메뉴 건너뛰기




Volumn 426, Issue 7, 2014, Pages 1439-1451

Galectin-3 Interactions with Glycosphingolipids

Author keywords

carbohydrate recognition; galectin; ganglioside; glycosphingolipid; X ray structures

Indexed keywords

BETA GALACTOSIDE; CARBOHYDRATE; EPITOPE; GALACTOSE; GALECTIN 3; GANGLIOSIDE GM3; GLYCAN; GLYCOSPHINGOLIPID; N ACETYLLACTOSAMINE SYNTHASE; OLIGOSACCHARIDE; GANGLIOSIDE;

EID: 84895928786     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.12.004     Document Type: Article
Times cited : (66)

References (65)
  • 1
    • 70349853957 scopus 로고    scopus 로고
    • Galectins
    • A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, 2nd ed. Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • R.D. Cummings, and F.T. Liu Galectins A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, Essentials of Glycobiology 2nd ed. 2009 Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • (2009) Essentials of Glycobiology
    • Cummings, R.D.1    Liu, F.T.2
  • 3
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins
    • S.H. Barondes, D.N. Cooper, M.A. Gitt, and H. Leffler Galectins. Structure and function of a large family of animal lectins J Biol Chem 269 1994 20807 20810
    • (1994) J Biol Chem , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Leffler, H.4
  • 4
    • 0027422375 scopus 로고
    • Primary structure of the soluble lactose binding lectin L-29 from rat and dog and interaction of its non-collagenous proline-, glycine-, tyrosine-rich sequence with bacterial and tissue collagenase
    • J. Herrmann, C.W. Turck, R.E. Atchison, M.E. Huflejt, L. Poulter, and M.A. Gitt et al. Primary structure of the soluble lactose binding lectin L-29 from rat and dog and interaction of its non-collagenous proline-, glycine-, tyrosine-rich sequence with bacterial and tissue collagenase J Biol Chem 268 1993 26704 26711
    • (1993) J Biol Chem , vol.268 , pp. 26704-26711
    • Herrmann, J.1    Turck, C.W.2    Atchison, R.E.3    Huflejt, M.E.4    Poulter, L.5    Gitt, M.A.6
  • 5
    • 67649781736 scopus 로고    scopus 로고
    • T-cell growth, cell surface organization, and the galectin-glycoprotein lattice
    • A. Grigorian, S. Torossian, and M. Demetriou T-cell growth, cell surface organization, and the galectin-glycoprotein lattice Immunol Rev 230 2009 232 246
    • (2009) Immunol Rev , vol.230 , pp. 232-246
    • Grigorian, A.1    Torossian, S.2    Demetriou, M.3
  • 6
    • 1542373596 scopus 로고    scopus 로고
    • Regulation of cellular homeostasis by galectins
    • D.K. Hsu, and F.T. Liu Regulation of cellular homeostasis by galectins Glycoconjugate J 19 2004 507 515
    • (2004) Glycoconjugate J , vol.19 , pp. 507-515
    • Hsu, D.K.1    Liu, F.T.2
  • 8
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • G.R. Vasta Roles of galectins in infection Nat Rev Microbiol 7 2009 424 438
    • (2009) Nat Rev Microbiol , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 9
    • 0037300960 scopus 로고    scopus 로고
    • Galectins in cell growth and apoptosis
    • R.Y. Yang, and F.T. Liu Galectins in cell growth and apoptosis Cell Mol Life Sci 60 2003 267 276
    • (2003) Cell Mol Life Sci , vol.60 , pp. 267-276
    • Yang, R.Y.1    Liu, F.T.2
  • 10
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • F.T. Liu, and G.A. Rabinovich Galectins as modulators of tumour progression Nat Rev Cancer 5 2005 29 41
    • (2005) Nat Rev Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 11
    • 0033777862 scopus 로고    scopus 로고
    • Galectins: A new family of regulators of inflammation
    • F.T. Liu Galectins: a new family of regulators of inflammation Clin Immunol 97 2000 79 88
    • (2000) Clin Immunol , vol.97 , pp. 79-88
    • Liu, F.T.1
  • 13
    • 77955274627 scopus 로고    scopus 로고
    • Glycosphingolipids
