메뉴 건너뛰기




Volumn 70, Issue 7, 2013, Pages 1185-1206

Recent progress in intein research: From mechanism to directed evolution and applications

Author keywords

Enzyme mechanism; Post translational modification; Protein chemistry; Protein engineering; Protein semisynthesis; Protein splicing

Indexed keywords

EXTEIN; INTEIN;

EID: 84876461880     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1120-4     Document Type: Review
Times cited : (94)

References (137)
  • 1
    • 0025240361 scopus 로고
    • Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
    • 2139027 1:CAS:528:DyaK3cXkslahsL4%3D
    • Hirata R, Ohsumk Y, Nakano A, Kawasaki H, Suzuki K, Anraku Y (1990) Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J Biol Chem 265:6726-6733
    • (1990) J Biol Chem , vol.265 , pp. 6726-6733
    • Hirata, R.1    Ohsumk, Y.2    Nakano, A.3    Kawasaki, H.4    Suzuki, K.5    Anraku, Y.6
  • 2
    • 0025226104 scopus 로고
    • +-adenosine triphosphatase
    • Kane PM, Yamashiro CT, Wolczyk DF, Neff N, Goebl M, Stevens TH (1990) Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase. Science 250:651-657 (Pubitemid 120034281)
    • (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
  • 3
    • 0032498234 scopus 로고    scopus 로고
    • Protein splicing of inteins and hedgehog autoproteolysis: Structure, function, and evolution
    • DOI 10.1016/S0092-8674(00)80892-2
    • Perler FB (1998) Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution. Cell 92:1-4 (Pubitemid 28053291)
    • (1998) Cell , vol.92 , Issue.1 , pp. 1-4
    • Perler, F.B.1
  • 4
    • 0034511180 scopus 로고    scopus 로고
    • Protein-splicing intein: Genetic mobility, origin, and evolution
    • DOI 10.1146/annurev.genet.34.1.61
    • Liu XQ (2000) Protein-splicing intein: genetic mobility, origin, and evolution. Annu Rev Genet 34:61-76 (Pubitemid 32065916)
    • (2000) Annual Review of Genetics , vol.34 , pp. 61-76
    • Liu, X.-Q.1
  • 5
    • 0035425040 scopus 로고    scopus 로고
    • Intein spread and extinction in evolution
    • DOI 10.1016/S0168-9525(01)02365-4, PII S0168952501023654
    • Pietrokovski S (2001) Intein spread and extinction in evolution. Trends Genet 17:465-472 (Pubitemid 32727239)
    • (2001) Trends in Genetics , vol.17 , Issue.8 , pp. 465-472
    • Pietrokovski, S.1
  • 7
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The intein database
    • 11752343 1:CAS:528:DC%2BD38Xht12rsb0%3D 10.1093/nar/30.1.383
    • Perler FB (2002) InBase: the intein database. Nucleic Acids Res 30:383-384
    • (2002) Nucleic Acids Res , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 8
    • 0342813091 scopus 로고    scopus 로고
    • Crystal structure of a Hedgehog autoprocessing domain: Homology between Hedgehog and self-splicing proteins
    • DOI 10.1016/S0092-8674(01)80011-8
    • Hall TM, Porter JA, Young KE, Koonin EV, Beachy PA, Leahy DJ (1997) Crystal structure of a Hedgehog autoprocessing domain: homology between Hedgehog and self-splicing proteins. Cell 91:85-97 (Pubitemid 27431315)
    • (1997) Cell , vol.91 , Issue.1 , pp. 85-97
    • Tanaka Hall, T.M.1    Porter, J.A.2    Young, K.E.3    Koonin, E.V.4    Beachy, P.A.5    Leahy, D.J.6
  • 9
    • 3543025094 scopus 로고    scopus 로고
    • Protein splicing and auto-cleavage of bacterial intein-like domains lacking a C′-flanking nucleophilic residue
    • DOI 10.1074/jbc.M404562200
    • Dassa B, Haviv H, Amitai G, Pietrokovski S (2004) Protein splicing and auto-cleavage of bacterial intein-like domains lacking a C′-flanking nucleophilic residue. J Biol Chem 279:32001-32007 (Pubitemid 39014644)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32001-32007
    • Bassa, B.1    Haviv, H.2    Amitai, G.3    Pietrokovski, S.4
  • 10
    • 4744359173 scopus 로고    scopus 로고
    • New type of polyubiquitin-like genes with intein-like autoprocessing domains
    • DOI 10.1016/j.tig.2004.08.010, PII S0168952504002446
    • Dassa B, Yanai I, Pietrokovski S (2004) New type of polyubiquitin-like genes with intein-like autoprocessing domains. Trends Genet 20:538-542 (Pubitemid 39314559)
    • (2004) Trends in Genetics , vol.20 , Issue.11 , pp. 538-542
    • Dassa, B.1    Yanai, I.2    Pietrokovski, S.3
  • 11
    • 0030763705 scopus 로고    scopus 로고
    • Compilation and analysis of intein sequences
    • DOI 10.1093/nar/25.6.1087
    • Perler FB, Olsen GJ, Adam E (1997) Compilation and analysis of intein sequences. Nucleic Acids Res 25:1087-1093 (Pubitemid 27303196)
    • (1997) Nucleic Acids Research , vol.25 , Issue.6 , pp. 1087-1093
    • Perler, F.B.1    Olsen, G.J.2    Adam, E.3
  • 12
    • 77249097494 scopus 로고    scopus 로고
    • Splicing of the mycobacteriophage Bethlehem DnaB intein: Identification of a new mechanistic class of inteins that contain an obligate block F nucleophile
    • 19940146 1:CAS:528:DC%2BC3cXlvFClsA%3D%3D 10.1074/jbc.M109.069567
    • Tori K, Dassa B, Johnson MA, Southworth MW, Brace LE, Ishino Y, Pietrokovski S, Perler FB (2010) Splicing of the mycobacteriophage Bethlehem DnaB intein: identification of a new mechanistic class of inteins that contain an obligate block F nucleophile. J Biol Chem 285:2515-2526
    • (2010) J Biol Chem , vol.285 , pp. 2515-2526
    • Tori, K.1    Dassa, B.2    Johnson, M.A.3    Southworth, M.W.4    Brace, L.E.5    Ishino, Y.6    Pietrokovski, S.7    Perler, F.B.8
  • 13
    • 70350533119 scopus 로고    scopus 로고
    • Split inteins as versatile tools for protein semisynthesis
    • 19708049 1:CAS:528:DC%2BD1MXhtlans7nP 10.1002/cbic.200900370
    • Mootz HD (2009) Split inteins as versatile tools for protein semisynthesis. Chem Bio Chem 10:2579-2589
    • (2009) Chem Bio Chem , vol.10 , pp. 2579-2589
    • Mootz, H.D.1
  • 14
    • 77953043452 scopus 로고    scopus 로고
    • Inteins, valuable genetic elements in molecular biology and biotechnology
    • 20449740 1:CAS:528:DC%2BC3cXmtlGrs7s%3D 10.1007/s00253-010-2628-x
    • Elleuche S, Poggeler S (2010) Inteins, valuable genetic elements in molecular biology and biotechnology. Appl Microbiol Biotechnol 87:479-489
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 479-489
    • Elleuche, S.1    Poggeler, S.2
  • 15
    • 77957758860 scopus 로고    scopus 로고
    • Biological applications of protein splicing
    • 20946979 1:CAS:528:DC%2BC3cXht12qurnM 10.1016/j.cell.2010.09.031
    • Vila-Perello M, Muir TW (2010) Biological applications of protein splicing. Cell 143:191-200
    • (2010) Cell , vol.143 , pp. 191-200
    • Vila-Perello, M.1    Muir, T.W.2
  • 16
    • 77957907731 scopus 로고    scopus 로고
    • Protein trans-splicing and its use in structural biology: Opportunities and limitations
    • 1:CAS:528:DC%2BC3cXht1Kqt7fJ 10.1039/c0mb00034e
    • Volkmann G, Iwaï H (2010) Protein trans-splicing and its use in structural biology: opportunities and limitations. Mol Biosys 6:2110-2121
    • (2010) Mol Biosys , vol.6 , pp. 2110-2121
    • Volkmann, G.1    Iwaï, H.2
  • 17
    • 84876695347 scopus 로고    scopus 로고
    • Protein trans-splicing as a protein ligation tool to study protein structure and function
    • 10.1515/bmc.2011.014
    • Aranko AS, Volkmann G (2011) Protein trans-splicing as a protein ligation tool to study protein structure and function. Biomol Concepts 2:183-198
