메뉴 건너뛰기




Volumn 8, Issue SUPPL., 2003, Pages

Inteins as targets for potential antimycobacterial drugs

Author keywords

Antimycobacterial Drugs; CcdB toxin; DNA gyrase; DnaB; Drug Screening; Drug Targets; Fluorescent Protein; Green; High Throughput Screening; Inteins; Mycobacterium Tuberculosis; Protein Splicing; RecA; Review; Thymidylate synthase

Indexed keywords

ANTIBIOTIC AGENT; ANTIMYCOBACTERIAL AGENT; DNA B; DNA TOPOISOMERASE (ATP HYDROLYSING) A; ETHAMBUTOL; GREEN FLUORESCENT PROTEIN; INTEIN; ISONIAZID; OFLOXACIN; PYRAZINAMIDE; QUINOLONE; RECA PROTEIN; RIFAMPICIN; STREPTOMYCIN; THYMIDYLATE SYNTHASE; TOXIN; BACTERIAL PROTEIN; DNAB HELICASE; HELICASE; TUBERCULOSTATIC AGENT;

EID: 3042840324     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1195     Document Type: Review
Times cited : (36)

References (54)
  • 2
    • 0025990865 scopus 로고
    • Novel structure of the recA locus of Mycobacterium tuberculosis implies processing of the gene product
    • Davis, E.O., S.G. Sedgwick & M.J. Colston: Novel structure of the recA locus of Mycobacterium tuberculosis implies processing of the gene product. J Bacteriol 173, 5653-5662 (1991)
    • (1991) J Bacteriol , vol.173 , pp. 5653-5662
    • Davis, E.O.1    Sedgwick, S.G.2    Colston, M.J.3
  • 3
    • 0026774103 scopus 로고
    • Protein splicing in the maturation of M. tuberculosis RecA protein: A mechanism for tolerating a novel class of intervening sequence
    • Davis, E.O., P.J. Jenner, P.C. Brooks, M.J. Colston & S.G. Sedgwick: Protein splicing in the maturation of M. tuberculosis RecA protein: A mechanism for tolerating a novel class of intervening sequence. Cell 71, 201-210 (1992)
    • (1992) Cell , vol.71 , pp. 201-210
    • Davis, E.O.1    Jenner, P.J.2    Brooks, P.C.3    Colston, M.J.4    Sedgwick, S.G.5
  • 4
    • 0027972347 scopus 로고
    • Evidence for selection for protein introns in the RecAs of pathogenic mycobacteria
    • Davis, E.O., H.S. Thangaraj, P.C. Brooks & M.J. Colston: Evidence for selection for protein introns in the RecAs of pathogenic mycobacteria. EMBO J 13, 699-703 (1994)
    • (1994) EMBO J , vol.13 , pp. 699-703
    • Davis, E.O.1    Thangaraj, H.S.2    Brooks, P.C.3    Colston, M.J.4
  • 5
    • 85049057432 scopus 로고    scopus 로고
    • The molecular basis of mycobacterial infection
    • Colston, M.J.: The molecular basis of mycobacterial infection. Mol Aspects Med 17, 385-454 (1996)
    • (1996) Mol Aspects Med , vol.17 , pp. 385-454
    • Colston, M.J.1
  • 6
    • 0036084146 scopus 로고    scopus 로고
    • InBase, the intein database
    • Perler, F.B.: InBase, the intein database. Nucl Acids Res 30, 383-384 (2002)
    • (2002) Nucl Acids Res , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 7
    • 0027753790 scopus 로고
    • In vitro protein splicing of purified precursor and the identification of a branched intermediate
    • Xu, M.-Q., M.W. Southworth, F.B. Mersha, L.J. Hornstra & F.B. Perler: In vitro protein splicing of purified precursor and the identification of a branched intermediate. Cell 75, 1371-1377 (1993)
    • (1993) Cell , vol.75 , pp. 1371-1377
    • Xu, M.-Q.1    Southworth, M.W.2    Mersha, F.B.3    Hornstra, L.J.4    Perler, F.B.5
  • 8
    • 0032359384 scopus 로고    scopus 로고
    • The chemical basis of protein splicing
    • Paulus, H.: The chemical basis of protein splicing. Chem Soc Rev 27, 375-386 (1998)
