메뉴 건너뛰기




Volumn 341, Issue 4, 2004, Pages 1063-1076

Erratum: Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12 (Journal of Molecular Biology (2004) 341 (1063-1076) DOI: 10.1016/j.jmb.2004.06.039);Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12

Author keywords

AH, acetohydroxamate; chronic obstructive pulmonary disease; COPD, chronic obstructive pulmonary disease; crystal structure; ECM, extracellular matrix; HTS, high throughput screening; macrophage metalloelastase; MMP 12; non zinc chelator

Indexed keywords

2 (1,3 DIOXO 1,3 DIHYDRO 2H ISOINDOL 2 YL)ETHYL 4 [4I ETHOXY (1,1I BIPHENYL) 4 YL]OXOBUTANOIC ACID; 3 [[4 [(PYRIDIN 4 YL)PHENYL]THIEN 2 YL]CARBOXAMIDO](PHENYL)PROPANOIC ACID; CHELATING AGENT; CP 271485; MACROPHAGE ELASTASE; PF 00356231; PF 0359601; UNCLASSIFIED DRUG;

EID: 3843152629     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.09.006     Document Type: Erratum
Times cited : (77)

References (49)
  • 1
    • 0029939467 scopus 로고    scopus 로고
    • Multiple sclerosis: A coordinated immunological attack against myelin in the central nervous system
    • Steinman L. Multiple sclerosis: a coordinated immunological attack against myelin in the central nervous system. Cell. 85:1996;299-302
    • (1996) Cell , vol.85 , pp. 299-302
    • Steinman, L.1
  • 2
    • 0001651169 scopus 로고    scopus 로고
    • Design and therapeutic application of matrix metalloproteinase inhibitors
    • Whittaker M., Floyd C.D., Brown P., Gearing A.J. Design and therapeutic application of matrix metalloproteinase inhibitors. Chem. Rev. 99:1999;2735-2776
    • (1999) Chem. Rev. , vol.99 , pp. 2735-2776
    • Whittaker, M.1    Floyd, C.D.2    Brown, P.3    Gearing, A.J.4
  • 3
    • 0033931053 scopus 로고    scopus 로고
    • Structural studies of matrix metalloproteinases
    • Borkakoti N. Structural studies of matrix metalloproteinases. J. Mol. Med. 78:2000;261-268
    • (2000) J. Mol. Med. , vol.78 , pp. 261-268
    • Borkakoti, N.1
  • 6
    • 0029758751 scopus 로고    scopus 로고
    • Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides
    • Nagase H., Fields G.B. Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers. 40:1996;399-416
    • (1996) Biopolymers , vol.40 , pp. 399-416
    • Nagase, H.1    Fields, G.B.2
  • 7
    • 0031041647 scopus 로고    scopus 로고
    • Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution
    • Pendas A.M., Knauper V., Puente X.S., Llano E., Mattei M.G., Apte S., et al. Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution. J. Biol. Chem. 272:1997;4281-4286
    • (1997) J. Biol. Chem. , vol.272 , pp. 4281-4286
    • Pendas, A.M.1    Knauper, V.2    Puente, X.S.3    Llano, E.4    Mattei, M.G.5    Apte, S.6
  • 8
    • 0026701322 scopus 로고
    • Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase
    • Shapiro S.D., Griffin G.L., Gilbert D.J., Jenkins N.A., Copeland N.G., Welgus H.G., et al. Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase. J. Biol. Chem. 267:1992;4664-4671
    • (1992) J. Biol. Chem. , vol.267 , pp. 4664-4671
    • Shapiro, S.D.1    Griffin, G.L.2    Gilbert, D.J.3    Jenkins, N.A.4    Copeland, N.G.5    Welgus, H.G.6
  • 9
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro S.D., Kobayashi D.K., Ley T.J. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J. Biol. Chem. 268:1993;23824-23829
    • (1993) J. Biol. Chem. , vol.268 , pp. 23824-23829
    • Shapiro, S.D.1    Kobayashi, D.K.2    Ley, T.J.3
  • 10
    • 0029005284 scopus 로고
    • Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression
    • Belaaouaj A., Shipley J.M., Kobayashi D.K., Zimonjic D.B., Popescu N., Silverman G.A., Shapiro S.D. Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression. J. Biol. Chem. 270:1995;14568-14575
    • (1995) J. Biol. Chem. , vol.270 , pp. 14568-14575
