메뉴 건너뛰기




Volumn 14, Issue 3, 2004, Pages 313-324

A structural perspective on protein-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; BIOINFORMATICS; COMPLEX FORMATION; ELECTRON MICROSCOPY; ESCHERICHIA COLI; HYBRIDIZATION; MACROMOLECULE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

EID: 2942582560     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.04.006     Document Type: Review
Times cited : (240)

References (187)
  • 3
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell. 92:1998;291-294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 4
    • 0037044756 scopus 로고    scopus 로고
    • Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain
    • Goto N.K., Zor T., Martinez-Yamout M., Dyson H.J., Wright P.E. Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain. J Biol Chem. 277:2002;43168-43174
    • (2002) J Biol Chem , vol.277 , pp. 43168-43174
    • Goto, N.K.1    Zor, T.2    Martinez-Yamout, M.3    Dyson, H.J.4    Wright, P.E.5
  • 6
    • 0035799284 scopus 로고    scopus 로고
    • Cooperativity in transcriptional control
    • Courey A.J. Cooperativity in transcriptional control. Curr Biol. 11:2001;R250-R252
    • (2001) Curr Biol , vol.11 , pp. 250-R252
    • Courey, A.J.1
  • 7
    • 0035910414 scopus 로고    scopus 로고
    • The rotary machine in the cell, ATP synthase
    • Noji H., Yoshida M. The rotary machine in the cell, ATP synthase. J Biol Chem. 276:2001;1665-1668
    • (2001) J Biol Chem , vol.276 , pp. 1665-1668
    • Noji, H.1    Yoshida, M.2
  • 8
    • 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 , pp. 1-F10
    • Nogales, E.1    Grigorieff, N.2
  • 9
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol. 148:2000;635-651
    • (2000) J Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 10
    • 0037308665 scopus 로고    scopus 로고
    • Bacterial RNA polymerases: The wholo story
    • Murakami K.S., Darst S.A. Bacterial RNA polymerases: the wholo story. Curr Opin Struct Biol. 13:2003;31-39
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 31-39
    • Murakami, K.S.1    Darst, S.A.2
  • 11
    • 0034503071 scopus 로고    scopus 로고
    • Recent structural insights into transcription preinitiation complexes
    • Nogales E. Recent structural insights into transcription preinitiation complexes. J Cell Sci. 113:2000;4391-4397
    • (2000) J Cell Sci , vol.113 , pp. 4391-4397
    • Nogales, E.1
  • 12
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale R.D. The molecular motor toolbox for intracellular transport. Cell. 112:2003;467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 13
    • 0034078008 scopus 로고    scopus 로고
    • Microtubule-based transport systems in neurons: The roles of kinesins and dyneins
    • Goldstein L.S., Yang Z. Microtubule-based transport systems in neurons: the roles of kinesins and dyneins. Annu Rev Neurosci. 23:2000;39-71
    • (2000) Annu Rev Neurosci , vol.23 , pp. 39-71
    • Goldstein, L.S.1    Yang, Z.2
  • 14
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale R.D., Milligan R.A. The way things move: looking under the hood of molecular motor proteins. Science. 288:2000;88-95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 15
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy M.B. Signal-processing machines at the postsynaptic density. Science. 290:2000;750-754
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 16
    • 0035970298 scopus 로고    scopus 로고
    • Mapping protein family interactions: Intramolecular and intermolecular protein family interaction repertoires in the PDB and yeast
    • Park J., Lappe M., Teichmann S.A. Mapping protein family interactions: intramolecular and intermolecular protein family interaction repertoires in the PDB and yeast. J Mol Biol. 307:2001;929-938
    • (2001) J Mol Biol , vol.307 , pp. 929-938
    • Park, J.1    Lappe, M.2    Teichmann, S.A.3
  • 17
    • 0037163883 scopus 로고    scopus 로고
    • Potential artefacts in protein-interaction networks
    • Aloy P., Russell R.B. Potential artefacts in protein-interaction networks. FEBS Lett. 530:2002;253-254
    • (2002) FEBS Lett , vol.530 , pp. 253-254
    • Aloy, P.1    Russell, R.B.2
  • 18
    • 0036805329 scopus 로고    scopus 로고
    • Bridging structural biology and genomics: Assessing protein-interaction data with known complexes
    • Edwards A., Kus B., Jansen R., Greenbaum D., Greenblatt J., Gerstein M. Bridging structural biology and genomics: assessing protein-interaction data with known complexes. Trends Genet. 18:2002;529-536
    • (2002) Trends Genet , vol.18 , pp. 529-536
    • Edwards, A.1    Kus, B.2    Jansen, R.3    Greenbaum, D.4    Greenblatt, J.5    Gerstein, M.6
  • 19
    • 0037435031 scopus 로고    scopus 로고
    • From words to literature in structural proteomics
    • This review summarizes current efforts in structural proteomics. It provides a plethora of references for the various experimental and theoretical methods used to obtain structural information about macromolecular assemblies.
    • Sali A., Glaeser R., Earnest T., Baumeister W. From words to literature in structural proteomics. Nature. 422:2003;216-225 This review summarizes current efforts in structural proteomics. It provides a plethora of references for the various experimental and theoretical methods used to obtain structural information about macromolecular assemblies.
    • (2003) Nature , vol.422 , pp. 216-225
    • Sali, A.1    Glaeser, R.2    Earnest, T.3    Baumeister, W.4
  • 20
    • 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
  • 22
    • 0010656061 scopus 로고    scopus 로고
    • Exploring the protein interactome using comprehensive two-hybrid projects
    • Ito T., Chiba T., Yoshida M. Exploring the protein interactome using comprehensive two-hybrid projects. Trends Biotechnol. 19:2001;S23-S27
    • (2001) Trends Biotechnol , vol.19 , pp. 23-S27
    • Ito, T.1    Chiba, T.2    Yoshida, M.3
  • 28
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • This review provides a good overview of the role of mass-spectrometry- based proteomics in the study of protein-protein interactions, the mapping of cell organelles and the generation of quantitative protein profiles for a variety of species.
    • Aebersold R., Mann M. Mass spectrometry-based proteomics. Nature. 422:2003;198-207 This review provides a good overview of the role of mass-spectrometry-based proteomics in the study of protein-protein interactions, the mapping of cell organelles and the generation of quantitative protein profiles for a variety of species.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 29
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M. Proteomic characterization of the human centrosome by protein correlation profiling. Nature. 426:2003;570-574
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 30
    • 0037050020 scopus 로고    scopus 로고
    • Protein complexes take the bait
    • Kumar A., Snyder M. Protein complexes take the bait. Nature. 415:2002;123-124
    • (2002) Nature , vol.415 , pp. 123-124
    • Kumar, A.1    Snyder, M.2
  • 31
  • 32
    • 0037182924 scopus 로고    scopus 로고
    • Proteomics: The society of proteins
    • Abbott A. Proteomics: the society of proteins. Nature. 417:2002;894-896
    • (2002) Nature , vol.417 , pp. 894-896
    • Abbott, A.1
  • 33
    • 0036815763 scopus 로고    scopus 로고
    • Electron tomography: Towards visualizing the molecular organization of the cytoplasm
    • Baumeister W. Electron tomography: towards visualizing the molecular organization of the cytoplasm. Curr Opin Struct Biol. 12:2002;679-684
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 679-684
    • Baumeister, W.1
  • 34
    • 0033436315 scopus 로고    scopus 로고
    • Challenges at the frontiers of structural biology
    • Sali A., Kuriyan J. Challenges at the frontiers of structural biology. Trends Cell Biol. 9:1999;M20-M24
    • (1999) Trends Cell Biol , vol.9 , pp. 20-M24
    • Sali, A.1    Kuriyan, J.2
  • 35
    • 2942604261 scopus 로고    scopus 로고
    • Structure determination of macromolecular complexes by experiment and computation
    • Edited by Bujnicki JM.: Springer-Verlag
    • Alber F, Eswar N, Sali A: Structure determination of macromolecular complexes by experiment and computation. In Nucleic Acids and Molecular Biology, Volume 15, Practical Bioinformatics. Edited by Bujnicki JM. :Springer-Verlag; 2004:73-96.
