메뉴 건너뛰기




Volumn 58, Issue 21, 2013, Pages 2640-2645

A multiple-labelling method for cells using Au nanoparticles with different shapes

Author keywords

gold nanoparticles; low vacuum SEM; multiple labelling; TPL

Indexed keywords


EID: 84880638600     PISSN: 10016538     EISSN: 18619541     Source Type: Journal    
DOI: 10.1007/s11434-013-5794-2     Document Type: Article
Times cited : (2)

References (33)
  • 1
    • 35548942611 scopus 로고    scopus 로고
    • Tether and trap: Regulation of membrane-raft dynamics by actin-binding proteins
    • Viola A, Gupta N. Tether and trap: Regulation of membrane-raft dynamics by actin-binding proteins. Nat Rev Immunol, 2007, 7: 889-896.
    • (2007) Nat Rev Immunol , vol.7 , pp. 889-896
    • Viola, A.1    Gupta, N.2
  • 3
    • 0035263288 scopus 로고    scopus 로고
    • Stimulation of β1 integrin down-regulates ICAM-1 expression and ICAM-1-dependent adhesion of lung cancer cells through focal adhesion kinase
    • Yasuda M, Tanaka Y, Tamura M, et al. Stimulation of β1 integrin down-regulates ICAM-1 expression and ICAM-1-dependent adhesion of lung cancer cells through focal adhesion kinase. Cancer Res, 2001, 61: 2022-2030.
    • (2001) Cancer Res , vol.61 , pp. 2022-2030
    • Yasuda, M.1    Tanaka, Y.2    Tamura, M.3
  • 4
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain
    • Hemler M E. Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain. Annu Rev Cell Dev Biol, 2003, 19: 397-422.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 5
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M E. Tetraspanin functions and associated microdomains. Nat Rev Mol Cell Biol, 2005, 6: 801-811.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 6
    • 33845975257 scopus 로고    scopus 로고
    • Membrane microdomains and proteomics: Lessons from tetraspanin microdomains and comparison with lipid rafts
    • Naour F L, André M, Boucheix C, et al. Membrane microdomains and proteomics: Lessons from tetraspanin microdomains and comparison with lipid rafts. Proteomics, 2006, 6: 6447-6454.
    • (2006) Proteomics , vol.6 , pp. 6447-6454
    • Naour, F.L.1    André, M.2    Boucheix, C.3
  • 7
    • 33745235141 scopus 로고    scopus 로고
    • Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-Å resolution
    • Min G W, Wang H B, Sun T T, et al. Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-Å resolution. J Cell Biol, 2006, 173: 975-983.
    • (2006) J Cell Biol , vol.173 , pp. 975-983
    • Min, G.W.1    Wang, H.B.2    Sun, T.T.3
  • 8
    • 56149120891 scopus 로고    scopus 로고
    • Endothelial adhesion receptors are recruited to adherent leukocytes by inclusion in preformed tetraspanin nanoplatforms
    • Barreiro O, Zamai M, Yáñez-Mó M, et al. Endothelial adhesion receptors are recruited to adherent leukocytes by inclusion in preformed tetraspanin nanoplatforms. J Cell Biol, 2008, 183: 527-542.
    • (2008) J Cell Biol , vol.183 , pp. 527-542
    • Barreiro, O.1    Zamai, M.2    Yáñez-Mó, M.3
  • 9
    • 0030878409 scopus 로고    scopus 로고
    • Perspectives series: Cell adhesion in vascular biology. Integrin signaling in vascular biology
    • Shattil S J, Ginsberg M H. Perspectives series: Cell adhesion in vascular biology. Integrin signaling in vascular biology. J Clin Invest, 1997, 100: 1-5.
    • (1997) J Clin Invest , vol.100 , pp. 1-5
    • Shattil, S.J.1    Ginsberg, M.H.2
  • 10
    • 34248225277 scopus 로고    scopus 로고
    • Two-photon luminescence imaging of cancer cells using molecularly targeted gold nanorods
    • Durr N J, Larson T, Smith D K, et al. Two-photon luminescence imaging of cancer cells using molecularly targeted gold nanorods. Nano Lett, 2007, 7: 941-945.
    • (2007) Nano Lett , vol.7 , pp. 941-945
    • Durr, N.J.1    Larson, T.2    Smith, D.K.3
  • 11
    • 27644447874 scopus 로고    scopus 로고
    • In vitro and in vivo two-photon luminescence imaging of single gold nanorods
    • Wang H F, Huff T B, Zweifel D A, et al. In vitro and in vivo two-photon luminescence imaging of single gold nanorods. Proc Natl Acad Sci USA, 2005, 102: 15752-15756.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15752-15756
    • Wang, H.F.1    Huff, T.B.2    Zweifel, D.A.3
  • 12
    • 70449397729 scopus 로고    scopus 로고
