol.6 , pp. 42
    • Butler, M.I.1    Gray, J.2    Goodwin, T.J.3    Poulter, R.T.4
  • 41
    • 0030840519 scopus 로고    scopus 로고
    • Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae
    • 10.1002/(SICI)1097-0061(19970915)13:11<1065::AID-YEA159>3.0.CO;2-K, 9290211
    • Wach A, Brachat A, Alberti-Segui C, Rebischung C, Philippsen P. Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae. Yeast 1997, 13(11):1065-1075. 10.1002/(SICI)1097-0061(19970915)13:11<1065::AID-YEA159>3.0.CO;2-K, 9290211.
    • (1997) Yeast , vol.13 , Issue.11 , pp. 1065-1075
    • Wach, A.1    Brachat, A.2    Alberti-Segui, C.3    Rebischung, C.4    Philippsen, P.5
  • 42
    • 0141755113 scopus 로고    scopus 로고
    • Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing
    • 10.1074/jbc.M306197200, 12878593
    • Ding Y, Xu MQ, Ghosh I, Chen X, Ferrandon S, Lesage G, Rao Z. Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing. The Journal of biological chemistry 2003, 278(40):39133-39142. 10.1074/jbc.M306197200, 12878593.
    • (2003) The Journal of biological chemistry , vol.278 , Issue.40 , pp. 39133-39142
    • Ding, Y.1    Xu, M.Q.2    Ghosh, I.3    Chen, X.4    Ferrandon, S.5    Lesage, G.6    Rao, Z.7
  • 43
    • 0342813091 scopus 로고    scopus 로고
    • Crystal structure of a Hedgehog autoprocessing domain: homology between Hedgehog and self-splicing proteins
    • 10.1016/S0092-8674(01)80011-8, 9335337
    • Hall TM, Porter JA, Young KE, Koonin EV, Beachy PA, Leahy DJ. Crystal structure of a Hedgehog autoprocessing domain: homology between Hedgehog and self-splicing proteins. Cell 1997, 91(1):85-97. 10.1016/S0092-8674(01)80011-8, 9335337.
    • (1997) Cell , vol.91 , Issue.1 , pp. 85-97
    • Hall, T.M.1    Porter, J.A.2    Young, K.E.3    Koonin, E.V.4    Beachy, P.A.5    Leahy, D.J.6
  • 44
    • 0031975772 scopus 로고    scopus 로고
    • Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing
    • 10.1038/nsb0198-31, 9437427
    • Klabunde T, Sharma S, Telenti A, Jacobs WR, Sacchettini JC. Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing. Nature structural biology 1998, 5(1):31-36. 10.1038/nsb0198-31, 9437427.
    • (1998) Nature structural biology , vol.5 , Issue.1 , pp. 31-36
    • Klabunde, T.1    Sharma, S.2    Telenti, A.3    Jacobs, W.R.4    Sacchettini, J.C.5
  • 45
    • 0028944672 scopus 로고
    • A protein splice-junction motif in hedgehog family proteins
    • 10.1016/S0968-0004(00)88989-6, 7770912
    • Koonin EV. A protein splice-junction motif in hedgehog family proteins. Trends Biochem Sci 1995, 20(4):141-142. 10.1016/S0968-0004(00)88989-6, 7770912.
    • (1995) Trends Biochem Sci , vol.20 , Issue.4 , pp. 141-142
    • Koonin, E.V.1
  • 46
    • 0032498234 scopus 로고    scopus 로고
    • Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution
    • 10.1016/S0092-8674(00)80892-2, 9527442
    • Perler FB. Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution. Cell 1998, 92(1):1-4. 10.1016/S0092-8674(00)80892-2, 9527442.
    • (1998) Cell , vol.92 , Issue.1 , pp. 1-4
    • Perler, F.B.1
  • 47
    • 27144547019 scopus 로고    scopus 로고
    • Crystal structures of an intein from the split dnaE gene of Synechocystis sp. PCC6803 reveal the catalytic model without the penultimate histidine and the mechanism of zinc ion inhibition of protein splicing
    • 10.1016/j.jmb.2005.09.039, 16219320
    • Sun P, Ye S, Ferrandon S, Evans TC, Xu MQ, Rao Z. Crystal structures of an intein from the split dnaE gene of Synechocystis sp. PCC6803 reveal the catalytic model without the penultimate histidine and the mechanism of zinc ion inhibition of protein splicing. Journal of molecular biology 2005, 353(5):1093-1105. 10.1016/j.jmb.2005.09.039, 16219320.