    • (2004) Nucleic Acids and Molecular Biology, Volume 15, Practical Bioinformatics , vol.15 , pp. 73-96
    • Alber, F.1    Eswar, N.2    Sali, A.3
  • 36
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., Darst S.A. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell. 98:1999;811-824
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6
  • 37
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 38
  • 43
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science. 268:1995;533-539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 46
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • Ben-Shem A., Frolow F., Nelson N. Crystal structure of plant photosystem I. Nature. 426:2003;630-635
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 47
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution
    • Liu Z., Yan H., Wang K., Kuang T., Zhang J., Gui L., An X., Chang W. Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature. 428:2004;287-292
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 48
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • The 1.9 Å X-ray structure of a complex formed by two GTPases, the signal recognition particle (SRP) and its receptor (SR), demonstrates a novel mode of substrate twinning. The structure suggests a unique activation mechanism for the SRP family of GTPases.
    • Egea P.F., Shan S.O., Napetschnig J., Savage D.F., Walter P., Stroud R.M. Substrate twinning activates the signal recognition particle and its receptor. Nature. 427:2004;215-221 The 1.9 Å X-ray structure of a complex formed by two GTPases, the signal recognition particle (SRP) and its receptor (SR), demonstrates a novel mode of substrate twinning. The structure suggests a unique activation mechanism for the SRP family of GTPases.
    • (2004) Nature , vol.427 , pp. 215-221
    • Egea, P.F.1    Shan, S.O.2    Napetschnig, J.3    Savage, D.F.4    Walter, P.5    Stroud, R.M.6
  • 49
    • 0028874050 scopus 로고
    • The crystal structure of bluetongue virus VP7
    • Grimes J., Basak A.K., Roy P., Stuart D. The crystal structure of bluetongue virus VP7. Nature. 373:1995;167-170
    • (1995) Nature , vol.373 , pp. 167-170
    • Grimes, J.1    Basak, A.K.2    Roy, P.3    Stuart, D.4
  • 54
    • 0036302354 scopus 로고    scopus 로고
    • Determination of the interface of a large protein complex by transferred cross-saturation measurements
    • Nakanishi T., Miyazawa M., Sakakura M., Terasawa H., Takahashi H., Shimada I. Determination of the interface of a large protein complex by transferred cross-saturation measurements. J Mol Biol. 318:2002;245-249
    • (2002) J Mol Biol , vol.318 , pp. 245-249
    • Nakanishi, T.1    Miyazawa, M.2    Sakakura, M.3    Terasawa, H.4    Takahashi, H.5    Shimada, I.6
  • 55
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg E.R. Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry. 41:2002;1-7
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 58
    • 0141928674 scopus 로고    scopus 로고
    • TROSY in NMR studies of the structure and function of large biological macromolecules
    • Fernandez C., Wider G. TROSY in NMR studies of the structure and function of large biological macromolecules. Curr Opin Struct Biol. 13:2003;570-580
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 570-580
    • Fernandez, C.1    Wider, G.2
  • 60
    • 0036089703 scopus 로고    scopus 로고
    • Single-particle imaging of macromolecules by cryo-electron microscopy
    • Frank J. Single-particle imaging of macromolecules by cryo-electron microscopy. Annu Rev Biophys Biomol Struct. 31:2002;303-319
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 303-319
    • Frank, J.1
  • 61
    • 0033082710 scopus 로고    scopus 로고
    • Electron tomography of molecules and cells
    • Baumeister W., Grimm R., Walz J. Electron tomography of molecules and cells. Trends Cell Biol. 9:1999;81-85
    • (1999) Trends Cell Biol , vol.9 , pp. 81-85
    • Baumeister, W.1    Grimm, R.2    Walz, J.3
  • 62
    • 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
  • 63
    • 0038275890 scopus 로고    scopus 로고
    • Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement
    • Forty-four atomic models built by comparative modeling were fit into the cryo-EM density map of the 70S unit of the E. coli ribosome (11.5 Å resolution) in two different functional states. The work demonstrates that the ribosome changes from a compact structure to a looser one, coupled with the rearrangement of many of the proteins.
    • Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Roey P.V., Agrawal R.K., Harvey S.C., Sali A., et al. Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement. Cell. 113:2003;789-801 Forty-four atomic models built by comparative modeling were fit into the cryo-EM density map of the 70S unit of the E. coli ribosome (11.5 Å resolution) in two different functional states. The work demonstrates that the ribosome changes from a compact structure to a looser one, coupled with the rearrangement of many of the proteins.
    • (2003) Cell , vol.113 , pp. 789-801
    • Gao, H.1    Sengupta, J.2    Valle, M.3    Korostelev, A.4    Eswar, N.5    Stagg, S.M.6    Roey, P.V.7    Agrawal, R.K.8    Harvey, S.C.9    Sali, A.10
  • 64
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M., Becker T., Pool M.R., Spahn C.M., Grassucci R.A., Frank J., Beckmann R. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature. 427:2004;808-814
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 65
    • 0036671095 scopus 로고    scopus 로고
    • Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction
    • Davis J.A., Takagi Y., Kornberg R.D., Asturias F.A. Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction. Mol Cell. 10:2002;409-415
    • (2002) Mol Cell , vol.10 , pp. 409-415
    • Davis, J.A.1    Takagi, Y.2    Kornberg, R.D.3    Asturias, F.A.4
  • 66
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature. 424:2003;643-650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 67
    • 0141843643 scopus 로고    scopus 로고
    • Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • The fitting of atomic models of actin and the myosin cross-bridge into 14 Å cryo-EM maps shows that the closing of the actin-binding cleft upon actin binding is structurally coupled to the opening of the nucleotide-binding pocket.
    • Holmes K.C., Angert I., Kull F.J., Jahn W., Schroder R.R. Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature. 425:2003;423-427 The fitting of atomic models of actin and the myosin cross-bridge into 14 Å cryo-EM maps shows that the closing of the actin-binding cleft upon actin binding is structurally coupled to the opening of the nucleotide-binding pocket.
    • (2003) Nature , vol.425 , pp. 423-427
    • Holmes, K.C.1    Angert, I.2    Kull, F.J.3    Jahn, W.4    Schroder, R.R.5
  • 68
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • Structural analysis of bacteriophage P22 in two different functional states using cryo-EM density at subnanometer resolution shows that a large conformational change of the P22 capsid during maturation transition involves both domain movement of individual subunits and refolding of the capsid protein.
