메뉴 건너뛰기




Volumn 18, Issue 10, 2010, Pages 1109-1114

Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE; THERMOLYSIN; ZINC BINDING PROTEIN;

EID: 80455122899     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2127     Document Type: Article
Times cited : (97)

References (60)
  • 2
    • 37949056062 scopus 로고
    • Densitometric analysis of body composition: Revision of some quantitative assumptions
    • Brozek, J., Grande, F., Anderson, J.T. & Keys, A. Densitometric analysis of body composition: revision of some quantitative assumptions. Ann. NY Acad. Sci. 110, 113-140 (1963)
    • (1963) Ann. NY Acad. Sci , vol.110 , pp. 113-140
    • Brozek, J.1    Grande, F.2    Anderson, J.T.3    Keys, A.4
  • 3
    • 51049121850 scopus 로고    scopus 로고
    • Candidate cell and matrix interaction domains on the collagen fbril, the predominant protein of vertebrates.
    • Sweeney, S.M. et al. Candidate cell and matrix interaction domains on the collagen fbril, the predominant protein of vertebrates. J. Biol. Chem. 283, 21187-21197 (2008)
    • (2008) J. Biol. Chem , vol.283 , pp. 21187-21197
    • Sweeney, S.M.1
  • 4
    • 0021766908 scopus 로고
    • Purifcation and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography
    • Bond, M.D. & Van Wart, H.E. Purifcation and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography. Biochemistry 23, 3077-3085 (1984)
    • (1984) Biochemistry , vol.23 , pp. 3077-3085
    • Bond, M.D.1    Van Wart, H.E.2
  • 7
    • 0029644935 scopus 로고
    • Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller
    • Li, J. et al. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller. Structure 3, 541-549 (1995)
    • (1995) Structure , vol.3 , pp. 541-549
    • Li, J.1
  • 9
    • 33747610734 scopus 로고    scopus 로고
    • Crystal Structure of an Active Form of Human MMP-1
    • DOI 10.1016/j.jmb.2006.06.079, PII S0022283606008369
    • Iyer, S., Visse, R., Nagase, H. & Acharya, K.R. Crystal structure of an active form of human MMP-1. J. Mol. Biol. 362, 78-88 (2006) (Pubitemid 44262357)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.1 , pp. 78-88
    • Iyer, S.1    Visse, R.2    Nagase, H.3    Acharya, K.R.4
  • 10
    • 79951545991 scopus 로고    scopus 로고
    • Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1
    • Adhikari, A.S., Chai, J. & Dunn, A.R. Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1. J. Am. Chem. Soc. 133, 1686-1689 (2011)
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 1686-1689
    • Adhikari, A.S.1    Chai, J.2    Dunn, A.R.3
  • 11
    • 77954570937 scopus 로고    scopus 로고
    • Molecular mechanism of type i collagen homotrimer resistance to mammalian collagenases.
    • Han, S. et al. Molecular mechanism of type I collagen homotrimer resistance to mammalian collagenases. J. Biol. Chem. 285, 22276-22281 (2010)
    • (2010) J. Biol. Chem , vol.285 , pp. 22276-22281
    • Han, S.1
  • 12
    • 4444290999 scopus 로고    scopus 로고
    • Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability
    • DOI 10.1021/bi048938i
    • Minond, D., Lauer-Fields, J.L., Nagase, H. & Fields, G.B. Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability. Biochemistry 43, 11474-11481 (2004) (Pubitemid 39186968)
    • (2004) Biochemistry , vol.43 , Issue.36 , pp. 11474-11481
    • Minond, D.1    Lauer-Fields, J.L.2    Nagase, H.3    Fields, G.B.4
  • 14
    • 5744251586 scopus 로고    scopus 로고
    • Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): The differential roles of the MMP hemopexin C domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities
    • DOI 10.1074/jbc.M407186200
    • Tam, E.M., Moore, T.R., Butler, G.S. & Overall, C.M. Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin C domains and the MMP-2 fbronectin type II modules in collagen triple helicase activities. J. Biol. Chem. 279, 43336-43344 (2004) (Pubitemid 39377771)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 43336-43344
    • Tam, E.M.1    Moore, T.B.2    Butler, G.S.3    Overall, C.M.4
  • 15
    • 0031868477 scopus 로고    scopus 로고