    • (1998) Chem Soc Rev , vol.27 , pp. 375-386
    • Paulus, H.1
  • 9
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus, H.: Protein splicing and related forms of protein autoprocessing. Annu Rev Biochem 69, 447-496 (2000)
    • (2000) Annu Rev Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 10
    • 0035572943 scopus 로고    scopus 로고
    • Inteins as enzymes
    • Paulus, H.: Inteins as enzymes. Bioorg Chem 29, 119-129 (2001)
    • (2001) Bioorg Chem , vol.29 , pp. 119-129
    • Paulus, H.1
  • 11
    • 0030611387 scopus 로고    scopus 로고
    • Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity
    • Duan, X., F.S. Gimble & F.A. Quiocho: Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Cell 89, 555-564 (1997)
    • (1997) Cell , vol.89 , pp. 555-564
    • Duan, X.1    Gimble, F.S.2    Quiocho, F.A.3
  • 12
    • 0034595699 scopus 로고    scopus 로고
    • Structural insights into the protein splicing mechanism of PI-SceI
    • Poland, B.W., M.-Q. Xu & F.A. Quiocho: Structural insights into the protein splicing mechanism of PI-SceI. J Biol Chem 275, 16408-16413 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 16408-16413
    • Poland, B.W.1    Xu, M.-Q.2    Quiocho, F.A.3
  • 13
    • 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
    • Mizutani, R., S. Nogami, M. Kawasaki, Y. Ohya, Y. Anraku & Y. Satow: 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 (2002)
    • (2002) J Mol Biol , vol.316 , pp. 919-929
    • Mizutani, R.1    Nogami, S.2    Kawasaki, M.3    Ohya, Y.4    Anraku, Y.5    Satow, Y.6
  • 14
    • 0037106450 scopus 로고    scopus 로고
    • High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI
    • Werner, E., W. Wende, A. Pingoud & U. Heinemann: High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI. Nucleic Acids Res 30, 3962-3971 (2002)
    • (2002) Nucleic Acids Res , vol.30 , pp. 3962-3971
    • Werner, E.1    Wende, W.2    Pingoud, A.3    Heinemann, U.4
  • 15
    • 0031975772 scopus 로고    scopus 로고
    • Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing
    • Klabunde, T., S. Sharma, A. Telenti, W.R. Jacobs & J.C. Sacchettini: Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing. Nature Struct Biol 5, 31-36 (1998)
    • (1998) Nature Struct Biol , vol.5 , pp. 31-36
    • Klabunde, T.1    Sharma, S.2    Telenti, A.3    Jacobs, W.R.4    Sacchettini, J.C.5
  • 16
    • 0034697993 scopus 로고    scopus 로고
    • Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI
    • Ichiyanagi, K., Y. Ishino, M. Ariyoshi, K. Komori & K. Morikawa: Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI. J Mol Biol 300, 889-901 (2000)
    • (2000) J Mol Biol , vol.300 , pp. 889-901
    • Ichiyanagi, K.1    Ishino, Y.2    Ariyoshi, M.3    Komori, K.4    Morikawa, K.5
  • 18
    • 0030958621 scopus 로고    scopus 로고
    • Determination of DNA sequences required for regulated Mycobacterium tuberculosis RecA expression in response to DNA-damaging agents suggests that two modes of regulation exist
    • Movahedzadeh, F., M.J. Colston & E.O. Davis: Determination of DNA sequences required for regulated Mycobacterium tuberculosis RecA expression in response to DNA-damaging agents suggests that two modes of regulation exist. J Bacteriol 179, 3509-3518 (1997)
    • (1997) J Bacteriol , vol.179 , pp. 3509-3518
