메뉴 건너뛰기




Volumn 144, Issue 1-2, 2003, Pages 104-113

FEMME database: Topologic and geometric information of macromolecules

Author keywords

Macromolecular structures; Structural databases; Three dimensional electron microscopy; Shape representation

Indexed keywords

ARTICLE; BIBLIOGRAPHIC DATABASE; BIOINFORMATICS; ELECTRON MICROSCOPY; ELECTRON SPIN RESONANCE; GEOMETRY; IMAGE ENHANCEMENT; INFORMATION PROCESSING; MACROMOLECULE; MEDICAL INFORMATICS; PRIORITY JOURNAL;

EID: 0344983360     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2003.09.014     Document Type: Article
Times cited : (4)

References (50)
  • 2
    • 0032489015 scopus 로고    scopus 로고
    • Three-dimensional fold of the human AQP1water channel determined at 4 Å resolution by electron crystallography of two-dimensional crystals embedded in ice
    • Alberts B. Three-dimensional fold of the human AQP1water channel determined at 4. Å resolution by electron crystallography of two-dimensional crystals embedded in ice Cell. 92:1998;291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 5
    • 0032807499 scopus 로고    scopus 로고
    • The BioImage Database Project: Organizing multidimensional biological images in an object-relational database
    • Carazo J.M., Stelzer E.H. The BioImage Database Project: organizing multidimensional biological images in an object-relational database. J. Struct. Biol. 125:1999;97-102.
    • (1999) J. Struct. Biol. , vol.125 , pp. 97-102
    • Carazo, J.M.1    Stelzer, E.H.2
  • 6
    • 0037436340 scopus 로고    scopus 로고
    • Mega-Dalton biomolecular motion captured from electron microscopy reconstructions
    • Chacón P., Tama F., Wriggers W. Mega-Dalton biomolecular motion captured from electron microscopy reconstructions. J. Mol. Biol. 326:2003;485-492.
    • (2003) J. Mol. Biol. , vol.326 , pp. 485-492
    • Chacón, P.1    Tama, F.2    Wriggers, W.3
  • 8
    • 0027214794 scopus 로고
    • Teaching electron diffraction and imaging of macromolecules
    • Chiu W., Schmid M.F., Prasad B.V.V. Teaching electron diffraction and imaging of macromolecules. Biophys. J. 64:1993;1610-1625.
    • (1993) Biophys. J. , vol.64 , pp. 1610-1625
    • Chiu, W.1    Schmid, M.F.2    Prasad, B.V.V.3
  • 9
    • 0035996965 scopus 로고    scopus 로고
    • Modeling shape and topology of low-resolution density maps of biological macromolecules
    • De-Alarcón P.A., Pascual-Montano A., Gupta A., Carazo J.M. Modeling shape and topology of low-resolution density maps of biological macromolecules. Biophys. J. 83:2002;619-632.
    • (2002) Biophys. J. , vol.83 , pp. 619-632
    • De-Alarcón, P.A.1    Pascual-Montano, A.2    Gupta, A.3    Carazo, J.M.4
  • 10
    • 84937564210 scopus 로고    scopus 로고
    • Spin images and neural networks for efficient content-based retrieval in 3D object databases
    • De-Alarcón P.A., Pascual-Montano A., Carazo J.M. Spin images and neural networks for efficient content-based retrieval in 3D object databases. Lecture Notes on Computer Science. 238:2002;225-234.
    • (2002) Lecture Notes on Computer Science , vol.238 , pp. 225-234
    • De-Alarcón, P.A.1    Pascual-Montano, A.2    Carazo, J.M.3
  • 11
    • 34250098710 scopus 로고
    • Using Canny's criteria to derive a recursively implemented optimal edge detector
    • Deriche R. Using Canny's criteria to derive a recursively implemented optimal edge detector. Image Vision Comput. 1:1987;167-187.
    • (1987) Image Vision Comput. , vol.1 , pp. 167-187
    • Deriche, R.1
  • 14
    • 51249162203 scopus 로고
    • The union of balls and its dual shape
    • Edelsbrunner H. The union of balls and its dual shape. Discr. Comput. Geom. 13:1995;415-440.
    • (1995) Discr. Comput. Geom. , vol.13 , pp. 415-440
    • Edelsbrunner, H.1
  • 17
    • 0030310298 scopus 로고    scopus 로고
    • On the definition and the construction of pockets in macromolecules
    • Edelsbrunner H., Facello M.A., Liagn J. On the definition and the construction of pockets in macromolecules. Pac. Symp. Biocomput. 1996;272-287.
    • (1996) Pac. Symp. Biocomput. , pp. 272-287
    • Edelsbrunner, H.1    Facello, M.A.2    Liagn, J.3
