메뉴 건너뛰기




Volumn 14, Issue 1, 2010, Pages 57-63

Fluorescent small-molecule probes of biochemistry at the plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; MEMBRANE LIPID; MEMBRANE PROTEIN; MEMBRANE RECEPTOR;

EID: 75149179997     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2009.09.032     Document Type: Review
Times cited : (58)

References (57)
  • 1
    • 53849087812 scopus 로고    scopus 로고
    • Fluorescent probes for bioimaging applications
    • Terai T., and Nagano T. Fluorescent probes for bioimaging applications. Curr Opin Chem Biol 12 (2008) 515-521
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 515-521
    • Terai, T.1    Nagano, T.2
  • 2
    • 67650391443 scopus 로고    scopus 로고
    • Monitoring biophysical properties of lipid membranes by environment-sensitive fluorescent probes
    • Demchenko A.P., Mély Y., Duportail G., and Klymchenko A.S. Monitoring biophysical properties of lipid membranes by environment-sensitive fluorescent probes. Biophys J 96 (2009) 3461-3470
    • (2009) Biophys J , vol.96 , pp. 3461-3470
    • Demchenko, A.P.1    Mély, Y.2    Duportail, G.3    Klymchenko, A.S.4
  • 3
    • 0036293267 scopus 로고    scopus 로고
    • Fluorescent lipid probes: some properties and applications (a review)
    • Maier O., Oberle V., and Hoekstra D. Fluorescent lipid probes: some properties and applications (a review). Chem Phys Lipids 116 (2002) 3-18
    • (2002) Chem Phys Lipids , vol.116 , pp. 3-18
    • Maier, O.1    Oberle, V.2    Hoekstra, D.3
  • 4
    • 33846867956 scopus 로고    scopus 로고
    • Fluorescent sterols as tools in membrane biophysics and cell biology
    • A comprehensive review on fluorescent sterols.
    • Wustner D. Fluorescent sterols as tools in membrane biophysics and cell biology. Chem Phys Lipids 146 (2007) 1-25. A comprehensive review on fluorescent sterols.
    • (2007) Chem Phys Lipids , vol.146 , pp. 1-25
    • Wustner, D.1
  • 6
    • 67349204082 scopus 로고    scopus 로고
    • The fluorescent cholesterol analog dehydroergosterol induces liquid-ordered domains in model membranes
    • Garvik O., Benediktson P., Simonsen A.C., Ipsen J.H., and Wüstner D. The fluorescent cholesterol analog dehydroergosterol induces liquid-ordered domains in model membranes. Chem Phys Lipids 159 (2009) 114-118
    • (2009) Chem Phys Lipids , vol.159 , pp. 114-118
    • Garvik, O.1    Benediktson, P.2    Simonsen, A.C.3    Ipsen, J.H.4    Wüstner, D.5
  • 7
    • 49649109827 scopus 로고    scopus 로고
    • Visualization of sialyl LewisX glycosphingolipid microdomains in model membranes as selectin recognition motifs using a fluorescence label
    • Gege C., Schumacher G., Rothe U., Schmidt R.R., and Bendas G. Visualization of sialyl LewisX glycosphingolipid microdomains in model membranes as selectin recognition motifs using a fluorescence label. Carbohydr Res 343 (2008) 2361-2368
    • (2008) Carbohydr Res , vol.343 , pp. 2361-2368
    • Gege, C.1    Schumacher, G.2    Rothe, U.3    Schmidt, R.R.4    Bendas, G.5
  • 8
    • 51049094897 scopus 로고    scopus 로고
    • Cu-catalyzed azide-alkyne cycloaddition
    • Meldal M., and Tornoe C.W. Cu-catalyzed azide-alkyne cycloaddition. Chem Rev 108 (2008) 2952-3015
    • (2008) Chem Rev , vol.108 , pp. 2952-3015
    • Meldal, M.1    Tornoe, C.W.2
  • 9
    • 52249114702 scopus 로고    scopus 로고
    • Synthesis and convenient functionalization of azide-labeled diacylglycerol analogues for modular access to biologically active lipid probes
