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Volumn 11, Issue , 2011, Pages

The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE RACEMASE; BACTERIAL ENZYME;

EID: 80055068595     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-11-116     Document Type: Review
Times cited : (30)

References (78)
  • 2
    • 0034971094 scopus 로고    scopus 로고
    • Pneumococcal virulence factors: Structure and function
    • DOI 10.1128/MMBR.65.2.187-207.2001
    • Pneumococcal virulence factors: structure and function. MJ Jedrzejas, Microbiol Mol Biol Rev 2001 65 187 207 10.1128/MMBR.65.2.187-207.2001 11381099 (Pubitemid 32538177)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.2 , pp. 187-207
    • Jedrzejas, M.J.1
  • 3
    • 33744520754 scopus 로고    scopus 로고
    • Antibiotics in childhood pneumonia
    • DOI 10.1016/j.prrv.2006.03.011, PII S1526054206000315
    • Antibiotics in childhood pneumonia. KA Hale D Isaacs, Paediatr Respir Rev 2006 7 145 151 10.1016/j.prrv.2006.03.011 16765302 (Pubitemid 43812271)
    • (2006) Paediatric Respiratory Reviews , vol.7 , Issue.2 , pp. 145-151
    • Hale, K.A.1    Isaacs, D.2
  • 4
    • 0009134424 scopus 로고    scopus 로고
    • World Health Organization Initiative for Vaccine Research
    • Acute Respiratory Infections (Update September 2009). World Health Organization Initiative for Vaccine Research, http://www.who.int/vaccine- research/diseases/ari/en/
    • Acute Respiratory Infections (Update September 2009)
  • 7
    • 0347364864 scopus 로고    scopus 로고
    • Community-acquired pneumonia
    • 10.1016/S0140-6736(03)15021-0. 14683661
    • Community-acquired pneumonia. TM File, Lancet 2003 362 1991 2001 10.1016/S0140-6736(03)15021-0 14683661
    • (2003) Lancet , vol.362 , pp. 1991-2001
    • File, T.M.1
  • 8
    • 33646023997 scopus 로고    scopus 로고
    • Interactions between influenza and bacterial respiratory pathogens: Implications for pandemic preparedness
    • 10.1016/S1473-3099(06)70466-2. 16631551
    • Interactions between influenza and bacterial respiratory pathogens: implications for pandemic preparedness. JF Brundage, Lancet Infect Dis 2006 6 303 312 10.1016/S1473-3099(06)70466-2 16631551
    • (2006) Lancet Infect Dis , vol.6 , pp. 303-312
    • Brundage, J.F.1
  • 9
    • 34147138871 scopus 로고    scopus 로고
    • Pneumococcal vaccines and flu preparedness
    • 17412937
    • Pneumococcal vaccines and flu preparedness. KP Klugman SA Madhi, Science 2007 316 49 50 17412937
    • (2007) Science , vol.316 , pp. 49-50
    • Klugman, K.P.1    Madhi, S.A.2
  • 12
    • 63149089810 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Does antimicrobial resistance matter?