    • Belaaouaj, A.1    Shipley, J.M.2    Kobayashi, D.K.3    Zimonjic, D.B.4    Popescu, N.5    Silverman, G.A.6    Shapiro, S.D.7
  • 11
    • 0034815950 scopus 로고    scopus 로고
    • Induction of human matrix metalloproteinase-12 gene transcriptional activity by GM-CSF requires the AP-1 binding site in human U937 monocytic cells
    • Wu L., Tanimoto A., Murata Y., Fan J., Sasaguri Y., Watanab T. Induction of human matrix metalloproteinase-12 gene transcriptional activity by GM-CSF requires the AP-1 binding site in human U937 monocytic cells. Biochem. Biophys. Res. Commun. 285:2001;300-307
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 300-307
    • Wu, L.1    Tanimoto, A.2    Murata, Y.3    Fan, J.4    Sasaguri, Y.5    Watanab, T.6
  • 12
    • 0037361991 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): A therapeutic role for inhibitors of MMPs
    • Belvisi M.G., Bottomley K.M. The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): a therapeutic role for inhibitors of MMPs. Inflamm. Res. 52:2003;95-100
    • (2003) Inflamm. Res. , vol.52 , pp. 95-100
    • Belvisi, M.G.1    Bottomley, K.M.2
  • 15
  • 16
    • 0028805811 scopus 로고
    • Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
    • Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., Fitzgerald P.M., et al. Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein Sci. 4:1995;1966-1976
    • (1995) Protein Sci. , vol.4 , pp. 1966-1976
    • Becker, J.W.1    Marcy, A.I.2    Rokosz, L.L.3    Axel, M.G.4    Burbaum, J.J.5    Fitzgerald, P.M.6
  • 17
    • 0030609810 scopus 로고    scopus 로고
    • 1.8-Å crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile
    • Betz M., Huxley P., Davies S.J., Mushtaq Y., Pieper M., Tschesche H., et al. 1.8-Å crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile. Eur. J. Biochem. 247:1997;356-363
    • (1997) Eur. J. Biochem. , vol.247 , pp. 356-363
    • Betz, M.1    Huxley, P.2    Davies, S.J.3    Mushtaq, Y.4    Pieper, M.5    Tschesche, H.6
  • 18
    • 0028324076 scopus 로고
    • The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity
    • Bode W., Reinemer P., Huber R., Kleine T., Schnierer S., Tschesche H. The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. 13:1994;1263-1269
    • (1994) EMBO J. , vol.13 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 19
    • 0029866390 scopus 로고    scopus 로고
    • Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding
    • Botos I., Scapozza L., Zhang D., Liotta L.A., Meyer E.F. Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding. Proc. Natl Acad. Sci. USA. 93:1996;2749-2754
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2749-2754
    • Botos, I.1    Scapozza, L.2    Zhang, D.3    Liotta, L.A.4    Meyer, E.F.5
  • 22
    • 0034638377 scopus 로고    scopus 로고
    • Structure-based design of a novel, potent, and selective inhibitors for MMP-13 utilising NMR spectroscopy and computer aided molecular design
    • Chen J.M., et al. Structure-based design of a novel, potent, and selective inhibitors for MMP-13 utilising NMR spectroscopy and computer aided molecular design. J. Am. Chem. Soc. 122:2000;9648-9654
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9648-9654
    • Chen, J.M.1
  • 23
    • 0035965125 scopus 로고    scopus 로고
    • Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 Å crystal structure
    • Lang R., Kocourek A., Braun M., Tschesche H., Huber R., Bode W., Maskos K. Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 Å crystal structure. J. Mol. Biol. 312:2001;731-742
    • (2001) J. Mol. Biol. , vol.312 , pp. 731-742
    • Lang, R.1    Kocourek, A.2    Braun, M.3    Tschesche, H.4    Huber, R.5    Bode, W.6    Maskos, K.7
  • 24
    • 0035965133 scopus 로고    scopus 로고
    • Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor
    • Nar H., Werle K., Bauer M.M.T., Dollinger H., Jung B. Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor. J. Mol. Biol. 312:2001;743-751
    • (2001) J. Mol. Biol. , vol.312 , pp. 743-751
    • Nar, H.1    Werle, K.2    Bauer, M.M.T.3    Dollinger, H.4    Jung, B.5
  • 25
    • 0037142342 scopus 로고    scopus 로고
    • Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach
    • Terp G.E., Cruciani G., Christensen I.T., Jorgensen F.S. Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach. J. Med. Chem. 45:2002;2675-2684
    • (2002) J. Med. Chem. , vol.45 , pp. 2675-2684
    • Terp, G.E.1    Cruciani, G.2    Christensen, I.T.3    Jorgensen, F.S.4
  • 26
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner M.F., Smith W.W., Castelhano A.L. Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry. 34:1995;6602-6610
    • (1995) Biochemistry. , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 27
    • 0037205902 scopus 로고    scopus 로고
    • Crystal engineering for topochemical polymerisation of muconic esters using halogen-halogen and CH/pi interactions as weak intermolecular interactions
    • Akikazu M., et al. Crystal engineering for topochemical polymerisation of muconic esters using halogen-halogen and CH/pi interactions as weak intermolecular interactions. J. Am. Chem. Soc. 124:2002;8891-8902
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8891-8902
    • Akikazu, M.1
  • 29
    • 0031882946 scopus 로고    scopus 로고
    • Results of single and repeat dose studies of the oral matrix metalloproteinase inhibitor marimastat in healthy male volunteers
    • Millar A.W., Brown P.D., Moore J., Galloway W.A., Cornish A.G., Lenehan T.J., Lynch K.P. Results of single and repeat dose studies of the oral matrix metalloproteinase inhibitor marimastat in healthy male volunteers. Br. J. Clin. Pharmacol. 45:1998;21-26
    • (1998) Br. J. Clin. Pharmacol. , vol.45 , pp. 21-26
    • Millar, A.W.1    Brown, P.D.2    Moore, J.3    Galloway, W.A.4    Cornish, A.G.5    Lenehan, T.J.6    Lynch, K.P.7
  • 30
    • 0035907237 scopus 로고    scopus 로고
    • The 1.8-Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition
    • Brandstetter H., Grams F., Glitz D., Lang A., Huber R., Bode W., et al. The 1.8-Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition. J. Biol. Chem. 276:2001;17405-17412
    • (2001) J. Biol. Chem. , vol.276 , pp. 17405-17412
    • Brandstetter, H.1    Grams, F.2    Glitz, D.3    Lang, A.4    Huber, R.5    Bode, W.6
  • 31
    • 0033048045 scopus 로고    scopus 로고
    • Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors
    • Lovejoy B., Welch A.R., Carr S., Luong C., Broka C., Hendricks R.T., et al. Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors. Nature Struct. Biol. 6:1999;217-221
    • (1999) Nature Struct. Biol. , vol.6 , pp. 217-221
    • Lovejoy, B.1    Welch, A.R.2    Carr, S.3    Luong, C.4    Broka, C.5    Hendricks, R.T.6
  • 32
    • 0031798691 scopus 로고    scopus 로고
    • Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data
    • Brandstetter H., Engh R.A., Von Roedern E.G., Moroder L., Huber R., Bode W., Grams F. Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data. Protein Sci. 7:1998;1303-1309
    • (1998) Protein Sci. , vol.7 , pp. 1303-1309
    • Brandstetter, H.1    Engh, R.A.2    Von Roedern, E.G.3    Moroder, L.4    Huber, R.5    Bode, W.6    Grams, F.7
  • 33
    • 0033519654 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field analysis and X-ray structure analysis
    • Matter H., Schwab W., Barbier D., Billen G., Haase B., Neises B., et al. Quantitative structure-activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field analysis and X-ray structure analysis. J. Med. Chem. 42:1999;1908-1920
    • (1999) J. Med. Chem. , vol.42 , pp. 1908-1920
