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Volumn 12, Issue 5, 2013, Pages 1451-1467

Protein interactions, post-translational modifications and topologies in human cells

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOL RECEPTOR; HISTONE; NUCLEAR PROTEIN;

EID: 84877623973     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.024497     Document Type: Article
Times cited : (93)

References (68)
  • 1
    • 0014505028 scopus 로고
    • Fixatives and fixation: A review
    • Hopwood, D. (1969) Fixatives and fixation: a review. Histochem. J. 1, 323-360
    • (1969) Histochem. J. , vol.1 , pp. 323-360
    • Hopwood, D.1
  • 3
    • 8644282069 scopus 로고    scopus 로고
    • Chemical cross-linking and protein-protein interactions - A review with illustrative protocols
    • DOI 10.1016/j.bioorg.2004.08.002, PII S0045206804000641
    • Kluger, R., and Alagic, A. (2004) Chemical cross-linking and protein-protein interactions-a review with illustrative protocols. Bioorg. Chem. 32, 451-472 (Pubitemid 39504941)
    • (2004) Bioorganic Chemistry , vol.32 , Issue.6 , pp. 451-472
    • Kluger, R.1    Alagic, A.2
  • 4
    • 0042417261 scopus 로고
    • The reaction of bovine serum albumin with the bifunctional reagent p,p′-difluoro-m,m′-dinitro-diphenyl-sulfone
    • Wold, F. (1961) The reaction of bovine serum albumin with the bifunctional reagent p,p′-difluoro-m,m′-dinitro-diphenyl-sulfone. J. Biol. Chem. 236, 106-111
    • (1961) J. Biol. Chem. , vol.236 , pp. 106-111
    • Wold, F.1
  • 7
    • 0042349690 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for protein structural modeling
    • DOI 10.1016/S0022-2836(03)00721-6
    • Back, J. W., de Jong, L., Muijsers, A. O., and de Koster, C. G. (2003) Chemical cross-linking and mass spectrometry for protein structural modeling. J. Mol. Biol. 331, 303-313 (Pubitemid 36904016)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.2 , pp. 303-313
    • Back, J.W.1    De Jong, L.2    Muijsers, A.O.3    De Koster, C.G.4
  • 9
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • DOI 10.1038/340245a0
    • Fields, S., and Song, O. (1989) A novel genetic system to detect protein-protein interactions. Nature 340, 245-246 (Pubitemid 19171591)
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.-K.2
  • 10
    • 0037294003 scopus 로고    scopus 로고
    • Affinity purification-mass spectrometry: Powerful tools for the characterization of protein complexes
    • DOI 10.1046/j.1432-1033.2003.03428.x
    • Bauer, A., and Kuster, B. (2003) Affinity purification-mass spectrometry. Powerful tools for the characterization of protein complexes. Eur. J. Biochem. FEBS 270, 570-578 (Pubitemid 36286570)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.4 , pp. 570-578
    • Bauer, A.1    Kuster, B.2
  • 12
    • 79961213851 scopus 로고    scopus 로고
    • Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry
    • Lauber, M. A., and Reilly, J. P. (2011) Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry. J. Prtteome Res. 10, 3604-3616
    • (2011) J. Prtteome Res. , vol.10 , pp. 3604-3616
    • Lauber, M.A.1    Reilly, J.P.2
  • 13
    • 84860602175 scopus 로고    scopus 로고
    • Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions
    • Chavez, J. D., Cilia, M., Weisbrod, C. R., Ju, H. J., Eng, J. K., Gray, S. M., and Bruce, J. E. (2012) Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions. .J. Proteome Res. 11, 2968-2981
    • (2012) J. Proteome Res. , vol.11 , pp. 2968-2981
    • Chavez, J.D.1    Cilia, M.2    Weisbrod, C.R.3    Ju, H.J.4    Eng, J.K.5    Gray, S.M.6    Bruce, J.E.7
  • 19
    • 84875913034 scopus 로고    scopus 로고
    • In vivo protein interaction network identified with novel chemical cross-linking technology
    • Available at: 10.1021/pr3011638
    • Weisbrod, C. R., Chavez, J. D., Eng, J. K., Yang, L., Zheng, C., and Bruce, J. E. (2012) In vivo protein interaction network identified with novel chemical cross-linking technology. J. Proteome Res. Available at: 10.1021/pr3011638
    • (2012) J. Proteome Res.
