메뉴 건너뛰기




Volumn 50, Issue 24, 2011, Pages 5453-5464

The E2 domains of APP and APLP1 share a conserved mode of dimerization

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; AMYLOID PRECURSOR PROTEINS; HEPARIN BINDING; MEMBRANE PROTEINS; MUTATIONAL ANALYSIS; OLIGOMERIC STRUCTURE; PHOSPHATE IONS; PROTEIN DIMERIZATION; PROTEIN RESIDUES; PROTEIN SURFACE; SECRETASES; SPACE GROUPS;

EID: 79959284264     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101846x     Document Type: Article
Times cited : (32)

References (48)
  • 1
    • 77953886784 scopus 로고    scopus 로고
    • Current status on Alzheimer disease molecular genetics: From past, to present, to future
    • Bettens, K., Sleegers, K., and Van Broeckhoven, C. (2010) Current status on Alzheimer disease molecular genetics: From past, to present, to future Hum. Mol. Genet. 19, R4-R11
    • (2010) Hum. Mol. Genet. , vol.19
    • Bettens, K.1    Sleegers, K.2    Van Broeckhoven, C.3
  • 2
    • 0026442891 scopus 로고
    • Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid ß protein precursor
    • Wasco, W., Bupp, K., Magendantz, M., Gusella, J. F., Tanzi, R. E., and Solomon, F. (1992) Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid ß protein precursor Proc. Natl. Acad. Sci. U.S.A. 89, 10758-10762
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10758-10762
    • Wasco, W.1    Bupp, K.2    Magendantz, M.3    Gusella, J.F.4    Tanzi, R.E.5    Solomon, F.6
  • 3
    • 0027240503 scopus 로고
    • Isolation and characterization of APLP2 encoding a homologue of the Alzheimer's associated amyloid β protein precursor
    • DOI 10.1038/ng0993-95
    • Wasco, W., Gurubhagavatula, S., Paradis, M. D., Romano, D. M., Sisodia, S. S., Hyman, B. T., Neve, R. L., and Tanzi, R. E. (1993) Isolation and characterization of APLP2 encoding a homologue of the Alzheimer's associated amyloid ß protein precursor Nat. Genet. 5, 95-100 (Pubitemid 23261528)
    • (1993) Nature Genetics , vol.5 , Issue.1 , pp. 95-100
    • Wasco, W.1    Gurubhagavatula, S.2    Paradis, M.D.3    Romano, D.M.4    Sisodia, S.S.5    Hyman, B.T.6    Neve, R.L.7    Tanzi, R.E.8
  • 4
    • 8144230876 scopus 로고    scopus 로고
    • Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members
    • DOI 10.1038/sj.emboj.7600390
    • Herms, J., Anliker, B., Heber, S., Ring, S., Fuhrmann, M., Kretzschmar, H., Sisodia, S., and Muller, U. (2004) Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members EMBO J. 23, 4106-4115 (Pubitemid 39472431)
    • (2004) EMBO Journal , vol.23 , Issue.20 , pp. 4106-4115
    • Herms, J.1    Anliker, B.2    Heber, S.3    Ring, S.4    Fuhrmann, M.5    Kretzschmar, H.6    Sisodia, S.7    Muller, U.8
  • 5
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • DOI 10.1038/325733a0
    • Kang, J., Lemaire, H. G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K. H., Multhaup, G., Beyreuther, K., and Muller-Hill, B. (1987) The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor Nature 325, 733-736 (Pubitemid 17054046)
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3
  • 6
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 7
    • 0027221517 scopus 로고
    • Amino acid sequence RERMS represents the active domain of amyloid β/A4 protein precursor that promotes fibroblast growth
    • Ninomiya, H., Roch, J. M., Sundsmo, M. P., Otero, D. A., and Saitoh, T. (1993) Amino acid sequence RERMS represents the active domain of amyloid ß/A4 protein precursor that promotes fibroblast growth J. Cell Biol. 121, 879-886 (Pubitemid 23143548)
    • (1993) Journal of Cell Biology , vol.121 , Issue.4 , pp. 879-886
    • Ninomiya, H.1    Roch, J.-M.2    Sundsmo, M.P.3    Otero, D.A.C.4    Saitoh, T.5