    • 10.1055/s-0029-1202939. 19296420
    • Streptococcus pneumoniae: does antimicrobial resistance matter? JP Lynch GG Zhanel, Semin Respir Crit Care Med 2009 30 210 238 10.1055/s-0029-1202939 19296420
    • (2009) Semin Respir Crit Care Med , vol.30 , pp. 210-238
    • Lynch, J.P.1    Zhanel, G.G.2
  • 13
    • 0027372678 scopus 로고
    • A brief history of the pneumococcus in biomedical research: A panoply of scientific discovery
    • A brief history of the pneumococcus in biomedical research: a panoply of scientific discovery. DA Watson DM Musher JW Jacobson J Verhoef, Clin Infect Dis 1993 17 913 924 10.1093/clinids/17.5.913 8286641 (Pubitemid 23321919)
    • (1993) Clinical Infectious Diseases , vol.17 , Issue.5 , pp. 913-924
    • Watson, D.A.1    Musher, D.M.2    Jacobson, J.W.3    Verhoef, J.4
  • 14
    • 33645817952 scopus 로고    scopus 로고
    • Clinical implications and treatment of multiresistant Streptococcus pneumoniae pneumonia
    • 16669927
    • Clinical implications and treatment of multiresistant Streptococcus pneumoniae pneumonia. TM File Jr, Clin Microbiol Infect 2006 12 Suppl 3 31 41 16669927
    • (2006) Clin Microbiol Infect , vol.12 , Issue.SUPPL. 3 , pp. 31-41
    • File Jr., T.M.1
  • 16
    • 65449169610 scopus 로고    scopus 로고
    • The antimicrobial resistance profile of Streptococcus pneumoniae
    • 19366363
    • The antimicrobial resistance profile of Streptococcus pneumoniae. RR Reinert, Clin Microbiol Infect 2009 15 Suppl 3 7 11 19366363
    • (2009) Clin Microbiol Infect , vol.15 , Issue.SUPPL. 3 , pp. 7-11
    • Reinert, R.R.1
  • 17
    • 39149101446 scopus 로고    scopus 로고
    • Distribution and antibacterial susceptibility of macrolide resistance genotypes in Streptococcus pneumoniae: PROTEKT Year 5 (2003-2004)
    • 10.1016/j.ijantimicag.2007.10.022. 18178388
    • Distribution and antibacterial susceptibility of macrolide resistance genotypes in Streptococcus pneumoniae: PROTEKT Year 5 (2003-2004). DJ Farrell C Couturier W Hryniewicz, Int J Antimicrob Agents 2008 31 245 249 10.1016/j.ijantimicag.2007.10.022 18178388
    • (2008) Int J Antimicrob Agents , vol.31 , pp. 245-249
    • Farrell, D.J.1    Couturier, C.2    Hryniewicz, W.3
  • 18
    • 0015310390 scopus 로고
    • Factors affecting the level of alanine racemase in Escherichia coli
    • 4551748
    • Factors affecting the level of alanine racemase in Escherichia coli. MP Lambert FC Neuhaus, J Bacteriol 1972 109 1156 1161 4551748
    • (1972) J Bacteriol , vol.109 , pp. 1156-1161
    • Lambert, M.P.1    Neuhaus, F.C.2
  • 19
    • 36549035341 scopus 로고    scopus 로고
    • The alanine racemase of Mycobacterium smegmatis is essential for growth in the absence of D-alanine
    • DOI 10.1128/JB.01201-07
    • The alanine racemase of Mycobacterium smegmatis is essential for growth in the absence of D-alanine. DL Milligan SL Tran U Strych GM Cook KL Krause, J Bacteriol 2007 189 8381 8386 10.1128/JB.01201-07 17827284 (Pubitemid 350178954)
    • (2007) Journal of Bacteriology , vol.189 , Issue.22 , pp. 8381-8386
    • Milligan, D.L.1    Tran, S.L.2    Strych, U.3    Cook, G.M.4    Krause, K.L.5
  • 20
    • 0036136146 scopus 로고    scopus 로고
    • Mycobacterium smegmatis D-alanine racemase mutants are not dependent on D-alanine for growth
    • DOI 10.1128/AAC.46.2.47-54.2002
    • Mycobacterium smegmatis D-Alanine Racemase Mutants Are Not Dependent on D-Alanine for Growth. O Chacon Z Feng NB Harris NE Caceres LG Adams RG Barletta, Antimicrob Agents Chemother 2002 46 47 54 10.1128/AAC.46.2.47-54.2002 11751110 (Pubitemid 34031601)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.1 , pp. 47-54