    • Jiang W., Li Z., Zhang Z., Baker M.L., Prevelige P.E. Jr., Chiu W. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Biol. 10:2003;131-135 Structural analysis of bacteriophage P22 in two different functional states using cryo-EM density at subnanometer resolution shows that a large conformational change of the P22 capsid during maturation transition involves both domain movement of individual subunits and refolding of the capsid protein.
    • (2003) Nat Struct Biol , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige Jr., P.E.5    Chiu, W.6
  • 69
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å
    • Zhang X., Walker S.B., Chipman P.R., Nibert M.L., Baker T.S. Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å Nat Struct Biol. 10:2003;1011-1018
    • (2003) Nat Struct Biol , vol.10 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5
  • 70
    • 0242574743 scopus 로고    scopus 로고
    • Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
    • Three-dimensional cryo-EM reconstruction (9.5 Å resolution) reveals secondary structural features of 180 envelope and 180 membrane proteins in the lipid envelope of mature dengue virus. This is one of only a few determinations of the disposition of transmembrane proteins in situ and it shows that the nucleocapsid core and envelope proteins do not directly interact in the mature virus.
    • Zhang W., Chipman P.R., Corver J., Johnson P.R., Zhang Y., Mukhopadhyay S., Baker T.S., Strauss J.H., Rossmann M.G., Kuhn R.J. Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat Struct Biol. 10:2003;907-912 Three-dimensional cryo-EM reconstruction (9.5 Å resolution) reveals secondary structural features of 180 envelope and 180 membrane proteins in the lipid envelope of mature dengue virus. This is one of only a few determinations of the disposition of transmembrane proteins in situ and it shows that the nucleocapsid core and envelope proteins do not directly interact in the mature virus.
    • (2003) Nat Struct Biol , vol.10 , pp. 907-912
    • Zhang, W.1    Chipman, P.R.2    Corver, J.3    Johnson, P.R.4    Zhang, Y.5    Mukhopadhyay, S.6    Baker, T.S.7    Strauss, J.H.8    Rossmann, M.G.9    Kuhn, R.J.10
  • 72
    • 0037438344 scopus 로고    scopus 로고
    • Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: Implications of crowding
    • Grunewald K., Medalia O., Gross A., Steven A.C., Baumeister W. Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: implications of crowding. Biophys Chem. 100:2003;577-591
    • (2003) Biophys Chem , vol.100 , pp. 577-591
    • Grunewald, K.1    Medalia, O.2    Gross, A.3    Steven, A.C.4    Baumeister, W.5
  • 73
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • Medalia O., Weber I., Frangakis A.S., Nicastro D., Gerisch G., Baumeister W. Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science. 298:2002;1209-1213
    • (2002) Science , vol.298 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerisch, G.5    Baumeister, W.6
  • 74
    • 0034687769 scopus 로고    scopus 로고
    • Toward detecting and identifying macromolecules in a cellular context: Template matching applied to electron tomograms
    • Bohm J., Frangakis A.S., Hegerl R., Nickell S., Typke D., Baumeister W. Toward detecting and identifying macromolecules in a cellular context: template matching applied to electron tomograms. Proc Natl Acad Sci USA. 97:2000;14245-14250
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14245-14250
    • Bohm, J.1    Frangakis, A.S.2    Hegerl, R.3    Nickell, S.4    Typke, D.5    Baumeister, W.6
  • 78
    • 0036849482 scopus 로고    scopus 로고
    • Analysis of membrane protein interactions using yeast-based technologies
    • Stagljar I., Fields S. Analysis of membrane protein interactions using yeast-based technologies. Trends Biochem Sci. 27:2002;559-563
    • (2002) Trends Biochem Sci , vol.27 , pp. 559-563
    • Stagljar, I.1    Fields, S.2
  • 79
    • 0037151050 scopus 로고    scopus 로고
    • Regulation of stress response signaling by the N-terminal dishevelled/EGL-10/pleckstrin domain of Sst2, a regulator of G protein signaling in Saccharomyces cerevisiae
    • Burchett S.A., Flanary P., Aston C., Jiang L., Young K.H., Uetz P., Fields S., Dohlman H.G. Regulation of stress response signaling by the N-terminal dishevelled/EGL-10/pleckstrin domain of Sst2, a regulator of G protein signaling in Saccharomyces cerevisiae. J Biol Chem. 277:2002;22156-22167
    • (2002) J Biol Chem , vol.277 , pp. 22156-22167
    • Burchett, S.A.1    Flanary, P.2    Aston, C.3    Jiang, L.4    Young, K.H.5    Uetz, P.6    Fields, S.7    Dohlman, H.G.8
  • 80
    • 0035424708 scopus 로고    scopus 로고
    • Exploring protein interactions by interaction-induced folding of proteins from complementary peptide fragments
    • Michnick S.W. Exploring protein interactions by interaction-induced folding of proteins from complementary peptide fragments. Curr Opin Struct Biol. 11:2001;472-477
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 472-477
    • Michnick, S.W.1
  • 81
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu C.D., Kerppola T.K. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat Biotechnol. 21:2003;539-545
    • (2003) Nat Biotechnol , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 82
    • 0037370399 scopus 로고    scopus 로고
    • The study of macromolecular complexes by quantitative proteomics
    • This paper describes a new generic strategy for determining the specific composition, changes in composition and changes in the abundance of protein complexes using mass spectrometry. Two examples are studied: the identification of genuine components of the RNA polymerase II pre-initiation complex within a high background of co-purifying proteins, and the detailed quantitative changes in the abundance and composition of immunopurified STE12 protein complexes from yeast cells exposed to different environmental conditions.
    • Ranish J.A., Yi E.C., Leslie D.M., Purvine S.O., Goodlett D.R., Eng J., Aebersold R. The study of macromolecular complexes by quantitative proteomics. Nat Genet. 33:2003;349-355 This paper describes a new generic strategy for determining the specific composition, changes in composition and changes in the abundance of protein complexes using mass spectrometry. Two examples are studied: the identification of genuine components of the RNA polymerase II pre-initiation complex within a high background of co-purifying proteins, and the detailed quantitative changes in the abundance and composition of immunopurified STE12 protein complexes from yeast cells exposed to different environmental conditions.
    • (2003) Nat Genet , vol.33 , pp. 349-355
    • Ranish, J.A.1    Yi, E.C.2    Leslie, D.M.3    Purvine, S.O.4    Goodlett, D.R.5    Eng, J.6    Aebersold, R.7
  • 83
    • 1342282907 scopus 로고    scopus 로고
    • Quantitative proteomic identification of six4 as the trex-binding factor in the muscle creatine kinase enhancer
    • Himeda C.L., Ranish J.A., Angello J.C., Maire P., Aebersold R., Hauschka S.D. Quantitative proteomic identification of six4 as the trex-binding factor in the muscle creatine kinase enhancer. Mol Cell Biol. 24:2004;2132-2143
    • (2004) Mol Cell Biol , vol.24 , pp. 2132-2143
    • Himeda, C.L.1    Ranish, J.A.2    Angello, J.C.3    Maire, P.4    Aebersold, R.5    Hauschka, S.D.6
  • 85
    • 19344377539 scopus 로고    scopus 로고
    • Protein interaction networks by proteome peptide scanning
    • A variant of the work described in [84]. Here, candidate peptides in the yeast genome that match the consensus derived from phage display are synthesized and fixed to cellulose membranes, and then probed by SH3 domains. This reveals distinct classes of binding preferences, as well as some overlapping specificities. The strategy can be easily modified to probe the entire proteome.