    • The potential of collagenase as a new therapy for separation of human retained placenta: Hydrolytic potency on human, equine and bovine placentae
    • DOI 10.1016/S0143-4004(98)90077-7
    • Fecteau, K.A., Haffner, J.C. & Eiler, H. The potential of collagenase as a new therapy for separation of human retained placenta: hydrolytic potency on human, equine and bovine placentae. Placenta 19, 379-383 (1998) (Pubitemid 28327696)
    • (1998) Placenta , vol.19 , Issue.5-6 , pp. 379-383
    • Fecteau, K.A.1    Haffner, J.C.2    Eiler, H.3
  • 16
    • 74549222674 scopus 로고    scopus 로고
    • Collagenase Santyl ointment: A selective agent for wound debridement
    • Shi, L. & Carson, D. Collagenase Santyl ointment: a selective agent for wound debridement. J. Wound Ostomy Continence Nurs. 36, S12-S16 (2009)
    • (2009) J. Wound Ostomy Continence Nurs , vol.36
    • Shi, L.1    Carson, D.2
  • 17
    • 0029557952 scopus 로고
    • Recombinant enzymes for islet isolation: Purification of a collagenase from Clostridium histolyticum and cloning/expression of the gene
    • Hesse, F., Burtscher, H., Popp, F. & Ambrosius, D. Recombinant enzymes for islet isolation: purifcation of a collagenase from Clostridium histolyticum and cloning/expression of the gene. Transplant. Proc. 27, 3287-3289 (1995) (Pubitemid 26016183)
    • (1995) Transplantation Proceedings , vol.27 , Issue.6 , pp. 3287-3289
    • Hesse, F.1    Burtscher, H.2    Popp, F.3    Ambrosius, D.4
  • 18
    • 67650720738 scopus 로고    scopus 로고
    • A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli
    • Ducka, P. et al. A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli. Appl. Microbiol. Biotechnol. 83, 1055-1065 (2009)
    • (2009) Appl. Microbiol. Biotechnol , vol.83 , pp. 1055-1065
    • Ducka, P.1
  • 19
    • 0344942600 scopus 로고    scopus 로고
    • A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation
    • DOI 10.1093/emboj/cdg172
    • Wilson, J.J., Matsushita, O., Okabe, A. & Sakon, J. A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation. EMBO J. 22, 1743-1752 (2003) (Pubitemid 36460131)
    • (2003) EMBO Journal , vol.22 , Issue.8 , pp. 1743-1752
    • Wilson, J.J.1    Matsushita, O.2    Okabe, A.3    Sakon, J.4
  • 20
    • 0033150672 scopus 로고    scopus 로고
    • Topological characteristics of helical repeat proteins
    • DOI 10.1016/S0959-440X(99)80052-9
    • Groves, M.R. & Barford, D. Topological characteristics of helical repeat proteins. Curr. Opin. Struct. Biol. 9, 383-389 (1999) (Pubitemid 29454508)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.3 , pp. 383-389
    • Groves, M.R.1    Barford, D.2
  • 21
    • 19544377390 scopus 로고    scopus 로고
    • Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations
    • DOI 10.1016/j.jmb.2005.03.070, PII S002228360500361X
    • Kyrieleis, O.J., Goettig, P., Kiefersauer, R., Huber, R. & Brandstetter, H. Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations. J. Mol. Biol. 349, 787-800 (2005) (Pubitemid 40731533)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.4 , pp. 787-800
    • Kyrieleis, O.J.P.1    Goettig, P.2    Kiefersauer, R.3    Huber, R.4    Brandstetter, H.5
  • 22
    • 0035146853 scopus 로고    scopus 로고
    • 4 hydrolase, a bifunctional enzyme in inflammation
    • DOI 10.1038/84117
    • Thunnissen, M.M., Nordlund, P. & Haeggstrom, J.Z. Crystal structure of human leukotriene A4 hydrolase, a bifunctional enzyme in infammation. Nat. Struct. Biol. 8, 131-135 (2001) (Pubitemid 32117699)
    • (2001) Nature Structural Biology , vol.8 , Issue.2 , pp. 131-135
    • Thunnissen, M.M.G.M.1    Nordlund, P.2    Haeggstrom, J.Z.3
  • 24
    • 0032947997 scopus 로고    scopus 로고
    • Identifcation of metal ligands in the Clostridium histolyticum ColH collagenase
    • Jung, C.M. et al. Identifcation of metal ligands in the Clostridium histolyticum ColH collagenase. J. Bacteriol. 181, 2816-2822 (1999)
    • (1999) J. Bacteriol , vol.181 , pp. 2816-2822
    • Jung, C.M.1
  • 25
    • 77951989369 scopus 로고    scopus 로고
    • Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: Binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix.
