메뉴 건너뛰기




Volumn 21, Issue 6, 2013, Pages 975-985

MgATP regulates allostery and fiber formation in IMPDHs

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; ENZYME VARIANT; INOSINATE DEHYDROGENASE; RECOMBINANT ENZYME;

EID: 84878836788     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.03.011     Document Type: Article
Times cited : (71)

References (54)
  • 2
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • S. An, R. Kumar, E.D. Sheets, and S.J. Benkovic Reversible compartmentalization of de novo purine biosynthetic complexes in living cells Science 320 2008 103 106
    • (2008) Science , vol.320 , pp. 103-106
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 3
    • 84858214646 scopus 로고    scopus 로고
    • Mutations of ATIC and ADSL affect purinosome assembly in cultured skin fibroblasts from patients with AICA-ribosiduria and ADSL deficiency
    • V. Baresova, V. Skopova, J. Sikora, D. Patterson, J. Sovova, M. Zikanova, and S. Kmoch Mutations of ATIC and ADSL affect purinosome assembly in cultured skin fibroblasts from patients with AICA-ribosiduria and ADSL deficiency Hum. Mol. Genet. 21 2012 1534 1543
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1534-1543
    • Baresova, V.1    Skopova, V.2    Sikora, J.3    Patterson, D.4    Sovova, J.5    Zikanova, M.6    Kmoch, S.7
  • 4
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • A. Bateman The structure of a domain common to archaebacteria and the homocystinuria disease protein Trends Biochem. Sci. 22 1997 12 13
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 12-13
    • Bateman, A.1
  • 8
    • 0027717956 scopus 로고
    • Characterization of human type i and type II IMP dehydrogenases
    • S.F. Carr, E. Papp, J.C. Wu, and Y. Natsumeda Characterization of human type I and type II IMP dehydrogenases J. Biol. Chem. 268 1993 27286 27290
    • (1993) J. Biol. Chem. , vol.268 , pp. 27286-27290
    • Carr, S.F.1    Papp, E.2    Wu, J.C.3    Natsumeda, Y.4
  • 9
    • 34447642328 scopus 로고    scopus 로고
    • Recent development of IMP dehydrogenase inhibitors for the treatment of cancer
    • L. Chen, and K.W. Pankiewicz Recent development of IMP dehydrogenase inhibitors for the treatment of cancer Curr. Opin. Drug Discov. Devel. 10 2007 403 412
    • (2007) Curr. Opin. Drug Discov. Devel. , vol.10 , pp. 403-412
    • Chen, L.1    Pankiewicz, K.W.2
  • 10
    • 0033616611 scopus 로고    scopus 로고
    • Crystal structure of human type II inosine monophosphate dehydrogenase: Implications for ligand binding and drug design
    • T.D. Colby, K. Vanderveen, M.D. Strickler, G.D. Markham, and B.M. Goldstein Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design Proc. Natl. Acad. Sci. USA 96 1999 3531 3536
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3531-3536
    • Colby, T.D.1    Vanderveen, K.2    Strickler, M.D.3    Markham, G.D.4    Goldstein, B.M.5
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 15
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • N. Grigorieff FREALIGN: high-resolution refinement of single particle structures J. Struct. Biol. 157 2007 117 125
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 16
    • 80052385397 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Also regulated by ADP?
    • D.G. Hardie, D. Carling, and S.J. Gamblin AMP-activated protein kinase: also regulated by ADP? Trends Biochem. Sci. 36 2011 470 477
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 470-477
    • Hardie, D.G.1    Carling, D.2    Gamblin, S.J.3
  • 17
    • 67650649489 scopus 로고    scopus 로고
    • IMP dehydrogenase: Structure, mechanism, and inhibition