    • Chacon, O.1    Feng, Z.2    Harris, N.B.3    Caceres, N.E.4    Adams, L.G.5    Barletta, R.G.6
  • 21
    • 34249800689 scopus 로고    scopus 로고
    • Purification and preliminary crystallization of alanine racemase from Streptococcus pneumoniae
    • 10.1186/1471-2180-7-40. 17509154
    • Purification and preliminary crystallization of alanine racemase from Streptococcus pneumoniae. U Strych M Davlieva J Longtin E Murphy H Im M Benedik K Krause, BMC Microbiol 2007 7 40 10.1186/1471-2180-7-40 17509154
    • (2007) BMC Microbiol , vol.7 , pp. 40
    • Strych, U.1    Davlieva, M.2    Longtin, J.3    Murphy, E.4    Im, H.5    Benedik, M.6    Krause, K.7
  • 22
    • 0002769785 scopus 로고
    • The potential use of mechanism-based enzyme inactivators in medicine
    • The potential use of mechanism-based enzyme inactivators in medicine. RB Silverman, J Enzyme Inhib 1988 2 73 90 10.3109/14756368809040714 3069967 (Pubitemid 18033735)
    • (1987) Journal of Enzyme Inhibition , vol.2 , Issue.2 , pp. 73-90
    • Silverman, R.B.1
  • 23
    • 0011875185 scopus 로고
    • Three dimensional structure-aided drug design
    • New York: John Wiley & Sons, Inc Wolff ME 5. 21611913
    • Three dimensional structure-aided drug design. B Veerapandian, Burger's Medicinal Chemistry and Drug Discovery Volume 1 New York: John Wiley & Sons, Inc, Wolff ME, 5 1995 303 348 21611913
    • (1995) Burger's Medicinal Chemistry and Drug Discovery Volume 1 , pp. 303-348
    • Veerapandian, B.1
  • 25
    • 0030574268 scopus 로고    scopus 로고
    • Structure-based drug design
    • DOI 10.1038/384023a0
    • Structure-based drug design. TL Blundell, Nature 1996 384 23 26 10.1038/384023a0 8900268 (Pubitemid 26374536)
    • (1996) Nature , vol.384 , Issue.6604 SUPPL. , pp. 23-26
    • Blundell, T.L.1
  • 26
    • 16844378698 scopus 로고    scopus 로고
    • Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase
    • DOI 10.1021/bi047842l
    • Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase. TD Fenn T Holyoak GF Stamper D Ringe, Biochemistry 2005 44 5317 5327 10.1021/bi047842l 15807525 (Pubitemid 40489971)
    • (2005) Biochemistry , vol.44 , Issue.14 , pp. 5317-5327
    • Fenn, T.D.1    Holyoak, T.2    Stamper, G.F.3    Ringe, D.4
  • 27
    • 0037952855 scopus 로고    scopus 로고
    • A side reaction of alanine racemase: Transamination of cycloserine
    • DOI 10.1021/bi027022d
    • A side reaction of alanine racemase: transamination of cycloserine. TD Fenn GF Stamper AA Morollo D Ringe, Biochemistry 2003 42 5775 5783 10.1021/bi027022d 12741835 (Pubitemid 36582869)
    • (2003) Biochemistry , vol.42 , Issue.19 , pp. 5775-5783
    • Fenn, T.D.1    Stamper, G.F.2    Morollo, A.A.3    Ringe, D.4
  • 28
    • 0033574155 scopus 로고    scopus 로고
    • Structure of a Michaelis complex analogue: Propionate binds in the substrate carboxylate site of alanine racemase
    • 10.1021/bi9822729. 10079072
    • Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase. AA Morollo GA Petsko D Ringe, Biochemistry 1999 38 3293 3301 10.1021/bi9822729 10079072
    • (1999) Biochemistry , vol.38 , pp. 3293-3301
    • Morollo, A.A.1    Petsko, G.A.2    Ringe, D.3
  • 29
    • 0031032448 scopus 로고    scopus 로고
    • Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution
    • DOI 10.1021/bi961856c
    • Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9- resolution. JP Shaw GA Petsko D Ringe, Biochemistry 1997 36 1329 1342 10.1021/bi961856c 9063881 (Pubitemid 27074957)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1329-1342
    • Shaw, J.P.1    Petsko, G.A.2    Ringe, D.3