    • Visualizing systemic clearance and cellular level biodistribution of gold nanorods by intrinsic two-photon luminescence
    • Tong L, He W, Zhang Y S, et al. Visualizing systemic clearance and cellular level biodistribution of gold nanorods by intrinsic two-photon luminescence. Langmuir, 2009, 25: 12454-12459.
    • (2009) Langmuir , vol.25 , pp. 12454-12459
    • Tong, L.1    He, W.2    Zhang, Y.S.3
  • 13
    • 33244457595 scopus 로고    scopus 로고
    • Cancer cell imaging and photothermal therapy in the near-infrared region by using gold nanorods
    • Huang X, El-Sayed I H, Qin W, et al. Cancer cell imaging and photothermal therapy in the near-infrared region by using gold nanorods. J Am Chem Soc, 2006, 128: 2115-2120.
    • (2006) J Am Chem Soc , vol.128 , pp. 2115-2120
    • Huang, X.1    El-Sayed, I.H.2    Qin, W.3
  • 14
    • 66449137797 scopus 로고    scopus 로고
    • Gastrin releasing protein receptor specific gold nanorods: Breast and prostate tumor avid nanovectors for molecular imaging
    • Chanda N, Shukla R, Katti K V, et al. Gastrin releasing protein receptor specific gold nanorods: Breast and prostate tumor avid nanovectors for molecular imaging. Nano Lett, 2009, 9: 1798-1805.
    • (2009) Nano Lett , vol.9 , pp. 1798-1805
    • Chanda, N.1    Shukla, R.2    Katti, K.V.3
  • 15
    • 69249157205 scopus 로고    scopus 로고
    • SERS imaging of HER2-over expressed MCF7 cells using antibody-conjugated gold nanorods
    • Park H, Lee S, Chen L, et al. SERS imaging of HER2-over expressed MCF7 cells using antibody-conjugated gold nanorods. Phys Chem Chem Phys, 2009, 11: 7444-7449.
    • (2009) Phys Chem Chem Phys , vol.11 , pp. 7444-7449
    • Park, H.1    Lee, S.2    Chen, L.3
  • 16
    • 22944464695 scopus 로고    scopus 로고
    • Fine-tuning the shape of gold nanorods
    • Guo L F, Murphy C J. Fine-tuning the shape of gold nanorods. Chem Mater, 2005, 17: 3668-3672.
    • (2005) Chem Mater , vol.17 , pp. 3668-3672
    • Guo, L.F.1    Murphy, C.J.2
  • 17
    • 41749122608 scopus 로고    scopus 로고
    • Tuning the morphology of gold nanocrystals by switching the growth of {110} facets from restriction to preference
    • Xiang Y J, Wu X C, Liu D F, et al. Tuning the morphology of gold nanocrystals by switching the growth of {110} facets from restriction to preference. J Phys Chem C, 2008, 112: 3203-3208.
    • (2008) J Phys Chem C , vol.112 , pp. 3203-3208
    • Xiang, Y.J.1    Wu, X.C.2    Liu, D.F.3
  • 18
    • 0035797987 scopus 로고    scopus 로고
    • Evidence for bilayer assembly of cationic surfactants on the surface of gold nanorods
    • Nikoobakht B, El-Sayed M A. Evidence for bilayer assembly of cationic surfactants on the surface of gold nanorods. Langmuir, 2001, 17: 6368-6374.
    • (2001) Langmuir , vol.17 , pp. 6368-6374
    • Nikoobakht, B.1    El-Sayed, M.A.2
  • 19
    • 0035954961 scopus 로고    scopus 로고
    • Tailoring the polyelectrolyte coating of metal nanoparticles
    • Gittins D I, Caruso F. Tailoring the polyelectrolyte coating of metal nanoparticles. J Phys Chem B, 2001, 105: 6846-6852.
    • (2001) J Phys Chem B , vol.105 , pp. 6846-6852
    • Gittins, D.I.1    Caruso, F.2
  • 20
    • 36949024455 scopus 로고    scopus 로고
    • Biorecognition-driven self-assembly of gold nanorods: A rapid and sensitive approach toward antibody sensing
    • Wang C G, Chen Y, Wang T T, et al. Biorecognition-driven self-assembly of gold nanorods: A rapid and sensitive approach toward antibody sensing. Chem Mater, 2007, 19: 5809-5811.
    • (2007) Chem Mater , vol.19 , pp. 5809-5811
    • Wang, C.G.1    Chen, Y.2    Wang, T.T.3
  • 21
    • 0029006254 scopus 로고
    • The interaction of the retina cell surface N-acetylgalactosaminylphosphotransferase with an endogenous proteoglycan ligand results in inhibition of cadherin-mediated adhesion
    • Balsamo J, Ernst H, Zanin M K, et al. The interaction of the retina cell surface N-acetylgalactosaminylphosphotransferase with an endogenous proteoglycan ligand results in inhibition of cadherin-mediated adhesion. J Cell Biol, 1995, 129: 1391-1401.
    • (1995) J Cell Biol , vol.129 , pp. 1391-1401
    • Balsamo, J.1    Ernst, H.2    Zanin, M.K.3
  • 22
    • 0034131169 scopus 로고    scopus 로고
