메뉴 건너뛰기




Volumn 7, Issue , 2007, Pages

Dimerization of inositol monophosphatase Mycobacterium tuberculosis SuhB is not constitutive, but induced by binding of the activator Mg2+

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; MAGNESIUM; SUHB ENZYME; UNCLASSIFIED DRUG; APOPROTEIN; BACTERIAL PROTEIN; MYO INOSITOL 1 (OR 4) MONOPHOSPHATASE; MYO-INOSITOL-1 (OR 4)-MONOPHOSPHATASE; PHOSPHATASE; PROTEIN SUBUNIT;

EID: 36248997046     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-7-55     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 0019127799 scopus 로고
    • The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain
    • 6253491
    • The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. LM Hallcher WR Sherman, J Biol Chem 1980 255 10896 10901 6253491
    • (1980) J Biol Chem , vol.255 , pp. 10896-10901
    • Hallcher, L.M.1    Sherman, W.R.2
  • 2
    • 0015242494 scopus 로고
    • Reduced brain inositol in lithium-treated rats
    • 10.1038/233330a0. 5288124
    • Reduced brain inositol in lithium-treated rats. JH Allison MA Stewart, Nat New Biol 1971 233 267 268 10.1038/233330a0 5288124
    • (1971) Nat New Biol , vol.233 , pp. 267-268
    • Allison, J.H.1    Stewart, M.A.2
  • 3
    • 33847790213 scopus 로고    scopus 로고
    • Myo-Inositol monophosphatase: A challenging target for mood stabilising drugs
    • 10.2174/138955707779802624. 17305585
    • myo-Inositol monophosphatase: a challenging target for mood stabilising drugs. DJ Miller RK Allemann, Mini Rev Med Chem 2007 7 107 113 10.2174/138955707779802624 17305585
    • (2007) Mini Rev Med Chem , vol.7 , pp. 107-113
    • Miller, D.J.1    Allemann, R.K.2
  • 4
    • 0029061399 scopus 로고
    • The envelope of mycobacteria
    • 10.1146/annurev.bi.64.070195.000333. 7574484
    • The envelope of mycobacteria. PJ Brennan H Nikaido, Annu Rev Biochem 1995 64 29 63 10.1146/annurev.bi.64.070195.000333 7574484
    • (1995) Annu Rev Biochem , vol.64 , pp. 29-63
    • Brennan, P.J.1    Nikaido, H.2
  • 5
    • 0031951727 scopus 로고    scopus 로고
    • Mycobacterial lipoarabinomannan: An extraordinary lipoheteroglycan with profound physiological effects
    • 10.1093/glycob/8.2.113. 9451020
    • Mycobacterial lipoarabinomannan: an extraordinary lipoheteroglycan with profound physiological effects. D Chatterjee KH Khoo, Glycobiology 1998 8 113 120 10.1093/glycob/8.2.113 9451020
    • (1998) Glycobiology , vol.8 , pp. 113-120
    • Chatterjee, D.1    Khoo, K.H.2
  • 6
    • 0032695546 scopus 로고    scopus 로고
    • Roles of lipoarabinomannan in the pathogenesis of tuberculosis
    • 10.1016/S1286-4579(99)80072-0. 10611748
    • Roles of lipoarabinomannan in the pathogenesis of tuberculosis. GR Strohmeier MJ Fenton, Microbes Infect 1999 1 709 717 10.1016/S1286-4579(99) 80072-0 10611748
    • (1999) Microbes Infect , vol.1 , pp. 709-717
    • Strohmeier, G.R.1    Fenton, M.J.2
  • 7
    • 0001023242 scopus 로고    scopus 로고
    • Relationships between the structure and the roles of lipoarabinomannans and related glycoconjugates in tuberculosis pathogenesis
    • 9696885
    • Relationships between the structure and the roles of lipoarabinomannans and related glycoconjugates in tuberculosis pathogenesis. A Vercellone J Nigou G Puzo, Front Biosci 1998 3 e149 63 9696885
    • (1998) Front Biosci , vol.3 , pp. 149-63
    • Vercellone, A.1    Nigou, J.2    Puzo, G.3
  • 8
    • 0034730751 scopus 로고    scopus 로고
    • Phosphatidylinositol is an essential phospholipid of mycobacteria
    • 10.1074/jbc.M004658200. 10889206
    • Phosphatidylinositol is an essential phospholipid of mycobacteria. M Jackson DC Crick PJ Brennan, J Biol Chem 2000 275 30092 30099 10.1074/jbc.M004658200 10889206
    • (2000) J Biol Chem , vol.275 , pp. 30092-30099
    • Jackson, M.1    Crick, D.C.2    Brennan, P.J.3
  • 9
    • 0014027508 scopus 로고