  • 30
    • 0032555181 scopus 로고    scopus 로고
    • Reaction of alanine racemase with 1-Aminoethylphosphonic acid forms a stable external aldimine
    • DOI 10.1021/bi980692s
    • Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine. GF Stamper AA Morollo D Ringe, Biochemistry 1998 37 10438 10445 10.1021/bi980692s 9671513 (Pubitemid 28357566)
    • (1998) Biochemistry , vol.37 , Issue.29 , pp. 10438-10445
    • Stamper, C.G.F.1    Morollo, A.A.2    Ringe, D.3
  • 31
    • 0037166337 scopus 로고    scopus 로고
    • Reaction mechanism of alanine racemase from Bacillus stearothermophilus
    • 10.1074/jbc.M201615200. 11886871
    • Reaction mechanism of alanine racemase from Bacillus stearothermophilus. A Watanabe T Yoshimura B Mikami H Hayashi H Kagamiyama N Esaki, J Biol Chem 2002 277 19166 19172 10.1074/jbc.M201615200 11886871
    • (2002) J Biol Chem , vol.277 , pp. 19166-19172
    • Watanabe, A.1    Yoshimura, T.2    Mikami, B.3    Hayashi, H.4    Kagamiyama, H.5    Esaki, N.6
  • 32
    • 0345734003 scopus 로고    scopus 로고
    • Crystal Structure at 1.45 A Resolution of Alanine Racemase from a Pathogenic Bacterium, Pseudomonas aeruginosa, Contains Both Internal and External Aldimine Forms
    • DOI 10.1021/bi030165v
    • Crystal structure at 1.45 resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms. P LeMagueres H Im A Dvorak U Strych M Benedik KL Krause, Biochemistry 2003 42 14752 14761 10.1021/bi030165v 14674749 (Pubitemid 37553503)
    • (2003) Biochemistry , vol.42 , Issue.50 , pp. 14752-14761
    • LeMagueres, P.1    Im, H.2    Dvorak, A.3    Strych, U.4    Benedik, M.5    Krause, K.L.6
  • 33
    • 8544247988 scopus 로고    scopus 로고
    • Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product
    • DOI 10.1074/jbc.M404605200
    • Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product. M Noda Y Matoba T Kumagai M Sugiyama, J Biol Chem 2004 279 46153 46161 10.1074/jbc.M404605200 15302886 (Pubitemid 39491610)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 46153-46161
    • Noda, M.1    Matoba, Y.2    Kumagai, T.3    Sugiyama, M.4
  • 34
    • 13444274582 scopus 로고    scopus 로고
    • The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site
    • DOI 10.1021/bi0486583
    • The 1.9 crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site. P LeMagueres H Im J Ebalunode U Strych MJ Benedik JM Briggs H Kohn KL Krause, Biochemistry 2005 44 1471 1481 10.1021/bi0486583 15683232 (Pubitemid 40204391)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1471-1481
    • LeMagueres, P.1    Im, H.2    Ebalunode, J.3    Strych, U.4    Benedik, M.J.5    Briggs, J.M.6    Kohn, H.7    Krause, K.L.8
  • 36
    • 70349602115 scopus 로고    scopus 로고
    • Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames)
    • 10.1186/1472-6807-9-53. 19695097
    • Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames). R Coũago M Davlieva U Strych R Hill K Krause, BMC Struct Biol 2009 9 53 10.1186/1472-6807-9-53 19695097
    • (2009) BMC Struct Biol , vol.9 , pp. 53
    • Coũago, R.1    Davlieva, M.2    Strych, U.3    Hill, R.4    Krause, K.5
  • 37
    • 44349161779 scopus 로고    scopus 로고
    • Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis
    • DOI 10.1110/ps.083495908
    • Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis. D Wu T Hu L Zhang J Chen J Du J Ding H Jiang X Shen, Protein Sci 2008 17 1066 1076 10.1110/ps.083495908 18434499 (Pubitemid 351749212)
    • (2008) Protein Science , vol.17 , Issue.6 , pp. 1066-1076
    • Wu, D.1    Hu, T.2    Zhang, L.3    Chen, J.4    Du, J.5    Ding, J.6    Jiang, H.7    Shen, X.8