  • 8
    • 0141483463 scopus 로고    scopus 로고
    • SAPP as a regulator of dendrite motility and melanin release in epidermal melanocytes and melanoma cells
    • Quast, T., Wehner, S., Kirfel, G., Jaeger, K., De Luca, M., and Herzog, V. (2003) sAPP as a regulator of dendrite motility and melanin release in epidermal melanocytes and melanoma cells FASEB J. 17, 1739-1741
    • (2003) FASEB J. , vol.17 , pp. 1739-1741
    • Quast, T.1    Wehner, S.2    Kirfel, G.3    Jaeger, K.4    De Luca, M.5    Herzog, V.6
  • 9
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev, A., McLaughlin, T., O'Leary, D. D., and Tessier-Lavigne, M. (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases Nature 457, 981-989
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 10
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptivety active complex of APP with Fe65 and histone acetyltransferase Tip60
    • DOI 10.1126/science.1058783
    • Cao, X. and Sudhof, T. C. (2001) A transcriptionally correction of transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60 Science 293, 115-120 (Pubitemid 32625507)
    • (2001) Science , vol.293 , Issue.5527 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 11
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein
    • DOI 10.1016/S0092-8674(02)00809-7
    • Baek, S. H., Ohgi, K. A., Rose, D. W., Koo, E. H., Glass, C. K., and Rosenfeld, M. G. (2002) Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-B and ß-amyloid precursor protein Cell 110, 55-67 (Pubitemid 34874606)
    • (2002) Cell , vol.110 , Issue.1 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 13
    • 70350350069 scopus 로고    scopus 로고
    • Induced dimerization of the amyloid precursor protein leads to decreased amyloid-ß protein production
    • Eggert, S., Midthune, B., Cottrell, B., and Koo, E. H. (2009) Induced dimerization of the amyloid precursor protein leads to decreased amyloid-ß protein production J. Biol. Chem. 284, 28943-28952
    • (2009) J. Biol. Chem. , vol.284 , pp. 28943-28952
    • Eggert, S.1    Midthune, B.2    Cottrell, B.3    Koo, E.H.4
  • 14
    • 67649366042 scopus 로고    scopus 로고
    • Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers
    • Gralle, M., Botelho, M. G., and Wouters, F. S. (2009) Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers J. Biol. Chem. 284, 15016-15025
    • (2009) J. Biol. Chem. , vol.284 , pp. 15016-15025
    • Gralle, M.1    Botelho, M.G.2    Wouters, F.S.3
  • 17
    • 33947597857 scopus 로고    scopus 로고
    • GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42
    • DOI 10.1038/sj.emboj.7601616, PII 7601616
    • Munter, L. M., Voigt, P., Harmeier, A., Kaden, D., Gottschalk, K. E., Weise, C., Pipkorn, R., Schaefer, M., Langosch, D., and Multhaup, G. (2007) GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aß42 EMBO J. 26, 1702-1712 (Pubitemid 46480941)
    • (2007) EMBO Journal , vol.26 , Issue.6 , pp. 1702-1712
    • Munter, L.-M.1    Voigt, P.2    Harmeier, A.3    Kaden, D.4    Gottschalk, K.E.5    Weise, C.6    Pipkorn, R.7    Schaefer, M.8    Langosch, D.9    Multhaup, G.10
  • 18
    • 65249143369 scopus 로고    scopus 로고
    • Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2
    • Kaden, D., Voigt, P., Munter, L. M., Bobowski, K. D., Schaefer, M., and Multhaup, G. (2009) Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2 J. Cell Sci. 122, 368-377
    • (2009) J. Cell Sci. , vol.122 , pp. 368-377
    • Kaden, D.1    Voigt, P.2    Munter, L.M.3    Bobowski, K.D.4    Schaefer, M.5    Multhaup, G.6
  • 19
    • 4143105782 scopus 로고    scopus 로고
    • The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