    • (2011) Biomol Concepts , vol.2 , pp. 183-198
    • Aranko, A.S.1    Volkmann, G.2
  • 18
    • 80155161989 scopus 로고    scopus 로고
    • Split inteins: Nature's protein ligases
    • 1:CAS:528:DC%2BC3MXhtl2gsbzP 10.1002/ijch.201100094
    • Shah NH, Muir TW (2011) Split inteins: nature's protein ligases. Isr J Chem 51:854-861
    • (2011) Isr J Chem , vol.51 , pp. 854-861
    • Shah, N.H.1    Muir, T.W.2
  • 19
    • 70349446285 scopus 로고    scopus 로고
    • Protein splicing: A versatile tool for drug discovery
    • 19442693 1:CAS:528:DC%2BD1MXht1Wrsb7K 10.1016/j.addr.2009.04.021
    • Cheriyan M, Perler FB (2009) Protein splicing: a versatile tool for drug discovery. Adv Drug Deliv Rev 61:899-907
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 899-907
    • Cheriyan, M.1    Perler, F.B.2
  • 20
    • 70349439112 scopus 로고    scopus 로고
    • Splicing up" drug discovery. Cell-based expression and screening of genetically encoded libraries of backbone-cyclized polypeptides
    • 19628015 1:CAS:528:DC%2BD1MXht1Wrsb7L 10.1016/j.addr.2009.07.003
    • Sancheti H, Camarero JA (2009) "Splicing up" drug discovery. Cell-based expression and screening of genetically encoded libraries of backbone-cyclized polypeptides. Adv Drug Deliv Rev 61:908-917
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 908-917
    • Sancheti, H.1    Camarero, J.A.2
  • 21
    • 0029838842 scopus 로고    scopus 로고
    • The mechanism of protein splicing and its modulation by mutation
    • Xu MQ, Perler FB (1996) The mechanism of protein splicing and its modulation by mutation. EMBO J 15:5146-5153 (Pubitemid 26336196)
    • (1996) EMBO Journal , vol.15 , Issue.19 , pp. 5146-5153
    • Xu, M.-Q.1    Perler, F.B.2
  • 22
    • 0034665054 scopus 로고    scopus 로고
    • An alternative protein splicing mechanism for inteins lacking an N-terminal nucleophile
    • 10990465 1:CAS:528:DC%2BD3cXntVartLk%3D 10.1093/emboj/19.18.5019
    • Southworth MW, Benner J, Perler FB (2000) An alternative protein splicing mechanism for inteins lacking an N-terminal nucleophile. EMBO J 19:5019-5026
    • (2000) EMBO J , vol.19 , pp. 5019-5026
    • Southworth, M.W.1    Benner, J.2    Perler, F.B.3
  • 23
    • 82955169570 scopus 로고    scopus 로고
    • Branched intermediate formation is the slowest step in the protein splicing reaction of the Ala1 KlbA intein from Methanococcus jannaschii
    • 10.1021/bi200810j 1:CAS:528:DC%2BC3MXhtlKjsrnE
    • Saleh L, Southworth MW, Considine N, O'Neill C, Benner J, Bollinger JM Jr, Perler FB (2012) Branched intermediate formation is the slowest step in the protein splicing reaction of the Ala1 KlbA intein from Methanococcus jannaschii. Biochemistry 50:10576-10589
    • (2012) Biochemistry , vol.50 , pp. 10576-10589
    • Saleh, L.1    Southworth, M.W.2    Considine, N.3    O'Neill, C.4    Benner, J.5    Bollinger Jr., J.M.6    Perler, F.B.7
  • 25
    • 77955120112 scopus 로고    scopus 로고
    • The Deinococcus radiodurans Snf2 intein caught in the act: Detection of the class 3 intein signature block F branched intermediate
    • 20521254 1:CAS:528:DC%2BC3cXptlarurc%3D 10.1002/pro.431
    • Brace LE, Southworth MW, Tori K, Cushing ML, Perler F (2010) The Deinococcus radiodurans Snf2 intein caught in the act: detection of the class 3 intein signature block F branched intermediate. Protein Sci 19:1525-1533
    • (2010) Protein Sci , vol.19 , pp. 1525-1533
    • Brace, L.E.1    Southworth, M.W.2    Tori, K.3    Cushing, M.L.4    Perler, F.5
  • 26
    • 79551469666 scopus 로고    scopus 로고
    • Canonical protein splicing of a class one intein that has a class three non-canonical sequence motif
    • 21131486 1:CAS:528:DC%2BC3MXhtVWkur7N 10.1128/JB.01287-10
    • Reitter JN, Mills KV (2011) Canonical protein splicing of a class one intein that has a class three non-canonical sequence motif. J Bacteriol 193:994-997
    • (2011) J Bacteriol , vol.193 , pp. 994-997
    • Reitter, J.N.1    Mills, K.V.2
  • 27
    • 79955387027 scopus 로고    scopus 로고
    • Expanding the definition of class 3 inteins and their proposed phage origin
    • 21317331 1:CAS:528:DC%2BC3MXotVyqtLk%3D 10.1128/JB.01407-10
    • Tori K, Perler FB (2011) Expanding the definition of class 3 inteins and their proposed phage origin. J Bacteriol 193:2035-2041
    • (2011) J Bacteriol , vol.193 , pp. 2035-2041
    • Tori, K.1    Perler, F.B.2
  • 28
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • 10966466 1:CAS:528:DC%2BD3cXnt1ajtbg%3D 10.1146/annurev.biochem.69.1.447
    • Paulus H (2000) Protein splicing and related forms of protein autoprocessing. Annu Rev Biochem 69:447-496
    • (2000) Annu Rev Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 29
    • 67650480533 scopus 로고    scopus 로고
    • Protein autoproteolysis: Conformational strain linked to the rate of peptide cleavage by the pH dependence of the N → O acyl shift reaction
    • 19534521 1:CAS:528:DC%2BD1MXnsVWgtb8%3D 10.1021/ja9010817
    • Johansson DG, Wallin G, Sandberg A, Macao B, Aqvist J, Hard T (2009) Protein autoproteolysis: conformational strain linked to the rate of peptide cleavage by the pH dependence of the N → O acyl shift reaction. J Am Chem Soc 131:9475-9477
    • (2009) J Am Chem Soc , vol.131 , pp. 9475-9477
    • Johansson, D.G.1    Wallin, G.2    Sandberg, A.3    MacAo, B.4    Aqvist, J.5    Hard, T.6
  • 30
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • 7477383 1:CAS:528:DyaK2MXps1amsLw%3D 10.1038/378416a0
    • Brannigan JA, Dodson G, Duggleby HJ, Moody PC, Smith JL, Tomchick DR, Murzin AG (1995) A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378:416-419
    • (1995) Nature , vol.378 , pp. 416-419
    • Brannigan, J.A.1    Dodson, G.2    Duggleby, H.J.3    Moody, P.C.4    Smith, J.L.5    Tomchick, D.R.6    Murzin, A.G.7
  • 32
    • 0030952831 scopus 로고    scopus 로고
    • Identification of three core regions essential for protein splicing of the yeast Vma1 protozyme. A random mutagenesis study of the entire VMA1- derived endonuclease sequence
    • DOI 10.1074/jbc.272.25.15668
    • Kawasaki M, Nogami S, Satow Y, Ohya Y, Anraku Y (1997) Identification of three core regions essential for protein splicing of the yeast Vma1 protozyme. A random mutagenesis study of the entire Vma1-derived endonuclease sequence. J Biol Chem 272:15668-15674 (Pubitemid 27265537)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 15668-15674
    • Kawasaki, M.1    Nogami, S.2    Satow, Y.3    Ohya, Y.4    Anraku, Y.5
  • 33
    • 0035968177 scopus 로고    scopus 로고
    • Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein
    • 11331276 1:CAS:528:DC%2BD3MXltVWis7o%3D 10.1074/jbc.M011049200
    • Ghosh I, Sun L, Xu MQ (2001) Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein. J Biol Chem 276:24051-24058
    • (2001) J Biol Chem , vol.276 , pp. 24051-24058
    • Ghosh, I.1    Sun, L.2    Xu, M.Q.3
  • 34
    • 0031975772 scopus 로고    scopus 로고
    • Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing
    • DOI 10.1038/nsb0198-31
    • Klabunde T, Sharma S, Telenti A, Jacobs WR Jr, Sacchettini JC (1998) Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing. Nat Struct Biol 5:31-36 (Pubitemid 28048974)
    • (1998) Nature Structural Biology , vol.5 , Issue.1 , pp. 31-36