    • Matter, H.1    Schwab, W.2    Barbier, D.3    Billen, G.4    Haase, B.5    Neises, B.6
  • 34
    • 0028838862 scopus 로고
    • Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor
    • Grams F., Crimmin M., Hinnes L., Huxley P., Pieper M., Tschesche H., Bode W. Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry. 34:1995;14012-14020
    • (1995) Biochemistry , vol.34 , pp. 14012-14020
    • Grams, F.1    Crimmin, M.2    Hinnes, L.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6    Bode, W.7
  • 35
    • 0032776835 scopus 로고    scopus 로고
    • X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: Implications for inhibitor selectivity
    • Pavlovsky A.G., Williams M.G., Ye Q.Z., Ortwine D.F., Purchase C.F. 2nd, White A.D., et al. X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity. Protein Sci. 8:1999;1455-1462
    • (1999) Protein Sci. , vol.8 , pp. 1455-1462
    • Pavlovsky, A.G.1    Williams, M.G.2    Ye, Q.Z.3    Ortwine, D.F.4    Purchase II, C.F.5    White, A.D.6
  • 36
    • 0032712582 scopus 로고    scopus 로고
    • Crystal structure of the stromelysin catalytic domain at 2.0 Å resolution: Inhibitor-induced conformational changes
    • Chen L., Rydel T.J., Gu F., Dunaway C.M., Pikul S., Dunham K.M., Barnett B.L. Crystal structure of the stromelysin catalytic domain at 2.0 Å resolution: inhibitor-induced conformational changes. J. Mol. Biol. 293:1999;545-557
    • (1999) J. Mol. Biol. , vol.293 , pp. 545-557
    • Chen, L.1    Rydel, T.J.2    Gu, F.3    Dunaway, C.M.4    Pikul, S.5    Dunham, K.M.6    Barnett, B.L.7
  • 41
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matric metalloproteinases
    • Knight C., Willenbrock F., Murphy G. A novel coumarin-labelled peptide for sensitive continuous assays of the matric metalloproteinases. FEBS Letters. 296:1992;263-266
    • (1992) FEBS Letters , vol.296 , pp. 263-266
    • Knight, C.1    Willenbrock, F.2    Murphy, G.3
  • 42
    • 0033769114 scopus 로고    scopus 로고
    • Large-scale expression, refolding, and purification of the catalytic domain of human macrophage metalloelastase (MMP-12) in Escherichia coli
    • Parkar A.A., Stow M.D., Smith K., Panicker A.K., Guilloteau J.P., Jupp R., Crowe S.J. Large-scale expression, refolding, and purification of the catalytic domain of human macrophage metalloelastase (MMP-12) in Escherichia coli. Protein Expt. Purif. 20:2000;152-161
    • (2000) Protein Expt. Purif. , vol.20 , pp. 152-161
    • Parkar, A.A.1    Stow, M.D.2    Smith, K.3    Panicker, A.K.4    Guilloteau, J.P.5    Jupp, R.6    Crowe, S.J.7
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Carter, C. W. Jr & Sweet, R. M., eds)
    • Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology Macromolecular Crystallography, part A (Carter, C. W. Jr & Sweet, R. M., eds), vol. 276, pp. 307-326.
    • (1997) Methods in Enzymology Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • Navaza. AmoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, .1
  • 45
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 46
    • 2142728675 scopus 로고    scopus 로고
    • San Diego, USA.
    • Accelrys Inc. (2000). QUANTA release 2000, San Diego, USA.
    • (2000) QUANTA Release 2000
  • 47
    • 0030845843 scopus 로고    scopus 로고
    • Model-building and refinement practice
    • Kleywegt G.J., Jones T.A. Model-building and refinement practice. Methods Enzymol. 277:1997;208-230
    • (1997) Methods Enzymol. , vol.277 , pp. 208-230
    • Kleywegt, G.J.1    Jones, T.A.2
  • 49
    • 3843098581 scopus 로고    scopus 로고
    • Sybyl® 6.92 Tripos Inc., 1699 South Hanley Rd., St. Louis, Missouri 63144, USA.
    • Sybyl® 6.92 Tripos Inc., 1699 South Hanley Rd., St. Louis, Missouri 63144, USA.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.