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Volumn 22, Issue 6, 2004, Pages 724-731

Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; INTEGRAL EQUATIONS; MASS SPECTROMETRY; PROTEINS; TISSUE;

EID: 2542583141     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt969     Document Type: Article
Times cited : (141)

References (48)
  • 1
    • 0035987407 scopus 로고    scopus 로고
    • The post-genomic era of interactive proteomics: Facts and perspectives
    • Auerbach, D., Thaminy, S., Hottiger, M.O. & Stagljar, I. The post-genomic era of interactive proteomics: facts and perspectives. Proteomics 2, 611-623 (2002).
    • (2002) Proteomics , vol.2 , pp. 611-623
    • Auerbach, D.1    Thaminy, S.2    Hottiger, M.O.3    Stagljar, I.4
  • 2
    • 0035575637 scopus 로고    scopus 로고
    • Drug discovery of the future: The implications of the human genome project
    • Reiss, T. Drug discovery of the future: the implications of the human genome project. Trends Biotechnol. 19, 496-499 (2001).
    • (2001) Trends Biotechnol. , vol.19 , pp. 496-499
    • Reiss, T.1
  • 3
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766 (2001).
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 4
    • 0036898485 scopus 로고    scopus 로고
    • Alzheimer disease gamma-secretase: A complex story of GxGD-type presenilin proteases
    • Haass, C. & Steiner, H. Alzheimer disease gamma-secretase: a complex story of GxGD-type presenilin proteases. Trends Cell Biol. 12, 556-562 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 556-562
    • Haass, C.1    Steiner, H.2
  • 5
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev, E.I. et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376, 775-778 (1995).
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1
  • 6
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington, R. et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375, 754-760 (1995).
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1
  • 7
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48-54 (2000).
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 8
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
    • Goutte, C., Tsunozaki, M., Hale, V.A. & Priess, J.R. APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc. Natl. Acad. Sci. USA 99, 775-779 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 9
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation
    • Francis, R. et al. aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1
  • 10
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky, A. & Harris, D.A. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J. Cell Biol. 129, 619-627 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 11
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky, N., Stein, R., Yanai, A., Friedlander, G. & Taraboulos, A. Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 272, 6324-6331 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 12
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform
    • Taraboulos, A. et al. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform. J. Cell Biol. 129, 121-132 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 121-132
    • Taraboulos, A.1
  • 13
    • 0029962468 scopus 로고    scopus 로고
    • Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains
    • Vey, M. et al. Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc. Natl. Acad. Sci. USA 93, 14945-14949 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14945-14949
    • Vey, M.1
  • 14
    • 0030964917 scopus 로고    scopus 로고
    • COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko, K. et al. COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl. Acad. Sci. USA 94, 2333-2338 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1
  • 15
    • 0037418828 scopus 로고    scopus 로고
    • Soluble dimeric prion protein binds PrPsc in vivo and antagonizes prion disease
    • Meier, P. et al. Soluble dimeric prion protein binds PrPsc in vivo and antagonizes prion disease. Cell 113, 49-60 (2003).
    • (2003) Cell , vol.113 , pp. 49-60
    • Meier, P.1
  • 16
    • 0036024957 scopus 로고    scopus 로고
    • Characterizing transcription factor binding sites using formaldehyde crosslinking and immunoprecipitation
    • Wells, J. & Farnham, P.J. Characterizing transcription factor binding sites using formaldehyde crosslinking and immunoprecipitation. Methods 26, 48-56 (2002).
    • (2002) Methods , vol.26 , pp. 48-56
    • Wells, J.1    Farnham, P.J.2
  • 17
    • 0032848160 scopus 로고    scopus 로고
    • Formaldehyde cross-linking for studying nucleosomal dynamics
    • Jackson, V. Formaldehyde cross-linking for studying nucleosomal dynamics. Methods 17, 125-139 (1999).
    • (1999) Methods , vol.17 , pp. 125-139
    • Jackson, V.1
  • 18
    • 0031080378 scopus 로고    scopus 로고
    • Analysis of chromatin structure by in vivo formaldehyde cross-linking
    • Orlando, V., Strutt, H. & Paro, R. Analysis of chromatin structure by in vivo formaldehyde cross-linking. Methods 11, 205-214 (1997).