  • 40
    • 0032757833 scopus 로고    scopus 로고
    • Tyrosine 265 of alanine racemase serves as a base abstracting α-hydrogen from L-alanine: The counterpart residue to lysine 39 specific to D-alanine
    • Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine. A Watanabe T Yoshimura B Mikami N Esaki, J Biochem 1999 126 781 786 10502689 (Pubitemid 29500401)
    • (1999) Journal of Biochemistry , vol.126 , Issue.4 , pp. 781-786
    • Watanabe, A.1    Yoshimura, T.2    Mikami, B.3    Esaki, N.4
  • 41
    • 0033616634 scopus 로고    scopus 로고
    • Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase
    • 10.1021/bi982924t. 10194319
    • Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase. S Sun MD Toney, Biochemistry 1999 38 4058 4065 10.1021/bi982924t 10194319
    • (1999) Biochemistry , vol.38 , pp. 4058-4065
    • Sun, S.1    Toney, M.D.2
  • 43
    • 0001841380 scopus 로고
    • On the rigid-body motion of molecules in crystals
    • 10.1107/S0567740868001718
    • On the rigid-body motion of molecules in crystals. V Schomaker KN Trueblood, Acta Crystallogr B 1968 24 63 76 10.1107/S0567740868001718
    • (1968) Acta Crystallogr B , vol.24 , pp. 63-76
    • Schomaker, V.1    Trueblood, K.N.2
  • 44
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • Collaborative Computational Project Number 4 10.1107/S0907444994003112. 15299374
    • The CCP4 Suite: Programs for Protein Crystallography. Collaborative Computational Project Number 4, Acta Crystallogr D Biol Crystallogr 1994 50 760 763 10.1107/S0907444994003112 15299374
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 45
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 10.1107/S0021889892009944
    • PROCHECK: a program to check the stereochemical quality of protein structures. RA Laskowski MW MacArthur DS Moss JM Thornton, J Appl Crystallogr 1993 26 283 291 10.1107/S0021889892009944
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 47
    • 0036068204 scopus 로고    scopus 로고
    • Mutant analysis shows that alanine racemases from Pseudomonas aeruginosa and Escherichia coli are dimeric
    • DOI 10.1128/JB.184.15.4321-4325.2002
    • Mutant analysis shows that alanine racemases from Pseudomonas aeruginosa and Escherichia coli are dimeric. U Strych MJ Benedik, J Bacteriol 2002 184 4321 4325 10.1128/JB.184.15.4321-4325.2002 12107154 (Pubitemid 34774317)
    • (2002) Journal of Bacteriology , vol.184 , Issue.15 , pp. 4321-4325
    • Strych, U.1    Benedik, M.J.2
  • 48
    • 0142093983 scopus 로고    scopus 로고
    • Subunit interaction of monomeric alanine racemases from four Shigella species in catalytic reaction
    • DOI 10.1016/S0378-1097(03)00216-7
    • Subunit interaction of monomeric alanine racemases from four Shigella species in catalytic reaction. K Yokoigawa Y Okubo K Soda, FEMS Microbiol Lett 2003 221 263 267 10.1016/S0378-1097(03)00216-7 12725937 (Pubitemid 41123073)
    • (2003) FEMS Microbiology Letters , vol.221 , Issue.2 , pp. 263-267
    • Yokoigawa, K.1    Okubo, Y.2    Soda, K.3
  • 49
    • 78650669920 scopus 로고    scopus 로고
    • Correlation between catalytic activity and monomer-dimer equilibrium of bacterial alanine racemases
    • 10.1093/jb/mvq120. 20971724
    • Correlation between catalytic activity and monomer-dimer equilibrium of bacterial alanine racemases. J Ju S Xu Y Furukawa Y Zhang H Misono T Minamino K Namba B Zhao K Ohnishi, J Biochem 2011 149 83 89 10.1093/jb/mvq120 20971724
    • (2011) J Biochem , vol.149 , pp. 83-89
    • Ju, J.1    Xu, S.2    Furukawa, Y.3    Zhang, Y.4    Misono, H.5    Minamino, T.6    Namba, K.7    Zhao, B.8    Ohnishi, K.9