    • A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, 2nd ed. Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • R.L. Schnaar, A. Suzuki, and P. Stanley Glycosphingolipids A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, Essentials of Glycobiology 2nd ed. 2009 Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • (2009) Essentials of Glycobiology
    • Schnaar, R.L.1    Suzuki, A.2    Stanley, P.3
  • 14
    • 0031080051 scopus 로고    scopus 로고
    • Glycosphingolipid antigens and cancer therapy
    • S. Hakomori, and Y. Zhang Glycosphingolipid antigens and cancer therapy Chem Biol 4 1997 97 104
    • (1997) Chem Biol , vol.4 , pp. 97-104
    • Hakomori, S.1    Zhang, Y.2
  • 16
    • 84866551704 scopus 로고    scopus 로고
    • Galectin-3 protein regulates mobility of N-cadherin and GM1 ganglioside at cell-cell junctions of mammary carcinoma cells
    • C. Boscher, Y.Z. Zheng, R. Lakshminarayan, L. Johannes, J.W. Dennis, and L.J. Foster et al. Galectin-3 protein regulates mobility of N-cadherin and GM1 ganglioside at cell-cell junctions of mammary carcinoma cells J Biol Chem 287 2012 32940 32952
    • (2012) J Biol Chem , vol.287 , pp. 32940-32952
    • Boscher, C.1    Zheng, Y.Z.2    Lakshminarayan, R.3    Johannes, L.4    Dennis, J.W.5    Foster, L.J.6
  • 17
    • 0035929631 scopus 로고    scopus 로고
    • Negative regulation of neuroblastoma cell growth by carbohydrate- dependent surface binding of galectin-1 and functional divergence from galectin-3
    • J. Kopitz, C. von Reitzenstein, S. Andre, H. Kaltner, J. Uhl, and V. Ehemann et al. Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3 J Biol Chem 276 2001 35917 35923
    • (2001) J Biol Chem , vol.276 , pp. 35917-35923
    • Kopitz, J.1    Von Reitzenstein, C.2    Andre, S.3    Kaltner, H.4    Uhl, J.5    Ehemann, V.6
  • 18
    • 0032502722 scopus 로고    scopus 로고
    • GM3-enriched microdomain involved in cell adhesion and signal transduction through carbohydrate-carbohydrate interaction in mouse melanoma B16 cells
    • K. Iwabuchi, S. Yamamura, A. Prinetti, K. Handa, and S. Hakomori GM3-enriched microdomain involved in cell adhesion and signal transduction through carbohydrate-carbohydrate interaction in mouse melanoma B16 cells J Biol Chem 273 1998 9130 9138
    • (1998) J Biol Chem , vol.273 , pp. 9130-9138
    • Iwabuchi, K.1    Yamamura, S.2    Prinetti, A.3    Handa, K.4    Hakomori, S.5
  • 19
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • H. Ideo, A. Seko, I. Ishizuka, and K. Yamashita The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity Glycobiology 13 2003 713 723
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 20
    • 77955345888 scopus 로고    scopus 로고
    • Lack of lacto/neolacto-glycolipids enhances the formation of glycolipid-enriched microdomains, facilitating B cell activation
    • A. Togayachi, Y. Kozono, Y. Ikehara, H. Ito, N. Suzuki, and Y. Tsunoda et al. Lack of lacto/neolacto-glycolipids enhances the formation of glycolipid-enriched microdomains, facilitating B cell activation Proc Natl Acad Sci U S A 107 2010 11900 11905
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11900-11905
    • Togayachi, A.1    Kozono, Y.2    Ikehara, Y.3    Ito, H.4    Suzuki, N.5    Tsunoda, Y.6
  • 21
    • 0026561874 scopus 로고
    • Glycolipid of human pancreatic cancer; The appearance of neolacto-series (type 2 chain) glycolipid and the presence of incompatible blood group antigen in tumor tissues
    • H. Hattori, K. Uemura, H. Ishihara, and H. Ogata Glycolipid of human pancreatic cancer; the appearance of neolacto-series (type 2 chain) glycolipid and the presence of incompatible blood group antigen in tumor tissues Biochim Biophys Acta 1125 1992 21 27
    • (1992) Biochim Biophys Acta , vol.1125 , pp. 21-27