    • (1997) Methods , vol.11 , pp. 205-214
    • Orlando, V.1    Strutt, H.2    Paro, R.3
  • 19
    • 0031079897 scopus 로고    scopus 로고
    • Analysis of in vivo nucleosome positions by determination of nucleosome-linker boundaries in crosslinked chromatin
    • Fragoso, G. & Hager, G.L. Analysis of in vivo nucleosome positions by determination of nucleosome-linker boundaries in crosslinked chromatin. Methods 11, 246-252 (1997).
    • (1997) Methods , vol.11 , pp. 246-252
    • Fragoso, G.1    Hager, G.L.2
  • 20
    • 0031725221 scopus 로고    scopus 로고
    • Differential extraction of proteins from paraformaldehyde-fixed cells: Lessons from Synaptophysin and other membrane proteins
    • Hannah, M.J., Weiss, U. & Huttner, W.B. Differential extraction of proteins from paraformaldehyde-fixed cells: lessons from Synaptophysin and other membrane proteins. Methods 16, 170-181 (1998).
    • (1998) Methods , vol.16 , pp. 170-181
    • Hannah, M.J.1    Weiss, U.2    Huttner, W.B.3
  • 21
    • 0035861987 scopus 로고    scopus 로고
    • Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein
    • Schmitt-Ulms, G. et al. Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. J. Mol. Biol. 314, 1209-1225 (2001).
    • (2001) J. Mol. Biol. , vol.314 , pp. 1209-1225
    • Schmitt-Ulms, G.1
  • 22
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of gamma-secretase activity
    • Edbauer, D. et al. Reconstitution of gamma-secretase activity. Nat. Cell Biol. 5, 486-488 (2003).
    • (2003) Nat. Cell Biol. , vol.5 , pp. 486-488
    • Edbauer, D.1
  • 23
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Büeler, H. et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577-582 (1992).
    • (1992) Nature , vol.356 , pp. 577-582
    • Büeler, H.1
  • 24
    • 0032478284 scopus 로고    scopus 로고
    • Allosteric modulation of AMPA-type glutamate receptors increases activity of the promoter for the neural cell adhesion molecule, N-CAM
    • Holst, B.D. et al. Allosteric modulation of AMPA-type glutamate receptors increases activity of the promoter for the neural cell adhesion molecule, N-CAM. Proc. Natl. Acad. Sci. USA 95, 2597-2602 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2597-2602
    • Holst, B.D.1
  • 25
    • 0345505687 scopus 로고    scopus 로고
    • Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival
    • Chen, S., Mange, A., Dong, L., Lehmann, S. & Schachner, M. Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol. Cell. Neurosci. 22, 227-233 (2003).
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 227-233
    • Chen, S.1    Mange, A.2    Dong, L.3    Lehmann, S.4    Schachner, M.5
  • 26
    • 0032568821 scopus 로고    scopus 로고
    • The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin
    • Yu, G. et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin. J. Biol. Chem. 273, 16470-16475 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 16470-16475
    • Yu, G.1
  • 27
    • 0037357117 scopus 로고    scopus 로고
    • Lipid rafts mediate the interaction between myelin-associated glycoprotein (MAG) on myelin and MAG-receptors on neurons
    • Vinson, M. et al. Lipid rafts mediate the interaction between myelin-associated glycoprotein (MAG) on myelin and MAG-receptors on neurons. Mol. Cell. Neurosci. 22, 344-352 (2003).
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 344-352
    • Vinson, M.1
  • 28
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt, R., Keller, P., Haass, C., Thiele, C. & Simons, K, Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J. Cell Biol. 160, 113-123 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 29
    • 0034623960 scopus 로고    scopus 로고
    • The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome
    • Jin, T. et al. The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome. J. Biol. Chem. 275, 38699-38704 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38699-38704
    • Jin, T.1
  • 30
    • 0030940607 scopus 로고    scopus 로고
    • Identification of candidate proteins binding to prion protein
    • Yehiely, F. et al. Identification of candidate proteins binding to prion protein. Neurobiol. Dis. 3, 339-355 (1997).