  • 50
    • 2942654629 scopus 로고    scopus 로고
    • Alanine racemase free energy profiles from global analyses of progress curves
    • DOI 10.1021/ja049579h
    • Alanine racemase free energy profiles from global analyses of progress curves. MA Spies JJ Woodward MR Watnik MD Toney, J Am Chem Soc 2004 126 7464 7475 10.1021/ja049579h 15198593 (Pubitemid 38781480)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.24 , pp. 7464-7475
    • Spies, M.A.1    Woodward, J.J.2    Watnik, M.R.3    Toney, M.D.4
  • 51
    • 0036902246 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance
    • DOI 10.1002/1439-7633(20020802)3:8<789::AID-CBIC789>3.0.CO;2-D
    • Site-directed mutagenesis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance. WM Patrick J Weisner JM Blackburn, Chembiochem 2002 3 789 792 10.1002/1439-7633(20020802)3:8<789:: AID-CBIC7893.0.CO;2-D 12203980 (Pubitemid 36004521)
    • (2002) ChemBioChem , vol.3 , Issue.8 , pp. 789-792
    • Patrick, W.M.1    Weisner, J.2    Blackburn, J.M.3
  • 52
    • 2942545807 scopus 로고    scopus 로고
    • On the function of the 14 A long internal cavity of histone deacetylase-like protein: Implications for the design of histone deacetylase inhibitors
    • DOI 10.1021/jm0498497
    • On the function of the 14 long internal cavity of histone deacetylase-like protein: implications for the design of histone deacetylase inhibitors. DF Wang O Wiest P Helquist HY Lan-Hargest NL Wiech, J Med Chem 2004 47 3409 3417 10.1021/jm0498497 15189037 (Pubitemid 38746091)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.13 , pp. 3409-3417
    • Wang, D.-F.1    Wiest, O.2    Helquist, P.3    Lan-Hargest, H.-Y.4    Wiech, N.L.5
  • 53
    • 0036753937 scopus 로고    scopus 로고
    • Dimerization inhibitors of HIV-1 protease
    • DOI 10.1515/BC.2002.150
    • Dimerization inhibitors of HIV-1 protease. N Boggetto M Reboud-Ravaux, Biol Chem 2002 383 1321 1324 10.1515/BC.2002.150 12437124 (Pubitemid 35282949)
    • (2002) Biological Chemistry , vol.383 , Issue.9 , pp. 1321-1324
    • Boggetto, N.1    Reboud-Ravaux, M.2
  • 54
    • 0035903892 scopus 로고    scopus 로고
    • Design and synthesis of new inhibitors of HIV-1 protease dimerization with conformationally constrained templates
    • DOI 10.1016/S0960-894X(01)00468-1, PII S0960894X01004681
    • Design and synthesis of new inhibitors of HIV-1 protease dimerization with conformationally constrained templates. M Song S Rajesh Y Hayashi Y Kiso, Bioorg Med Chem Lett 2001 11 2465 2468 10.1016/S0960-894X(01)00468-1 11549448 (Pubitemid 32823335)
    • (2001) Bioorganic and Medicinal Chemistry Letters , vol.11 , Issue.18 , pp. 2465-2468
    • Song, M.-C.1    Rajesh, S.2    Hayashi, Y.3    Kiso, Y.4
  • 55
    • 33646128970 scopus 로고    scopus 로고
    • Breaking the spell: Drug discovery based on modulating protein-protein interactions
    • 10.1586/14789450.1.2.141. 15966807
    • Breaking the spell: drug discovery based on modulating protein-protein interactions. AD Strosberg, Expert Rev Proteomics 2004 1 141 143 10.1586/14789450.1.2.141 15966807
    • (2004) Expert Rev Proteomics , vol.1 , pp. 141-143
    • Strosberg, A.D.1
  • 56
    • 33646727594 scopus 로고    scopus 로고
    • A common allosteric site and mechanism in caspases
    • 10.1073/pnas.0602571103. 16682620
    • A common allosteric site and mechanism in caspases. JM Scheer MJ Romanowski JA Wells, Proc Natl Acad Sci USA 2006 103 7595 7600 10.1073/pnas.0602571103 16682620
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7595-7600
    • Scheer, J.M.1    Romanowski, M.J.2    Wells, J.A.3
  • 57
