메뉴 건너뛰기




Volumn 192, Issue 19, 2010, Pages 5181-5191

Conserved motifs involved in ATP hydrolysis by MalT, a signal transduction ATPase with numerous domains from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; PROTEIN MALT; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE; ESCHERICHIA COLI PROTEIN;

EID: 77957342881     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00522-10     Document Type: Article
Times cited : (13)

References (54)
  • 2
    • 33845501864 scopus 로고    scopus 로고
    • Apoptosome: A platform for the activation of initiator caspases
    • Bao, Q., and Y. Shi. 2007. Apoptosome: a platform for the activation of initiator caspases. Cell Death Differ. 14:56-65.
    • (2007) Cell Death Differ , vol.14 , pp. 56-65
    • Bao, Q.1    Shi, Y.2
  • 3
    • 0034283843 scopus 로고    scopus 로고
    • Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network
    • Boos, W., and A. Böhm. 2000. Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network. Trends Genet. 16:404-409.
    • (2000) Trends Genet , vol.16 , pp. 404-409
    • Boos, W.1    Böhm, A.2
  • 4
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman, G. D., M. O'Donnell, and J. Kuriyan. 2004. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429:724-730.
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 5
    • 0034192263 scopus 로고    scopus 로고
    • DNA sequence elements located immediately upstream of the -10 hexamer in Escherichia coli promoters: A systematic study
    • Burr, T., J. Mitchell, A. Kolb, S. Minchin, and S. Busby. 2000. DNA sequence elements located immediately upstream of the -10 hexamer in Escherichia coli promoters: a systematic study. Nucleic Acids Res. 28:1864-1870.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1864-1870
    • Burr, T.1    Mitchell, J.2    Kolb, A.3    Minchin, S.4    Busby, S.5
  • 6
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M. J. 1976. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 7
    • 77954852400 scopus 로고    scopus 로고
    • The inducer maltotriose binds in the central cavity of the tetratricopeptide-like sensor domain of MalT, a bacterial STAND transcription factor
    • Danot, O. 2010. The inducer maltotriose binds in the central cavity of the tetratricopeptide-like sensor domain of MalT, a bacterial STAND transcription factor. Mol. Microbiol. 77:628-641.
    • (2010) Mol. Microbiol. , vol.77 , pp. 628-641
    • Danot, O.1
  • 8
    • 59649103157 scopus 로고    scopus 로고
    • Wheel of life, wheel of death: A mechanistic insight into signaling by STAND proteins
    • Danot, O., E. Marquenet, D. Vidal-Ingigliardi, and E. Richet. 2009. Wheel of life, wheel of death: a mechanistic insight into signaling by STAND proteins. Structure 17:172-182.
    • (2009) Structure , vol.17 , pp. 172-182
    • Danot, O.1    Marquenet, E.2    Vidal-Ingigliardi, D.3    Richet, E.4
  • 9
    • 0027943595 scopus 로고
    • Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT
    • Danot, O., and O. Raibaud. 1994. Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT. Mol. Microbiol. 14:335-346.
    • (1994) Mol. Microbiol. , vol.14 , pp. 335-346
    • Danot, O.1    Raibaud, O.2
  • 10
    • 0030582422 scopus 로고    scopus 로고
    • Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation
    • Danot, O., D. Vidal-Ingigliardi, and O. Raibaud. 1996. Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation. J. Mol. Biol. 262:1-11.
    • (1996) J. Mol. Biol. , vol.262 , pp. 1-11
    • Danot, O.1    Vidal-Ingigliardi, D.2    Raibaud, O.3
  • 11
    • 28844492475 scopus 로고    scopus 로고
    • The maltodextrin system of Escherichia coli: Glycogen-derived endogenous induction and osmoregulation
    • Dippel, R., T. Bergmiller, A. Böhm, and W. Boos. 2005. The maltodextrin system of Escherichia coli: glycogen-derived endogenous induction and osmoregulation. J. Bacteriol. 187:8332-8339.
    • (2005) J. Bacteriol. , vol.187 , pp. 8332-8339
    • Dippel, R.1    Bergmiller, T.2    Böhm, A.3    Boos, W.4
  • 12
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger, J. P., and J. M. Berger. 2006. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35:93-114.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 13
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
    • Erzberger, J. P., M. L. Mott, and J. M. Berger. 2006. Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat. Struct. Mol. Biol. 13:676-683.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 676-683
    • Erzberger, J.P.1    Mott, M.L.2    Berger, J.M.3
  • 14
    • 58049200723 scopus 로고    scopus 로고
    • Function of Nod-like receptors in microbial recognition and host defense
    • Franchi, L., N. Warner, K. Viani, and G. Nunez. 2009. Function of Nod-like receptors in microbial recognition and host defense. Immunol. Rev. 227: 106-128.