    • Hattori, H.1    Uemura, K.2    Ishihara, H.3    Ogata, H.4
  • 22
    • 68749105767 scopus 로고    scopus 로고
    • Understanding galectin structure-function relationships to design effective antagonists
    • A. Anatole, Z.J. Witczak, D.P. Klyosov, John Wiley & Sons Hoboken
    • I.V. Nesmelova, R.P.M. Dings, and K.H. Mayo Understanding galectin structure-function relationships to design effective antagonists A. Anatole, Z.J. Witczak, D.P. Klyosov, Galectins 2008 John Wiley & Sons Hoboken 33 69
    • (2008) Galectins , pp. 33-69
    • Nesmelova, I.V.1    Dings, R.P.M.2    Mayo, K.H.3
  • 24
    • 0027260299 scopus 로고
    • Carbohydrate-binding protein 35. II. Analysis of the interaction of the recombinant polypeptide with saccharides
    • R.N. Knibbs, N. Agrwal, J.L. Wang, and I.J. Goldstein Carbohydrate-binding protein 35. II. Analysis of the interaction of the recombinant polypeptide with saccharides J Biol Chem 268 1993 14940 14947
    • (1993) J Biol Chem , vol.268 , pp. 14940-14947
    • Knibbs, R.N.1    Agrwal, N.2    Wang, J.L.3    Goldstein, I.J.4
  • 25
    • 58149352519 scopus 로고    scopus 로고
    • Structural analysis of the recognition mechanism of poly-N- acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain
    • M. Nagae, N. Nishi, T. Murata, T. Usui, T. Nakamura, and S. Wakatsuki et al. Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain Glycobiology 19 2009 112 117
    • (2009) Glycobiology , vol.19 , pp. 112-117
    • Nagae, M.1    Nishi, N.2    Murata, T.3    Usui, T.4    Nakamura, T.5    Wakatsuki, S.6
  • 26
    • 0037301899 scopus 로고    scopus 로고
    • Why are glycoproteins modified by poly-N-acetyllactosamine glyco-conjugates?
    • D. Zhou Why are glycoproteins modified by poly-N-acetyllactosamine glyco-conjugates? Curr Protein Pept Sci 4 2003 1 9
    • (2003) Curr Protein Pept Sci , vol.4 , pp. 1-9
    • Zhou, D.1
  • 27
    • 62849091082 scopus 로고    scopus 로고
    • Structures common to different glycans
    • A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, 2nd ed. Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • P. Stanley, and R.D. Cummings Structures common to different glycans A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler, Essentials of Glycobiology 2nd ed. 2009 Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • (2009) Essentials of Glycobiology
    • Stanley, P.1    Cummings, R.D.2
  • 28
    • 64149125582 scopus 로고    scopus 로고
    • Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3
    • N. Srinivasan, S.M. Bane, S.D. Ahire, A.D. Ingle, and R.D. Kalraiya Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3 Glycoconjugate J 26 2009 445 456
    • (2009) Glycoconjugate J , vol.26 , pp. 445-456
    • Srinivasan, N.1    Bane, S.M.2    Ahire, S.D.3    Ingle, A.D.4    Kalraiya, R.D.5
  • 29
    • 79961023938 scopus 로고    scopus 로고
    • A novel strategy for evasion of NK cell immunity by tumours expressing core2 O-glycans
    • S. Tsuboi, M. Sutoh, S. Hatakeyama, N. Hiraoka, T. Habuchi, and Y. Horikawa et al. A novel strategy for evasion of NK cell immunity by tumours expressing core2 O-glycans EMBO J 30 2011 3173 3185
    • (2011) EMBO J , vol.30 , pp. 3173-3185
    • Tsuboi, S.1    Sutoh, M.2    Hatakeyama, S.3    Hiraoka, N.4    Habuchi, T.5    Horikawa, Y.6
  • 30
  • 32
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution
    • J. Seetharaman, A. Kanigsberg, R. Slaaby, H. Leffler, S.H. Barondes, and J.M. Rini X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution J Biol Chem 273 1998 13047 13052
    • (1998) J Biol Chem , vol.273 , pp. 13047-13052
    • Seetharaman, J.1    Kanigsberg, A.2    Slaaby, R.3    Leffler, H.4    Barondes, S.H.5    Rini, J.M.6
  • 33
  • 34
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • S. Kumar, and R. Nussinov Close-range electrostatic interactions in proteins ChemBioChem 3 2002 604 617