    • Movahedzadeh, F.1    Colston, M.J.2    Davis, E.O.3
  • 19
    • 0030029470 scopus 로고    scopus 로고
    • Functional chracterization of the precursor and spliced forms of recA protein of Mycobacterium tuberculosis
    • Kumar, R.A., M.B. Vaze, N.R. Chandra, M. Vijayan & K. Muniyappa: Functional chracterization of the precursor and spliced forms of recA protein of Mycobacterium tuberculosis. Biochemistry 35, 1793-1802 (1996)
    • (1996) Biochemistry , vol.35 , pp. 1793-1802
    • Kumar, R.A.1    Vaze, M.B.2    Chandra, N.R.3    Vijayan, M.4    Muniyappa, K.5
  • 21
    • 0031736728 scopus 로고    scopus 로고
    • Construction and complementation of a recA deletion mutant of Mycobacterium smegmatis reveals that the intein in Mycobacterium tuberculosis recA does not affect RecA function
    • Papavinasasundaram, K.P., M.J. Colston & E.O. Davis: Construction and complementation of a recA deletion mutant of Mycobacterium smegmatis reveals that the intein in Mycobacterium tuberculosis recA does not affect RecA function. Mol Microbiol 30, 525-534 (1998)
    • (1998) Mol Microbiol , vol.30 , pp. 525-534
    • Papavinasasundaram, K.P.1    Colston, M.J.2    Davis, E.O.3
  • 22
    • 0031715468 scopus 로고    scopus 로고
    • Investigation of mycobacterial recA function: Protein introns in the RecA of pathogenic mycobacteria do not affect competency for homologous recombination
    • Frischkorn, K., P. Sander, M. Scholz, K. Teschner, T. Prammananan & E.C. Bottger: Investigation of mycobacterial recA function: protein introns in the RecA of pathogenic mycobacteria do not affect competency for homologous recombination. Mol Microbiol 29, 1203-1214 (1998)
    • (1998) Mol Microbiol , vol.29 , pp. 1203-1214
    • Frischkorn, K.1    Sander, P.2    Scholz, M.3    Teschner, K.4    Prammananan, T.5    Bottger, E.C.6
  • 23
    • 0027416848 scopus 로고
    • Recombination-deficient mutants of Salmonella typhimurium are avirulent and sensitive to the oxidative burst of macrophages
    • Buchmeier, N.A., C.L. Lipps, M.Y.H. So & F. Heffron: Recombination-deficient mutants of Salmonella typhimurium are avirulent and sensitive to the oxidative burst of macrophages. Mol Microbiol 7, 933-936 (1993)
    • (1993) Mol Microbiol , vol.7 , pp. 933-936
    • Buchmeier, N.A.1    Lipps, C.L.2    So, M.Y.H.3    Heffron, F.4
  • 26
    • 0030246868 scopus 로고    scopus 로고
    • Cloning and manipulation of the Corynebacterium pseudotuberculosis recA gene for live vaccine development
    • Pogson, C.A., C.P. Simmons, R.A. Strugnell & A.L. Hodgson: Cloning and manipulation of the Corynebacterium pseudotuberculosis recA gene for live vaccine development. FEMS Microbiol Lett 142, 139-145 (1996)
    • (1996) FEMS Microbiol Lett , vol.142 , pp. 139-145
    • Pogson, C.A.1    Simmons, C.P.2    Strugnell, R.A.3    Hodgson, A.L.4
  • 27
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti, C.M., D.H. Boyd & E.J. Rubin: Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48, 77-84 (2003)
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 28
    • 0035002098 scopus 로고    scopus 로고
    • Mycobacterium bovis BCG recA deletion mutant shows increased susceptibility to DNA-damaging agetns but wild-type survival in a mouse infection model