    • Landgraf C., Panni S., Montecchi-Palazzi L., Castagnoli L., Schneider-Mergener J., Volkmer-Engert R., Cesareni G. Protein interaction networks by proteome peptide scanning. PLoS Biol. 2:2004;E14 A variant of the work described in [84]. Here, candidate peptides in the yeast genome that match the consensus derived from phage display are synthesized and fixed to cellulose membranes, and then probed by SH3 domains. This reveals distinct classes of binding preferences, as well as some overlapping specificities. The strategy can be easily modified to probe the entire proteome.
    • (2004) PLoS Biol , vol.2 , pp. 14
    • Landgraf, C.1    Panni, S.2    Montecchi-Palazzi, L.3    Castagnoli, L.4    Schneider-Mergener, J.5    Volkmer-Engert, R.6    Cesareni, G.7
  • 86
    • 0036899363 scopus 로고    scopus 로고
    • The third dimension for protein interactions and complexes
    • Aloy P., Russell R.B. The third dimension for protein interactions and complexes. Trends Biochem Sci. 27:2002;633-638
    • (2002) Trends Biochem Sci , vol.27 , pp. 633-638
    • Aloy, P.1    Russell, R.B.2
  • 87
    • 0024504877 scopus 로고
    • Receptor and antibody epitopes in human growth hormone identified by homolog-scanning mutagenesis
    • Cunningham B.C., Jhurani P., Ng P., Wells J.A. Receptor and antibody epitopes in human growth hormone identified by homolog-scanning mutagenesis. Science. 243:1989;1330-1336
    • (1989) Science , vol.243 , pp. 1330-1336
    • Cunningham, B.C.1    Jhurani, P.2    Ng, P.3    Wells, J.A.4
  • 88
    • 0037462921 scopus 로고    scopus 로고
    • Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry
    • Lanman J., Lam T.T., Barnes S., Sakalian M., Emmett M.R., Marshall A.G., Prevelige P.E. Jr. Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry. J Mol Biol. 325:2003;759-772
    • (2003) J Mol Biol , vol.325 , pp. 759-772
    • Lanman, J.1    Lam, T.T.2    Barnes, S.3    Sakalian, M.4    Emmett, M.R.5    Marshall, A.G.6    Prevelige Jr., P.E.7
  • 89
    • 0344392715 scopus 로고    scopus 로고
    • Identification of the protein kinase a regulatory RIalpha-catalytic subunit interface by amide H/2H exchange and protein docking
    • The authors identify the interface between the two subunits (catalytic and regulatory) of protein kinase A (PKA) by computational docking and subsequent filtering of the solutions based on amide hydrogen-deuterium exchange interface protection data.
    • Anand G.S., Law D., Mandell J.G., Snead A.N., Tsigelny I., Taylor S.S., Eyck L.F.T., Komives E.A. Identification of the protein kinase A regulatory RIalpha-catalytic subunit interface by amide H/2H exchange and protein docking. Proc Natl Acad Sci USA. 100:2003;13264-13269 The authors identify the interface between the two subunits (catalytic and regulatory) of protein kinase A (PKA) by computational docking and subsequent filtering of the solutions based on amide hydrogen-deuterium exchange interface protection data.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13264-13269
    • Anand, G.S.1    Law, D.2    Mandell, J.G.3    Snead, A.N.4    Tsigelny, I.5    Taylor, S.S.6    Eyck, L.F.T.7    Komives, E.A.8
  • 90
    • 0142072242 scopus 로고    scopus 로고
    • Structural reorganization of proteins revealed by radiolysis and mass spectrometry: G-actin solution structure is divalent cation dependent
    • Guan J.Q., Almo S.C., Reisler E., Chance M.R. Structural reorganization of proteins revealed by radiolysis and mass spectrometry: G-actin solution structure is divalent cation dependent. Biochemistry. 42:2003;11992-12000
    • (2003) Biochemistry , vol.42 , pp. 11992-12000
    • Guan, J.Q.1    Almo, S.C.2    Reisler, E.3    Chance, M.R.4
  • 92
    • 0042349690 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for protein structural modeling
    • Back J.W., de Jong L., Muijsers A.O., de Koster C.G. Chemical cross-linking and mass spectrometry for protein structural modeling. J Mol Biol. 331:2003;303-313
    • (2003) J Mol Biol , vol.331 , pp. 303-313
    • Back, J.W.1    De Jong, L.2    Muijsers, A.O.3    De Koster, C.G.4
  • 93
    • 0242515762 scopus 로고    scopus 로고
    • Characterization of the last subunit of the Arabidopsis COP9 signalosome: Implications for the overall structure and origin of the complex
    • Serino G., Su H., Peng Z., Tsuge T., Wei N., Gu H., Deng X.W. Characterization of the last subunit of the Arabidopsis COP9 signalosome: implications for the overall structure and origin of the complex. Plant Cell. 15:2003;719-731
    • (2003) Plant Cell , vol.15 , pp. 719-731
    • Serino, G.1    Su, H.2    Peng, Z.3    Tsuge, T.4    Wei, N.5    Gu, H.6    Deng, X.W.7
  • 94
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo
    • Truong K., Ikura M. The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Curr Opin Struct Biol. 11:2001;573-578
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 95
    • 0142138241 scopus 로고    scopus 로고
    • Analysis of protein interactions using fluorescence technologies
    • Yan Y., Marriott G. Analysis of protein interactions using fluorescence technologies. Curr Opin Chem Biol. 7:2003;635-640
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 635-640
    • Yan, Y.1    Marriott, G.2
  • 96
    • 0037137216 scopus 로고    scopus 로고
    • A new approach to the study of protein-protein interaction by FTIR: Complex formation between cytochrome P450BM-3 heme domain and FMN reductase domain
    • Kariakin A., Davydov D., Peterson J.A., Jung C. A new approach to the study of protein-protein interaction by FTIR: complex formation between cytochrome P450BM-3 heme domain and FMN reductase domain. Biochemistry. 41:2002;13514-13525
    • (2002) Biochemistry , vol.41 , pp. 13514-13525
    • Kariakin, A.1    Davydov, D.2    Peterson, J.A.3    Jung, C.4
  • 98
    • 0031751233 scopus 로고    scopus 로고
    • A model of the quaternary structure of the Escherichia coli F1 ATPase from X-ray solution scattering and evidence for structural changes in the delta subunit during ATP hydrolysis
    • Svergun D.I., Aldag I., Sieck T., Altendorf K., Koch M.H., Kane D.J., Kozin M.B., Gruber G. A model of the quaternary structure of the Escherichia coli F1 ATPase from X-ray solution scattering and evidence for structural changes in the delta subunit during ATP hydrolysis. Biophys J. 75:1998;2212-2219
    • (1998) Biophys J , vol.75 , pp. 2212-2219
    • Svergun, D.I.1    Aldag, I.2    Sieck, T.3    Altendorf, K.4    Koch, M.H.5    Kane, D.J.6    Kozin, M.B.7    Gruber, G.8
  • 100
    • 0036468385 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions by docking methods
    • Smith G.R., Sternberg M.J. Prediction of protein-protein interactions by docking methods. Curr Opin Struct Biol. 12:2002;28-35
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 28-35
    • Smith, G.R.1    Sternberg, M.J.2
  • 103
    • 0026572775 scopus 로고
    • Molecular surface recognition: Determination of geometric fit between proteins and their ligands by correlation techniques
    • Katchalski-Katzir E., Shariv I., Eisenstein M., Friesem A.A., Aflalo C., Vakser I.A. Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques. Proc Natl Acad Sci USA. 89:1992;2195-2199