    • Klabunde, T.1    Sharma, S.2    Telenti, A.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 35
    • 0034595699 scopus 로고    scopus 로고
    • Structural insights into the protein splicing mechanism of PI-SceI
    • DOI 10.1074/jbc.275.22.16408
    • Poland BW, Xu MQ, Quiocho FA (2000) Structural insights into the protein splicing mechanism of PI-SceI. J Biol Chem 275:16408-16413 (Pubitemid 30398859)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16408-16413
    • Poland, B.W.1    Xu, M.-Q.2    Quiocho, F.A.3
  • 36
    • 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
    • DOI 10.1074/jbc.M306197200
    • Ding Y, Xu MQ, Ghosh I, Chen X, Ferrandon S, Lesage G, Rao Z (2003) Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing. J Biol Chem 278:39133-39142 (Pubitemid 37221816)
    • (2003) 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
  • 37
    • 0036295886 scopus 로고    scopus 로고
    • Protein-splicing reaction via a thiazolidine intermediate: Crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides
    • DOI 10.1006/jmbi.2001.5357
    • Mizutani R, Nogami S, Kawasaki M, Ohya Y, Anraku Y, Satow Y (2002) Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides. J Mol Biol 316:919-929 (Pubitemid 34722131)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.4 , pp. 919-929
    • Mizutani, R.1    Nogami, S.2    Kawasaki, M.3    Ohya, Y.4    Anraku, Y.5    Satow, Y.6
  • 38
    • 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
    • DOI 10.1016/j.jmb.2005.09.039, PII S0022283605011058
    • Sun P, Ye S, Ferrandon S, Evans TC, Xu MQ, Rao Z (2005) 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. J Mol Biol 353:1093-1105 (Pubitemid 41503274)
    • (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
  • 39
    • 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
    • DOI 10.1016/j.jmb.2006.12.050, PII S0022283606017281
    • Van Roey P, Pereira B, Li Z, Hiraga K, Belfort M, Derbyshire V (2007) Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue. J Mol Biol 367:162-173 (Pubitemid 46274715)
    • (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
  • 40
    • 68849086984 scopus 로고    scopus 로고
    • Highly conserved histidine plays a dual catalytic role in protein splicing: A pKa shift mechanism
    • 19630416 1:CAS:528:DC%2BD1MXovF2lsrY%3D 10.1021/ja904318w
    • Du Z, Shemella PT, Liu Y, McCallum SA, Pereira B, Nayak SK, Belfort G, Belfort M, Wang C (2009) Highly conserved histidine plays a dual catalytic role in protein splicing: a pKa shift mechanism. J Am Chem Soc 131:11581-11589
    • (2009) J Am Chem Soc , vol.131 , pp. 11581-11589
    • Du, Z.1    Shemella, P.T.2    Liu, Y.3    McCallum, S.A.4    Pereira, B.5    Nayak, S.K.6    Belfort, G.7    Belfort, M.8    Wang, C.9
  • 42
    • 34250196882 scopus 로고    scopus 로고
    • Sequence requirements for splicing by the Cne PRP8 intein
    • DOI 10.1016/j.febslet.2007.05.060, PII S0014579307005960
    • Pearl EJ, Tyndall JD, Poulter RT, Wilbanks SM (2007) Sequence requirements for splicing by the Cne PRP8 intein. FEBS Lett 581:3000-3004 (Pubitemid 46899045)
    • (2007) FEBS Letters , vol.581 , Issue.16 , pp. 3000-3004
    • Pearl, E.J.1    Tyndall, J.D.A.2    Poulter, R.T.M.3    Wilbanks, S.M.4
  • 44
    • 0031938897 scopus 로고    scopus 로고
    • Modular organization of inteins and C-terminal autocatalytic domains
    • Pietrokovski S (1998) Modular organization of inteins and C-terminal autocatalytic domains. Protein Sci 7:64-71 (Pubitemid 28133746)
    • (1998) Protein Science , vol.7 , Issue.1 , pp. 64-71
    • Pietrokovski, S.1
  • 45
    • 84859165560 scopus 로고    scopus 로고
    • The Thermococcus kodakaraensis Tko CDC21-1 intein activates its N-terminal splice junction in the absence of a conserved histidine by a compensatory mechanism
    • 22380677 1:CAS:528:DC%2BC38XjtVWitLY%3D 10.1021/bi201840k
    • Tori K, Cheriyan M, Pedamallu CS, Contreras MA, Perler FB (2012) The Thermococcus kodakaraensis Tko CDC21-1 intein activates its N-terminal splice junction in the absence of a conserved histidine by a compensatory mechanism. Biochemistry 51:2496-2505
    • (2012) Biochemistry , vol.51 , pp. 2496-2505
    • Tori, K.1    Cheriyan, M.2    Pedamallu, C.S.3    Contreras, M.A.4    Perler, F.B.5
  • 46
    • 79959880313 scopus 로고    scopus 로고
    • PK(a) coupling at the intein active site: Implications for the coordination mechanism of protein splicing with a conserved aspartate
    • 21604815 1:CAS:528:DC%2BC3MXnt1ahtbo%3D 10.1021/ja203209f
    • Du Z, Zheng Y, Patterson M, Liu Y, Wang C (2011) pK(a) coupling at the intein active site: implications for the coordination mechanism of protein splicing with a conserved aspartate. J Am Chem Soc 133:10275-10282
    • (2011) J Am Chem Soc , vol.133 , pp. 10275-10282
    • Du, Z.1    Zheng, Y.2    Patterson, M.3    Liu, Y.4    Wang, C.5
  • 47
    • 84856847690 scopus 로고    scopus 로고
    • Probing intein-catalyzed thioester formation by unnatural amino acid substitutions in the active site
    • 22182201 1:CAS:528:DC%2BC3MXhs1ers73P 10.1021/bi2014823
    • Schwarzer D, Ludwig C, Thiel IV, Mootz HD (2012) Probing intein-catalyzed thioester formation by unnatural amino acid substitutions in the active site. Biochemistry 51:233-242
    • (2012) Biochemistry , vol.51 , pp. 233-242
    • Schwarzer, D.1    Ludwig, C.2    Thiel, I.V.3    Mootz, H.D.4
  • 48
    • 65249150809 scopus 로고    scopus 로고
    • Novel Split Intein for trans-splicing synthetic peptide onto C-terminus of protein
    • 19136555 1:CAS:528:DC%2BD1MXisVSkt7Y%3D 10.1074/jbc.M805474200
    • Appleby JH, Zhou K, Volkmann G, Liu XQ (2009) Novel Split Intein for trans-splicing synthetic peptide onto C-terminus of protein. J Biol Chem 284:6194-6199
    • (2009) J Biol Chem , vol.284 , pp. 6194-6199
    • Appleby, J.H.1    Zhou, K.2    Volkmann, G.3    Liu, X.Q.4
  • 49
    • 80052469458 scopus 로고    scopus 로고
    • Intein lacking conserved C-terminal motif G retains controllable N-cleavage activity
    • 21787376 1:CAS:528:DC%2BC3MXht1SitrfO 10.1111/j.1742-4658.2011.08266.x
    • Volkmann G, Liu XQ (2011) Intein lacking conserved C-terminal motif G retains controllable N-cleavage activity. FEBS J 278:3431-3446
    • (2011) FEBS J , vol.278 , pp. 3431-3446
    • Volkmann, G.1    Liu, X.Q.2
  • 50
    • 54449093009 scopus 로고    scopus 로고
    • Interaction studies and alanine scanning analysis of a semi-synthetic split intein reveal thiazoline ring formation from an intermediate of the protein splicing reaction
    • 18625708 1:CAS:528:DC%2BD1cXhtVyisLrO 10.1074/jbc.M802972200
    • Ludwig C, Schwarzer D, Mootz HD (2008) Interaction studies and alanine scanning analysis of a semi-synthetic split intein reveal thiazoline ring formation from an intermediate of the protein splicing reaction. J Biol Chem 283:25264-25272
    • (2008) J Biol Chem , vol.283 , pp. 25264-25272
    • Ludwig, C.1    Schwarzer, D.2    Mootz, H.D.3
  • 51
    • 58149471991 scopus 로고    scopus 로고
    • 3-Mercaptopropionic acid-mediated synthesis of peptide and protein thioesters
    • Kang J, Richardson JP, Macmillan D (2009) 3-Mercaptopropionic acid-mediated synthesis of peptide and protein thioesters. Chem Commun (Camb) 407-409
    • (2009) Chem Commun (Camb) , pp. 407-409