    • Sander, P., K.G. Papavinasundaram, T. Dick, E. Stavropoulos, K. Ellrott, B. Springer, M.J. Colston & E.C. Bottker: Mycobacterium bovis BCG recA deletion mutant shows increased susceptibility to DNA-damaging agetns but wild-type survival in a mouse infection model. Inf Immun 69, 3562-3568 (2001)
    • (2001) Inf Immun , vol.69 , pp. 3562-3568
    • Sander, P.1    Papavinasundaram, K.G.2    Dick, T.3    Stavropoulos, E.4    Ellrott, K.5    Springer, B.6    Colston, M.J.7    Bottker, E.C.8
  • 29
    • 0038931706 scopus 로고
    • A general priming system employing only dnaB protein and primase for DNA replication
    • Arai, K.I. & A. Kornberg: A general priming system employing only dnaB protein and primase for DNA replication. Proc Natl Acad Sci USA 76, 4308-4312 (1979)
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4308-4312
    • Arai, K.I.1    Kornberg, A.2
  • 30
    • 0028821014 scopus 로고
    • Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454
    • Saluja, D. & G.N. Godson: Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252,dnaB70, dnaB43, and dnaB454. J Bacteriol 177, 1104-1111 (1995)
    • (1995) J Bacteriol , vol.177 , pp. 1104-1111
    • Saluja, D.1    Godson, G.N.2
  • 31
    • 0017262957 scopus 로고
    • Tw types of temperature sensitivity in DNA replication of an Escherichia coli dnaB mutant
    • Kogama, T.: Tw types of temperature sensitivity in DNA replication of an Escherichia coli dnaB mutant. J Mol Biol 103, 191-197 (1976)
    • (1976) J Mol Biol , vol.103 , pp. 191-197
    • Kogama, T.1
  • 32
    • 0034635137 scopus 로고    scopus 로고
    • Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus
    • Bird, L.E., H. Pan, P. Soultanas & D.B. Wigley: Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry 39, 171-182 (2000)
    • (2000) Biochemistry , vol.39 , pp. 171-182
    • Bird, L.E.1    Pan, H.2    Soultanas, P.3    Wigley, D.B.4
  • 33
    • 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
    • Kawasaki, M., S. Nogami, Y. Satow, Y. Ohya & Y. Anraku: 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 (1997)
    • (1997) J Biol Chem , vol.272 , pp. 15668-15674
    • Kawasaki, M.1    Nogami, S.2    Satow, Y.3    Ohya, Y.4    Anraku, Y.5
  • 34
    • 0030982430 scopus 로고    scopus 로고
    • Probing novel elements for protein splicing in the yeast VmaI protozyme: A study of replacement mutagenesis and intragenic suppression
    • Nogami, S., Y. Satow, Y. Ohya & Y. Anraku: Probing novel elements for protein splicing in the yeast VmaI protozyme: a study of replacement mutagenesis and intragenic suppression. Genetics 147, 73-85 (1997)
    • (1997) Genetics , vol.147 , pp. 73-85
    • Nogami, S.1    Satow, Y.2    Ohya, Y.3    Anraku, Y.4
  • 35
    • 0033055899 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis recA intein can be used in an ORFTRAP to select for open reading frames
    • Daugelat, S. & W.R. Jacobs: The Mycobacterium tuberculosis recA intein can be used in an ORFTRAP to select for open reading frames. Prot Sci 8, 644-653 (1999)
    • (1999) Prot Sci , vol.8 , pp. 644-653
    • Daugelat, S.1    Jacobs, W.R.2
  • 36
    • 0030803760 scopus 로고    scopus 로고
    • Genetic definition of a protein-splicing domain: Functional mini-inteins support structure predictions and a model for intein evolution
    • Derbyshire, V., D.W. Wood, W. Wu, J.T. Dansereau, L.Z. Dalgaard & M. Belfort: Genetic definition of a protein-splicing domain: Functional mini-inteins support structure predictions and a model for intein evolution. Proc Natl Acad Sci USA 94, 11466-11471 (1997)