    • DOI 10.1016/j.molcel.2004.06.037, PII S109727650400379X
    • Wang, Y. and Ha, Y. (2004) The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain Mol. Cell 15, 343-353 (Pubitemid 39092751)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 343-353
    • Wang, Y.1    Ha, Y.2
  • 20
    • 77950385325 scopus 로고    scopus 로고
    • Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein
    • Dahms, S. O., Hoefgen, S., Roeser, D., Schlott, B., Guhrs, K. H., and Than, M. E. (2010) Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein Proc. Natl. Acad. Sci. U.S.A. 107, 5381-5386
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5381-5386
    • Dahms, S.O.1    Hoefgen, S.2    Roeser, D.3    Schlott, B.4    Guhrs, K.H.5    Than, M.E.6
  • 23
    • 16644362379 scopus 로고    scopus 로고
    • Cloning, expression, crystallization and initial crystallographic analysis of the C-terminal domain of the amyloid precursor protein APP
    • DOI 10.1107/S0907444904015343
    • Keil, C., Huber, R., Bode, W., and Than, M. E. (2004) Cloning, expression, crystallization and initial crystallographic analysis of the C-terminal domain of the amyloid precursor protein APP Acta Crystallogr. D60, 1614-1617 (Pubitemid 41103536)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.9 , pp. 1614-1617
    • Keil, C.1    Huber, R.2    Bode, W.3    Than, M.E.4
  • 24
    • 3342915630 scopus 로고    scopus 로고
    • Three-dimensional structure of an independently folded extracellular domain of human amyloid-β precursor protein
    • DOI 10.1021/bi049041o
    • Dulubova, I., Ho, A., Huryeva, I., Sudhof, T. C., and Rizo, J. (2004) Three-dimensional structure of an independently folded extracellular domain of human amyloid-ß precursor protein Biochemistry 43, 9583-9588 (Pubitemid 38993808)
    • (2004) Biochemistry , vol.43 , Issue.30 , pp. 9583-9588
    • Dulubova, I.1    Ho, A.2    Huryeva, I.3    Sudhof, T.C.4    Rizo, J.5
  • 25
    • 76249098107 scopus 로고    scopus 로고
    • Structural characterization of the E2 domain of APL-1, a Caenorhabditis elegans homolog of human amyloid precursor protein, and its heparin binding site
    • Hoopes, J. T., Liu, X., Xu, X., Demeler, B., Folta-Stogniew, E., Li, C., and Ha, Y. (2010) Structural characterization of the E2 domain of APL-1, a Caenorhabditis elegans homolog of human amyloid precursor protein, and its heparin binding site J. Biol. Chem. 285, 2165-2173
    • (2010) J. Biol. Chem. , vol.285 , pp. 2165-2173
    • Hoopes, J.T.1    Liu, X.2    Xu, X.3    Demeler, B.4    Folta-Stogniew, E.5    Li, C.6    Ha, Y.7
  • 27
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for macromolecular phasing with SHELX programs
    • Pape, T. and Schneider, T. R. (2004) HKL2MAP: A graphical user interface for macromolecular phasing with SHELX programs J. Appl. Crystallogr. 37, 843-844
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 29
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS Refinement in REFMAC at Moderate Resolutions
    • DOI 10.1016/S0076-6879(03)74014-2
    • Winn, M. D., Murshudov, G. N., and Papiz, M. Z. (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions Methods Enzymol. 374, 300-321 (Pubitemid 37531815)
    • (2003) Methods in Enzymology , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A47 (Part 2) 110-119
    • (1991) Acta Crystallogr. , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 33744816438 scopus 로고    scopus 로고
    • UltraScan: A Comprehensive Data Analysis Software Package for Analytical Ultracentrifugation Experiments
    • (Scott, D., Harding, S., and Rowe, A., Eds.) Royal Society of Chemistry, Cambridge, U.K.