    • Kang, J.1    Richardson, J.P.2    MacMillan, D.3
  • 52
    • 77951100124 scopus 로고    scopus 로고
    • Peptide and protein thioester synthesis via N → S acyl transfer
    • 20401371 1:CAS:528:DC%2BC3cXkvVent7o%3D 10.1039/b925075a
    • Kang J, Macmillan D (2010) Peptide and protein thioester synthesis via N → S acyl transfer. Org Biomol Chem 8:1993-2002
    • (2010) Org Biomol Chem , vol.8 , pp. 1993-2002
    • Kang, J.1    MacMillan, D.2
  • 53
    • 33846923785 scopus 로고    scopus 로고
    • Sequential peptide ligation by using a controlled cysteinyl prolyl ester (CPE) autoactivating unit
    • DOI 10.1016/j.tetlet.2007.01.086, PII S0040403907001530
    • Kawakami T, Aimoto S (2007) Sequential peptide ligation by using a controlled cysteinyl prolyl ester (CPE) autoactivating unit. Tetrahedron Lett 48:1903-1905 (Pubitemid 46241320)
    • (2007) Tetrahedron Letters , vol.48 , Issue.11 , pp. 1903-1905
    • Kawakami, T.1    Aimoto, S.2
  • 54
    • 79551681995 scopus 로고    scopus 로고
    • Spontaneous proton transfer to a conserved intein residue determines on-pathway protein splicing
    • 21185311 1:CAS:528:DC%2BC3MXhsFOntbk%3D 10.1016/j.jmb.2010.12.024
    • Pereira B, Shemella PT, Amitai G, Belfort G, Nayak SK, Belfort M (2011) Spontaneous proton transfer to a conserved intein residue determines on-pathway protein splicing. J Mol Biol 406:430-442
    • (2011) J Mol Biol , vol.406 , pp. 430-442
    • Pereira, B.1    Shemella, P.T.2    Amitai, G.3    Belfort, G.4    Nayak, S.K.5    Belfort, M.6
  • 55
    • 0032562685 scopus 로고    scopus 로고
    • Modulation of protein splicing of the Saccharomyces cerevisiae vacuolar membrane ATPase intein
    • DOI 10.1074/jbc.273.17.10567
    • Chong S, Williams KS, Wotkowicz C, Xu MQ (1998) Modulation of protein splicing of the Saccharomyces cerevisiae vacuolar membrane ATPase intein. J Biol Chem 273:10567-10577 (Pubitemid 28227668)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.17 , pp. 10567-10577
    • Chong, S.1    Williams, K.S.2    Wotkowicz, C.3    Xu, M.-Q.4
  • 56
    • 0035814803 scopus 로고    scopus 로고
    • Characterization of a naturally occurring trans-splicing intein from Synechocystis sp. PCC6803
    • DOI 10.1021/bi001786g
    • Martin DD, Xu MQ, Evans TC Jr (2001) Characterization of a naturally occurring trans-splicing intein from Synechocystis sp. PCC6803. Biochemistry 40:1393-1402 (Pubitemid 32142901)
    • (2001) Biochemistry , vol.40 , Issue.5 , pp. 1393-1402
    • Martin, D.D.1    Xu, M.-Q.2    Evans Jr., T.C.3
  • 57
    • 60749092724 scopus 로고    scopus 로고
    • The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction
    • 19302791 1:CAS:528:DC%2BD1MXis1aqtb0%3D 10.1016/j.febslet.2009.02.003
    • Zettler J, Schutz V, Mootz HD (2009) The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction. FEBS Lett 583:909-914
    • (2009) FEBS Lett , vol.583 , pp. 909-914
    • Zettler, J.1    Schutz, V.2    Mootz, H.D.3
  • 58
    • 77953806959 scopus 로고    scopus 로고
    • Branched intermediate formation stimulates peptide bond cleavage in protein splicing
    • 20495572 1:CAS:528:DC%2BC3cXmsVWnt78%3D 10.1038/nchembio.371
    • Frutos S, Goger M, Giovani B, Cowburn D, Muir TW (2010) Branched intermediate formation stimulates peptide bond cleavage in protein splicing. Nat Chem Biol 6:527-533
    • (2010) Nat Chem Biol , vol.6 , pp. 527-533
    • Frutos, S.1    Goger, M.2    Giovani, B.3    Cowburn, D.4    Muir, T.W.5
  • 59
    • 0027984269 scopus 로고
    • Protein splicing: An analysis of the branched intermediate and its resolution by succinimide formation
    • Xu MQ, Comb DG, Paulus H, Noren CJ, Shao Y, Perler FB (1994) Protein splicing: an analysis of the branched intermediate and its resolution by succinimide formation. EMBO J 13:5517-5522 (Pubitemid 24363018)
    • (1994) EMBO Journal , vol.13 , Issue.23 , pp. 5517-5522
    • Xu, M.-Q.1    Comb, D.G.2    Paulus, H.3    Noren, C.J.4    Shao, Y.5    Perler, F.B.6
  • 60
    • 0029124041 scopus 로고
    • Protein splicing: Characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence
    • 7662664 1:CAS:528:DyaK2MXnsVKrtbk%3D 10.1021/bi00034a017
    • Shao Y, Xu MQ, Paulus H (1995) Protein splicing: characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence. Biochemistry 34:10844-10850
    • (1995) Biochemistry , vol.34 , pp. 10844-10850
    • Shao, Y.1    Xu, M.Q.2    Paulus, H.3
  • 61
    • 0024516367 scopus 로고
    • Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins
    • Stephenson RC, Clarke S (1989) Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J Biol Chem 264:6164-6170 (Pubitemid 19106686)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.11 , pp. 6164-6170
    • Stephenson, R.C.1    Clarke, S.2
  • 62
    • 84962374624 scopus 로고    scopus 로고
    • Mechanism for intein C-terminal cleavage: A proposal from quantum mechanical calculations
    • DOI 10.1529/biophysj.106.092049
    • Shemella P, Pereira B, Zhang Y, Van Roey P, Belfort G, Garde S, Nayak SK (2007) Mechanism for intein C-terminal cleavage: a proposal from quantum mechanical calculations. Biophys J 92:847-853 (Pubitemid 46203214)
    • (2007) Biophysical Journal , vol.92 , Issue.3 , pp. 847-853
    • Shemella, P.1    Pereira, B.2    Zhang, Y.3    Van Roey, P.4    Belfort, G.5    Garde, S.6    Nayak, S.K.7
  • 63
    • 0032832776 scopus 로고    scopus 로고
    • A genetic system yields self-cleaving inteins for bioseparations
    • DOI 10.1038/12879
    • Wood DW, Wu W, Belfort G, Derbyshire V, Belfort M (1999) A genetic system yields self-cleaving inteins for bioseparations. Nat Biotechnol 17:889-892 (Pubitemid 29416663)
    • (1999) Nature Biotechnology , vol.17 , Issue.9 , pp. 889-892
    • Wood, D.W.1    Wu, W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5
  • 64
    • 0033614484 scopus 로고    scopus 로고
    • Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: Facile production of protein building blocks for protein ligation
    • DOI 10.1016/S0378-1119(99)00103-1, PII S0378111999001031
    • Mathys S, Evans TC, Chute IC, Wu H, Chong S, Benner J, Liu XQ, Xu MQ (1999) Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: facile production of protein building blocks for protein ligation. Gene 231:1-13 (Pubitemid 29307767)
    • (1999) Gene , vol.231 , Issue.1-2 , pp. 1-13
    • Mathys, S.1    Evans Jr., T.C.2    Chute, I.C.3    Wu, H.4    Chong, S.5    Benner, J.6    Liu, X.-Q.7    Xu, M.-Q.8
  • 65
    • 0034518359 scopus 로고    scopus 로고
    • Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor
    • DOI 10.1021/bp0000858
    • Wood DW, Derbyshire V, Wu W, Chartrain M, Belfort M, Belfort G (2000) Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor. Biotechnol Prog 16:1055-1063 (Pubitemid 32044859)
    • (2000) Biotechnology Progress , vol.16 , Issue.6 , pp. 1055-1063
    • Wood, D.W.1    Derbyshire, V.2    Wu, W.3    Chartrain, M.4    Belfort, M.5    Belfort, G.6
  • 66
    • 66349131346 scopus 로고    scopus 로고
    • Modeling protein splicing: Reaction pathway for C-terminal splice and intein scission
    • 19326906 1:CAS:528:DC%2BD1MXjslels7Y%3D 10.1021/jp808911p
    • Mujika JI, Lopez X, Mulholland AJ (2009) Modeling protein splicing: reaction pathway for C-terminal splice and intein scission. J Phys Chem B 113:5607-5616