    • Weisbrod, C.R.1    Chavez, J.D.2    Eng, J.K.3    Yang, L.4    Zheng, C.5    Bruce, J.E.6
  • 20
    • 84875955676 scopus 로고    scopus 로고
    • CrossLink-DB: Database and software tools for storing and visualizing protein interaction topology data
    • Available at: 10.1021/pr301162j
    • Zheng, C., Weisbrod, C. R., Chavez, J. D., Eng, J. K., Sharma, V., Wu, X., and Bruce, J. E. (2012) CrossLink-DB: database and software tools for storing and visualizing protein interaction topology data. J. Proteome Res. Available at: 10.1021/pr301162j
    • (2012) J. Proteome Res.
    • Zheng, C.1    Weisbrod, C.R.2    Chavez, J.D.3    Eng, J.K.4    Sharma, V.5    Wu, X.6    Bruce, J.E.7
  • 21
    • 84862687131 scopus 로고    scopus 로고
    • In vivo protein complex topologies: Sights through a cross-linking lens
    • Bruce, J. E. (2012) In vivo protein complex topologies: sights through a cross-linking lens. Proteomics 12, 1565-1575
    • (2012) Proteomics , vol.12 , pp. 1565-1575
    • Bruce, J.E.1
  • 22
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human disease
    • Vidal, M., Cusick, M. E., and Barabasi, A. L. Interactome networks and human disease. Cell 144, 986-998
    • Cell , vol.144 , pp. 986-998
    • Vidal, M.1    Cusick, M.E.2    Barabasi, A.L.3
  • 23
    • 75749140161 scopus 로고    scopus 로고
    • Reactivity and applications of new amine reactive cross-linkers for mass spectrometric detection of protein-protein complexes
    • Bich, C., Maedler, S., Chiesa, K., DeGiacomo, F., Bogliotti, N., and Zenobi, R. (2010) Reactivity and applications of new amine reactive cross-linkers for mass spectrometric detection of protein-protein complexes. Anal. Chem. 82, 172-179
    • (2010) Anal. Chem. , vol.82 , pp. 172-179
    • Bich, C.1    Maedler, S.2    Chiesa, K.3    DeGiacomo, F.4    Bogliotti, N.5    Zenobi, R.6
  • 24
    • 34948860098 scopus 로고    scopus 로고
    • Informatics strategies for large-scale novel cross-linking analysis
    • DOI 10.1021/pr070035z
    • Anderson, G. A., Tolic, N., Tang, X., Zheng, C., and Bruce, J. E. (2007) Informatics strategies for large-scale novel cross-linking analysis. J. Proteome Res. 6, 3412-3421 (Pubitemid 47522731)
    • (2007) Journal of Proteome Research , vol.6 , Issue.9 , pp. 3412-3421
    • Anderson, G.A.1    Tolic, N.2    Tang, X.3    Zheng, C.4    Bruce, J.E.5
  • 26
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L. A., and Sternberg, M. J. (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protocols 4, 363-371
    • (2009) Nat. Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 27
    • 21644476468 scopus 로고    scopus 로고
    • PatchDock and SymmDock: Servers for rigid and symmetric docking
    • DOI 10.1093/nar/gki481
    • Schneidman-Duhovny, D., Inbar, Y., Nussinov, R., and Wolfson, H. J. (2005) PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res. 33, W363-367 (Pubitemid 44529944)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Schneidman-Duhovny, D.1    Inbar, Y.2    Nussinov, R.3    Wolfson, H.J.4
  • 28
    • 33847345976 scopus 로고    scopus 로고
    • Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes
    • DOI 10.1021/pr060480e
    • Tang, X., Yi, W., Munske, G. R., Adhikari, D. P., Zakharova, N. L., and Bruce, J. E. (2007) Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes. J. Proteome Res. 6, 724-734 (Pubitemid 46340175)
    • (2007) Journal of Proteome Research , vol.6 , Issue.2 , pp. 724-734
    • Tang, X.1    Yi, W.2    Munske, G.R.3    Adhikari, D.P.4    Zakharova, N.L.5    Bruce, J.E.6
  • 29
    • 63049119068 scopus 로고    scopus 로고
    • Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry
    • Zhang, H., Tang, X., Munske, G. R., Tolic, N., Anderson, G. A., and Bruce, J. E. (2009) Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry. Mol. Cell. Proteomics 8, 409-420
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 409-420
