메뉴 건너뛰기




Volumn 13, Issue 3, 2003, Pages 383-388

Genome-wide studies of protein-protein interaction

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTIC METHOD; CELLULAR DISTRIBUTION; EVALUATION; EXPERIMENT; FUNCTIONAL ASSESSMENT; GENE SEQUENCE; GENOME; GENOMICS; MASS SPECTROMETRY; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN TARGETING; RELIABILITY; REVIEW; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; SIMULATION; STOICHIOMETRY; STRUCTURE ANALYSIS; TWO HYBRID SYSTEM; YEAST;

EID: 0038169958     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(03)00064-2     Document Type: Review
Times cited : (37)

References (36)
  • 1
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 340:1989;245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 2
    • 0033621537 scopus 로고    scopus 로고
    • Mass spectrometry. From genomics to proteomics
    • Yates JR III: Mass spectrometry. From genomics to proteomics. Trends Genet 2000, 16:5-8.
    • (2000) Trends Genet , vol.16 , pp. 5-8
    • Yates J.R. III1
  • 4
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Séraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol. 17:1999;1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6
  • 5
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • A high-throughput study of protein interaction in yeast relying on immunoprecipitation and mass spectrometry.
    • Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., Millar A., Taylor P., Bennett K., Boutilier K.et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature. 415:2002;180-183 A high-throughput study of protein interaction in yeast relying on immunoprecipitation and mass spectrometry.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5    Adams, S.L.6    Millar, A.7    Taylor, P.8    Bennett, K.9    Boutilier, K.10
  • 6
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • A high-quality analysis of hundreds of protein complexes in yeast using the TAP method and mass spectrometry, providing, for the first time, an overview of protein association in a eukaryotic cell. Results also demonstrate the conservation of protein complexes from yeast to human.
    • Gavin A.C., Bosche M., Krause R., Grandi P., Marzioch M., Bauer A., Schultz J., Rick J.M., Michon A.M., Cruciat C.M.et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature. 415:2002;141-147 A high-quality analysis of hundreds of protein complexes in yeast using the TAP method and mass spectrometry, providing, for the first time, an overview of protein association in a eukaryotic cell. Results also demonstrate the conservation of protein complexes from yeast to human.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5    Bauer, A.6    Schultz, J.7    Rick, J.M.8    Michon, A.M.9    Cruciat, C.M.10
  • 7
    • 0023057604 scopus 로고
    • Most of the yeast genomic sequences are not essential for cell growth and division
    • Goebl M.G., Petes T.D. Most of the yeast genomic sequences are not essential for cell growth and division. Cell. 46:1986;983-992.
    • (1986) Cell , vol.46 , pp. 983-992
    • Goebl, M.G.1    Petes, T.D.2
  • 8
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • This manuscript describes an efficient and original method for complex purification that is particularly well adapted to proteomic studies.
    • Puig O., Caspary F., Rigaut G., Rutz B., Bouveret E., Bragado-Nilsson E., Wilm M., Séraphin B. The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods. 24:2001;218-229 This manuscript describes an efficient and original method for complex purification that is particularly well adapted to proteomic studies.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Séraphin, B.8
  • 9
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR III: Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates J.R. III3
  • 14
    • 0035898660 scopus 로고    scopus 로고
    • The exosome of Trypanosoma brucei
    • Estevez A.M., Kempf T., Clayton C. The exosome of Trypanosoma brucei. EMBO J. 20:2001;3831-3839.
    • (2001) EMBO J , vol.20 , pp. 3831-3839
    • Estevez, A.M.1    Kempf, T.2    Clayton, C.3
  • 15
    • 0036468385 scopus 로고    scopus 로고
    • Prediction of protein interactions by docking methods
    • Smith G.R., Sternberg M.J.E. Prediction of 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.E.2
  • 16
    • 0036468396 scopus 로고    scopus 로고
    • Protein-protein association kinetics and protein docking
    • Camacho C.J., Vajda S. Protein-protein association kinetics and protein docking. Curr Opin Struct Biol. 12:2002;36-40.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 36-40
    • Camacho, C.J.1    Vajda, S.2
  • 17
    • 0036601150 scopus 로고    scopus 로고
    • Computational methods for the prediction of protein interactions
    • Valencia A., Pazos F. Computational methods for the prediction of protein interactions. Curr Opin Struct Biol. 12:2002;368-373.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 368-373
    • Valencia, A.1    Pazos, F.2
  • 18
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • Wodak S.J., Janin J. Structural basis of macromolecular recognition. Adv Protein Chem. 61:2002;9-73.
    • (2002) Adv Protein Chem , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 19
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • Halperin I., Ma B., Wolfson H., Nussinov R. Principles of docking: an overview of search algorithms and a guide to scoring functions. Proteins. 47:2002;409-443.
    • (2002) Proteins , vol.47 , pp. 409-443
    • Halperin, I.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 20
    • 0036568319 scopus 로고    scopus 로고
    • In silico two-hybrid system for the selection of physically interacting protein pairs
    • Pazos F., Valencia A. In silico two-hybrid system for the selection of physically interacting protein pairs. Proteins. 47:2002;219-227.
    • (2002) Proteins , vol.47 , pp. 219-227
    • Pazos, F.1    Valencia, A.2
  • 21
    • 0038187616 scopus 로고    scopus 로고
    • Weighted geometric docking: Incorporating external information in the rotation-translation scan