    • (2009) J Phys Chem B , vol.113 , pp. 5607-5616
    • Mujika, J.I.1    Lopez, X.2    Mulholland, A.J.3
  • 67
    • 54349101831 scopus 로고    scopus 로고
    • Site-specific chemical modification of proteins with a prelabelled cysteine tag using the artificially split Mxe GyrA intein
    • 18756552 1:CAS:528:DC%2BD1cXht1CltrfI 10.1002/cbic.200800319
    • Kurpiers T, Mootz HD (2008) Site-specific chemical modification of proteins with a prelabelled cysteine tag using the artificially split Mxe GyrA intein. ChemBioChem 9:2317-2325
    • (2008) ChemBioChem , vol.9 , pp. 2317-2325
    • Kurpiers, T.1    Mootz, H.D.2
  • 68
    • 0030800808 scopus 로고    scopus 로고
    • Protein splicing: Estimation of the rate of O-N and S-N acyl rearrangements, the last step of the splicing process
    • Shao Y, Paulus H (1997) Protein splicing: estimation of the rate of O-N and S-N acyl rearrangements, the last step of the splicing process. J Pept Res 50:193-198 (Pubitemid 27381448)
    • (1997) Journal of Peptide Research , vol.50 , Issue.3 , pp. 193-198
    • Shao, Y.1    Paulus, H.2
  • 69
    • 67650492166 scopus 로고    scopus 로고
    • Modulation of intein activity by its neighboring extein substrates
    • 19541659 1:CAS:528:DC%2BD1MXptVSnurs%3D 10.1073/pnas.0904366106
    • Amitai G, Callahan BP, Stanger MJ, Belfort G, Belfort M (2009) Modulation of intein activity by its neighboring extein substrates. Proc Natl Acad Sci USA 106:11005-11010
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11005-11010
    • Amitai, G.1    Callahan, B.P.2    Stanger, M.J.3    Belfort, G.4    Belfort, M.5
  • 70
    • 80255122748 scopus 로고    scopus 로고
    • Evaluation and comparison of protein splicing by exogenous inteins with foreign exteins in Escherichia coli
    • 22001202 10.1016/j.febslet.2011.10.005 1:CAS:528:DC%2BC3MXhtl2ru7bL
    • Ellila S, Jurvansuu JM, Iwai H (2011) Evaluation and comparison of protein splicing by exogenous inteins with foreign exteins in Escherichia coli. FEBS Lett 585:3471-3477
    • (2011) FEBS Lett , vol.585 , pp. 3471-3477
    • Ellila, S.1    Jurvansuu, J.M.2    Iwai, H.3
  • 71
    • 84863893133 scopus 로고    scopus 로고
    • Ultrafast protein splicing is common among cyanobacterial split inteins: Implications for protein engineering
    • 22734434 1:CAS:528:DC%2BC38XptF2iu7Y%3D 10.1021/ja303226x
    • Shah NH, Dann GP, Vila-Perello M, Liu Z, Muir TW (2012) Ultrafast protein splicing is common among cyanobacterial split inteins: implications for protein engineering. J Am Chem Soc 134(28):11338-11341
    • (2012) J Am Chem Soc , vol.134 , Issue.28 , pp. 11338-11341
    • Shah, N.H.1    Dann, G.P.2    Vila-Perello, M.3    Liu, Z.4    Muir, T.W.5
  • 72
    • 84863505557 scopus 로고    scopus 로고
    • NMR and crystal structures of the Pyrococcus horikoshii RadA intein guide a strategy for engineering a highly efficient and promiscuous intein
    • 10.1016/j.jmb.2012.04.029 1:CAS:528:DC%2BC38Xns1Wjtro%3D
    • Øemig JS, Zhou D, Kajander T, Wlodawer A, Iwai H (2012) NMR and crystal structures of the Pyrococcus horikoshii RadA intein guide a strategy for engineering a highly efficient and promiscuous intein. J Mol Biol 421(1):85-99
    • (2012) J Mol Biol , vol.421 , Issue.1 , pp. 85-99
    • Øemig, J.S.1    Zhou, D.2    Kajander, T.3    Wlodawer, A.4    Iwai, H.5
  • 73
    • 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 (2002) 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 4:479-487 (Pubitemid 35291216)
    • (2002) Journal of Molecular Microbiology and Biotechnology , vol.4 , Issue.5 , pp. 479-487
    • Adam, E.1    Perler, F.B.2
  • 75
  • 76
    • 70350161834 scopus 로고    scopus 로고
    • Temperature-sensitive mutations made easy: Generating conditional mutations by using temperature-sensitive inteins that function within different temperature ranges
    • 19596904 1:CAS:528:DC%2BD1MXhtlWksbnI 10.1534/genetics.109.104794
    • Tan G, Chen M, Foote C, Tan C (2009) Temperature-sensitive mutations made easy: generating conditional mutations by using temperature-sensitive inteins that function within different temperature ranges. Genetics 183:13-22
    • (2009) Genetics , vol.183 , pp. 13-22
    • Tan, G.1    Chen, M.2    Foote, C.3    Tan, C.4
  • 78
    • 28444477686 scopus 로고    scopus 로고
    • Minimization and stabilization of the Mycobacterium tuberculosis recA intein
    • DOI 10.1016/j.jmb.2005.09.088, PII S0022283605011009
    • Hiraga K, Derbyshire V, Dansereau JT, Van Roey P, Belfort M (2005) Minimization and stabilization of the Mycobacterium tuberculosis recA intein. J Mol Biol 354:916-926 (Pubitemid 41735512)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.4 , pp. 916-926
    • Hiraga, K.1    Derbyshire, V.2    Dansereau, J.T.3    Van Roey, P.4    Belfort, M.5
  • 79
    • 67650472128 scopus 로고    scopus 로고
    • Traceless protein splicing utilizing evolved split inteins
    • 19541616 1:CAS:528:DC%2BD1MXptVSnuro%3D 10.1073/pnas.0902964106
    • Lockless SW, Muir TW (2009) Traceless protein splicing utilizing evolved split inteins. Proc Natl Acad Sci USA 106:10999-11004
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10999-11004
    • Lockless, S.W.1    Muir, T.W.2
  • 82
    • 80053206211 scopus 로고    scopus 로고
    • Highly efficient and more general cis- and trans-splicing inteins through sequential directed evolution
    • 21832069 1:CAS:528:DC%2BC3MXht1ajtbrP 10.1074/jbc.M111.277350
    • Appleby-Tagoe JH, Thiel IV, Wang Y, Wang Y, Mootz HD, Liu XQ (2011) Highly efficient and more general cis- and trans-splicing inteins through sequential directed evolution. J Biol Chem 286:34440-34447
    • (2011) J Biol Chem , vol.286 , pp. 34440-34447
    • Appleby-Tagoe, J.H.1    Thiel, I.V.2    Wang, Y.3    Wang, Y.4    Mootz, H.D.5    Liu, X.Q.6
  • 83
    • 77954386029 scopus 로고    scopus 로고
    • Backbone dynamics and global effects of an activating mutation in minimized Mtu RecA inteins
    • 20562025 1:CAS:528:DC%2BC3cXos1yrsrk%3D 10.1016/j.jmb.2010.05.044
    • Du Z, Liu Y, Ban D, Lopez MM, Belfort M, Wang C (2010) Backbone dynamics and global effects of an activating mutation in minimized Mtu RecA inteins. J Mol Biol 400:755-767
    • (2010) J Mol Biol , vol.400 , pp. 755-767
    • Du, Z.1    Liu, Y.2    Ban, D.3    Lopez, M.M.4    Belfort, M.5    Wang, C.6
  • 84
    • 0347517763 scopus 로고    scopus 로고
    • Distribution of split DnaE inteins in cyanobacteria
    • DOI 10.1046/j.1365-2958.2003.03825.x
    • Caspi J, Amitai G, Belenkiy O, Pietrokovski S (2003) Distribution of split DnaE inteins in cyanobacteria. Mol Microbiol 50:1569-1577 (Pubitemid 38010453)
    • (2003) Molecular Microbiology , vol.50 , Issue.5 , pp. 1569-1577
    • Caspi, J.1    Amitai, G.2    Belenkiy, O.3    Pietrokovski, S.4
  • 85
    • 33644912308 scopus 로고    scopus 로고
    • Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme
    • 16516207 1:CAS:528:DC%2BD28Xis1Wht74%3D 10.1016/j.febslet.2006.02.045
    • Iwai H, Züger S, Jin J, Tam PH (2006) Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme. FEBS Lett 580:1853-1858
    • (2006) FEBS Lett , vol.580 , pp. 1853-1858
    • Iwai, H.1    Züger, S.2    Jin, J.3    Tam, P.H.4
  • 86
    • 33846072572 scopus 로고    scopus 로고