    • Tetraspanins are localized at motility-related structures and involved in normal human keratinocyte wound healing migration
    • Peñas P F, García-Díez A, Sánchez-Madrid F, et al. Tetraspanins are localized at motility-related structures and involved in normal human keratinocyte wound healing migration. J Invest Derm, 2000, 114: 1126-1135.
    • (2000) J Invest Derm , vol.114 , pp. 1126-1135
    • Peñas, P.F.1    García-Díez, A.2    Sánchez-Madrid, F.3
  • 24
    • 0037077718 scopus 로고    scopus 로고
    • E-selectin and ICAM-1 are incorporated into detergent-insoluble membrane domains following clustering in endothelial cells
    • Tilghman R W, Hoover R L. E-selectin and ICAM-1 are incorporated into detergent-insoluble membrane domains following clustering in endothelial cells. FEBS Lett, 2002, 525: 83-87.
    • (2002) FEBS Lett , vol.525 , pp. 83-87
    • Tilghman, R.W.1    Hoover, R.L.2
  • 25
    • 0037166942 scopus 로고    scopus 로고
    • Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes
    • Barreiro O, Yáñez-Mó M, Serrador J M, et al. Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J Cell Biol, 2002, 157: 1233-1245.
    • (2002) J Cell Biol , vol.157 , pp. 1233-1245
    • Barreiro, O.1    Yáñez-Mó, M.2    Serrador, J.M.3
  • 26
    • 15944361837 scopus 로고    scopus 로고
    • Endothelial tetraspanin microdomains regulate leukocyte firm adhesion during extravasation
    • Barreiro O, Yáñez-Mó M, Sala-Valdés M, et al. Endothelial tetraspanin microdomains regulate leukocyte firm adhesion during extravasation. Blood, 2005, 105: 2852-2861.
    • (2005) Blood , vol.105 , pp. 2852-2861
    • Barreiro, O.1    Yáñez-Mó, M.2    Sala-Valdés, M.3
  • 27
    • 34748905448 scopus 로고    scopus 로고
    • RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration
    • Buul J D, Allingham M J, Samson T, et al. RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration. J Cell Biol, 2007, 178: 1279-1293.
    • (2007) J Cell Biol , vol.178 , pp. 1279-1293
    • Buul, J.D.1    Allingham, M.J.2    Samson, T.3
  • 28
    • 0030062129 scopus 로고    scopus 로고
    • Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins)
    • Berditchevski F, Zutter M M, Hemler M E. Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins). Mol Biol Cell, 1996, 7: 193-207.
    • (1996) Mol Biol Cell , vol.7 , pp. 193-207
    • Berditchevski, F.1    Zutter, M.M.2    Hemler, M.E.3
  • 29
    • 0028999004 scopus 로고
    • Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites
    • Nakamura K, Iwamoto R, Mekada E. Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites. J Cell Biol, 1995, 129: 1691-1705.
    • (1995) J Cell Biol , vol.129 , pp. 1691-1705
    • Nakamura, K.1    Iwamoto, R.2    Mekada, E.3
  • 30
    • 0032189153 scopus 로고    scopus 로고
    • Integrins take partners: Cross-talk between integrins and other membrane receptors
    • Porter J C, Hogg N. Integrins take partners: Cross-talk between integrins and other membrane receptors. Trends Cell Biol, 1998, 8: 390-396.
    • (1998) Trends Cell Biol , vol.8 , pp. 390-396
    • Porter, J.C.1    Hogg, N.2
  • 31
    • 0033952054 scopus 로고    scopus 로고
    • CD9 Participates in endothelial cell migration during in vitro wound repair
    • Klein-Soyer C, Azorsa D O, Cazenave J P, et al. CD9 Participates in endothelial cell migration during in vitro wound repair. Annu Rev Cell Dev Biol, 2000, 20: 360-369.
    • (2000) Annu Rev Cell Dev Biol , vol.20 , pp. 360-369
    • Klein-Soyer, C.1    Azorsa, D.O.2    Cazenave, J.P.3
  • 32
    • 0032948124 scopus 로고    scopus 로고
    • PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function
    • Sincock P M, Fitter S, Parton R G, et al. PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function. J Cell Sci, 1999, 112: 833-844.
    • (1999) J Cell Sci , vol.112 , pp. 833-844
    • Sincock, P.M.1    Fitter, S.2    Parton, R.G.3
  • 33
    • 0038610891 scopus 로고    scopus 로고
    • Tetraspanin CD151 regulates α6β1 integrin adhesion strengthening
    • Lammerding J, Kazarov A R, Huang H, et al. Tetraspanin CD151 regulates α6β1 integrin adhesion strengthening. Proc Natl Acad Sci USA, 2003, 100: 7616-7621.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7616-7621
    • Lammerding, J.1    Kazarov, A.R.2    Huang, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.