    • (1997) Neurobiol. Dis. , vol.3 , pp. 339-355
    • Yehiely, F.1
  • 31
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM 10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent, B. et al. The disintegrins ADAM 10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J. Biol. Chem. 276, 37743-37746 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1
  • 32
    • 0029598484 scopus 로고
    • The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein
    • Fiore, F. et al. The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein, J. Biol. Chem. 270, 30853-30856 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 30853-30856
    • Fiore, F.1
  • 33
    • 0028805468 scopus 로고
    • The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum
    • Olive, S., Dubois, C., Schachner, M. & Rougon, G. The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum. J. Neurochem. 65, 2307-2317 (1995).
    • (1995) J. Neurochem. , vol.65 , pp. 2307-2317
    • Olive, S.1    Dubois, C.2    Schachner, M.3    Rougon, G.4
  • 34
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro, S. Lipid rafts: elusive or illusive? Cell 115, 377-388 (2003).
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 35
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A. & Rose, J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544 (1992).
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 36
    • 0035433580 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains
    • von Haller, P.D., Donohoe, S., Goodlett, D.R., Aebersold, R. & Watts, J.D. Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains. Proteomics 1, 1010-1021 (2001).
    • (2001) Proteomics , vol.1 , pp. 1010-1021
    • Von Haller, P.D.1    Donohoe, S.2    Goodlett, D.R.3    Aebersold, R.4    Watts, J.D.5
  • 37
    • 0347298692 scopus 로고    scopus 로고
    • Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering
    • Bini, L. et al. Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering. Biochem. J. 369, 301-309 (2003).
    • (2003) Biochem. J. , vol.369 , pp. 301-309
    • Bini, L.1
  • 38
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L.J., De Hoog, C.L. & Mann, M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. USA 100, 5813-5818 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 39
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore, N. et al. Functionally different GPI proteins are organized in different domains on the neuronal surface. EMBO J. 18, 6917-6926 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6917-6926
    • Madore, N.1
  • 40
    • 0029932417 scopus 로고    scopus 로고
    • Axonal amyloid precursor protein expressed by neurons in vitro is present in a membrane fraction with caveolae-like properties
    • Bouillot, C., Prochiantz, A., Rougon, G. & Allinquant, B. Axonal amyloid precursor protein expressed by neurons in vitro is present in a membrane fraction with caveolae-like properties. J. Biol. Chem. 271, 7640-7644 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 7640-7644
    • Bouillot, C.1    Prochiantz, A.2    Rougon, G.3    Allinquant, B.4
  • 41
    • 0032562615 scopus 로고    scopus 로고
    • Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein
    • Ikezu, T. et al. Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein. J. Biol. Chem. 273, 10485-10495 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10485-10495
    • Ikezu, T.1
  • 42
    • 0347052880 scopus 로고    scopus 로고
    • Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95
    • Wong, W. & Schlichter, L.C. Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95. J. Biol. Chem. 279, 444-452 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 444-452
    • Wong, W.1    Schlichter, L.C.2
  • 43
    • 0037421685 scopus 로고    scopus 로고
    • The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical component of neuronal A-type K+ channels
    • Nadal, M.S. et al. The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical component of neuronal A-type K+ channels. Neuron 37, 449-461 (2003).
    • (2003) Neuron , vol.37 , pp. 449-461
    • Nadal, M.S.1
  • 44
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans, L., Puntener, D. & Helenius, A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296, 535-539 (2002).
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 45
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • Nabi, I.R. & Le, P.U. Caveolae/raft-dependent endocytosis. J. Cell Biol. 161, 673-677 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 46
    • 0035152345 scopus 로고    scopus 로고
    • Identification of two prion protein regions that modify scrapie incubation time
    • Supattapone, S. et al. Identification of two prion protein regions that modify scrapie incubation time. J. Virol. 75, 1408-1413 (2001).
    • (2001) J. Virol. , vol.75 , pp. 1408-1413
    • Supattapone, S.1
  • 47
    • 0031710237 scopus 로고    scopus 로고
    • Mapping the prion protein using recombinant antibodies
    • Williamson, R.A. et al. Mapping the prion protein using recombinant antibodies. J. Virol. 72, 9413-9418 (1998).
    • (1998) J. Virol. , vol.72 , pp. 9413-9418
    • Williamson, R.A.1
  • 48
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser, K.R., Baker, P. & Burlingame, A.L. Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal. Chem. 71, 2871-2882 (1999).
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3


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