    • Trans protein splicing of cyanobacterial split inteins in endogenous and exogenous combinations
    • DOI 10.1021/bi0611762
    • Dassa B, Amitai G, Caspi J, Schueler-Furman O, Pietrokovski S (2007) Trans protein splicing of cyanobacterial split inteins in endogenous and exogenous combinations. Biochemistry 46:322-330 (Pubitemid 46067761)
    • (2007) Biochemistry , vol.46 , Issue.1 , pp. 322-330
    • Dassa, B.1    Amitai, G.2    Caspi, J.3    Schueler-Furman, O.4    Pietrokovski, S.5
  • 87
    • 79957473350 scopus 로고    scopus 로고
    • Directed evolution of a small-molecule-triggered intein with improved splicing properties in mammalian cells
    • 21609843 1:CAS:528:DC%2BC3MXmslOksLs%3D 10.1016/j.chembiol.2011.02.014
    • Peck SH, Chen I, Liu DR (2011) Directed evolution of a small-molecule-triggered intein with improved splicing properties in mammalian cells. Chem Biol 18:619-630
    • (2011) Chem Biol , vol.18 , pp. 619-630
    • Peck, S.H.1    Chen, I.2    Liu, D.R.3
  • 88
    • 13244252218 scopus 로고    scopus 로고
    • Regulation of protein activity with small-molecule-controlled inteins
    • DOI 10.1110/ps.04996905
    • Skretas G, Wood DW (2005) Regulation of protein activity with small-molecule-controlled inteins. Protein Sci 14:523-532 (Pubitemid 40194605)
    • (2005) Protein Science , vol.14 , Issue.2 , pp. 523-532
    • Skretas, G.1    Wood, D.W.2
  • 90
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • DOI 10.1146/annurev.biochem.72.121801.161900
    • Muir TW (2003) Semisynthesis of proteins by expressed protein ligation. Annu Rev Biochem 72:249-289 (Pubitemid 36930447)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 91
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element
    • Evans TC Jr, Benner J, Xu MQ (1998) Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci 7:2256-2264 (Pubitemid 28506942)
    • (1998) Protein Science , vol.7 , Issue.11 , pp. 2256-2264
    • Evans Jr., T.C.1    Benner, J.2    Xu, M.-Q.3
  • 92
    • 0037208835 scopus 로고    scopus 로고
    • Purification of recombinant proteins from E. coli by engineered inteins
    • 12491879 1:CAS:528:DC%2BD38Xptleguro%3D
    • Xu MQ, Evans TC Jr (2003) Purification of recombinant proteins from E. coli by engineered inteins. Methods Mol Biol 205:43-68
    • (2003) Methods Mol Biol , vol.205 , pp. 43-68
    • Xu, M.Q.1    Evans Jr., T.C.2
  • 93
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • DOI 10.1038/nmeth886, PII N886
    • Muralidharan V, Muir TW (2006) Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat Methods 3:429-438 (Pubitemid 43811554)
    • (2006) Nature Methods , vol.3 , Issue.6 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 94
    • 18244394306 scopus 로고    scopus 로고
    • Development of a tandem protein trans-splicing system based on native and engineered split inteins
    • DOI 10.1021/ja042287w
    • Shi J, Muir TW (2005) Development of a tandem protein trans-splicing system based on native and engineered split inteins. J Am Chem Soc 127:6198-6206 (Pubitemid 40627742)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.17 , pp. 6198-6206
    • Shi, J.1    Muir, T.W.2
  • 95
    • 79954422992 scopus 로고    scopus 로고
    • Split intein facilitated tag affinity purification for recombinant proteins with controllable tag removal by inducible auto-cleavage
    • 21397239 1:CAS:528:DC%2BC3MXkvFWrt7k%3D 10.1016/j.chroma.2011.02.053
    • Lu W, Sun Z, Tang Y, Chen J, Tang F, Zhang J, Liu JN (2011) Split intein facilitated tag affinity purification for recombinant proteins with controllable tag removal by inducible auto-cleavage. J Chromatogr A 1218:2553-2560
    • (2011) J Chromatogr A , vol.1218 , pp. 2553-2560
    • Lu, W.1    Sun, Z.2    Tang, Y.3    Chen, J.4    Tang, F.5    Zhang, J.6    Liu, J.N.7
  • 96
    • 34447329908 scopus 로고    scopus 로고
    • Regioselective cysteine bioconjugation by appending a labeled cystein tag to a protein by using protein splicing in trans
    • DOI 10.1002/anie.200700719
    • Kurpiers T, Mootz HD (2007) Regioselective cysteine bioconjugation by appending a labeled cystein tag to a protein by using protein splicing in trans. Angew Chem Int Ed Engl 46:5234-5237 (Pubitemid 47051298)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.27 , pp. 5234-5237
    • Kurpiers, T.1    Mootz, H.D.2
  • 97
    • 65549084736 scopus 로고    scopus 로고
    • Expanding the scope of protein trans-splicing to fragment ligation of an integral membrane protein: Towards modulation of porin-based ion channels by chemical modification
    • 19322843 1:CAS:528:DC%2BD1MXltVOlsLo%3D 10.1002/cbic.200900039
    • Brenzel S, Cebi M, Reiss P, Koert U, Mootz HD (2009) Expanding the scope of protein trans-splicing to fragment ligation of an integral membrane protein: towards modulation of porin-based ion channels by chemical modification. ChemBioChem 10:983-986
    • (2009) ChemBioChem , vol.10 , pp. 983-986
    • Brenzel, S.1    Cebi, M.2    Reiss, P.3    Koert, U.4    Mootz, H.D.5
  • 98
    • 33747321396 scopus 로고    scopus 로고
    • Ligation of a synthetic peptide to the N-terminus of a recombinant protein using semisynthetic protein trans-splicing
    • 16823791 1:CAS:528:DC%2BD28Xot12mtbY%3D 10.1002/anie.200600570
    • Ludwig C, Pfeiff M, Linne U, Mootz HD (2006) Ligation of a synthetic peptide to the N-terminus of a recombinant protein using semisynthetic protein trans-splicing. Angew Chem Int Ed Engl 45:5218-5221
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 5218-5221
    • Ludwig, C.1    Pfeiff, M.2    Linne, U.3    Mootz, H.D.4
  • 99
    • 77954058847 scopus 로고    scopus 로고
    • Protein C-terminal labeling and biotinylation using synthetic peptide and split-intein
    • 20027230 10.1371/journal.pone.0008381 1:CAS:528:DC%2BD1MXhs1SitrbO
    • Volkmann G, Liu XQ (2009) Protein C-terminal labeling and biotinylation using synthetic peptide and split-intein. PLoS ONE 4:e8381
    • (2009) PLoS ONE , vol.4 , pp. 8381
    • Volkmann, G.1    Liu, X.Q.2
  • 100
    • 69049115141 scopus 로고    scopus 로고
    • Site-specific two-color protein labeling for FRET studies using split inteins
    • 19645470 1:CAS:528:DC%2BD1MXpt1KjsLg%3D 10.1021/ja9030215
    • Yang JY, Yang WY (2009) Site-specific two-color protein labeling for FRET studies using split inteins. J Am Chem Soc 131:11644-11645
    • (2009) J Am Chem Soc , vol.131 , pp. 11644-11645
    • Yang, J.Y.1    Yang, W.Y.2
  • 101
    • 36649015993 scopus 로고    scopus 로고
    • Construction of a small-molecule-integrated semisynthetic split intein for in vivo protein ligation
    • DOI 10.1039/b712843f
    • Ando T, Tsukiji S, Tanaka T, Nagamune T (2007) Construction of a small-molecule-integrated semisynthetic split intein for in vivo protein ligation. Chem Commun (Camb) 4995-4997 (Pubitemid 350197666)
    • (2007) Chemical Communications , Issue.47 , pp. 4995-4997
    • Ando, T.1    Tsukiji, S.2    Tanaka, T.3    Nagamune, T.4
  • 102
    • 74549213819 scopus 로고    scopus 로고
    • Intein-mediated site-specific conjugation of quantum dots to proteins in vivo
    • 10.1186/1477-3155-7-9 1:CAS:528:DC%2BD1MXhsFyhurbO
    • Charalambous A, Andreou M, Skourides PA (2009) Intein-mediated site-specific conjugation of quantum dots to proteins in vivo. J Nanobiotechnol 7:9