    • (2002) ChemBioChem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 35
    • 78449264527 scopus 로고    scopus 로고
    • X-ray structures of human galectin-9C-terminal domain in complexes with a biantennary oligosaccharide and sialyllactose
    • H. Yoshida, M. Teraoka, N. Nishi, S. Nakakita, T. Nakamura, and M. Hirashima et al. X-ray structures of human galectin-9C-terminal domain in complexes with a biantennary oligosaccharide and sialyllactose J Biol Chem 285 2010 36969 36976
    • (2010) J Biol Chem , vol.285 , pp. 36969-36976
    • Yoshida, H.1    Teraoka, M.2    Nishi, N.3    Nakakita, S.4    Nakamura, T.5    Hirashima, M.6
  • 36
    • 80052949203 scopus 로고    scopus 로고
    • Structural basis for distinct binding properties of the human galectins to Thomsen-Friedenreich antigen
    • C.F. Bian, Y. Zhang, H. Sun, D.F. Li, and D.C. Wang Structural basis for distinct binding properties of the human galectins to Thomsen-Friedenreich antigen PLoS One 6 2011 e25007
    • (2011) PLoS One , vol.6 , pp. 25007
    • Bian, C.F.1    Zhang, Y.2    Sun, H.3    Li, D.F.4    Wang, D.C.5
  • 37
    • 0022854422 scopus 로고
    • Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides
    • H. Leffler, and S.H. Barondes Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides J Biol Chem 261 1986 10119 10126
    • (1986) J Biol Chem , vol.261 , pp. 10119-10126
    • Leffler, H.1    Barondes, S.H.2
  • 38
    • 44049104824 scopus 로고    scopus 로고
    • Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens
    • S.R. Stowell, C.M. Arthur, P. Mehta, K.A. Slanina, O. Blixt, and H. Leffler et al. Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens J Biol Chem 283 2008 10109 10123
    • (2008) J Biol Chem , vol.283 , pp. 10109-10123
    • Stowell, S.R.1    Arthur, C.M.2    Mehta, P.3    Slanina, K.A.4    Blixt, O.5    Leffler, H.6
  • 39
    • 0031445110 scopus 로고    scopus 로고
    • Expression cloning of cDNA encoding a human beta-1,3-N- acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis
    • K. Sasaki, K. Kurata-Miura, M. Ujita, K. Angata, S. Nakagawa, and S.N. Sekine Expression cloning of cDNA encoding a human beta-1,3-N- acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis Proc Natl Acad Sci U S A 94 1997 14294 14299
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 14294-14299
    • Sasaki, K.1    Kurata-Miura, K.2    Ujita, M.3    Angata, K.4    Nakagawa, S.5    Sekine, S.N.6
  • 40
    • 0032964308 scopus 로고    scopus 로고
    • Galectin-1 and galectin-3 expression in human bladder transitional-cell carcinomas
    • L. Cindolo, G. Benvenuto, P. Salvatore, R. Pero, G. Salvatore, and V. Mirone et al. Galectin-1 and galectin-3 expression in human bladder transitional-cell carcinomas Int J Cancer 84 1999 39 43
    • (1999) Int J Cancer , vol.84 , pp. 39-43
    • Cindolo, L.1    Benvenuto, G.2    Salvatore, P.3    Pero, R.4    Salvatore, G.5    Mirone, V.6
  • 42
    • 33947301415 scopus 로고    scopus 로고
    • Slow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: Possible implications for ligand-exchange protocols
    • P.M. Collins, K.I. Hidari, and H. Blanchard Slow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: possible implications for ligand-exchange protocols Acta Crystallogr Sect D Biol Crystallogr 63 2007 415 419
    • (2007) Acta Crystallogr Sect D Biol Crystallogr , vol.63 , pp. 415-419
    • Collins, P.M.1    Hidari, K.I.2    Blanchard, H.3
  • 44
    • 0036849859 scopus 로고    scopus 로고
    • Blu-Ice and the Distributed Control System: Software for data acquisition and instrument control at macromolecular crystallography beamlines
    • T.M. McPhillips, S.E. McPhillips, H.J. Chiu, A.E. Cohen, A.M. Deacon, and P.J. Ellis et al. Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines J Synchrotron Radiat 9 2002 401 406