    • Biochemical studies on inositol. IX. D-Inositol 1-phosphate as intermediate in the biosynthesis of inositol from glucose 6-phosphate, and characteristics of two reactions in this biosynthesis
    • 4287852
    • Biochemical studies on inositol. IX. D-Inositol 1-phosphate as intermediate in the biosynthesis of inositol from glucose 6-phosphate, and characteristics of two reactions in this biosynthesis. IW Chen CF Charalampous, J Biol Chem 1966 241 2194 2199 4287852
    • (1966) J Biol Chem , vol.241 , pp. 2194-2199
    • Chen, I.W.1    Charalampous, C.F.2
  • 10
    • 0037081779 scopus 로고    scopus 로고
    • Characterization and regulation of inositol monophosphatase activity in Mycobacterium smegmatis
    • 11772411
    • Characterization and regulation of inositol monophosphatase activity in Mycobacterium smegmatis. J Nigou GS Besra, Biochem J 2002 361 385 390 11772411
    • (2002) Biochem J , vol.361 , pp. 385-390
    • Nigou, J.1    Besra, G.S.2
  • 12
    • 0037006993 scopus 로고    scopus 로고
    • Purification and biochemical characterization of Mycobacterium tuberculosis SuhB, an inositol monophosphatase involved in inositol biosynthesis
    • 10.1021/bi0160056. 11914086
    • Purification and biochemical characterization of Mycobacterium tuberculosis SuhB, an inositol monophosphatase involved in inositol biosynthesis. J Nigou LG Dover GS Besra, Biochemistry 2002 41 4392 4398 10.1021/bi0160056 11914086
    • (2002) Biochemistry , vol.41 , pp. 4392-4398
    • Nigou, J.1    Dover, L.G.2    Besra, G.S.3
  • 13
    • 0034636139 scopus 로고    scopus 로고
    • Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: Comparison with bacterial and archaeal inositol monophosphatases
    • 10.1021/bi992424f. 10747806
    • Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases. L Chen MF Roberts, Biochemistry 2000 39 4145 4153 10.1021/bi992424f 10747806
    • (2000) Biochemistry , vol.39 , pp. 4145-4153
    • Chen, L.1    Roberts, M.F.2
  • 14
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • 10.1046/j.1365-2958.2003.03425.x. 12657046
    • Genes required for mycobacterial growth defined by high density mutagenesis. CM Sassetti DH Boyd EJ Rubin, Mol Microbiol 2003 48 77 84 10.1046/j.1365-2958.2003.03425.x 12657046
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 15
    • 28844475855 scopus 로고    scopus 로고
    • Rv2131c gene product: An unconventional enzyme that is both inositol monophosphatase and fructose-1,6-bisphosphatase
    • 10.1016/j.bbrc.2005.11.088. 16325768
    • Rv2131c gene product: an unconventional enzyme that is both inositol monophosphatase and fructose-1,6-bisphosphatase. X Gu M Chen H Shen X Jiang Y Huang H Wang, Biochem Biophys Res Commun 2006 339 897 904 10.1016/j.bbrc.2005. 11.088 16325768
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 897-904
    • Gu, X.1    Chen, M.2    Shen, H.3    Jiang, X.4    Huang, Y.5    Wang, H.6
  • 16
    • 0026493674 scopus 로고
    • Structure of inositol monophosphatase, the putative target of lithium therapy
    • 1332026. 10.1073/pnas.89.21.10031
    • Structure of inositol monophosphatase, the putative target of lithium therapy. R Bone JP Springer JR Atack, Proc Natl Acad Sci U S A 1992 89 10031 10035 1332026 10.1073/pnas.89.21.10031
    • (1992) Proc Natl Acad Sci U S a , vol.89 , pp. 10031-10035
    • Bone, R.1    Springer, J.P.2    Atack, J.R.3
  • 18
    • 0033756225 scopus 로고    scopus 로고
    • MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase
    • 10.1038/80968. 11062561
    • MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. B Stec H Yang KA Johnson L Chen MF Roberts, Nat Struct Biol 2000 7 1046 1050 10.1038/80968 11062561
    • (2000) Nat Struct Biol , vol.7 , pp. 1046-1050
    • Stec, B.1    Yang, H.2    Johnson, K.A.3    Chen, L.4    Roberts, M.F.5
  • 19
    • 0029036695 scopus 로고
    • Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure
    • 7761465. 10.1073/pnas.92.11.5149
    • Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. JD York JW Ponder PW Majerus, Proc Natl Acad Sci U S A 1995 92 5149 5153 7761465 10.1073/pnas.92.11.5149
    • (1995) Proc Natl Acad Sci U S a , vol.92 , pp. 5149-5153
    • York, J.D.1    Ponder, J.W.2    Majerus, P.W.3
  • 20
    • 0027305053 scopus 로고
    • Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase
    • 10.1006/bbrc.1993.1159. 8382485
    • Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase. Y Zhang JY Liang WN Lipscomb, Biochem Biophys Res Commun 1993 190 1080 1083 10.1006/bbrc.1993.1159 8382485
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 1080-1083
    • Zhang, Y.1    Liang, J.Y.2    Lipscomb, W.N.3
  • 21
    • 0034723159 scopus 로고    scopus 로고
    • X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity
    • 10.1006/jmbi.1999.3408. 10656801
    • X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity. A Albert L Yenush MR Gil-Mascarell PL Rodriguez S Patel M Martinez-Ripoll TL Blundell R Serrano, J Mol Biol 2000 295 927 938 10.1006/jmbi.1999.3408 10656801
    • (2000) J Mol Biol , vol.295 , pp. 927-938
    • Albert, A.1    Yenush, L.2    Gil-Mascarell, M.R.3    Rodriguez, P.L.4    Patel, S.5    Martinez-Ripoll, M.6    Blundell, T.L.7    Serrano, R.8
  • 22
    • 0036305698 scopus 로고    scopus 로고
    • Crystal structure of an enzyme displaying both inositol-polyphosphate-1- phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: A novel target of lithium therapy
    • 10.1006/jmbi.2001.5271. 11812139
    • Crystal structure of an enzyme displaying both inositol-polyphosphate-1- phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a novel target of lithium therapy. S Patel L Yenush PL Rodriguez R Serrano TL Blundell, J Mol Biol 2002 315 677 685 10.1006/jmbi.2001.5271 11812139
    • (2002) J Mol Biol , vol.315 , pp. 677-685
    • Patel, S.1    Yenush, L.2    Rodriguez, P.L.3    Serrano, R.4    Blundell, T.L.5
  • 23
    • 34247208019 scopus 로고    scopus 로고
    • Crystal structure of human myo-inositol monophosphatase 2, the product of the putative susceptibility gene for bipolar disorder, schizophrenia, and febrile seizures
    • 10.1002/prot.21299. 17340635
    • Crystal structure of human myo-inositol monophosphatase 2, the product of the putative susceptibility gene for bipolar disorder, schizophrenia, and febrile seizures. R Arai K Ito T Ohnishi H Ohba R Akasaka Y Bessho K Hanawa-Suetsugu T Yoshikawa M Shirouzu S Yokoyama, Proteins 2007 67 732 742 10.1002/prot.21299 17340635
    • (2007) Proteins , vol.67 , pp. 732-742
    • Arai, R.1    Ito, K.2    Ohnishi, T.3    Ohba, H.4    Akasaka, R.5    Bessho, Y.6    Hanawa-Suetsugu, K.7    Yoshikawa, T.8    Shirouzu, M.9    Yokoyama, S.10
  • 24
    • 0035936567 scopus 로고    scopus 로고
    • Crystal structure and catalytic mechanism of the MJ0109 gene product: A bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities
    • 10.1021/bi0016422. 11170378
    • Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities. KA Johnson L Chen H Yang MF Roberts B Stec, Biochemistry 2001 40 618 630 10.1021/bi0016422 11170378
    • (2001) Biochemistry , vol.40 , pp. 618-630
    • Johnson, K.A.1    Chen, L.2    Yang, H.3    Roberts, M.F.4    Stec, B.5
  • 25
    • 0037151076 scopus 로고    scopus 로고
    • Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. the story of a mobile loop
    • 10.1074/jbc.M201042200. 11940584
    • Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. KA Stieglitz KA Johnson H Yang MF Roberts BA Seaton JF Head B Stec, J Biol Chem 2002 277 22863 22874 10.1074/jbc.M201042200 11940584
    • (2002) J Biol Chem , vol.277 , pp. 22863-22874
    • Stieglitz, K.A.1    Johnson, K.A.2    Yang, H.3    Roberts, M.F.4    Seaton, B.A.5    Head, J.F.6    Stec, B.7
  • 26
    • 0025160386 scopus 로고
    • Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium
    • 2164670. 10.1073/pnas.87.14.5243
    • Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium. HM Ke YP Zhang WN Lipscomb, Proc Natl Acad Sci U S A 1990 87 5243 5247 2164670 10.1073/pnas.87.14.5243
    • (1990) Proc Natl Acad Sci U S a , vol.87 , pp. 5243-5247
    • Ke, H.M.1    Zhang, Y.P.2    Lipscomb, W.N.3
  • 27
    • 34247605062 scopus 로고    scopus 로고
    • Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima
    • 10.1111/j.0014-2956.2007.05779.x. 17419729
    • Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima. KA Stieglitz MF Roberts W Li B Stec, FEBS J 2007 274 2461 2469 10.1111/j.0014-2956.2007.05779.x 17419729
    • (2007) FEBS J , vol.274 , pp. 2461-2469
    • Stieglitz, K.A.1    Roberts, M.F.2    Li, W.3    Stec, B.4
  • 28
    • 0028105959 scopus 로고
    • Structural studies of metal binding by inositol monophosphatase: Evidence for two-metal ion catalysis
    • 10.1021/bi00198a012. 8068621
    • Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis. R Bone L Frank JP Springer JR Atack, Biochemistry 1994 33 9468 9476 10.1021/bi00198a012 8068621
    • (1994) Biochemistry , vol.33 , pp. 9468-9476
    • Bone, R.1    Frank, L.2    Springer, J.P.3    Atack, J.R.4
  • 31
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystallline state
    • doi:10.1016/j.jmb.2007.05.022:available online 13 May 2007. 17681537
    • Inference of macromolecular assemblies from crystallline state. E Krissinel K Henrick, J Mol Biol 2007 doi:10.1016/j.jmb.2007.05.022:available online 13 May 2007. 17681537
    • (2007) J Mol Biol
    • Krissinel, E.1    Henrick, K.2
  • 32
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • 10.1016/S0003-2697(03)00289-6. 12895474
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. P Schuck, Anal Biochem 2003 320 104 124 10.1016/S0003-2697(03)00289-6 12895474
    • (2003) Anal Biochem , vol.320 , pp. 104-124
    • Schuck, P.1
  • 33
    • 0031813850 scopus 로고    scopus 로고
    • Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme
    • 9647837
    • Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme. L Chen MF Roberts, Appl Environ Microbiol 1998 64 2609 2615 9647837
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2609-2615
    • Chen, L.1    Roberts, M.F.2
  • 34
    • 0032861041 scopus 로고    scopus 로고
    • Characterization of a tetrameric inositol monophosphatase from the hyperthermophilic bacterium Thermotoga maritima
    • 10508089
    • Characterization of a tetrameric inositol monophosphatase from the hyperthermophilic bacterium Thermotoga maritima. L Chen MF Roberts, Appl Environ Microbiol 1999 65 4559 4567 10508089
    • (1999) Appl Environ Microbiol , vol.65 , pp. 4559-4567
    • Chen, L.1    Roberts, M.F.2
  • 36
    • 0025331691 scopus 로고
    • Kinetic studies with myo-inositol monophosphatase from bovine brain
    • 10.1021/bi00477a026. 2166573
    • Kinetic studies with myo-inositol monophosphatase from bovine brain. AJ Ganzhorn MC Chanal, Biochemistry 1990 29 6065 6071 10.1021/bi00477a026 2166573
    • (1990) Biochemistry , vol.29 , pp. 6065-6071
    • Ganzhorn, A.J.1    Chanal, M.C.2
  • 37
    • 0029781838 scopus 로고    scopus 로고
    • The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase
    • 10.1021/bi9603837. 8718889
    • The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase. AJ Ganzhorn P Lepage PD Pelton F Strasser P Vincendon JM Rondeau, Biochemistry 1996 35 10957 10966 10.1021/bi9603837 8718889
    • (1996) Biochemistry , vol.35 , pp. 10957-10966
    • Ganzhorn, A.J.1    Lepage, P.2    Pelton, P.D.3    Strasser, F.4    Vincendon, P.5    Rondeau, J.M.6
  • 38
    • 0028930516 scopus 로고
    • Kinetic characterization of enzyme forms involved in metal ion activation and inhibition of myo-inositol monophosphatase
    • 7733900
    • Kinetic characterization of enzyme forms involved in metal ion activation and inhibition of myo-inositol monophosphatase. F Strasser PD Pelton AJ Ganzhorn, Biochem J 1995 307 585 593 7733900