    • (2009) Immunol. Rev. , vol.227 , pp. 106-128
    • Franchi, L.1    Warner, N.2    Viani, K.3    Nunez, G.4
  • 15
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • Gai, D., R. Zhao, D. Li, C. V. Finkielstein, and X. S. Chen. 2004. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 119:47-60.
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 16
    • 44949197849 scopus 로고    scopus 로고
    • Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase
    • Greenleaf, W. B., J. Shen, D. Gai, and X. S. Chen. 2008. Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase. J. Virol. 82:6017-6023.
    • (2008) J. Virol. , vol.82 , pp. 6017-6023
    • Greenleaf, W.B.1    Shen, J.2    Gai, D.3    Chen, X.S.4
  • 17
    • 0015969332 scopus 로고
    • malB region of Escherichia coli K-12: Characterization of new mutations
    • Hofnung, M., D. Hatfield, and M. Schwartz. 1974. malB region of Escherichia coli K-12: characterization of new mutations. J. Bacteriol. 117:40-47.
    • (1974) J. Bacteriol. , vol.117 , pp. 40-47
    • Hofnung, M.1    Hatfield, D.2    Schwartz, M.3
  • 18
    • 35448968986 scopus 로고    scopus 로고
    • Coupling nucleotide hydrolysis to transcription activation performance in a bacterial enhancer binding protein
    • Joly, N., M. Rappas, S. R. Wigneshweraraj, X. Zhang, and M. Buck. 2007. Coupling nucleotide hydrolysis to transcription activation performance in a bacterial enhancer binding protein. Mol. Microbiol. 66:583-595.
    • (2007) Mol. Microbiol. , vol.66 , pp. 583-595
    • Joly, N.1    Rappas, M.2    Wigneshweraraj, S.R.3    Zhang, X.4    Buck, M.5
  • 19
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 20
    • 6344242971 scopus 로고    scopus 로고
    • Oligomeric assemblies of the Escherichia coli MalT transcriptional activator revealed by cryo-electron microcopy and image processing
    • Larquet, E., V. Schreiber, N. Boisset, and E. Richet. 2004. Oligomeric assemblies of the Escherichia coli MalT transcriptional activator revealed by cryo-electron microcopy and image processing. J. Mol. Biol. 343:1159-1169.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1159-1169
    • Larquet, E.1    Schreiber, V.2    Boisset, N.3    Richet, E.4
  • 21
    • 4644247731 scopus 로고    scopus 로고
    • STAND, a class of P-Loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer
    • Leipe, D. D., E. V. Koonin, and L. Aravind. 2004. STAND, a class of P-Loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer. J. Mol. Biol. 343:1-28.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 22
    • 77956357508 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Protein Kinase K confers survival advantage during early infection in mice and regulates growth in culture and during persistent infection: Implications in immune modulation
    • 3 June Epub ahead of print. doi:10.1099/mic.0.040675-0
    • Malhotra, V., L. T. Arteaga-Cortes, G. Clay, and J. E. Clark-Curtiss. 3 June 2010. Mycobacterium tuberculosis Protein Kinase K confers survival advantage during early infection in mice and regulates growth in culture and during persistent infection: implications in immune modulation. Microbiology. [Epub ahead of print.] doi:10.1099/mic.0.040675-0.
    • (2010) Microbiology
    • Malhotra, V.1    Arteaga-Cortes, L.T.2    Clay, G.3    Clark-Curtiss, J.E.4
  • 23
    • 35349014682 scopus 로고    scopus 로고
    • How integration of positive and negative regulatory signals by a STAND signaling protein depends on ATP hydrolysis
    • Marquenet, E., and E. Richet. 2007. How integration of positive and negative regulatory signals by a STAND signaling protein depends on ATP hydrolysis. Mol. Cell 28:187-199.
    • (2007) Mol. Cell , vol.28 , pp. 187-199
    • Marquenet, E.1    Richet, E.2
  • 24
    • 77952909070 scopus 로고    scopus 로고
    • Engineering of regulatory cascades and networks controlling antibiotic biosynthesis in Streptomyces
    • Martin, J. F., and P. Liras. 2010. Engineering of regulatory cascades and networks controlling antibiotic biosynthesis in Streptomyces. Curr. Opin. Microbiol. 13:263-273.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 263-273
    • Martin, J.F.1    Liras, P.2
  • 25
  • 27
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., L. Aravind, J. L. Spouge, and E. V. Koonin. 1999. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 28
    • 1642377971 scopus 로고    scopus 로고
    • Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    • Ogura, T., S. W. Whiteheart, and A. J. Wilkinson. 2004. Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases. J. Struct. Biol. 146:106-112.