    • (2002) J Synchrotron Radiat , vol.9 , pp. 401-406
    • McPhillips, T.M.1    McPhillips, S.E.2    Chiu, H.J.3    Cohen, A.E.4    Deacon, A.M.5    Ellis, P.J.6
  • 46
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallogr Sect A Found Crystallogr 50 1994 157 163
    • (1994) Acta Crystallogr Sect A Found Crystallogr , vol.50 , pp. 157-163
    • Navaza, J.1
  • 51
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • A.A. Vaguine, J. Richelle, and S.J. Wodak SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr Sect D Biol Crystallogr 55 1999 191 205
    • (1999) Acta Crystallogr Sect D Biol Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 53
    • 84880623416 scopus 로고    scopus 로고
    • Investigation into the feasibility of thioditaloside as a novel scaffold for galectin-3 specific inhibitors
    • K. Bum-erdene, I.A. Gagarinov, P.M. Collins, M. Winger, A.G. Pearson, and J.C. Wilson et al. Investigation into the feasibility of thioditaloside as a novel scaffold for galectin-3 specific inhibitors ChemBioChem 14 2013 1331 1342
    • (2013) ChemBioChem , vol.14 , pp. 1331-1342
    • Bum-Erdene, K.1    Gagarinov, I.A.2    Collins, P.M.3    Winger, M.4    Pearson, A.G.5    Wilson, J.C.6
  • 54
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J Chem Theory Comput 4 2008 435 447
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 55
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • K. Lindorff-Larsen, S. Piana, K. Palmo, P. Maragakis, J.L. Klepeis, and R.O. Dror et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field Proteins 78 2010 1950 1958
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1    Piana, S.2    Palmo, K.3    Maragakis, P.4    Klepeis, J.L.5    Dror, R.O.6
  • 57
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • B. Hess P-LINCS: a parallel linear constraint solver for molecular simulation J Chem Theory Comput 4 2008 116 122
    • (2008) J Chem Theory Comput , vol.4 , pp. 116-122
    • Hess, B.1
  • 60
    • 84865228751 scopus 로고    scopus 로고
    • ACPYPE - AnteChamber PYthon Parser interfacE
    • A.W. Sousa da Silva, and W.F. Vranken ACPYPE - AnteChamber PYthon Parser interfacE BMC Res Notes 5 2012 367
    • (2012) BMC Res Notes , vol.5 , pp. 367
    • Sousa Da Silva, A.W.1    Vranken, W.F.2
  • 61
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • J. Wang, W. Wang, P.A. Kollman, and D.A. Case Automatic atom type and bond type perception in molecular mechanical calculations J Mol Graphics Modell 25 2006 247 260
    • (2006) J Mol Graphics Modell , vol.25 , pp. 247-260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 62
    • 0036890178 scopus 로고    scopus 로고
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation
    • A. Jakalian, D.B. Jack, and C.I. Bayly Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation J Comput Chem 23 2002 1623 1641
    • (2002) J Comput Chem , vol.23 , pp. 1623-1641
    • Jakalian, A.1    Jack, D.B.2    Bayly, C.I.3
  • 63
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity-rescaling
    • G. Bussi, D. Donadio, and M. Parrinello Canonical sampling through velocity-rescaling J Chem Phys 126 2007 014101
    • (2007) J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 64
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • M. Parrinello, and A. Rahman Polymorphic transitions in single crystals: a new molecular dynamics method J Appl Phys 52 1981 7182 7190
    • (1981) J Appl Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 65
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • S. Nose, and M.L. Klein Constant pressure molecular dynamics for molecular systems Mol Phys 50 1983 1055 1076
    • (1983) Mol Phys , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.