    • 2942641889 scopus 로고    scopus 로고
    • Cluster analysis of water molecules in alanine racemase and their putative structural role
    • DOI 10.1093/protein/gzh033
    • Cluster analysis of water molecules in alanine racemase and their putative structural role. G Mustata JM Briggs, Protein Eng Des Sel 2004 17 223 234 10.1093/protein/gzh033 15115851 (Pubitemid 38781194)
    • (2004) Protein Engineering, Design and Selection , vol.17 , Issue.3 , pp. 223-234
    • Mustata, G.1    Briggs, J.M.2
  • 58
    • 0001554681 scopus 로고
    • Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin
    • 10.1073/pnas.81.19.6014. 16593516
    • Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin. MM Teeter, Proc Natl Acad Sci USA 1984 81 6014 6018 10.1073/pnas.81.19.6014 16593516
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 6014-6018
    • Teeter, M.M.1
  • 59
    • 0002617578 scopus 로고
    • Antimicrobial agents: Drugs used in the chemotherapy of tuberculosis and leprosy
    • New York: Macmillan Publishing Co. Inc Goodman LS,Gilman A 5
    • Antimicrobial agents: drugs used in the chemotherapy of tuberculosis and leprosy. L Weinstein, The pharmacological basis of therapeutics New York: Macmillan Publishing Co. Inc, Goodman LS,Gilman A, 5 1975 1201 1223
    • (1975) The Pharmacological Basis of Therapeutics , pp. 1201-1223
    • Weinstein, L.1
  • 60
    • 0037499658 scopus 로고    scopus 로고
    • A structure-based design approach for the identification of novel inhibitors: Application to an alanine racemase
    • DOI 10.1023/A:1023875514454
    • A structure-based design approach for the identification of novel inhibitors: application to an alanine racemase. GI Mustata JM Briggs, J Comput Aided Mol Des 2002 16 935 953 10.1023/A:1023875514454 12825624 (Pubitemid 36701527)
    • (2002) Journal of Computer-Aided Molecular Design , vol.16 , Issue.12 , pp. 935-953
    • Mustata, G.I.1    Briggs, J.M.2
  • 61
    • 77951223140 scopus 로고    scopus 로고
    • The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding
    • 10.1074/jbc.M109.050062. 20106978
    • The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. MA Smith V Mack A Ebneth I Moraes B Felicetti M Wood D Schonfeld O Mather A Cesura J Barker, J Biol Chem 2010 285 12873 12881 10.1074/jbc.M109.050062 20106978
    • (2010) J Biol Chem , vol.285 , pp. 12873-12881
    • Smith, M.A.1    MacK, V.2    Ebneth, A.3    Moraes, I.4    Felicetti, B.5    Wood, M.6    Schonfeld, D.7    Mather, O.8    Cesura, A.9    Barker, J.10
  • 63
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Processing of X-ray diffraction data collected in oscillation mode. Z Otwinowski W Minor, Methods Enzymol 1997 276 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 64
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • 10.1016/0022-2836(68)90205-2. 5700707
    • Solvent content of protein crystals. BW Matthews, J Mol Biol 1968 33 491 497 10.1016/0022-2836(68)90205-2 5700707
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 65
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • DOI 10.1016/S0076-6879(97)77016-2
    • Automated refinement for protein crystallography. VS Lamzin KS Wilson, Methods Enzymol 1997 277 269 305 18488314 (Pubitemid 27390926)
    • (1997) Methods in Enzymology , vol.277 , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 66
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • 10.1107/S0907444906005270. 16552146
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. J Painter EA Merritt, Acta Crystallogr D Biol Crystallogr 2006 62 439 450 10.1107/S0907444906005270 16552146