    • Wang, Y.K. et al. Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix. J. Biol. Chem. 285, 14285-14291 (2010)
    • (2010) J. Biol. Chem , vol.285 , pp. 14285-14291
    • Wang, Y.K.1
  • 26
    • 0027409432 scopus 로고
    • Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins
    • Sanchez-Lopez, R., Alexander, C.M., Behrendtsen, O., Breathnach, R. & Werb, Z. Role of zinc-binding-and hemopexin domain-encoded sequences in the substrate specifcity of collagenase and stromelysin-2 as revealed by chimeric proteins. J. Biol. Chem. 268, 7238-7247 (1993). (Pubitemid 23105614)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.10 , pp. 7238-7247
    • Sanchez-Lopez, R.1    Alexander, C.M.2    Behrendtsen, O.3    Breathnach, R.4    Werb, Z.5
  • 27
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • DOI 10.1021/bi00476a001
    • Vallee, B.L. & Auld, D.S. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29, 5647-5659 (1990). (Pubitemid 20192431)
    • (1990) Biochemistry , vol.29 , Issue.24 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 28
    • 58249106774 scopus 로고    scopus 로고
    • Biochemical characterization of the catalytic domains of three different Clostridial collagenases
    • Eckhard, U. et al. Biochemical characterization of the catalytic domains of three different Clostridial collagenases. Biol. Chem. 390, 11-18 (2009).
    • (2009) Biol. Chem. , vol.390 , pp. 11-18
    • Eckhard, U.1
  • 29
    • 0022412297 scopus 로고
    • Mode of hydrolysis of collagen-like peptides by class I and class II Clostridium histolyticum collagenases: Evidence for both endopeptidase and tripeptidylcarboxypeptidase activities
    • DOI 10.1021/bi00344a033
    • Mookhtiar, K.A., Steinbrink, D.R. & Van Wart, H.E. Mode of hydrolysis of collagenlike peptides by class I and class II Clostridium histolyticum collagenases: evidence for both endopeptidase and tripeptidylcarboxypeptidase activities. Biochemistry 24, 6527-6533 (1985). (Pubitemid 16207126)
    • (1985) Biochemistry , vol.24 , Issue.23 , pp. 6527-6533
    • Mookhtiar, K.A.1    Steinbrink, D.R.2    Van Wart, H.E.3
  • 30
    • 0037041031 scopus 로고    scopus 로고
    • Rapid determination of substrate specificity of Clostridium histolyticum β-collagenase using an immobilized peptide library
    • DOI 10.1074/jbc.M111042200
    • Hu, Y. et al. Rapid determination of substrate specifcity of Clostridium histolyticum beta-collagenase using an immobilized peptide library. J. Biol. Chem. 277, 8366-8371 (2002). (Pubitemid 34968296)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 8366-8371
    • Hu, Y.1    Webb, E.2    Singh, J.3    Morgan, B.A.4    Gainor, J.A.5    Gordon, T.D.6    Siahaan, T.J.7
  • 31
    • 0026538063 scopus 로고
    • Identifcation of Clostridium histolyticum collagenase hyperreactive sites in type i II and III collagens: Lack of correlation with local triple helical stability
    • French, M.F., Bhown, A. & Van Wart, H.E. Identifcation of Clostridium histolyticum collagenase hyperreactive sites in type I, II, and III collagens: lack of correlation with local triple helical stability. J. Protein Chem. 11, 83-97 (1992).