    • (1995) Biochem J , vol.307 , pp. 585-593
    • Strasser, F.1    Pelton, P.D.2    Ganzhorn, A.J.3
  • 39
    • 0027456612 scopus 로고
    • Reversible unfolding of myo-inositol monophosphatase
    • 8385126
    • Reversible unfolding of myo-inositol monophosphatase. OS Kwon SC Lo F Kwok JE Churchich, J Biol Chem 1993 268 7912 7916 8385126
    • (1993) J Biol Chem , vol.268 , pp. 7912-7916
    • Kwon, O.S.1    Lo, S.C.2    Kwok, F.3    Churchich, J.E.4
  • 40
    • 33745854135 scopus 로고    scopus 로고
    • Novel allosteric activation site in Escherichia coli fructose-1,6- bisphosphatase
    • 10.1074/jbc.M602553200. 16670087
    • Novel allosteric activation site in Escherichia coli fructose-1,6- bisphosphatase. JK Hines HJ Fromm RB Honzatko, J Biol Chem 2006 281 18386 18393 10.1074/jbc.M602553200 16670087
    • (2006) J Biol Chem , vol.281 , pp. 18386-18393
    • Hines, J.K.1    Fromm, H.J.2    Honzatko, R.B.3
  • 41
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • 10.1006/jmbi.1996.0399. 8757792
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. B Miroux JE Walker, J Mol Biol 1996 260 289 298 10.1006/jmbi.1996.0399 8757792
    • (1996) J Mol Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Processing of X-ray diffraction data collected in oscillation mode. Z Otwinowski W Minor, Methods Enzymol 1997 276 307 326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 10.1107/S0907444994003112. 15299374
    • The CCP4 suite: programs for protein crystallography. CCP4, Acta Crystallogr D Biol Crystallogr 1994 50 760 763 10.1107/S0907444994003112 15299374
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 44
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 10.1107/S0108767390010224. 2025413
    • Improved methods for building protein models in electron density maps and the location of errors in these models. TA Jones JY Zou SW Cowan M Kjeldgaard, Acta Crystallogr A 1991 47 110 119 10.1107/S0108767390010224 2025413
    • (1991) Acta Crystallogr a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 45
    • 84945096204 scopus 로고
    • Model bias in crystal structures
    • 10.1107/S0108767392006044
    • Model bias in crystal structures. A Hodel S-H Kim AT Brünger, Acta Crystallogr A 1992 48 851 858 10.1107/S0108767392006044
    • (1992) Acta Crystallogr a , vol.48 , pp. 851-858
    • Hodel, A.1    Kim, S.-H.2    Brünger, A.T.3
  • 47
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • 10.1107/S0907444996012255. 15299926
    • Refinement of macromolecular structures by the maximum-likelihood method. GN Murshudov AA Vagin EJ Dodson, Acta Crystallogr D Biol Crystallogr 1997 53 240 255 10.1107/S0907444996012255 15299926
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 50
    • 0034096904 scopus 로고    scopus 로고
    • Protein structure computing in the genomic era
    • 10.1016/S0923-2508(00)00121-2. 10865955
    • Protein structure computing in the genomic era. T Schwede A Diemand N Guex MC Peitsch, Res Microbiol 2000 151 107 112 10.1016/S0923-2508(00)00121-2 10865955
    • (2000) Res Microbiol , vol.151 , pp. 107-112
    • Schwede, T.1    Diemand, A.2    Guex, N.3    Peitsch, M.C.4
  • 52
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • 10692345
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. P Schuck, Biophys J 2000 78 1606 1619 10692345
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 53
    • 0035012982 scopus 로고    scopus 로고
    • STRAP: Editor for STRuctural Alignments of Proteins
    • 10.1093/bioinformatics/17.4.377. 11301311
    • STRAP: editor for STRuctural Alignments of Proteins. C Gille C Frommel, Bioinformatics 2001 17 377 378 10.1093/bioinformatics/17.4.377 11301311
    • (2001) Bioinformatics , vol.17 , pp. 377-378
    • Gille, C.1    Frommel, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.