    • Demeler, B. (2005) UltraScan: A Comprehensive Data Analysis Software Package for Analytical Ultracentrifugation Experiments. In Modern Analytical Ultracentrifugation: Techniques and Methods (Scott, D., Harding, S., and Rowe, A., Eds.) pp 210-229, Royal Society of Chemistry, Cambridge, U.K.
    • (2005) Modern Analytical Ultracentrifugation: Techniques and Methods , pp. 210-229
    • Demeler, B.1
  • 35
    • 38649090374 scopus 로고    scopus 로고
    • Parallel computational techniques for the analysis of sedimentation velocity experiments in UltraScan
    • Brookes, E. and Demeler, B. (2008) Parallel computational techniques for the analysis of sedimentation velocity experiments in UltraScan Colloid Polym. Sci. 286, 138-148
    • (2008) Colloid Polym. Sci. , vol.286 , pp. 138-148
    • Brookes, E.1    Demeler, B.2
  • 37
    • 77950581757 scopus 로고    scopus 로고
    • A two-dimensional spectrum analysis for sedimentation velocity experiments of mixtures with heterogeneity in molecular weight and shape
    • Brookes, E., Cao, W., and Demeler, B. (2010) A two-dimensional spectrum analysis for sedimentation velocity experiments of mixtures with heterogeneity in molecular weight and shape Eur. Biophys. J. 39, 405-414
    • (2010) Eur. Biophys. J. , vol.39 , pp. 405-414
    • Brookes, E.1    Cao, W.2    Demeler, B.3
  • 38
    • 8844265931 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of highly heterogeneous systems
    • DOI 10.1016/j.ab.2004.08.039, PII S0003269704007225
    • Demeler, B. and van Holde, K. E. (2004) Sedimentation velocity analysis of highly heterogeneous systems Anal. Biochem. 335, 279-288 (Pubitemid 39535193)
    • (2004) Analytical Biochemistry , vol.335 , Issue.2 , pp. 279-288
    • Demeler, B.1    Van Holde, K.E.2
  • 39
    • 33749430638 scopus 로고    scopus 로고
    • Genetic Algorithm Optimization for Obtaining Accurate Molecular Weight Distributions from Sedimentation Velocity Experiments
    • (Wandrey, C. and Cölfen, H., Eds.) Springer, Berlin.
    • Brookes, E. and Demeler, B. (2006) Genetic Algorithm Optimization for Obtaining Accurate Molecular Weight Distributions from Sedimentation Velocity Experiments. In Analytical Ultracentrifugation VIII (Wandrey, C. and Cölfen, H., Eds.) pp 33-40, Springer, Berlin.
    • (2006) Analytical Ultracentrifugation VIII , pp. 33-40
    • Brookes, E.1    Demeler, B.2
  • 40
    • 34548101735 scopus 로고    scopus 로고
    • Parsimonious regularization using genetic algorithms applied to the analysis of analytical ultracentrifugation experiments
    • DOI 10.1145/1276958.1277035, Proceedings of GECCO 2007: Genetic and Evolutionary Computation Conference
    • Brookes, E. H. and Demeler, B. (2007) Parsimonious regularization using genetic algorithms applied to the analysis of analytical ultracentrifugation experiments. In Proceedings of the 9th annual conference on genetic and evolutionary computation, pp 361-368, ACM, London. (Pubitemid 47291544)
    • (2007) Proceedings of GECCO 2007: Genetic and Evolutionary Computation Conference , pp. 361-368
    • Brookes, E.H.1    Demeler, B.2
  • 41
    • 38649117291 scopus 로고    scopus 로고
    • Monte Carlo analysis of sedimentation experiments
    • DOI 10.1007/s00396-007-1699-4
    • Demeler, B. and Brookes, E. (2008) Monte Carlo analysis of sedimentation experiments Colloid Polym. Sci. 286, 129-137 (Pubitemid 351168131)
    • (2008) Colloid and Polymer Science , vol.286 , Issue.2 , pp. 129-137