    • (2005) Journal of molecular biology , vol.353 , Issue.5 , pp. 1093-1105
    • Sun, P.1    Ye, S.2    Ferrandon, S.3    Evans, T.C.4    Xu, M.Q.5    Rao, Z.6
  • 48
    • 33847071304 scopus 로고    scopus 로고
    • Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue
    • 10.1016/j.jmb.2006.12.050, 1852430, 17254599
    • Van Roey P, Pereira B, Li Z, Hiraga K, Belfort M, Derbyshire V. Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue. Journal of molecular biology 2007, 367(1):162-173. 10.1016/j.jmb.2006.12.050, 1852430, 17254599.
    • (2007) Journal of molecular biology , vol.367 , Issue.1 , pp. 162-173
    • Van Roey, P.1    Pereira, B.2    Li, Z.3    Hiraga, K.4    Belfort, M.5    Derbyshire, V.6
  • 49
    • 12844284527 scopus 로고    scopus 로고
    • The N-terminal to C-terminal motif in protein folding and function
    • 10.1073/pnas.0409114102, 545867, 15657118
    • Krishna MM, Englander SW. The N-terminal to C-terminal motif in protein folding and function. Proc Natl Acad Sci USA 2005, 102(4):1053-1058. 10.1073/pnas.0409114102, 545867, 15657118.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.4 , pp. 1053-1058
    • Krishna, M.M.1    Englander, S.W.2
  • 50
    • 66149124852 scopus 로고    scopus 로고
    • Nonrandom distribution of intramolecular contacts in native single-domain proteins
    • 10.1002/prot.22258, 18831044
    • Mounce BC, Kurt N, Ellison PA, Cavagnero S. Nonrandom distribution of intramolecular contacts in native single-domain proteins. Proteins 2009, 75(2):404-412. 10.1002/prot.22258, 18831044.
    • (2009) Proteins , vol.75 , Issue.2 , pp. 404-412
    • Mounce, B.C.1    Kurt, N.2    Ellison, P.A.3    Cavagnero, S.4
  • 51
    • 33846661178 scopus 로고    scopus 로고
    • A tale of two tails: why are terminal residues of proteins exposed?
    • 10.1093/bioinformatics/btl318, 17237096
    • Jacob E, Unger R. A tale of two tails: why are terminal residues of proteins exposed?. Bioinformatics 2007, 23(2):e225-230. 10.1093/bioinformatics/btl318, 17237096.
    • (2007) Bioinformatics , vol.23 , Issue.2
    • Jacob, E.1    Unger, R.2
  • 52
    • 0034680759 scopus 로고    scopus 로고
    • A novel strategy for constructing N-terminal chromosomal fusions to green fluorescent protein in the yeast Saccharomyces cerevisiae
    • 10.1016/S0014-5793(00)02179-7, 11086160
    • Prein B, Natter K, Kohlwein SD. A novel strategy for constructing N-terminal chromosomal fusions to green fluorescent protein in the yeast Saccharomyces cerevisiae. FEBS Lett 2000, 485(1):29-34. 10.1016/S0014-5793(00)02179-7, 11086160.
    • (2000) FEBS Lett , vol.485 , Issue.1 , pp. 29-34
    • Prein, B.1    Natter, K.2    Kohlwein, S.D.3
  • 53
    • 13444274743 scopus 로고    scopus 로고
    • New modules for the repeated internal and N-terminal epitope tagging of genes in Saccharomyces cerevisiae
    • 10.1002/yea.1187, 15565729
    • Gauss R, Trautwein M, Sommer T, Spang A. New modules for the repeated internal and N-terminal epitope tagging of genes in Saccharomyces cerevisiae. Yeast 2005, 22(1):1-12. 10.1002/yea.1187, 15565729.