    • (2004) J. Struct. Biol. , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 30
    • 0026329253 scopus 로고
    • Genetic studies on the promoter of malT, the gene that encodes the activator of the Escherichia coli maltose regulon
    • Raibaud, O., D. Vidal-Ingigliardi, and A. Kolb. 1991. Genetic studies on the promoter of malT, the gene that encodes the activator of the Escherichia coli maltose regulon. Res. Microbiol. 142:937-942.
    • (1991) Res. Microbiol. , vol.142 , pp. 937-942
    • Raibaud, O.1    Vidal-Ingigliardi, D.2    Kolb, A.3
  • 31
    • 33344469160 scopus 로고    scopus 로고
    • Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF
    • Rappas, M., J. Schumacher, H. Niwa, M. Buck, and X. Zhang. 2006. Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF. J. Mol. Biol. 357:481-492.
    • (2006) J. Mol. Biol. , vol.357 , pp. 481-492
    • Rappas, M.1    Schumacher, J.2    Niwa, H.3    Buck, M.4    Zhang, X.5
  • 32
    • 0025848324 scopus 로고
    • The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system
    • Reidl, J., and W. Boos. 1991. The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system. J. Bacteriol. 173:4862-4876.
    • (1991) J. Bacteriol. , vol.173 , pp. 4862-4876
    • Reidl, J.1    Boos, W.2
  • 33
    • 70450263353 scopus 로고    scopus 로고
    • A new model for the transition of APAF-1 from inactive monomer to caspase-activating apoptosome
    • Reubold, T. F., S. Wohlgemuth, and S. Eschenburg. 2009. A new model for the transition of APAF-1 from inactive monomer to caspase-activating apoptosome. J. Biol. Chem. 284:32717-32724.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32717-32724
    • Reubold, T.F.1    Wohlgemuth, S.2    Eschenburg, S.3
  • 34
    • 0030596146 scopus 로고    scopus 로고
    • On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter
    • Richet, E. 1996. On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter. J. Mol. Biol. 264:852-862.
    • (1996) J. Mol. Biol. , vol.264 , pp. 852-862
    • Richet, E.1
  • 35
    • 14144251709 scopus 로고    scopus 로고
    • Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK
    • Richet, E., N. Joly, and O. Danot. 2005. Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK. J. Mol. Biol. 347:1-10.
    • (2005) J. Mol. Biol. , vol.347 , pp. 1-10
    • Richet, E.1    Joly, N.2    Danot, O.3
  • 36
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl, S. J., W. Li, Y. Chao, R. Schwarzenbacher, and Y. Shi. 2005. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434: 926-933.
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 37
    • 0030581165 scopus 로고    scopus 로고
    • Tomato Prf is a member of the leucine-rich repeat class of plant disease resistance genes and lies embedded within the Pto kinase gene cluster
    • Salmeron, J. M., G. E. Oldroyd, C. M. Rommens, S. R. Scofield, H. S. Kim, D. T. Lavelle, D. Dahlbeck, and B. J. Staskawicz. 1996. Tomato Prf is a member of the leucine-rich repeat class of plant disease resistance genes and lies embedded within the Pto kinase gene cluster. Cell 86:123-133.
    • (1996) Cell , vol.86 , pp. 123-133
    • Salmeron, J.M.1    Oldroyd, G.E.2    Rommens, C.M.3    Scofield, S.R.4    Kim, H.S.5    Lavelle, D.T.6    Dahlbeck, D.7    Staskawicz, B.J.8
  • 38
    • 0036096732 scopus 로고    scopus 로고
    • The N-terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY
    • Schlegel, A., O. Danot, E. Richet, T. Ferenci, and W. Boos. 2002. The N-terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY. J. Bacteriol. 184:3069-3077.
    • (2002) J. Bacteriol. , vol.184 , pp. 3069-3077
    • Schlegel, A.1    Danot, O.2    Richet, E.3    Ferenci, T.4    Boos, W.5
  • 39
    • 0033585068 scopus 로고    scopus 로고
    • Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP
    • Schreiber, V., and E. Richet. 1999. Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP. J. Biol. Chem. 274:33220-33226.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33220-33226
    • Schreiber, V.1    Richet, E.2
  • 40
    • 0033968803 scopus 로고    scopus 로고
    • A new mechanism for the control of a prokaryotic transcriptional regulator: Antagonistic binding of positive and negative effectors
    • Schreiber, V., C. Steegborn, T. Clausen, W. Boos, and E. Richet. 2000. A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors. Mol. Microbiol. 35:765-776.