    • Demeler, B.1    Brookes, E.2
  • 42
    • 77954570163 scopus 로고    scopus 로고
    • Characterization of reversible associations by sedimentation velocity with UltraScan
    • Demeler, B., Brookes, E., Wang, R., Schirf, V., and Kim, C. A. (2010) Characterization of reversible associations by sedimentation velocity with UltraScan Macromol. Biosci. 10, 775-782
    • (2010) Macromol. Biosci. , vol.10 , pp. 775-782
    • Demeler, B.1    Brookes, E.2    Wang, R.3    Schirf, V.4    Kim, C.A.5
  • 43
    • 46749141705 scopus 로고    scopus 로고
    • Modeling analytical ultracentrifugation experiments with an adaptive space-time finite element solution for multicomponent reacting systems
    • Cao, W. and Demeler, B. (2008) Modeling analytical ultracentrifugation experiments with an adaptive space-time finite element solution for multicomponent reacting systems Biophys. J. 95, 54-65
    • (2008) Biophys. J. , vol.95 , pp. 54-65
    • Cao, W.1    Demeler, B.2
  • 44
    • 0028136865 scopus 로고
    • Peptides containing the RERMS sequence of amyloid β/A4 protein precursor bind cell surface and promote neurite extension
    • Jin, L. W., Ninomiya, H., Roch, J. M., Schubert, D., Masliah, E., Otero, D. A., and Saitoh, T. (1994) Peptides containing the RERMS sequence of amyloid ß/A4 protein precursor bind cell surface and promote neurite extension J. Neurosci. 14, 5461-5470 (Pubitemid 24279065)
    • (1994) Journal of Neuroscience , vol.14 , Issue.9 , pp. 5461-5470
    • Jin, L.-W.1    Ninomiya, H.2    Roch, J.-M.3    Schubert, D.4    Masliah, E.5    Otero, D.A.C.6    Saitoh, T.7
  • 45
    • 0040652143 scopus 로고    scopus 로고
    • Growth regulation of rat thyrocytes (FRTL-5 cells) by the secreted ectodomain of β-amyloid precursor-like proteins
    • DOI 10.1210/en.137.5.1975
    • Popp, G. M., Graebert, K. S., Pietrzik, C. U., Rosentreter, S. M., Lemansky, P., and Herzog, V. (1996) Growth regulation of rat thyrocytes (FRTL-5 cells) by the secreted ectodomain of ß-amyloid precursor-like proteins Endocrinology 137, 1975-1983 (Pubitemid 26133974)
    • (1996) Endocrinology , vol.137 , Issue.5 , pp. 1975-1983
    • Popp, G.M.1    Graebert, K.S.2    Pietrzik, C.U.3    Rosentreter, S.M.4    Lemansky, P.5    Herzog, V.6
  • 46
    • 0030030005 scopus 로고    scopus 로고
    • Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I
    • DOI 10.1074/jbc.271.3.1613
    • Beher, D., Hesse, L., Masters, C. L., and Multhaup, G. (1996) Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I J. Biol. Chem. 271, 1613-1620 (Pubitemid 26028652)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.3 , pp. 1613-1620
    • Beher, D.1    Hesse, L.2    Masters, C.L.3    Multhaup, G.4
  • 47
    • 18844473445 scopus 로고    scopus 로고
    • Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease
    • DOI 10.1016/S0014-5793(97)01146-0, PII S0014579397011460
    • Mok, S. S., Sberna, G., Heffernan, D., Cappai, R., Galatis, D., Clarris, H. J., Sawyer, W. H., Beyreuther, K., Masters, C. L., and Small, D. H. (1997) Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease FEBS Lett. 415, 303-307 (Pubitemid 27451954)
    • (1997) FEBS Letters , vol.415 , Issue.3 , pp. 303-307
    • Mok, S.S.1    Sberna, G.2    Heffernan, D.3    Cappai, R.4    Galatis, D.5    Clarris, H.J.6    Sawyer, W.H.7    Beyreuther, K.8    Masters, C.L.9    Small, D.H.10
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24, 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.