  • 18
    • 0032538274 scopus 로고    scopus 로고
    • The first step: Activation of the Semliki Forest virus spike protein precursor causes a localized conformational change in the trimeric spike
    • Ferlenghi I., Gowen B., de Haas F., Mancini E.J., Garoff H., Sjoberg M., Fuller S.D. The first step: activation of the Semliki Forest virus spike protein precursor causes a localized conformational change in the trimeric spike. J. Mol. Biol. 283:1998;71-81.
    • (1998) J. Mol. Biol. , vol.283 , pp. 71-81
    • Ferlenghi, I.1    Gowen, B.2    De Haas, F.3    Mancini, E.J.4    Garoff, H.5    Sjoberg, M.6    Fuller, S.D.7
  • 21
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P.N.T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 257:1975;28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 22
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick K., Thornton J.M. PQS: a protein quaternary structure file server. Trends Biochem. Sci. 23:1998;358-361.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 23
    • 0035906702 scopus 로고    scopus 로고
    • Bringing the information gap: Computational tools for intermediate resolution structure interpretation
    • Jiang W., Baker M.L., Ludtke S.J., Chiu W. Bringing the information gap: computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 308:2001;1033-1044.
    • (2001) J. Mol. Biol. , vol.308 , pp. 1033-1044
    • Jiang, W.1    Baker, M.L.2    Ludtke, S.J.3    Chiu, W.4
  • 24
    • 0032685832 scopus 로고    scopus 로고
    • Using spin-images for efficient multiple model recognition in cluttered 3-d scenes
    • Johnson A.E., Hebert M. Using spin-images for efficient multiple model recognition in cluttered 3-d scenes. IEEE Trans. Pattern Anal. Mach. Intell. 21:1999;433-449.
    • (1999) IEEE Trans. Pattern Anal. Mach. Intell. , vol.21 , pp. 433-449
    • Johnson, A.E.1    Hebert, M.2
  • 25
    • 0034695259 scopus 로고    scopus 로고
    • 15 Å resolution model of the monomeric kinesin motor, KIF1A
    • Kikkawa M., Okada Y., Hirokawa N. 15. Å resolution model of the monomeric kinesin motor, KIF1A Cell. 100:2000;241-252.
    • (2000) Cell , vol.100 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 26
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • Liang J., Edelsbrunner H., Woodward C. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Sci. 7:1998;1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 27
    • 0032190305 scopus 로고    scopus 로고
    • Analytical shape computation of macromolecules I: Molecular area and volume through alpha shape
    • Liang J., Edelsbrunner H., Fu P., Sudhakar P.V. Analytical shape computation of macromolecules I: molecular area and volume through alpha shape. Proteins. 33:1998;1-17.
    • (1998) Proteins , vol.33 , pp. 1-17
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.V.4
  • 29
    • 0037062479 scopus 로고    scopus 로고
    • Domain movements in human fatty acid synthase by quantized elastic deformational model
    • Ming D., Kong Y., Wakil S.J., Brink J., Ma J. Domain movements in human fatty acid synthase by quantized elastic deformational model. Proc. Natl. Acad. Sci. USA. 99:2002;7895-7899.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7895-7899
    • Ming, D.1    Kong, Y.2    Wakil, S.J.3    Brink, J.4    Ma, J.5
  • 30
    • 0035783172 scopus 로고    scopus 로고
    • Lumbricus terrestris hemoglobin - The architecture of linker chains and structural variation of the central toroid
    • Mouche F., Boisset N., Penczek P.A. Lumbricus terrestris hemoglobin - the architecture of linker chains and structural variation of the central toroid. J. Struct. Biol. 133:2001;176-192.
    • (2001) J. Struct. Biol. , vol.133 , pp. 176-192
    • Mouche, F.1    Boisset, N.2    Penczek, P.A.3
  • 32
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., Downing K.H. Structure of the alpha beta tubulin dimer by electron crystallography. Nature. 391:1998;199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 33
    • 0035825140 scopus 로고    scopus 로고
    • Molecular machines: Putting the pieces together