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2195-2199
    • Katchalski-Katzir, E.1    Shariv, I.2    Eisenstein, M.3    Friesem, A.A.4    Aflalo, C.5    Vakser, I.A.6
  • 104
    • 0031565730 scopus 로고    scopus 로고
    • Modelling protein docking using shape complementarity, electrostatics and biochemical information
    • Gabb H.A., Jackson R.M., Sternberg M.J. Modelling protein docking using shape complementarity, electrostatics and biochemical information. J Mol Biol. 272:1997;106-120
    • (1997) J Mol Biol , vol.272 , pp. 106-120
    • Gabb, H.A.1    Jackson, R.M.2    Sternberg, M.J.3
  • 106
    • 0032512619 scopus 로고    scopus 로고
    • Rapid refinement of protein interfaces incorporating solvation: Application to the docking problem
    • Jackson R.M., Gabb H.A., Sternberg M.J. Rapid refinement of protein interfaces incorporating solvation: application to the docking problem. J Mol Biol. 276:1998;265-285
    • (1998) J Mol Biol , vol.276 , pp. 265-285
    • Jackson, R.M.1    Gabb, H.A.2    Sternberg, M.J.3
  • 107
    • 0028984540 scopus 로고
    • Protein docking for low-resolution structures
    • Vakser I.A. Protein docking for low-resolution structures. Protein Eng. 8:1995;371-377
    • (1995) Protein Eng , vol.8 , pp. 371-377
    • Vakser, I.A.1
  • 109
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen R., Li L., Weng Z. ZDOCK: an initial-stage protein-docking algorithm. Proteins. 52:2003;80-87
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 110
    • 0034193510 scopus 로고    scopus 로고
    • Protein docking using spherical polar Fourier correlations
    • Ritchie D.W., Kemp G.J. Protein docking using spherical polar Fourier correlations. Proteins. 39:2000;178-194
    • (2000) Proteins , vol.39 , pp. 178-194
    • Ritchie, D.W.1    Kemp, G.J.2
  • 111
    • 0036149480 scopus 로고    scopus 로고
    • Soft protein-protein docking in internal coordinates
    • Fernandez-Recio J., Totrov M., Abagyan R. Soft protein-protein docking in internal coordinates. Protein Sci. 11:2002;280-291
    • (2002) Protein Sci , vol.11 , pp. 280-291
    • Fernandez-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 112
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • Gray J.J., Moughon S., Wang C., Schueler-Furman O., Kuhlman B., Rohl C.A., Baker D. Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. J Mol Biol. 331:2003;281-299
    • (2003) J Mol Biol , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5    Rohl, C.A.6    Baker, D.7
  • 113
    • 0035830963 scopus 로고    scopus 로고
    • Protein-protein association: Investigation of factors influencing association rates by Brownian dynamics simulations
    • Gabdoulline R.R., Wade R.C. Protein-protein association: investigation of factors influencing association rates by Brownian dynamics simulations. J Mol Biol. 306:2001;1139-1155
    • (2001) J Mol Biol , vol.306 , pp. 1139-1155
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 114
    • 0038697837 scopus 로고    scopus 로고
    • Guided docking: First step to locate potential binding sites
    • Fitzjohn P.W., Bates P.A. Guided docking: first step to locate potential binding sites. Proteins. 52:2003;28-32
    • (2003) Proteins , vol.52 , pp. 28-32
    • Fitzjohn, P.W.1    Bates, P.A.2
  • 116
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: Current status of docking methods
    • This paper reviews the results from the first two rounds of the CAPRI community-wide docking experiment, in which 19 groups attempted to predict the structures of seven protein-protein complexes. The targets, as well as the docking methods and protocols used in the predictions, are described. In total, five of the seven target complexes were predicted to an acceptable accuracy.
    • Mendez R., Leplae R., De Maria L., Wodak S.J. Assessment of blind predictions of protein-protein interactions: current status of docking methods. Proteins. 52:2003;51-67 This paper reviews the results from the first two rounds of the CAPRI community-wide docking experiment, in which 19 groups attempted to predict the structures of seven protein-protein complexes. The targets, as well as the docking methods and protocols used in the predictions, are described. In total, five of the seven target complexes were predicted to an acceptable accuracy.
    • (2003) Proteins , vol.52 , pp. 51-67
    • Mendez, R.1    Leplae, R.2    De Maria, L.3    Wodak, S.J.4
  • 117
    • 1242270553 scopus 로고    scopus 로고
    • Protein-protein docking: Is the glass half-full or half-empty?
    • Vajda S., Camacho C.J. Protein-protein docking: is the glass half-full or half-empty? Trends Biotechnol. 22:2004;110-116
    • (2004) Trends Biotechnol , vol.22 , pp. 110-116
    • Vajda, S.1    Camacho, C.J.2
  • 119
    • 0037192836 scopus 로고    scopus 로고
    • Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: Mutational analysis of a malonyl-CoA affinity domain
    • Morillas M., Gomez-Puertas P., Rubi B., Clotet J., Arino J., Valencia A., Hegardt F.G., Serra D., Asins G. Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain. J Biol Chem. 277:2002;11473-11480
    • (2002) J Biol Chem , vol.277 , pp. 11473-11480
    • Morillas, M.1    Gomez-Puertas, P.2    Rubi, B.3    Clotet, J.4    Arino, J.5    Valencia, A.6    Hegardt, F.G.7    Serra, D.8    Asins, G.9
  • 120
    • 0041319073 scopus 로고    scopus 로고
    • Filtering and selection of structural models: Combining docking and NMR
    • The authors demonstrate an approach to protein complex structure determination that first generates structural models by computational docking of the subunits and then filters these using experimental NMR constraints (residual dipolar couplings and chemical shift mapping).
    • Dobrodumov A., Gronenborn A.M. Filtering and selection of structural models: combining docking and NMR. Proteins. 53:2003;18-32 The authors demonstrate an approach to protein complex structure determination that first generates structural models by computational docking of the subunits and then filters these using experimental NMR constraints (residual dipolar couplings and chemical shift mapping).
    • (2003) Proteins , vol.53 , pp. 18-32
    • Dobrodumov, A.1    Gronenborn, A.M.2
  • 121
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C., Boelens R., Bonvin A.M. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J Am Chem Soc. 125:2003;1731-1737
    • (2003) J Am Chem Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 123
    • 0037197902 scopus 로고    scopus 로고
    • Interrogating protein interaction networks through structural biology
    • Aloy P., Russell R.B. Interrogating protein interaction networks through structural biology. Proc Natl Acad Sci USA. 99:2002;5896-5901
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5896-5901
    • Aloy, P.1    Russell, R.B.2
  • 124
    • 12144290243 scopus 로고    scopus 로고
    • Structure-based assembly of protein complexes in yeast
    • Large-scale structural analysis of complexes in yeast using bioinformatics and EM. As complete models as possible were built for over 100 yeast complexes and all complex-complex interactions. For some, EM maps could be used to confirm models or combine separately modeled subcomplexes.