    • Zhang, H.1    Tang, X.2    Munske, G.R.3    Tolic, N.4    Anderson, G.A.5    Bruce, J.E.6
  • 30
    • 84862638898 scopus 로고    scopus 로고
    • Two steps forward-one step back: Advances in affinity purification mass spectrometry of macromolecular complexes
    • Oeffinger, M. (2012) Two steps forward-one step back: advances in affinity purification mass spectrometry of macromolecular complexes. Proteomics 12, 1591-1608
    • (2012) Proteomics , vol.12 , pp. 1591-1608
    • Oeffinger, M.1
  • 32
    • 0033669189 scopus 로고    scopus 로고
    • A network of proteinprotein interactions in yeast
    • Schwikowski, B., Uetz, P., and Fields, S. (2000) A network of proteinprotein interactions in yeast. Nat. Biotechnol. 18, 1257-1261
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1257-1261
    • Schwikowski, B.1    Uetz, P.2    Fields, S.3
  • 33
    • 0028334718 scopus 로고
    • DNA transport by a type II DNA topoisomerase: Evidence in favor of a two-gate mechanism
    • Roca, J., and Wang, J. C. (1994) DNA transport by a type II DNA topoisomerase: evidence in favor of a two-gate mechanism. Cell 77, 609-616
    • (1994) Cell , vol.77 , pp. 609-616
    • Roca, J.1    Wang, J.C.2
  • 34
    • 79960400833 scopus 로고    scopus 로고
    • Xwalk: Computing and visualizing distances in cross-linking experiments
    • Kahraman, A., Malmstrom, L., and Aebersold, R. (2011) Xwalk: computing and visualizing distances in cross-linking experiments. Bioinformatics 27, 2163-2164
    • (2011) Bioinformatics , vol.27 , pp. 2163-2164
    • Kahraman, A.1    Malmstrom, L.2    Aebersold, R.3
  • 35
    • 21244464335 scopus 로고    scopus 로고
    • Binding properties and evolution of homodimers in protein-protein interaction networks
    • DOI 10.1093/nar/gki678
    • Ispolatov, I., Yuryev, A., Mazo, I., and Maslov, S. (2005) Binding properties and evolution of homodimers in protein-protein interaction networks. Nucleic Acids Res. 33, 3629-3635 (Pubitemid 41430585)
    • (2005) Nucleic Acids Research , vol.33 , Issue.11 , pp. 3629-3635
    • Ispolatov, I.1    Yuryev, A.2    Mazo, I.3    Maslov, S.4
  • 36
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • DOI 10.1038/nature06524, PII NATURE06524
    • Kuriyan, J., and Eisenberg, D. (2007) The origin of protein interactions and allostery in colocalization. Nature 450, 983-990 (Pubitemid 350273628)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 38
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • DOI 10.1038/nrc1716
    • Whitesell, L., and Lindquist, S. L. (2005) HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 5, 761-772 (Pubitemid 41400776)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 40
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • DOI 10.1146/annurev.biochem.75.103004.142738
    • Pearl, L. H., and Prodromou, C. (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294 (Pubitemid 44118034)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 41
    • 62949238913 scopus 로고    scopus 로고
    • New developments in Hsp90 inhibitors as anti-cancer therapeutics: Mechanisms, clinical perspective and more potential
    • Li, Y., Zhang, T., Schwartz, S. J., and Sun, D. (2009) New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential. Drug Resistance Updates 12, 17-27
    • (2009) Drug Resistance Updates , vol.12 , pp. 17-27
    • Li, Y.1    Zhang, T.2    Schwartz, S.J.3    Sun, D.4
  • 42
    • 28644443855 scopus 로고    scopus 로고
    • The HSP90 family of genes in the human genome: Insights into their divergence and evolution
    • DOI 10.1016/j.ygeno.2005.08.012, PII S0888754305002430
    • Chen, B., Piel, W. H., Gui, L., Bruford, E., and Monteiro, A. (2005) The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86, 627-637 (Pubitemid 41752943)
    • (2005) Genomics , vol.86 , Issue.6 , pp. 627-637
    • Chen, B.1    Piel, W.H.2    Gui, L.3    Bruford, E.4    Monteiro, A.5
  • 43
    • 0025874261 scopus 로고
    • Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90
    • Minami, Y., Kawasaki, H., Miyata, Y., Suzuki, K., and Yahara, I. (1991) Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90. J. Biol. Chem. 266, 10099-10103 (Pubitemid 21906773)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.16 , pp. 10099-10103
    • Minami, Y.1    Kawasaki, H.2    Miyata, Y.3    Suzuki, K.4    Yahara, I.5
  • 44
    • 0032032934 scopus 로고    scopus 로고
    • Oligomeric forms of the 90-kDa heat shock protein
    • Nemoto, T., and Sato, N. (1998) Oligomeric forms of the 90-kDa heat shock protein. Biochem. J. 330 (Pt 2), 989-995 (Pubitemid 28112007)
    • (1998) Biochemical Journal , vol.330 , Issue.2 , pp. 989-995
    • Nemoto, T.1    Sato, N.2
  • 45
    • 0027135268 scopus 로고
    • Localization and characterization of the 86- and 84-kDa heat shock proteins in hepa 1c1c7 cells
    • DOI 10.1006/excr.1993.1320
    • Perdew, G. H., Hord, N., Hollenback, C. E., and Welsh, M. J. (1993) Localization and characterization of the 86- and 84-kDa heat shock proteins in Hepa 1c1c7 cells. Exp. Cell Res. 209, 350-356 (Pubitemid 24005321)
    • (1993) Experimental Cell Research , vol.209 , Issue.2 , pp. 350-356
    • Perdew, G.H.1    Hord, N.2    Hollenback, C.E.3    Welsh, M.J.4
  • 50
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • DOI 10.1016/S0022-2836(02)00161-4
    • Smith, T. J., Schmidt, T., Fang, J., Wu, J., Siuzdak, G., and Stanley, C. A. (2002) The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J. Mol. Biol. 318, 765-777 (Pubitemid 34729367)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.3 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 51
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein, T., and Allis, C. D. (2001) Translating the histone code. Science 293, 1074-1080 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 53
    • 0037164741 scopus 로고    scopus 로고
    • Gene-specific targeting of H3K9 methylation is sufficient for initiating repression in vivo
    • DOI 10.1016/S0960-9822(02)01391-X, PII S096098220201391X
    • Snowden, A. W., Gregory, P. D., Case, C. C., and Pabo, C. O. (2002) Gene-specific targeting of H3K9 methylation is sufficient for initiating repression in vivo. Current Biol. 12, 2159-2166 (Pubitemid 36021896)
    • (2002) Current Biology , vol.12 , Issue.24 , pp. 2159-2166
    • Snowden, A.W.1    Gregory, P.D.2    Case, C.C.3    Pabo, C.O.4
  • 54
    • 0242362808 scopus 로고    scopus 로고
    • Molecular cloning of a novel human gene encoding histone acetyltransferase-like protein involved in transcriptional activation of hTERT
    • DOI 10.1016/j.bbrc.2003.09.235
    • Lv, J., Liu, H., Wang, Q., Tang, Z., Hou, L., and Zhang, B. (2003) Molecular cloning of a novel human gene encoding histone acetyltransferase-like protein involved in transcriptional activation of hTERT. Biochem. Biophys. Res. Commun. 311, 506-513 (Pubitemid 37340108)
    • (2003) Biochemical and Biophysical Research Communications , vol.311 , Issue.2 , pp. 506-513
    • Lv, J.1    Liu, H.2    Wang, Q.3    Tang, Z.4    Hou, L.5    Zhang, B.6
  • 55
    • 78651246115 scopus 로고    scopus 로고
    • Chromatin landscape: Methylation beyond transcription
    • Black, J. C., and Whetstine, J. R. (2010) Chromatin landscape: methylation beyond transcription. Epigenetics 6, 9-15
    • (2010) Epigenetics , vol.6 , pp. 9-15
    • Black, J.C.1    Whetstine, J.R.2
  • 56
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • DOI 10.1126/science.1124000
    • Shogren-Knaak, M., Ishii, H., Sun, J. M., Pazin, M. J., Davie, J. R., and Peterson, C. L. (2006) Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311, 844-847 (Pubitemid 43228847)
    • (2006) Science , vol.311 , Issue.5762 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.-M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 57
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • DOI 10.1016/j.cell.2004.05.023, PII S0092867404005367