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11466-11471
    • Derbyshire, V.1    Wood, D.W.2    Wu, W.3    Dansereau, J.T.4    Dalgaard, L.Z.5    Belfort, M.6
  • 37
    • 3142778149 scopus 로고    scopus 로고
    • Inteins as antimicrobial targets: genetic screen for intein function. US Patent 5,798,731
    • Belfort, M.: Inteins as antimicrobial targets: genetic screen for intein function. US Patent 5,798,731 (1998)
    • (1998)
    • Belfort, M.1
  • 38
    • 0032832776 scopus 로고    scopus 로고
    • A genetic system yields self-cleaving inteins for bioseparations
    • Wood, D.W., W. Wu, G. Belfort, V. Derbyshire & M. Belfort: A genetic system yields self-cleaving inteins for bioseparations. Nature Biotech 17, 889-892 (1999)
    • (1999) Nature Biotech , vol.17 , pp. 889-892
    • Wood, D.W.1    Wu, W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5
  • 39
    • 0036753960 scopus 로고    scopus 로고
    • Development of a positive genetic selection system for inhibition of protein splicing using mycobacterial inteins in Escherichia coli gyrase subunit A
    • Adam, E. & F.B. Perler: Development of a positive genetic selection system for inhibition of protein splicing using mycobacterial inteins in Escherichia coli gyrase subunit A. J Molec Microbiol Biotech 4, 479-487 (2002)
    • (2002) J Molec Microbiol Biotech , vol.4 , pp. 479-487
    • Adam, E.1    Perler, F.B.2
  • 40
    • 0032696759 scopus 로고    scopus 로고
    • Addiction modules and programmed cell death and antideath in bacterial cultures
    • Engelberg-Kulka, H. & G. Glaser: Addiction modules and programmed cell death and antideath in bacterial cultures. Annu Rev Microbiol 53, 43-70 (1999)
    • (1999) Annu Rev Microbiol , vol.53 , pp. 43-70
    • Engelberg-Kulka, H.1    Glaser, G.2
  • 41
    • 0028006860 scopus 로고
    • Positive-selection vectors using the F plasmid ccdB killer gene
    • Bernard, P., P. Gabarit, E.M. Bahassi & M. Couturier: Positive-selection vectors using the F plasmid ccdB killer gene. Gene 148, 71-74 (1994)
    • (1994) Gene , vol.148 , pp. 71-74
    • Bernard, P.1    Gabarit, P.2    Bahassi, E.M.3    Couturier, M.4
  • 42
    • 0029741707 scopus 로고    scopus 로고
    • Positive selection of recombinant DNA by CcdB
    • Bernard, P.: Positive selection of recombinant DNA by CcdB. Biotechniques 21, 320-323 (1996)
    • (1996) Biotechniques , vol.21 , pp. 320-323
    • Bernard, P.1
  • 43
    • 0037045404 scopus 로고    scopus 로고
    • An in vivo screening system against protein splicing useful for the isolation of non-splicing mutants or inhibitors of the RecA intein of Mycobacterium tuberculosis
    • Lew, B.M. & H. Paulus: An in vivo screening system against protein splicing useful for the isolation of non-splicing mutants or inhibitors of the RecA intein of Mycobacterium tuberculosis. Gene 282, 169-177 (2002)
    • (2002) Gene , vol.282 , pp. 169-177
    • Lew, B.M.1    Paulus, H.2
  • 44
    • 0034329620 scopus 로고    scopus 로고
    • A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing
    • Ozawa, T., S. Nogami, M. Sato, Y. Ohya & Y. Umezawa: A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing. Anal Chem 72, 5151-5157 (2000)
    • (2000) Anal Chem , vol.72 , pp. 5151-5157