    • L. Hedstrom IMP dehydrogenase: structure, mechanism, and inhibition Chem. Rev. 109 2009 2903 2928
    • (2009) Chem. Rev. , vol.109 , pp. 2903-2928
    • Hedstrom, L.1
  • 18
    • 79957938394 scopus 로고    scopus 로고
    • The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors
    • L. Hedstrom, G. Liechti, J.B. Goldberg, and D.R. Gollapalli The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors Curr. Med. Chem. 18 2011 1909 1918
    • (2011) Curr. Med. Chem. , vol.18 , pp. 1909-1918
    • Hedstrom, L.1    Liechti, G.2    Goldberg, J.B.3    Gollapalli, D.R.4
  • 19
    • 27744463780 scopus 로고    scopus 로고
    • CBS domains: Structure, function, and pathology in human proteins
    • S. Ignoul, and J. Eggermont CBS domains: structure, function, and pathology in human proteins Am. J. Physiol. Cell Physiol. 289 2005 C1369 C1378
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Ignoul, S.1    Eggermont, J.2
  • 20
    • 33644872520 scopus 로고    scopus 로고
    • Regulation of the interaction of inosine monophosphate dehydrogenase with mycophenolic Acid by GTP
    • Y. Ji, J. Gu, A.M. Makhov, J.D. Griffith, and B.S. Mitchell Regulation of the interaction of inosine monophosphate dehydrogenase with mycophenolic Acid by GTP J. Biol. Chem. 281 2006 206 212
    • (2006) J. Biol. Chem. , vol.281 , pp. 206-212
    • Ji, Y.1    Gu, J.2    Makhov, A.M.3    Griffith, J.D.4    Mitchell, B.S.5
  • 21
    • 0036501462 scopus 로고    scopus 로고
    • Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice
    • A. Kennan, A. Aherne, A. Palfi, M. Humphries, A. McKee, A. Stitt, D.A. Simpson, K. Demtroder, T. Orntoft, and C. Ayuso Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice Hum. Mol. Genet. 11 2002 547 557
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 547-557
    • Kennan, A.1    Aherne, A.2    Palfi, A.3    Humphries, M.4    McKee, A.5    Stitt, A.6    Simpson, D.A.7    Demtroder, K.8    Orntoft, T.9    Ayuso, C.10
  • 24
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 25
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • S.J. Ludtke, P.R. Baldwin, and W. Chiu EMAN: semiautomated software for high-resolution single-particle reconstructions J. Struct. Biol. 128 1999 82 97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 26
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • J.A. Mindell, and N. Grigorieff Accurate determination of local defocus and specimen tilt in electron microscopy J. Struct. Biol. 142 2003 334 347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 27
    • 23944520368 scopus 로고    scopus 로고
    • Autosomal dominant retinitis pigmentosa mutations in inosine 5′-monophosphate dehydrogenase type i disrupt nucleic acid binding
    • S.E. Mortimer, and L. Hedstrom Autosomal dominant retinitis pigmentosa mutations in inosine 5′-monophosphate dehydrogenase type I disrupt nucleic acid binding Biochem. J. 390 2005 41 47
    • (2005) Biochem. J. , vol.390 , pp. 41-47
    • Mortimer, S.E.1    Hedstrom, L.2
  • 30
    • 36849021519 scopus 로고    scopus 로고
    • Inosine monophosphate dehydrogenase as a probe in antiviral drug discovery
    • V. Nair, and Q. Shu Inosine monophosphate dehydrogenase as a probe in antiviral drug discovery Antivir. Chem. Chemother. 18 2007 245 258
    • (2007) Antivir. Chem. Chemother. , vol.18 , pp. 245-258
    • Nair, V.1    Shu, Q.2
  • 33
    • 77955906574 scopus 로고    scopus 로고
    • Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster
    • C. Noree, B.K. Sato, R.M. Broyer, and J.E. Wilhelm Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster J. Cell Biol. 190 2010 541 551
    • (2010) J. Cell Biol. , vol.190 , pp. 541-551
    • Noree, C.1    Sato, B.K.2    Broyer, R.M.3    Wilhelm, J.E.4