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 67
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • 10.1107/S0021889805038987
    • TLSMD web server for the generation of multi-group TLS models. J Painter EA Merritt, J Appl Crystallogr 2006 39 109 111 10.1107/S0021889805038987
    • (2006) J Appl Crystallogr , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 68
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. E Krissinel K Henrick, Acta Crystallogr D Biol Crystallogr 2004 60 2256 2268 10.1107/S0907444904026460 15572779 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 69
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Inference of macromolecular assemblies from crystalline state. E Krissinel K Henrick, J Mol Biol 2007 372 774 797 10.1016/j.jmb.2007.05.022 17681537 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 70
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein-protein interaction analysis server
    • 10.1093/bioinformatics/btn584. 19001476
    • ProtorP: a protein-protein interaction analysis server. C Reynolds D Damerell S Jones, Bioinformatics 2009 25 413 414 10.1093/bioinformatics/btn584 19001476
    • (2009) Bioinformatics , vol.25 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 72
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • 10.1093/bioinformatics/btp033. 19151095
    • Jalview Version 2 - a multiple sequence alignment editor and analysis workbench. AM Waterhouse JB Procter DM Martin M Clamp GJ Barton, Bioinformatics 2009 25 1189 1191 10.1093/bioinformatics/btp033 19151095
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 74
    • 3242886771 scopus 로고    scopus 로고
    • PDB 2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • 10.1093/nar/gkh381. 15215472
    • PDB 2PQR : an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. TJ Dolinsky JE Nielsen JA McCammon NA Baker, Nucleic Acids Res 2004 32 665 667 10.1093/nar/gkh381 15215472
    • (2004) Nucleic Acids Res , vol.32 , pp. 23665-667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 76
    • 0022452427 scopus 로고
    • Thermostable alanine racemase from Bacillus stearothermophilus: Molecular cloning of the gene, enzyme purification, and characterization
    • Thermostable alanine racemase from Bacillus stearothermophilus: molecular cloning of the gene, enzyme purification, and characterization. K Inagaki K Tanizawa B Badet CT Walsh H Tanaka K Soda, Biochemistry 1986 25 3268 3274 10.1021/bi00359a028 3015202 (Pubitemid 16056969)
    • (1986) Biochemistry , vol.25 , Issue.11 , pp. 3268-3274
    • Inagaki, K.1    Tanizawa, K.2    Badet, B.3
  • 77
    • 22544449871 scopus 로고    scopus 로고
    • A novel assay method for an amino acid racemase reaction based on circular dichroism
    • DOI 10.1042/BJ20041649
    • A novel assay method for an amino acid racemase reaction based on circular dichroism. M Noda Y Matoba T Kumagai M Sugiyama, Biochem J 2005 389 491 496 10.1042/BJ20041649 15796715 (Pubitemid 41021153)
    • (2005) Biochemical Journal , vol.389 , Issue.2 , pp. 491-496
    • Noda, M.1    Matoba, Y.2    Kumagai, T.3    Sugiyama, M.4
  • 78
    • 0021928231 scopus 로고
    • Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by (1-aminoethyl)phosphonic acid enantiomers
    • DOI 10.1021/bi00327a010
    • Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by (1-aminoethyl)phosphonic acid enantiomers. B Badet C Walsh, Biochemistry 1985 24 1333 1341 10.1021/bi00327a010 3921052 (Pubitemid 15091390)
    • (1985) Biochemistry , vol.24 , Issue.6 , pp. 1333-1341
    • Badet, B.1    Walsh, C.2


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