    • Nogales E., Grigorieff N. Molecular machines: putting the pieces together. J. Cell Biol. 152:2001;F1-F10.
    • (2001) J. Cell Biol. , vol.152
    • Nogales, E.1    Grigorieff, N.2
  • 34
    • 0020488742 scopus 로고
    • Collective variable description of small-amplitude conformational fluctuations in a globular protein
    • Noguti T., Go N. Collective variable description of small-amplitude conformational fluctuations in a globular protein. Nature. 296:1982;668-776.
    • (1982) Nature , vol.296 , pp. 668-776
    • Noguti, T.1    Go, N.2
  • 36
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P., Radermacher M., Frank J. Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy. 40:1992;33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 38
    • 0028375920 scopus 로고
    • Three-dimensional reconstruction from random projections: Orientational alignment via Radon transforms
    • Radermacher M. Three-dimensional reconstruction from random projections: orientational alignment via Radon transforms. Ultramicroscopy. 53:1994;121-136.
    • (1994) Ultramicroscopy. , vol.53 , pp. 121-136
    • Radermacher, M.1
  • 39
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Å resolution
    • Reinisch K.M., Nibert M.L., Harrison S.C. Structure of the reovirus core at 3.6. Å resolution Nature. 404:2000;960-967.
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 40
    • 0035783162 scopus 로고    scopus 로고
    • Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy
    • Roseman A.M., Ranson N.A., Gowen B., Fuller S.D., Saibil H.R. Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy. J. Struct. Biol. 135:2001;115-125.
    • (2001) J. Struct. Biol. , vol.135 , pp. 115-125
    • Roseman, A.M.1    Ranson, N.A.2    Gowen, B.3    Fuller, S.D.4    Saibil, H.R.5
  • 41
    • 0033813317 scopus 로고    scopus 로고
    • Conformational changes studied by cryo-electron microscopy
    • Saibil H.R. Conformational changes studied by cryo-electron microscopy. Nat. Struct. Biol. 7:2000;711-714.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 711-714
    • Saibil, H.R.1
  • 42
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae - TRNA-ribosome and subunit-subunit interactions
    • Spahn C.M., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J. Structure of the 80S ribosome from Saccharomyces cerevisiae - tRNA-ribosome and subunit-subunit interactions. Cell. 107:2001;373-386.
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 44
    • 0036382958 scopus 로고    scopus 로고
    • Exploring global distortions of biological macromolecules and assemblies from low-resolution structural information and elastic network theory
    • Tama F., Wriggers W., Brooks II C.L. Exploring global distortions of biological macromolecules and assemblies from low-resolution structural information and elastic network theory. J. Mol. Biol. 321:2002;297-305.
    • (2002) J. Mol. Biol. , vol.321 , pp. 297-305
    • Tama, F.1    Wriggers, W.2    Brooks II, C.L.3
  • 46
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
    • Van Heel M. Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction. Ultramicroscopy. 21:1987;111-123.
    • (1987) Ultramicroscopy , vol.21 , pp. 111-123
    • Van Heel, M.1
  • 47
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8-Å resolution
    • Zhang P., Toyoshima C., Yonekura K., Green N.M., Stokes D.L. Structure of the calcium pump from sarcoplasmic reticulum at 8-Å resolution. Nature. 392:1998;835-839.
    • (1998) Nature , vol.392 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, N.M.4    Stokes, D.L.5
  • 50
    • 0030960710 scopus 로고    scopus 로고
    • Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: Procedure and application to the 70S Escherichia coli ribosome
    • Zhu J., Penczek P.A., Schroder R., Frank J. Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: procedure and application to the 70S Escherichia coli ribosome. J. Struct. Biol. 118:1997;197-219.
    • (1997) J. Struct. Biol. , vol.118 , pp. 197-219
    • Zhu, J.1    Penczek, P.A.2    Schroder, R.3    Frank, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.