    • (2000) Mol. Microbiol. , vol.35 , pp. 765-776
    • Schreiber, V.1    Steegborn, C.2    Clausen, T.3    Boos, W.4    Richet, E.5
  • 42
    • 4744353204 scopus 로고    scopus 로고
    • Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix
    • Singleton, M. R., R. Morales, I. Grainge, N. Cook, M. N. Isupov, and D. B. Wigley. 2004. Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix. J. Mol. Biol. 343:547-557.
    • (2004) J. Mol. Biol. , vol.343 , pp. 547-557
    • Singleton, M.R.1    Morales, R.2    Grainge, I.3    Cook, N.4    Isupov, M.N.5    Wigley, D.B.6
  • 44
    • 0035179356 scopus 로고    scopus 로고
    • Crystal structure of transcription factor MalT domain III: A domain helix repeat fold implicated in regulated oligomerization
    • Steegborn, C., O. Danot, R. Huber, and T. Clausen. 2001. Crystal structure of transcription factor MalT domain III: a domain helix repeat fold implicated in regulated oligomerization. Structure 9:1051-1060.
    • (2001) Structure , vol.9 , pp. 1051-1060
    • Steegborn, C.1    Danot, O.2    Huber, R.3    Clausen, T.4
  • 45
    • 65649140098 scopus 로고    scopus 로고
    • To nibble at plant resistance proteins
    • Takken, F. L., and W. I. Tameling. 2009. To nibble at plant resistance proteins. Science 324:744-746.
    • (2009) Science , vol.324 , pp. 744-746
    • Takken, F.L.1    Tameling, W.I.2
  • 48
    • 0025849091 scopus 로고
    • Two MalT binding sites in direct repeat. A structural motif involved in the activation of all the promoters of the maltose regulons in Escherichia coli and Klebsiella pneumoniae
    • Vidal-Ingigliardi, D., E. Richet, and O. Raibaud. 1991. Two MalT binding sites in direct repeat. A structural motif involved in the activation of all the promoters of the maltose regulons in Escherichia coli and Klebsiella pneumoniae. J. Mol. Biol. 218:323-334.
    • (1991) J. Mol. Biol. , vol.218 , pp. 323-334
    • Vidal-Ingigliardi, D.1    Richet, E.2    Raibaud, O.3
  • 49
    • 28844446882 scopus 로고    scopus 로고
    • Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein
    • Wang, Q., C. Song, L. Irizarry, R. Dai, X. Zhang, and C. C. Li. 2005. Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein. J. Biol. Chem. 280:40515-40523.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40515-40523
    • Wang, Q.1    Song, C.2    Irizarry, L.3    Dai, R.4    Zhang, X.5    Li, C.C.6
  • 50
    • 0042858475 scopus 로고    scopus 로고
    • Characterization of a trap mutant of the AAA+ chaperone ClpB
    • Weibezahn, J., C. Schlieker, B. Bukau, and A. Mogk. 2003. Characterization of a trap mutant of the AAA+ chaperone ClpB. J. Biol. Chem. 278:32608-32617.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32608-32617
    • Weibezahn, J.1    Schlieker, C.2    Bukau, B.3    Mogk, A.4
  • 52
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan, N., J. Chai, E. S. Lee, L. Gu, Q. Liu, J. He, J. W. Wu, D. Kokel, H. Li, Q. Hao, D. Xue, and Y. Shi. 2005. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437:831-837.
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1    Chai, J.2    Lee, E.S.3    Gu, L.4    Liu, Q.5    He, J.6    Wu, J.W.7    Kokel, D.8    Li, H.9    Hao, Q.10    Xue, D.11    Shi, Y.12
  • 53
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R. C., P. I. Hanson, R. Jahn, and A. T. Brunger. 1998. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5:803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 54
    • 77952652352 scopus 로고    scopus 로고
    • Structure of an apoptosome-procaspase-9 CARD complex
    • Yuan, S., X. Yu, M. Topf, S. J. Ludtke, X. Wang, and C. W. Akey. 2010. Structure of an apoptosome-procaspase-9 CARD complex. Structure 18: 571-583.
    • (2010) Structure , vol.18 , pp. 571-583
    • Yuan, S.1    Yu, X.2    Topf, M.3    Ludtke, S.J.4    Wang, X.5    Akey, C.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.