  • 36
    • 41049085632 scopus 로고    scopus 로고
    • The CBS subdomain of inosine 5′-monophosphate dehydrogenase regulates purine nucleotide turnover
    • M. Pimkin, and G.D. Markham The CBS subdomain of inosine 5′-monophosphate dehydrogenase regulates purine nucleotide turnover Mol. Microbiol. 68 2008 342 359
    • (2008) Mol. Microbiol. , vol.68 , pp. 342-359
    • Pimkin, M.1    Markham, G.D.2
  • 37
    • 65549120315 scopus 로고    scopus 로고
    • A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis
    • M. Pimkin, J. Pimkina, and G.D. Markham A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis J. Biol. Chem. 284 2009 7960 7969
    • (2009) J. Biol. Chem. , vol.284 , pp. 7960-7969
    • Pimkin, M.1    Pimkina, J.2    Markham, G.D.3
  • 38
    • 33748604738 scopus 로고    scopus 로고
    • Inosine 5′-monophosphate dehydrogenase inhibitors for the treatment of autoimmune diseases
    • A.J. Ratcliffe Inosine 5′-monophosphate dehydrogenase inhibitors for the treatment of autoimmune diseases Curr. Opin. Drug Discov. Devel. 9 2006 595 605
    • (2006) Curr. Opin. Drug Discov. Devel. , vol.9 , pp. 595-605
    • Ratcliffe, A.J.1
  • 40
    • 39549088916 scopus 로고    scopus 로고
    • Inosine monophosphate dehydrogenase (IMPDH) as a target in drug discovery
    • Q. Shu, and V. Nair Inosine monophosphate dehydrogenase (IMPDH) as a target in drug discovery Med. Res. Rev. 28 2008 219 232
    • (2008) Med. Res. Rev. , vol.28 , pp. 219-232
    • Shu, Q.1    Nair, V.2
  • 42
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Cryst. 25 1992 495 503
    • (1992) J. Appl. Cryst. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 43
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • D.I. Svergun, M.V. Petoukhov, and M.H.J. Koch Determination of domain structure of proteins from X-ray solution scattering Biophys. J. 80 2001 2946 2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 45
    • 84870949744 scopus 로고    scopus 로고
    • Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms
    • E.C. Thomas, J.H. Gunter, J.A. Webster, N.L. Schieber, V. Oorschot, R.G. Parton, and J.P. Whitehead Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms PLoS ONE 7 2012 e51096
    • (2012) PLoS ONE , vol.7 , pp. 51096
    • Thomas, E.C.1    Gunter, J.H.2    Webster, J.A.3    Schieber, N.L.4    Oorschot, V.5    Parton, R.G.6    Whitehead, J.P.7
  • 48
    • 0022734418 scopus 로고
    • Resolution criteria for three dimensional reconstruction
    • M. van Heel, and G. Harauz Resolution criteria for three dimensional reconstruction Optik (Stuttg.) 73 1986 119 122
    • (1986) Optik (Stuttg.) , vol.73 , pp. 119-122
    • Van Heel, M.1    Harauz, G.2
  • 50
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Cryst. 36 2003 860 864
    • (2003) J. Appl. Cryst. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 52
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallogr. D Biol. Crystallogr. 57 2001 122 133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 53
    • 78651267246 scopus 로고    scopus 로고
    • Pseudomonas Genome Database: Improved comparative analysis and population genomics capability for Pseudomonas genomes
    • G.L. Winsor, D.K. Lam, L. Fleming, R. Lo, M.D. Whiteside, N.Y. Yu, R.E. Hancock, and F.S. Brinkman Pseudomonas Genome Database: improved comparative analysis and population genomics capability for Pseudomonas genomes Nucleic Acids Res. 39 Database issue 2011 D596 D600
    • (2011) Nucleic Acids Res. , vol.39 , Issue.DATABASE ISSUE
    • Winsor, G.L.1    Lam, D.K.2    Fleming, L.3    Lo, R.4    Whiteside, M.D.5    Yu, N.Y.6    Hancock, R.E.7    Brinkman, F.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.