    • Aloy P., Bottcher B., Ceulemans H., Leutwein C., Mellwig C., Fischer S., Gavin A.C., Bork P., Superti-Furga G., Serrano L., et al. Structure-based assembly of protein complexes in yeast. Science. 303:2004;2026-2029 Large-scale structural analysis of complexes in yeast using bioinformatics and EM. As complete models as possible were built for over 100 yeast complexes and all complex-complex interactions. For some, EM maps could be used to confirm models or combine separately modeled subcomplexes.
    • (2004) Science , vol.303 , pp. 2026-2029
    • Aloy, P.1    Bottcher, B.2    Ceulemans, H.3    Leutwein, C.4    Mellwig, C.5    Fischer, S.6    Gavin, A.C.7    Bork, P.8    Superti-Furga, G.9    Serrano, L.10
  • 127
    • 0042386609 scopus 로고    scopus 로고
    • The relationship between sequence and interaction divergence in proteins
    • This study finds that the structural binding modes of proteins are conserved at around 30% sequence identity. Below this cutoff, the binding mode may or may not be similar.
    • Aloy P., Ceulemans H., Stark A., Russell R.B. The relationship between sequence and interaction divergence in proteins. J Mol Biol. 332:2003;989-998 This study finds that the structural binding modes of proteins are conserved at around 30% sequence identity. Below this cutoff, the binding mode may or may not be similar.
    • (2003) J Mol Biol , vol.332 , pp. 989-998
    • Aloy, P.1    Ceulemans, H.2    Stark, A.3    Russell, R.B.4
  • 128
    • 1842577654 scopus 로고    scopus 로고
    • Computational redesign of protein-protein interaction specificity
    • The authors develop a computational strategy to redesign specificity at protein-protein interfaces and apply it to create new specifically interacting DNase-inhibitor protein pairs. In addition to in vitro and in vivo biochemical confirmation of the specificities, a crystal structure of one of the pairs confirms the computationally designed interface structure to an impressive 0.62 Å all-atom rmsd.
    • Kortemme T., Joachimiak L.A., Bullock A.N., Schuler A.D., Stoddard B.L., Baker D. Computational redesign of protein-protein interaction specificity. Nat Struct Mol Biol. 11:2004;371-379 The authors develop a computational strategy to redesign specificity at protein-protein interfaces and apply it to create new specifically interacting DNase-inhibitor protein pairs. In addition to in vitro and in vivo biochemical confirmation of the specificities, a crystal structure of one of the pairs confirms the computationally designed interface structure to an impressive 0.62 Å all-atom rmsd.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 371-379
    • Kortemme, T.1    Joachimiak, L.A.2    Bullock, A.N.3    Schuler, A.D.4    Stoddard, B.L.5    Baker, D.6
  • 130
    • 0037250158 scopus 로고    scopus 로고
    • InterPreTS: Protein interaction prediction through tertiary structure
    • Aloy P., Russell R.B. InterPreTS: protein interaction prediction through tertiary structure. Bioinformatics. 19:2003;161-162
    • (2003) Bioinformatics , vol.19 , pp. 161-162
    • Aloy, P.1    Russell, R.B.2
  • 131
    • 0037110589 scopus 로고    scopus 로고
    • MULTIPROSPECTOR: An algorithm for the prediction of protein-protein interactions by multimeric threading
    • Lu L., Lu H., Skolnick J. MULTIPROSPECTOR: an algorithm for the prediction of protein-protein interactions by multimeric threading. Proteins. 49:2002;350-364
    • (2002) Proteins , vol.49 , pp. 350-364
    • Lu, L.1    Lu, H.2    Skolnick, J.3
  • 132
    • 0038817799 scopus 로고    scopus 로고
    • Multimeric threading-based prediction of protein-protein interactions on a genomic scale: Application to the Saccharomyces cerevisiae proteome
    • The authors predict the protein interaction network in S. cerevisiae by applying their MULTIPROSPECTOR threading algorithm to the entire proteome.
    • Lu L., Arakaki A.K., Lu H., Skolnick J. Multimeric threading-based prediction of protein-protein interactions on a genomic scale: application to the Saccharomyces cerevisiae proteome. Genome Res. 13:2003 June;1146-1154 The authors predict the protein interaction network in S. cerevisiae by applying their MULTIPROSPECTOR threading algorithm to the entire proteome.
    • (2003) Genome Res , vol.13 , pp. 1146-1154
    • Lu, L.1    Arakaki, A.K.2    Lu, H.3    Skolnick, J.4
  • 134
    • 0030842428 scopus 로고    scopus 로고
    • Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes
    • Liou A.K., Willison K.R. Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes. EMBO J. 16:1997;4311-4316
    • (1997) EMBO J , vol.16 , pp. 4311-4316
    • Liou, A.K.1    Willison, K.R.2
  • 135
    • 0036308794 scopus 로고    scopus 로고
    • Protein-protein interactions of hCsl4p with other human exosome subunits
    • Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J. Protein-protein interactions of hCsl4p with other human exosome subunits. J Mol Biol. 315:2002;809-818
    • (2002) J Mol Biol , vol.315 , pp. 809-818
    • Raijmakers, R.1    Noordman, Y.E.2    Van Venrooij, W.J.3    Pruijn, G.J.4
  • 137
    • 0346555269 scopus 로고    scopus 로고
    • Optimization of specificity in a cellular protein interaction network by negative selection
    • Zarrinpar A., Park S.H., Lim W.A. Optimization of specificity in a cellular protein interaction network by negative selection. Nature. 426:2003;676-680
    • (2003) Nature , vol.426 , pp. 676-680
    • Zarrinpar, A.1    Park, S.H.2    Lim, W.A.3
  • 138
    • 0037609791 scopus 로고    scopus 로고
    • Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
    • Ma B., Elkayam T., Wolfson H., Nussinov R. Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces. Proc Natl Acad Sci USA. 100:2003;5772-5777
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5772-5777
    • Ma, B.1    Elkayam, T.2    Wolfson, H.3    Nussinov, R.4
  • 140
    • 0036122073 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites in heterocomplexes with neural networks
    • Fariselli P., Pazos F., Valencia A., Casadio R. Prediction of protein-protein interaction sites in heterocomplexes with neural networks. Eur J Biochem. 269:2002;1356-1361
    • (2002) Eur J Biochem , vol.269 , pp. 1356-1361
    • Fariselli, P.1    Pazos, F.2    Valencia, A.3    Casadio, R.4
  • 141
    • 0037470597 scopus 로고    scopus 로고
    • Automatic methods for predicting functionally important residues
    • del Sol Mesa A., Pazos F., Valencia A. Automatic methods for predicting functionally important residues. J Mol Biol. 326:2003;1289-1302
    • (2003) J Mol Biol , vol.326 , pp. 1289-1302
    • Del Sol Mesa, A.1    Pazos, F.2    Valencia, A.3
  • 142
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O., Bourne H.R., Cohen F.E. An evolutionary trace method defines binding surfaces common to protein families. J Mol Biol. 257:1996;342-358