    • (1992) J. Protein Chem. , vol.11 , pp. 83-97
    • French, M.F.1    Bhown, A.2    Van Wart, H.E.3
  • 32
    • 0023134098 scopus 로고
    • Limited proteolysis of type I collagen at hyperreactive sites by class I and II Clostridium histolyticum collagenases: Complementary digestion patterns
    • DOI 10.1021/bi00377a004
    • French, M.F., Mookhtiar, K.A. & Van Wart, H.E. Limited proteolysis of type I collagen at hyperreactive sites by class I and II Clostridium histolyticum collagenases: complementary digestion patterns. Biochemistry 26, 681-687 (1987). (Pubitemid 17021041)
    • (1987) Biochemistry , vol.26 , Issue.3 , pp. 681-687
    • French, M.F.1    Mookhtiar, K.A.2    Van Wart, H.E.3
  • 33
    • 0036447070 scopus 로고    scopus 로고
    • Building collagen molecules, fibrils, and suprafibrillar structures
    • DOI 10.1006/jsbi.2002.4450
    • Hulmes, D.J. Building collagen molecules, fbrils, and suprafbrillar structures. J. Struct. Biol. 137, 2-10 (2002). (Pubitemid 35430415)
    • (2002) Journal of Structural Biology , vol.137 , Issue.1-2 , pp. 2-10
    • Hulmes, D.J.S.1
  • 34
    • 17444374661 scopus 로고    scopus 로고
    • Collagen fbril form and function
    • Wess, T.J. Collagen fbril form and function. Adv. Protein Chem. 70, 341-374 (2005).
    • (2005) Adv. Protein Chem. , vol.70 , pp. 341-374
    • Wess, T.J.1
  • 35
    • 0034424953 scopus 로고    scopus 로고
    • Crystal structure of a collagenlike polypeptide with repeating sequence Pro-Hyp-Gly at 1.4 Å resolution: Implications for collagen hydration
    • Berisio, R., Vitagliano, L., Mazzarella, L. & Zagari, A. Crystal structure of a collagenlike polypeptide with repeating sequence Pro-Hyp-Gly at 1.4 Å resolution: implications for collagen hydration. Biopolymers 56, 8-13 (2001).
    • (2001) Biopolymers , vol.56 , pp. 8-13
    • Berisio, R.1    Vitagliano, L.2    Mazzarella, L.3    Zagari, A.4
  • 36
  • 37
    • 0031228939 scopus 로고    scopus 로고
    • Characterisation of equine matrix metalloproteinase 2 and 9; and identification of the cellular sources of these enzymes in joints
    • Clegg, P.D., Burke, R.M., Coughlan, A.R., Riggs, C.M. & Carter, S.D. Characterisation of equine matrix metalloproteinase 2 and 9; and identifcation of the cellular sources of these enzymes in joints. Equine Vet. J. 29, 335-342 (1997). (Pubitemid 127520918)
    • (1997) Equine Veterinary Journal , vol.29 , Issue.5 , pp. 335-342
    • Clegg, P.D.1    Burke, R.M.2    Coughlan, A.R.3    Riggs, C.M.4    Carter, S.D.5
  • 38
    • 33845396458 scopus 로고    scopus 로고
    • Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP
    • DOI 10.1091/mbc.E06-08-0740
    • Itoh, Y. et al. Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP. Mol. Biol. Cell 17, 5390-5399 (2006). (Pubitemid 44907378)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.12 , pp. 5390-5399
    • Itoh, Y.1    Ito, N.2    Nagase, H.3    Evans, R.D.4    Bird, S.A.5    Seiki, M.6
  • 39
    • 45149126165 scopus 로고    scopus 로고
    • The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface.
    • Itoh, Y., Ito, N., Nagase, H. & Seiki, M. The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface. J. Biol. Chem. 283, 13053-13062 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 13053-13062
    • Itoh, Y.1    Ito, N.2    Nagase, H.3    Seiki, M.4
  • 42
    • 6044274345 scopus 로고    scopus 로고
    • Interstitial collagenase is a brownian ratchet driven by proteolysis of collagen
    • DOI 10.1126/science.1099179
    • Saffarian, S., Collier, I.E., Marmer, B.L., Elson, E.L. & Goldberg, G. Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen. Science 306, 108-111 (2004). (Pubitemid 39451949)
    • (2004) Science , vol.306 , Issue.5693 , pp. 108-111
    • Saffarian, S.1    Collier, I.E.2    Marmer, B.L.3    Elson, E.L.4    Goldberg, G.5
  • 44
    • 79953224829 scopus 로고    scopus 로고
    • The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: Crystal structure and biological functions.