    • (2009) J Nanobiotechnol , vol.7 , pp. 9
    • Charalambous, A.1    Andreou, M.2    Skourides, P.A.3
  • 104
    • 78149365067 scopus 로고    scopus 로고
    • Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing
    • 20862726 1:CAS:528:DC%2BC3cXhtFyqtrrI 10.1002/psc.1227
    • Chu NK, Olschewski D, Seidel R, Winklhofer KF, Tatzelt J, Engelhard M, Becker CF (2010) Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing. J Pept Sci 16:582-588
    • (2010) J Pept Sci , vol.16 , pp. 582-588
    • Chu, N.K.1    Olschewski, D.2    Seidel, R.3    Winklhofer, K.F.4    Tatzelt, J.5    Engelhard, M.6    Becker, C.F.7
  • 105
    • 33746311225 scopus 로고    scopus 로고
    • Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing
    • DOI 10.1002/anie.200503475
    • Kwon Y, Coleman MA, Camarero JA (2006) Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing. Angew Chem Int Ed Engl 45:1726-1729 (Pubitemid 44105240)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.11 , pp. 1726-1729
    • Kwon, Y.1    Coleman, M.A.2    Camarero, J.A.3
  • 106
    • 0033492884 scopus 로고    scopus 로고
    • Characteristics of protein splicing in trans mediated by a semisynthetic split intein
    • DOI 10.1002/(SICI)1097-0282(1999)51:5 <355::AID-BIP5>3.0.CO;2-M
    • Lew BM, Mills KV, Paulus H (1999) Characteristics of protein splicing in trans-mediated by a semisynthetic split intein. Biopolymers 51:355-362 (Pubitemid 30117295)
    • (1999) Biopolymers - Peptide Science Section , vol.51 , Issue.5 , pp. 355-362
    • Lew, B.M.1    Mills, K.V.2    Paulus, H.3
  • 108
    • 67349189136 scopus 로고    scopus 로고
    • Solution structure of DnaE intein from Nostoc punctiforme: Structural basis for the design of a new split intein suitable for site-specific chemical modification
    • 10.1016/j.febslet.2009.03.058 1:CAS:528:DC%2BD1MXlsVKgsbw%3D
    • Øemig JS, Aranko AS, Djupsjöbacka J, Heinämäki K, Iwai H (2009) Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification. FEBS Lett 583:1451-1456
    • (2009) FEBS Lett , vol.583 , pp. 1451-1456
    • Øemig, J.S.1    Aranko, A.S.2    Djupsjöbacka, J.3    Heinämäki, K.4    Iwai, H.5
  • 109
    • 65249091343 scopus 로고    scopus 로고
    • In vivo and in vitro protein ligation by naturally occurring and engineered split DnaE inteins
    • 19365564 10.1371/journal.pone.0005185 1:CAS:528:DC%2BD1MXltFaitLs%3D
    • Aranko AS, Züger S, Buchinger E, Iwai H (2009) In vivo and in vitro protein ligation by naturally occurring and engineered split DnaE inteins. PLoS ONE 4:e5185
    • (2009) PLoS ONE , vol.4 , pp. 5185
    • Aranko, A.S.1    Züger, S.2    Buchinger, E.3    Iwai, H.4
  • 111
    • 84859592838 scopus 로고    scopus 로고
    • In-cell fluorescence activation and labeling of proteins mediated by FRET-quenched split inteins
    • 22404648 1:CAS:528:DC%2BC38Xjs1WksrY%3D 10.1021/ja300209u
    • Borra R, Dong D, Elnagar AY, Woldemariam GA, Camarero JA (2012) In-cell fluorescence activation and labeling of proteins mediated by FRET-quenched split inteins. J Am Chem Soc 134:6344-6353
    • (2012) J Am Chem Soc , vol.134 , pp. 6344-6353
    • Borra, R.1    Dong, D.2    Elnagar, A.Y.3    Woldemariam, G.A.4    Camarero, J.A.5
  • 112
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • 20307192 1:CAS:528:DC%2BC3cXpslShtrg%3D 10.1146/annurev.biochem.052308. 105824
    • Liu CC, Schultz PG (2010) Adding new chemistries to the genetic code. Annu Rev Biochem 79:413-444
    • (2010) Annu Rev Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 113
    • 84934437402 scopus 로고    scopus 로고
    • Bioluminescent imaging of MAPK function with intein-mediated reporter gene assay
    • 19685309 1:CAS:528:DC%2BC3cXos1Cmtbk%3D 10.1007/978-1-60327-321-3-15
    • Kanno A, Ozawa T, Umezawa Y (2009) Bioluminescent imaging of MAPK function with intein-mediated reporter gene assay. Methods Mol Biol 574:185-192
    • (2009) Methods Mol Biol , vol.574 , pp. 185-192
    • Kanno, A.1    Ozawa, T.2    Umezawa, Y.3
  • 114
    • 84934439113 scopus 로고    scopus 로고
    • Detection of apoptosis using cyclic luciferase in living mammals
    • 19685303 1:CAS:528:DC%2BC3cXos1CmtLk%3D 10.1007/978-1-60327-321-3-9
    • Kanno A, Umezawa Y, Ozawa T (2009) Detection of apoptosis using cyclic luciferase in living mammals. Methods Mol Biol 574:105-114
    • (2009) Methods Mol Biol , vol.574 , pp. 105-114
    • Kanno, A.1    Umezawa, Y.2    Ozawa, T.3
  • 115
    • 80655137633 scopus 로고    scopus 로고
    • Development of a novel DnaE intein-based assay for quantitative analysis of G-protein-coupled receptor internalization
    • 21726524 1:CAS:528:DC%2BC3MXptlCnsLo%3D 10.1016/j.ab.2011.06.005
    • Zhang Y, Yang W, Chen L, Shi Y, Li G, Zhou N (2011) Development of a novel DnaE intein-based assay for quantitative analysis of G-protein-coupled receptor internalization. Anal Biochem 417:65-72
    • (2011) Anal Biochem , vol.417 , pp. 65-72
    • Zhang, Y.1    Yang, W.2    Chen, L.3    Shi, Y.4    Li, G.5    Zhou, N.6
  • 116
    • 84856121254 scopus 로고    scopus 로고
    • Split-intein-mediated re-assembly of genetically encoded Ca(2+) indicators
    • 22133610 1:CAS:528:DC%2BC38Xht1Wku7g%3D 10.1016/j.ceca.2011.10.006
    • Wong SS, Kotera I, Mills E, Suzuki H, Truong K (2012) Split-intein-mediated re-assembly of genetically encoded Ca(2+) indicators. Cell Calcium 51:57-64
    • (2012) Cell Calcium , vol.51 , pp. 57-64
    • Wong, S.S.1    Kotera, I.2    Mills, E.3    Suzuki, H.4    Truong, K.5
  • 118
    • 62149136168 scopus 로고    scopus 로고
    • Intein-mediated protein assembly in transgenic wheat: Production of active barnase and acetolactate synthase from split genes
    • 19222807 1:CAS:528:DC%2BD1MXkslGqu7k%3D 10.1111/j.1467-7652.2008.00399.x
    • Kempe K, Rubtsova M, Gils M (2009) Intein-mediated protein assembly in transgenic wheat: production of active barnase and acetolactate synthase from split genes. Plant Biotechnol J 7:283-297
    • (2009) Plant Biotechnol J , vol.7 , pp. 283-297
    • Kempe, K.1    Rubtsova, M.2    Gils, M.3
  • 120
    • 33745968727 scopus 로고    scopus 로고
    • Control of transcription factor activity and osteoblast differentiation in mammalian cells using an evolved small-molecule-dependent intein
    • DOI 10.1021/ja062980e
    • Yuen CM, Rodda SJ, Vokes SA, McMahon AP, Liu DR (2006) Control of transcription factor activity and osteoblast differentiation in mammalian cells using an evolved small-molecule-dependent intein. J Am Chem Soc 128:8939-8946 (Pubitemid 44061552)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.27 , pp. 8939-8946
    • Yuen, C.M.1    Rodda, S.J.2    Vokes, S.A.3    McMahon, A.P.4    Liu, D.R.5
  • 121
  • 122
    • 0041854719 scopus 로고    scopus 로고
    • Conditional protein splicing: A new tool to control protein structure and function in vitro and in vivo
    • DOI 10.1021/ja0362813
    • Mootz HD, Blum ES, Tyszkiewicz AB, Muir TW (2003) Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo. J Am Chem Soc 125:10561-10569 (Pubitemid 37055907)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.35 , pp. 10561-10569
    • Mootz, H.D.1    Blum, E.S.2    Tyszkiewicz, A.B.3    Muir, T.W.4
  • 123
    • 6044271721 scopus 로고    scopus 로고
    • Activation of an autoregulated protein kinase by conditional protein splicing