    • (1996) J Mol Biol , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 143
    • 0034644783 scopus 로고    scopus 로고
    • Analysis and prediction of functional sub-types from protein sequence alignments
    • Hannenhalli S.S., Russell R.B. Analysis and prediction of functional sub-types from protein sequence alignments. J Mol Biol. 303:2000;61-76
    • (2000) J Mol Biol , vol.303 , pp. 61-76
    • Hannenhalli, S.S.1    Russell, R.B.2
  • 144
    • 0035838976 scopus 로고    scopus 로고
    • Automated structure-based prediction of functional sites in proteins: Applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking
    • Aloy P., Querol E., Aviles F.X., Sternberg M.J.E. Automated structure-based prediction of functional sites in proteins: applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking. J Mol Biol. 311:2001;395-408
    • (2001) J Mol Biol , vol.311 , pp. 395-408
    • Aloy, P.1    Querol, E.2    Aviles, F.X.3    Sternberg, M.J.E.4
  • 145
    • 0035853280 scopus 로고    scopus 로고
    • Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins
    • Landgraf R., Xenarios I., Eisenberg D. Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins. J Mol Biol. 307:2001;1487-1502
    • (2001) J Mol Biol , vol.307 , pp. 1487-1502
    • Landgraf, R.1    Xenarios, I.2    Eisenberg, D.3
  • 146
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • Kortemme T., Baker D. A simple physical model for binding energy hot spots in protein-protein complexes. Proc Natl Acad Sci USA. 99:2002;14116-14121
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 147
    • 0141527338 scopus 로고    scopus 로고
    • Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130
    • Boulanger M.J., Bankovich A.J., Kortemme T., Baker D., Garcia K.C. Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130. Mol Cell. 12:2003;577-589
    • (2003) Mol Cell , vol.12 , pp. 577-589
    • Boulanger, M.J.1    Bankovich, A.J.2    Kortemme, T.3    Baker, D.4    Garcia, K.C.5
  • 148
    • 0346160934 scopus 로고    scopus 로고
    • Symmetry recognizing asymmetry: Analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands
    • McFarland B.J., Kortemme T., Yu S.F., Baker D., Strong R.K. Symmetry recognizing asymmetry: analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands. Structure. 11:2003;411-422
    • (2003) Structure , vol.11 , pp. 411-422
    • McFarland, B.J.1    Kortemme, T.2    Yu, S.F.3    Baker, D.4    Strong, R.K.5
  • 150
    • 0033776245 scopus 로고    scopus 로고
    • Docking structures of domains into maps from cryo-electron microscopy using local correlation
    • Roseman A.M. Docking structures of domains into maps from cryo-electron microscopy using local correlation. Acta Crystallogr D Biol Crystallogr. 56:2000;1332-1340
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 1332-1340
    • Roseman, A.M.1
  • 151
    • 0035783173 scopus 로고    scopus 로고
    • Using situs for flexible and rigid-body fitting of multiresolution single-molecule data
    • Wriggers W., Birmanns S. Using situs for flexible and rigid-body fitting of multiresolution single-molecule data. J Struct Biol. 133:2001;193-202
    • (2001) J Struct Biol , vol.133 , pp. 193-202
    • Wriggers, W.1    Birmanns, S.2
  • 152
    • 1942521664 scopus 로고    scopus 로고
    • Fast fitting of atomic structures to lower resolution electron density maps by surface overlap maximization
    • Ceulemans H., Russell R.B. Fast fitting of atomic structures to lower resolution electron density maps by surface overlap maximization. J Mol Biol. 338:2004;783-793
    • (2004) J Mol Biol , vol.338 , pp. 783-793
    • Ceulemans, H.1    Russell, R.B.2
  • 153
    • 0032779888 scopus 로고    scopus 로고
    • Quantitative fitting of atomic models into observed densities derived by electron microscopy
    • Volkmann N., Hanein D. Quantitative fitting of atomic models into observed densities derived by electron microscopy. J Struct Biol. 125:1999;176-184
    • (1999) J Struct Biol , vol.125 , pp. 176-184
    • Volkmann, N.1    Hanein, D.2
  • 154
    • 0035783056 scopus 로고    scopus 로고
    • Combining electron microscopic with x-ray crystallographic structures
    • Rossmann M.G., Bernal R., Pletnev S.V. Combining electron microscopic with x-ray crystallographic structures. J Struct Biol. 136:2001;190-200
    • (2001) J Struct Biol , vol.136 , pp. 190-200
    • Rossmann, M.G.1    Bernal, R.2    Pletnev, S.V.3
  • 155
    • 0036535896 scopus 로고    scopus 로고
    • Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches
    • Chiu W., Baker M.L., Jiang W., Zhou Z.H. Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches. Curr Opin Struct Biol. 12:2002;263-269
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 263-269
    • Chiu, W.1    Baker, M.L.2    Jiang, W.3    Zhou, Z.H.4
  • 156
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacon P., Wriggers W. Multi-resolution contour-based fitting of macromolecular structures. J Mol Biol. 317:2002;375-384
    • (2002) J Mol Biol , vol.317 , pp. 375-384
    • Chacon, P.1    Wriggers, W.2
  • 158
    • 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
  • 159
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann R., Spahn C.M., Eswar N., Helmers J., Penczek P.A., Sali A., Frank J., Blobel G. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell. 107:2001;361-372
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1    Spahn, C.M.2    Eswar, N.3    Helmers, J.4    Penczek, P.A.5    Sali, A.6    Frank, J.7    Blobel, G.8
  • 160
    • 0041819526 scopus 로고    scopus 로고
    • Three-dimensional structure of bacteriophage T4 baseplate
    • Three-dimensional cryo-EM reconstruction of the baseplate-tail tube complex of bacteriophage T4 at 12 Å resolution. The X-ray structures of six proteins were fitted into the electron density and the location of four others was determined with the help of biochemical data. The overall structure suggests a mechanism of baseplate triggering and structural transition during the initial stages of T4 infection.
    • Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S., van Raaij M.J., Arisaka F., Mesyanzhinov V.V., Rossmann M.G. Three-dimensional structure of bacteriophage T4 baseplate. Nat Struct Biol. 10:2003;688-693 Three-dimensional cryo-EM reconstruction of the baseplate-tail tube complex of bacteriophage T4 at 12 Å resolution. The X-ray structures of six proteins were fitted into the electron density and the location of four others was determined with the help of biochemical data. The overall structure suggests a mechanism of baseplate triggering and structural transition during the initial stages of T4 infection.