    • Ozawa, T.1    Nogami, S.2    Sato, M.3    Ohya, Y.4    Umezawa, Y.5
  • 45
    • 0035894271 scopus 로고    scopus 로고
    • Protein splicing-based reconstitutition of split green fluorescent protein for monitoring protein-protein interactions in bacteria: Improved sensitivity and reduced screening time
    • Ozawa, T., M. Takeuchi, A. Kaihara, M. Sato & Y. Umezawa: Protein splicing-based reconstitutition of split green fluorescent protein for monitoring protein-protein interactions in bacteria: Improved sensitivity and reduced screening time. Anal Chem 73, 5866-5874 (2001)
    • (2001) Anal Chem , vol.73 , pp. 5866-5874
    • Ozawa, T.1    Takeuchi, M.2    Kaihara, A.3    Sato, M.4    Umezawa, Y.5
  • 46
    • 0035478478 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in vivo based on protein splicing
    • Ozawa, T. & Y. Umezawa: Detection of protein-protein interactions in vivo based on protein splicing. Curr Opin Chem Biol 5, 578-583 (2001)
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 578-583
    • Ozawa, T.1    Umezawa, Y.2
  • 47
    • 0037953089 scopus 로고    scopus 로고
    • An in itro screening system for protein splicing inhibitors based on Green Fluorescent Protein as an indicator
    • in press
    • Gangopadhyay, J.P., S.-q. Jiang & H. Paulus: An in itro screening system for protein splicing inhibitors based on Green Fluorescent Protein as an indicator. Anal Chem 75, in press (2003)
    • (2003) Anal Chem , vol.75
    • Gangopadhyay, J.P.1    Jiang, S.-Q.2    Paulus, H.3
  • 48
    • 0035815658 scopus 로고    scopus 로고
    • Reversible inhibition of protein splicing by zinc ion
    • Mills, K.V. & H. Paulus: Reversible inhibition of protein splicing by zinc ion. J Biol Chem 241, 10832-10838 (2001)
    • (2001) J Biol Chem , vol.241 , pp. 10832-10838
    • Mills, K.V.1    Paulus, H.2
  • 49
    • 0035968177 scopus 로고    scopus 로고
    • Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein
    • Ghosh, I., L. Sun & M.Q. Xu: 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)
    • (2001) J Biol Chem , vol.276 , pp. 24051-24058
    • Ghosh, I.1    Sun, L.2    Xu, M.Q.3
  • 50
    • 0028944672 scopus 로고
    • A protein splice-junction motif in hedgehog family proteins
    • Koonin, E.V.: A protein splice-junction motif in hedgehog family proteins. Trends Biochem Sci 20, 141-142 (1995)
    • (1995) Trends Biochem Sci , vol.20 , pp. 141-142
    • Koonin, E.V.1
  • 51
    • 0342813091 scopus 로고    scopus 로고
    • Crystal structure of a hedgehog protein autoprocessing domain: Homology between hedgehog and self-splicing proteins
    • Hall, T.M.T., J.A. Porter, K.E. Young, E.V. Koonin, P.E. Beachy & D.J. Leahy: Crystal structure of a hedgehog protein autoprocessing domain: homology between hedgehog and self-splicing proteins. Cell 91, 85-97 (1997)
    • (1997) Cell , vol.91 , pp. 85-97
    • Hall, T.M.T.1    Porter, J.A.2    Young, K.E.3    Koonin, E.V.4    Beachy, P.E.5    Leahy, D.J.6
  • 52
  • 54
    • 0031938897 scopus 로고    scopus 로고
    • Modular organization of inteins and C-terminal autocatalytic domains
    • Pietrokovski, S.: Modular organization of inteins and C-terminal autocatalytic domains. Protein Science 7, 64-71 (1998)
    • (1998) Protein Science , vol.7 , pp. 64-71
    • Pietrokovski, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.