    • Tochowicz, A. et al. The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions. J. Biol. Chem. 286, 7587-7600 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 7587-7600
    • Tochowicz, A.1
  • 45
    • 35148883112 scopus 로고    scopus 로고
    • Protease Yoga: Extreme Flexibility of a Matrix Metalloproteinase
    • DOI 10.1016/j.str.2007.10.001, PII S0969212607003371
    • Overall, C.M. & Butler, G.S. Protease yoga: extreme fexibility of a matrix metalloproteinase. Structure 15, 1159-1161 (2007). (Pubitemid 47539171)
    • (2007) Structure , vol.15 , Issue.10 , pp. 1159-1161
    • Overall, C.M.1    Butler, G.S.2
  • 46
    • 77955532367 scopus 로고    scopus 로고
    • A new method to value effciency of enzyme blends for pancreatic tissue digestion
    • Salamone, M. et al. A new method to value effciency of enzyme blends for pancreatic tissue digestion. Transplant. Proc. 42, 2043-2048 (2010).
    • (2010) Transplant. Proc. , vol.42 , pp. 2043-2048
    • Salamone, M.1
  • 49
    • 33847633917 scopus 로고    scopus 로고
    • A standardized approach for accurate quantification of murein hydrolase activity in high-throughput assays
    • DOI 10.1016/j.jbbm.2006.10.009, PII S0165022X06002053
    • Briers, Y., Lavigne, R., Volckaert, G. & Hertveldt, K. A standardized approach for accurate quantifcation of murein hydrolase activity in high-throughput assays. J. Biochem. Biophys. Methods 70, 531-533 (2007). (Pubitemid 46356578)
    • (2007) Journal of Biochemical and Biophysical Methods , vol.70 , Issue.3 , pp. 531-533
    • Briers, Y.1    Lavigne, R.2    Volckaert, G.3    Hertveldt, K.4
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4.
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 51
    • 23844492576 scopus 로고    scopus 로고
    • Auto-Rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment
    • DOI 10.1107/S0907444905001307
    • Panjikar, S., Parthasarathy, V., Lamzin, V.S., Weiss, M.S. & Tucker, P.A. Auto-Rickshaw: an automated crystal structure determination platform as an effcient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr. D Biol. Crystallogr. 61, 449-457 (2005). (Pubitemid 43934605)
    • (2005) Acta Crystallographica Section D: Biological Crystallography , vol.61 , Issue.4 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 52
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G.M. A short history of SHELX. Acta Crystallogr. A 64, 112-122 (2008).
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 53
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • DOI 10.1016/S0079-6107(99)00008-5, PII S0079610799000085
    • Cowtan, K.D. & Zhang, K.Y. Density modifcation for macromolecular phase improvement. Prog. Biophys. Mol. Biol. 72, 245-270 (1999). (Pubitemid 29485171)
    • (1999) Progress in Biophysics and Molecular Biology , vol.72 , Issue.3 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.J.2
  • 55
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J. & Merritt, E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 57
    • 13544251502 scopus 로고    scopus 로고
    • The case for open-source software in drug discovery
    • DeLano, W.L. The case for open-source software in drug discovery. Drug Discov. Today 10, 213-217 (2005).
    • (2005) Drug Discov. Today , vol.10 , pp. 213-217
    • Delano, W.L.1
  • 58
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • DOI 10.1006/jmbi.1993.1351
    • Laskowski, R.A., Moss, D.S. & Thornton, J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231, 1049-1067 (1993). (Pubitemid 23209879)
    • (1993) Journal of Molecular Biology , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 60
    • 34547593171 scopus 로고    scopus 로고
    • NQ-Flipper: Recognition and correction of erroneous asparagine and glutamine side-chain rotamers in protein structures
    • Weichenberger, C.X. & Sippl, M.J. NQ-Flipper: recognition and correction of erroneous asparagine and glutamine side-chain rotamers in protein structures. Nucleic Acids Res. 35, W403-W406 (2007).
    • (2007) Nucleic Acids Res. , vol.35
    • Weichenberger, C.X.1    Sippl, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.