    • (2003) Nat Struct Biol , vol.10 , pp. 688-693
    • Kostyuchenko, V.A.1    Leiman, P.G.2    Chipman, P.R.3    Kanamaru, S.4    Van Raaij, M.J.5    Arisaka, F.6    Mesyanzhinov, V.V.7    Rossmann, M.G.8
  • 161
    • 0038670209 scopus 로고    scopus 로고
    • Molecular architecture of the multiprotein splicing factor SF3b
    • Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H. Molecular architecture of the multiprotein splicing factor SF3b. Science. 300:2003;980-984
    • (2003) Science , vol.300 , pp. 980-984
    • Golas, M.M.1    Sander, B.2    Will, C.L.3    Luhrmann, R.4    Stark, H.5
  • 162
    • 0042738069 scopus 로고    scopus 로고
    • Full-length archaeal Rad51 structure and mutants: Mechanisms for RAD51 assembly and control by BRCA2
    • The crystal structure of full-length RAD51 (2.85 Å resolution), in combination with SAXS, cryo-EM and mutagenesis, was used to characterize a macromolecular machine with a central role in repairing DNA double-strand breaks by homologous recombination. The study suggests how BRC repeats may disrupt RAD51 ring assembly and direct RAD51 to form fibers in response to cellular DNA damage.
    • Shin D.S., Pellegrini L., Daniels D.S., Yelent B., Craig L., Bates D., Yu D.S., Shivji M.K., Hitomi C., Arvai A.S., et al. Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2. EMBO J. 22:2003;4566-4576 The crystal structure of full-length RAD51 (2.85 Å resolution), in combination with SAXS, cryo-EM and mutagenesis, was used to characterize a macromolecular machine with a central role in repairing DNA double-strand breaks by homologous recombination. The study suggests how BRC repeats may disrupt RAD51 ring assembly and direct RAD51 to form fibers in response to cellular DNA damage.
    • (2003) EMBO J , vol.22 , pp. 4566-4576
    • Shin, D.S.1    Pellegrini, L.2    Daniels, D.S.3    Yelent, B.4    Craig, L.5    Bates, D.6    Yu, D.S.7    Shivji, M.K.8    Hitomi, C.9    Arvai, A.S.10
  • 164
    • 0041347832 scopus 로고    scopus 로고
    • Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics
    • Baker M.L., Jiang W., Bowman B.R., Zhou Z.H., Quiocho F.A., Rixon F.J., Chiu W. Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics. J Mol Biol. 331:2003;447-456
    • (2003) J Mol Biol , vol.331 , pp. 447-456
    • Baker, M.L.1    Jiang, W.2    Bowman, B.R.3    Zhou, Z.H.4    Quiocho, F.A.5    Rixon, F.J.6    Chiu, W.7
  • 165
    • 0023305986 scopus 로고
    • Knowledge-based prediction of protein structures and the design of novel molecules
    • Blundell T.L., Sibanda B.L., Sternberg M.J., Thornton J.M. Knowledge-based prediction of protein structures and the design of novel molecules. Nature. 326:1987;347-352
    • (1987) Nature , vol.326 , pp. 347-352
    • Blundell, T.L.1    Sibanda, B.L.2    Sternberg, M.J.3    Thornton, J.M.4
  • 166
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine proteases
    • Greer J. Comparative modeling methods: application to the family of the mammalian serine proteases. Proteins. 7:1990;317-334
    • (1990) Proteins , vol.7 , pp. 317-334
    • Greer, J.1
  • 167
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol. 234:1993;779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 168
    • 0034565516 scopus 로고    scopus 로고
    • Genomic fold assignment and rational modeling of proteins of biological interest
    • Sauder J.M., Dunbrack R.L. Jr. Genomic fold assignment and rational modeling of proteins of biological interest. Proc Int Conf Intell Syst Mol Biol. 8:2000;296-306
    • (2000) Proc Int Conf Intell Syst Mol Biol , vol.8 , pp. 296-306
    • Sauder, J.M.1    Dunbrack Jr., R.L.2
  • 171
    • 0035812694 scopus 로고    scopus 로고
    • Protein structure prediction and structural genomics
    • Baker D., Sali A. Protein structure prediction and structural genomics. Science. 294:2001;93-96
    • (2001) Science , vol.294 , pp. 93-96
    • Baker, D.1    Sali, A.2
  • 172
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • Apic G., Gough J., Teichmann S.A. Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J Mol Biol. 310:2001;311-325
    • (2001) J Mol Biol , vol.310 , pp. 311-325
    • Apic, G.1    Gough, J.2    Teichmann, S.A.3
  • 173
    • 0041333147 scopus 로고    scopus 로고
    • NIH workshop on structural proteomics of biological complexes
    • Sali A. NIH workshop on structural proteomics of biological complexes. Structure. 11:2003;1043-1047
    • (2003) Structure , vol.11 , pp. 1043-1047
    • Sali, A.1
  • 174
    • 0025236617 scopus 로고
    • Prediction of the three-dimensional structure of Escherichia coli 30S ribosomal subunit: A molecular mechanics approach
    • Malhotra A., Tan R.K., Harvey S.C. Prediction of the three-dimensional structure of Escherichia coli 30S ribosomal subunit: a molecular mechanics approach. Proc Natl Acad Sci USA. 87:1990;1950-1954
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1950-1954
    • Malhotra, A.1    Tan, R.K.2    Harvey, S.C.3
  • 178
    • 0035996975 scopus 로고    scopus 로고
    • Relating molecular flexibility to function: A case study of tubulin
    • Keskin O., Durell S.R., Bahar I., Jernigan R.L., Covell D.G. Relating molecular flexibility to function: a case study of tubulin. Biophys J. 83:2002;663-680
    • (2002) Biophys J , vol.83 , pp. 663-680
    • Keskin, O.1    Durell, S.R.2    Bahar, I.3    Jernigan, R.L.4    Covell, D.G.5
  • 179
    • 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
  • 180
    • 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 C.L. III 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 III, C.L.3
  • 181
    • 0037436340 scopus 로고    scopus 로고
    • Mega-Dalton biomolecular motion captured from electron microscopy reconstructions
    • Chacon 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
    • Chacon, P.1    Tama, F.2    Wriggers, W.3
  • 182
    • 0037666985 scopus 로고    scopus 로고
    • Conformational flexibility of pyruvate dehydrogenase complexes: A computational analysis by quantized elastic deformational model
    • Kong Y., Ming D., Wu Y., Stoops J.K., Zhou Z.H., Ma J. Conformational flexibility of pyruvate dehydrogenase complexes: a computational analysis by quantized elastic deformational model. J Mol Biol. 330:2003;129-135
    • (2003) J Mol Biol , vol.330 , pp. 129-135
    • Kong, Y.1    Ming, D.2    Wu, Y.3    Stoops, J.K.4    Zhou, Z.H.5    Ma, J.6
  • 183
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons M.F., Jones G.H., Luisi B.F. A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure Fold Des. 8:2000;1215-1226
    • (2000) Structure Fold des , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 185
    • 0034747267 scopus 로고    scopus 로고
    • Electron cryo-microscopy and image reconstruction of adeno-associated virus type 2 empty capsids
    • Kronenberg S., Kleinschmidt J.A., Bottcher B. Electron cryo-microscopy and image reconstruction of adeno-associated virus type 2 empty capsids. EMBO Rep. 2:2001;997-1002
    • (2001) EMBO Rep , vol.2 , pp. 997-1002
    • Kronenberg, S.1    Kleinschmidt, J.A.2    Bottcher, B.3
  • 186
    • 0036469130 scopus 로고    scopus 로고
    • Two-hybrid arrays
    • Uetz P. Two-hybrid arrays. Curr Opin Chem Biol. 6:2002;57-62
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 57-62
    • Uetz, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.