    • (2005) Yeast , vol.22 , Issue.1 , pp. 1-12
    • Gauss, R.1    Trautwein, M.2    Sommer, T.3    Spang, A.4
  • 54
    • 0028841139 scopus 로고
    • Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae
    • 10.1002/yea.320111306, 8553697
    • Schneider BL, Seufert W, Steiner B, Yang QH, Futcher AB. Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae. Yeast 1995, 11(13):1265-1274. 10.1002/yea.320111306, 8553697.
    • (1995) Yeast , vol.11 , Issue.13 , pp. 1265-1274
    • Schneider, B.L.1    Seufert, W.2    Steiner, B.3    Yang, Q.H.4    Futcher, A.B.5
  • 55
    • 78649737930 scopus 로고    scopus 로고
    • Identification of Saccharomyces cerevisiae Spindle Pole Body Remodeling Factors
    • 10.1371/journal.pone.0015426, 2980476, 21103054
    • Greenland KB, Ding H, Costanzo M, Boone C, Davis TN. Identification of Saccharomyces cerevisiae Spindle Pole Body Remodeling Factors. PLoS One 2010, 5(11):e15426. 10.1371/journal.pone.0015426, 2980476, 21103054.
    • (2010) PLoS One , vol.5 , Issue.11
    • Greenland, K.B.1    Ding, H.2    Costanzo, M.3    Boone, C.4    Davis, T.N.5
  • 56
    • 0024324482 scopus 로고
    • A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase
    • 10.1016/0092-8674(89)90855-6, 2546682
    • Wallis JW, Chrebet G, Brodsky G, Rolfe M, Rothstein R. A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase. Cell 1989, 58(2):409-419. 10.1016/0092-8674(89)90855-6, 2546682.
    • (1989) Cell , vol.58 , Issue.2 , pp. 409-419
    • Wallis, J.W.1    Chrebet, G.2    Brodsky, G.3    Rolfe, M.4    Rothstein, R.5
  • 57
    • 79960649722 scopus 로고    scopus 로고
    • http://depts.washington.edu/yeastrc/
  • 58
    • 33745742246 scopus 로고    scopus 로고
    • Genetic mosaic with dual binary transcriptional systems in Drosophila
    • 10.1038/nn1681, 16582903
    • Lai SL, Lee T. Genetic mosaic with dual binary transcriptional systems in Drosophila. Nat Neurosci 2006, 9(5):703-709. 10.1038/nn1681, 16582903.
    • (2006) Nat Neurosci , vol.9 , Issue.5 , pp. 703-709
    • Lai, S.L.1    Lee, T.2
  • 59
    • 0021471049 scopus 로고
    • Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae
    • 368932, 6092912
    • Johnston M, Davis RW. Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae. Mol Cell Biol 1984, 4(8):1440-1448. 368932, 6092912.
    • (1984) Mol Cell Biol , vol.4 , Issue.8 , pp. 1440-1448
    • Johnston, M.1    Davis, R.W.2
  • 61
    • 0024567899 scopus 로고
    • Extraction and rapid inactivation of proteins from Saccharomyces cerevisiae by trichloroacetic acid precipitation
    • 10.1002/yea.320050107, 2648697
    • Wright AP, Bruns M, Hartley BS. Extraction and rapid inactivation of proteins from Saccharomyces cerevisiae by trichloroacetic acid precipitation. Yeast 1989, 5(1):51-53. 10.1002/yea.320050107, 2648697.
    • (1989) Yeast , vol.5 , Issue.1 , pp. 51-53
    • Wright, A.P.1    Bruns, M.2    Hartley, B.S.3
  • 62
    • 0028982225 scopus 로고
    • Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy
    • 10.1074/jbc.270.35.20643, 7657644
    • Moser MJ, Lee SY, Klevit RE, Davis TN. Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy. J Biol Chem 1995, 270(35):20643-20652. 10.1074/jbc.270.35.20643, 7657644.
    • (1995) J Biol Chem , vol.270 , Issue.35 , pp. 20643-20652
    • Moser, M.J.1    Lee, S.Y.2    Klevit, R.E.3    Davis, T.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.