    • Kurdistani, S. K., Tavazoie, S., and Grunstein, M. (2004) Mapping global histone acetylation patterns to gene expression. Cell 117, 721-733 (Pubitemid 38748889)
    • (2004) Cell , vol.117 , Issue.6 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 58
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine
    • Dever, T. E., Costello, C. E., Owens, C. L., Rosenberry, T. L., and Merrick, W. C. (1989) Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. J. Biol. Chem. 264, 20518-20525 (Pubitemid 20009242)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.34 , pp. 20518-20525
    • Dever, T.E.1    Costello, C.E.2    Owens, C.L.3    Rosenberry, T.L.4    Merrick, W.C.5
  • 59
    • 4143091385 scopus 로고    scopus 로고
    • The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: Review article
    • Lamberti, A., Caraglia, M., Longo, O., Marra, M., Abbruzzese, A., and Arcari, P. (2004) The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: review article. Amino Acids 26, 443-448 (Pubitemid 39093149)
    • (2004) Amino Acids , vol.26 , Issue.4 , pp. 443-448
    • Lamberti, A.1    Caraglia, M.2    Longo, O.3    Marra, M.4    Abbruzzese, A.5    Arcari, P.6
  • 60
    • 11144336620 scopus 로고    scopus 로고
    • Formation of membrane-bound ring complexes by prohibitins in mitochondria
    • DOI 10.1091/mbc.E04-09-0807
    • Tatsuta, T., Model, K., and Langer, T. (2005) Formation of membrane-bound ring complexes by prohibitins in mitochondria. Mol. Biol. Cell 16, 248-259 (Pubitemid 40024307)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.1 , pp. 248-259
    • Tatsuta, T.1    Model, K.2    Langer, T.3
  • 61
    • 70450265196 scopus 로고    scopus 로고
    • Prohibitins and the functional compartmentalization of mitochondrial membranes
    • Osman, C., Merkwirth, C., and Langer, T. (2009) Prohibitins and the functional compartmentalization of mitochondrial membranes. J. Cell Sci. 122, 3823-3830
    • (2009) J. Cell Sci. , vol.122 , pp. 3823-3830
    • Osman, C.1    Merkwirth, C.2    Langer, T.3
  • 62
    • 73949150062 scopus 로고    scopus 로고
    • Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycoprotein
    • Emerson, V., Holtkotte, D., Pfeiffer, T., Wang, I. H., Schnölzer, M., Kempf, T., and Bosch, V. (2010) Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycoprotein. J. Virol. 84, 1355-1365
    • (2010) J. Virol. , vol.84 , pp. 1355-1365
    • Emerson, V.1    Holtkotte, D.2    Pfeiffer, T.3    Wang, I.H.4    Schnölzer, M.5    Kempf, T.6    Bosch, V.7
  • 63
    • 79955659650 scopus 로고    scopus 로고
    • The role and therapeutic potential of prohibitin in disease
    • Theiss, A. L., and Sitaraman, S. V. (2011) The role and therapeutic potential of prohibitin in disease. Biochim. Biophys. Acta 1813, 1137-1143
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1137-1143
    • Theiss, A.L.1    Sitaraman, S.V.2
  • 65
    • 14244258608 scopus 로고    scopus 로고
    • Ribophorin I associates with a subset of membrane proteins after their integration at the Sec61 translocon
    • DOI 10.1074/jbc.M410329200
    • Wilson, C. M., Kraft, C., Duggan, C., Ismail, N., Crawshaw, S. G., and High, S. (2005) Ribophorin I associates with a subset of membrane proteins after their integration at the sec61 translocon. chemistry. Biol. Chem. 280, 4195-4206 (Pubitemid 40288585)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4195-4206
    • Wilson, C.M.1    Kraft, C.2    Duggan, C.3    Ismail, N.4    Crawshaw, S.G.5    High, S.6
  • 67
    • 78349290716 scopus 로고    scopus 로고
    • Multifunctional receptor stabilin-1 in homeostasis and disease
    • Kzhyshkowska, J. (2010) Multifunctional receptor stabilin-1 in homeostasis and disease. TheScientificWorldJournal 10, 2039-2053
    • (2010) TheScientificWorldJournal , vol.10 , pp. 2039-2053
    • Kzhyshkowska, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.