    • in press
    • Ben-Zeev E, Eisenstein M: Weighted geometric docking: Incorporating external information in the rotation-translation scan. Proteins 2003, (suppl 1):in press.
    • (2003) Proteins , Issue.SUPPL. 1
    • Ben-Zeev, E.1    Eisenstein, M.2
  • 22
    • 0036149480 scopus 로고    scopus 로고
    • Soft protein-protein docking in internal coordinates
    • Fernando-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
    • Fernando-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 23
    • 0037093643 scopus 로고    scopus 로고
    • Docking unbound proteins using shape complementarity, desolvation, and electrostatics
    • Chen R., Weng Z. Docking unbound proteins using shape complementarity, desolvation, and electrostatics. Proteins. 47:2002;281-294.
    • (2002) Proteins , vol.47 , pp. 281-294
    • Chen, R.1    Weng, Z.2
  • 26
    • 0037093640 scopus 로고    scopus 로고
    • Welcome to CAPRI: A critical assessment of predicted interactions
    • Janin J. Welcome to CAPRI: a critical assessment of predicted interactions. Proteins. 47:2002;257.
    • (2002) Proteins , vol.47 , pp. 257
    • Janin, J.1
  • 28
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: Current status of docking methods
    • in press
    • Mendez R, Leplae R, de Maria L, Wodak SJ: Assessment of blind predictions of protein-protein interactions: current status of docking methods. Proteins 2003, (suppl 1):in press.
    • (2003) Proteins , Issue.SUPPL. 1
    • Mendez, R.1    Leplae, R.2    De Maria, L.3    Wodak, S.J.4
  • 30
    • 0031307203 scopus 로고    scopus 로고
    • Evaluation of the CASP2 docking section
    • Dixon JS: Evaluation of the CASP2 docking section. Proteins 1997, (suppl 2):198-204.
    • (1997) Proteins , Issue.SUPPL. 2 , pp. 198-204
    • Dixon, J.S.1
  • 31
    • 0037189507 scopus 로고    scopus 로고
    • Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology
    • The X-ray structures of three VHH domains of a single-chain antibody bound to different epitopes on the same antigen show remarkable differences in the VHH domains and the way they recognize their epitope.
    • Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C. Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology. J Biol Chem. 277:2002;23645-23650 The X-ray structures of three VHH domains of a single-chain antibody bound to different epitopes on the same antigen show remarkable differences in the VHH domains and the way they recognize their epitope.
    • (2002) J Biol Chem , vol.277 , pp. 23645-23650
    • Desmyter, A.1    Spinelli, S.2    Payan, F.3    Lauwereys, M.4    Wyns, L.5    Muyldermans, S.6    Cambillau, C.7
  • 32
    • 0036063659 scopus 로고    scopus 로고
    • An antibody that prevents the hemagglutinin low pH transition
    • The X-ray structure of the flu virus hemagglutinin trimer in complex with a monoclonal antibody. The antibody binds at the top of the trimer, bridging two subunits and preventing their dissociation, which is a necessary step in the low pH transition of the hemagglutinin.
    • Barbey-Martin C., Gigant B., Bizebard T., Calder L.J., Wharton S.A., Skehel J.J., Knossow M. An antibody that prevents the hemagglutinin low pH transition. Virology. 294:2002;70-74 The X-ray structure of the flu virus hemagglutinin trimer in complex with a monoclonal antibody. The antibody binds at the top of the trimer, bridging two subunits and preventing their dissociation, which is a necessary step in the low pH transition of the hemagglutinin.
    • (2002) Virology , vol.294 , pp. 70-74
    • Barbey-Martin, C.1    Gigant, B.2    Bizebard, T.3    Calder, L.J.4    Wharton, S.A.5    Skehel, J.J.6    Knossow, M.7
  • 34
    • 0036091233 scopus 로고    scopus 로고
    • Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes
    • The two superantigen toxins from Streptococcus, SpeA and SpeC, are closely related, but they bind the TCR in different ways.
    • Sundberg E.J., Li H., Llera A.S., McCormick J.K., Tormo J., Schlievert P.M., Karjalainen K., Mariuzza R.A. Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes. Structure. 10:2002;687-699 The two superantigen toxins from Streptococcus, SpeA and SpeC, are closely related, but they bind the TCR in different ways.
    • (2002) Structure , vol.10 , pp. 687-699
    • Sundberg, E.J.1    Li, H.2    Llera, A.S.3    McCormick, J.K.4    Tormo, J.5    Schlievert, P.M.6    Karjalainen, K.7    Mariuzza, R.A.8
  • 35
    • 0037108941 scopus 로고    scopus 로고
    • X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr
    • The first X-ray structures of a complex of a serine protein kinase with its protein substrate. The target serine is either free or phosphorylated in the crystal.
    • Fieulaine S., Morera S., Poncet S., Mijakovic I., Galinier A., Janin J., Deutscher J., Nessler S. X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr. Proc Natl Acad Sci USA. 99:2002;13437-13441 The first X-ray structures of a complex of a serine protein kinase with its protein substrate. The target serine is either free or phosphorylated in the crystal.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13437-13441
    • Fieulaine, S.1    Morera, S.2    Poncet, S.3    Mijakovic, I.4    Galinier, A.5    Janin, J.6    Deutscher, J.7    Nessler, S.8
  • 36
    • 0037108947 scopus 로고    scopus 로고
    • Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: A relic of early life?
    • •], the authors show that HPr kinase can dephosphorylate Ser46 of its HPr substrate, and that the reaction is phosphorolysis rather than hydrolysis, as previously assumed: the kinase doubles up as a phosphorylase.
    • •], the authors show that HPr kinase can dephosphorylate Ser46 of its HPr substrate, and that the reaction is phosphorolysis rather than hydrolysis, as previously assumed: the kinase doubles up as a phosphorylase.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13442-13447
    • Mijakovic, I.1    Poncet, S.2    Galinier, A.3    Monedero, V.4    Fieulaine, S.5    Janin, J.6    Nessler, S.7    Marquez, J.A.8    Scheffzek, K.9    Hasenbein, S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.