    • DOI 10.1002/anie.200460941
    • Mootz HD, Blum ES, Muir TW (2004) Activation of an autoregulated protein kinase by conditional protein splicing. Angew Chem Int Ed Engl 43:5189-5192 (Pubitemid 39382538)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.39 , pp. 5189-5192
    • Mootz, H.D.1    Blum, E.S.2    Muir, T.W.3
  • 124
    • 33845723065 scopus 로고    scopus 로고
    • Post-translational enzyme activation in an animal via optimized conditional protein splicing
    • DOI 10.1038/nchembio832, PII NCHEMBIO832
    • Schwartz EC, Saez L, Young MW, Muir TW (2007) Post-translational enzyme activation in an animal via optimized conditional protein splicing. Nat Chem Biol 3:50-54 (Pubitemid 46005698)
    • (2007) Nature Chemical Biology , vol.3 , Issue.1 , pp. 50-54
    • Schwartz, E.C.1    Saez, L.2    Young, M.W.3    Muir, T.W.4
  • 125
    • 41449091908 scopus 로고    scopus 로고
    • Activation of protein splicing with light in yeast
    • DOI 10.1038/nmeth.1189, PII NMETH.1189
    • Tyszkiewicz AB, Muir TW (2008) Activation of protein splicing with light in yeast. Nat Methods 5:303-305 (Pubitemid 351455155)
    • (2008) Nature Methods , vol.5 , Issue.4 , pp. 303-305
    • Tyszkiewicz, A.B.1    Muir, T.W.2
  • 126
    • 79956121858 scopus 로고    scopus 로고
    • An intein-cassette integration approach used for the generation of a split TEV protease activated by conditional protein splicing
    • 21487580 1:CAS:528:DC%2BC3MXmtV2isb4%3D 10.1039/c1mb05025g
    • Sonntag T, Mootz HD (2011) An intein-cassette integration approach used for the generation of a split TEV protease activated by conditional protein splicing. Mol BioSyst 7:2031-2039
    • (2011) Mol BioSyst , vol.7 , pp. 2031-2039
    • Sonntag, T.1    Mootz, H.D.2
  • 127
    • 77954377503 scopus 로고    scopus 로고
    • Photomodulation of protein trans-splicing through backbone photocaging of the DnaE split intein
    • 20512791 1:CAS:528:DC%2BC3cXosVWltL4%3D 10.1002/cbic.201000157
    • Berrade L, Kwon Y, Camarero JA (2010) Photomodulation of protein trans-splicing through backbone photocaging of the DnaE split intein. Chem Bio Chem 11:1368-1372
    • (2010) Chem Bio Chem , vol.11 , pp. 1368-1372
    • Berrade, L.1    Kwon, Y.2    Camarero, J.A.3
  • 128
    • 54749102251 scopus 로고    scopus 로고
    • Activation of protein splicing by protease- or light-triggered O to N acyl migration
    • 18767096 1:CAS:528:DC%2BD1cXht1GmsL%2FJ 10.1002/anie.200802502
    • Vila-Perello M, Hori Y, Ribo M, Muir TW (2008) Activation of protein splicing by protease- or light-triggered O to N acyl migration. Angew Chem Int Ed Engl 47:7764-7767
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 7764-7767
    • Vila-Perello, M.1    Hori, Y.2    Ribo, M.3    Muir, T.W.4
  • 129
    • 79953009773 scopus 로고    scopus 로고
    • Photocontrol of protein activity mediated by the cleavage reaction of a split intein
    • 21384476 1:CAS:528:DC%2BC3MXjsFyruro%3D 10.1002/anie.201007078
    • Binschik J, Zettler J, Mootz HD (2011) Photocontrol of protein activity mediated by the cleavage reaction of a split intein. Angew Chem Int Ed Engl 50:3249-3252
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 3249-3252
    • Binschik, J.1    Zettler, J.2    Mootz, H.D.3
  • 130
    • 0033534179 scopus 로고    scopus 로고
    • NMR observation of selected segments in a larger protein: Central-segment isotope labeling through intein-mediated ligation
    • Otomo T, Ito N, Kyogoku Y, Yamazaki T (1999) NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation. Biochemistry 38:16040-16044 (Pubitemid 129520524)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16040-16044
    • Otomo, T.1    Ito, N.2    Kyogoku, Y.3    Yamazaki, T.4
  • 131
    • 32344433372 scopus 로고    scopus 로고
    • Engineering artificially split inteins for applications in protein chemistry: Biochemical characterization of the split Ssp DnaB intein and comparison to the split Sce VMA intein
    • DOI 10.1021/bi051697+
    • Brenzel S, Kurpiers T, Mootz HD (2006) Engineering artificially split inteins for applications in protein chemistry: biochemical characterization of the split Ssp DnaB intein and comparison to the split Sce VMA intein. Biochemistry 45:1571-1578 (Pubitemid 43222101)
    • (2006) Biochemistry , vol.45 , Issue.6 , pp. 1571-1578
    • Brenzel, S.1    Kurpiers, T.2    Mootz, H.D.3
  • 132
    • 70349907839 scopus 로고    scopus 로고
    • Segmental isotopic labeling of a central domain in a multidomain protein by protein trans-splicing using only one robust DnaE intein
    • 19591176 1:CAS:528:DC%2BD1MXptlCjsb0%3D 10.1002/anie.200901488
    • Busche AE, Aranko AS, Talebzadeh-Farooji M, Bernhard F, Dötsch V, Iwai H (2009) Segmental isotopic labeling of a central domain in a multidomain protein by protein trans-splicing using only one robust DnaE intein. Angew Chem Int Ed Engl 48:6128-6131
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 6128-6131
    • Busche, A.E.1    Aranko, A.S.2    Talebzadeh-Farooji, M.3    Bernhard, F.4    Dötsch, V.5    Iwai, H.6
  • 133
    • 79959981826 scopus 로고    scopus 로고
    • Kinetic control of one-pot trans-splicing reactions by using a wild-type and designed split intein
    • 21656885 1:CAS:528:DC%2BC3MXnt1eitbg%3D 10.1002/anie.201102909
    • Shah NH, Vila-Perello M, Muir TW (2011) Kinetic control of one-pot trans-splicing reactions by using a wild-type and designed split intein. Angew Chem Int Ed Engl 50:6511-6515
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 6511-6515
    • Shah, N.H.1    Vila-Perello, M.2    Muir, T.W.3
  • 134
    • 79955619798 scopus 로고    scopus 로고
    • Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
    • 21460844 1:CAS:528:DC%2BC3MXktFahtrw%3D 10.1038/nsmb.2041
    • Callahan BP, Topilina NI, Stanger MJ, Van Roey P, Belfort M (2011) Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications. Nat Struct Mol Biol 18:630-633
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 630-633
    • Callahan, B.P.1    Topilina, N.I.2    Stanger, M.J.3    Van Roey, P.4    Belfort, M.5
  • 135
    • 23444433268 scopus 로고    scopus 로고
    • Protein splicing mechanisms and applications
    • DOI 10.1080/15216540500163343
    • Perler FB (2005) Protein splicing mechanisms and applications. IUBMB Life 57:469-476 (Pubitemid 41112984)
    • (2005) IUBMB Life , vol.57 , Issue.7 , pp. 469-476
    • Perler, F.B.1
  • 136
    • 13244292480 scopus 로고    scopus 로고
    • Kinetic analysis of the individual steps of protein splicing for the Pyrococcus abyssi polII intein
    • DOI 10.1074/jbc.M412313200
    • Mills KV, Dorval DM, Lewandowski KT (2005) Kinetic analysis of the individual steps of protein splicing for the Pyrococcus abyssi PolII intein. J Biol Chem 280:2714-2720 (Pubitemid 40189377)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2714-2720
    • Mills, K.V.1    Dorval, D.M.2    Lewandowski, K.T.3
  • 137
    • 33748551323 scopus 로고    scopus 로고
    • Protein splicing in cis and in trans
    • DOI 10.1002/tcr.20082
    • Saleh L, Perler FB (2006) Protein splicing in cis and in trans. Chem Rec 6:183-193 (Pubitemid 44369414)
    • (2006) Chemical Record , vol.6 , Issue.4 , pp. 183-193
    • Saleh, L.1    Perler, F.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.