    • Smith M.D., Gong D., Sudhahar C.G., Reno J.C., Stahelin R.V., and Best M.D. Synthesis and convenient functionalization of azide-labeled diacylglycerol analogues for modular access to biologically active lipid probes. Bioconjugate Chem 19 (2008) 1855-1863
    • (2008) Bioconjugate Chem , vol.19 , pp. 1855-1863
    • Smith, M.D.1    Gong, D.2    Sudhahar, C.G.3    Reno, J.C.4    Stahelin, R.V.5    Best, M.D.6
  • 10
    • 70449631409 scopus 로고    scopus 로고
    • A modular synthesis of alkynyl-phosphocholine headgroups for labeling of sphingomyelin and phosphatidyl choline
    • in press
    • Sandbhor MS, Key JA, Strelkov IS, Cairo CW: A modular synthesis of alkynyl-phosphocholine headgroups for labeling of sphingomyelin and phosphatidyl choline. J Org Chem in press.
    • J Org Chem
    • Sandbhor, M.S.1    Key, J.A.2    Strelkov, I.S.3    Cairo, C.W.4
  • 11
    • 37649016975 scopus 로고    scopus 로고
    • Targeting phosphatidylserine on apoptotic cells with phages and peptides selected from a bacteriophage display library
    • Shao R., Xiong C., Wen X., Gelovani J.G., and Li C. Targeting phosphatidylserine on apoptotic cells with phages and peptides selected from a bacteriophage display library. Molecular Imaging 6 (2007) 417-426
    • (2007) Molecular Imaging , vol.6 , pp. 417-426
    • Shao, R.1    Xiong, C.2    Wen, X.3    Gelovani, J.G.4    Li, C.5
  • 12
    • 38449122910 scopus 로고    scopus 로고
    • Real-time cell assays of phospholipase A2s using fluorogenic phospholipids
    • Academic Press pp. 15-27
    • Manna D., Cho W., and Brown H.A. Real-time cell assays of phospholipase A2s using fluorogenic phospholipids. Methods Enzymol Volume 434 (2007), Academic Press pp. 15-27
    • (2007) Methods Enzymol , vol.434
    • Manna, D.1    Cho, W.2    Brown, H.A.3
  • 13
    • 0037960384 scopus 로고    scopus 로고
    • Allosteric interactions within subsites of a monomeric enzyme: kinetics of fluorogenic substrates of PI-specific phospholipase C
    • Birrell G.B., Zaikova T.O., Rukavishnikov A.V., Keana J.F.W., and Hayes Griffith O. Allosteric interactions within subsites of a monomeric enzyme: kinetics of fluorogenic substrates of PI-specific phospholipase C. Biophys J 84 (2003) 3264-3275
    • (2003) Biophys J , vol.84 , pp. 3264-3275
    • Birrell, G.B.1    Zaikova, T.O.2    Rukavishnikov, A.V.3    Keana, J.F.W.4    Hayes Griffith, O.5
  • 15
    • 33744768146 scopus 로고    scopus 로고
    • Fluorogenic phospholipids as head group-selective reporters of phospholipase A activity
    • Rose T.M., and Prestwich G.D. Fluorogenic phospholipids as head group-selective reporters of phospholipase A activity. ACS Chem Biol 1 (2006) 83-92
    • (2006) ACS Chem Biol , vol.1 , pp. 83-92
    • Rose, T.M.1    Prestwich, G.D.2
  • 16
    • 33745558112 scopus 로고    scopus 로고
    • Synthesis and evaluation of fluorogenic substrates for phospholipase D and phospholipase C
    • Rose T.M., and Prestwich G.D. Synthesis and evaluation of fluorogenic substrates for phospholipase D and phospholipase C. Org Lett 8 (2006) 2575-2578
    • (2006) Org Lett , vol.8 , pp. 2575-2578
    • Rose, T.M.1    Prestwich, G.D.2
  • 17
    • 34548769224 scopus 로고    scopus 로고
    • Probing phospholipase A2 with fluorescent phospholipid substrates
    • 2 both biochemically and using live cell imaging.
    • 2 both biochemically and using live cell imaging.
    • (2007) ChemBioChem , vol.8 , pp. 1555-1569
    • Wichmann, O.1    Gelb, M.H.2    Schultz, C.3
  • 18
    • 60349119099 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate lyase enzyme assay using a BODIPY-labeled substrate
    • Bandhuvula P., Li Z.G., Bittman R., and Saba JD. Sphingosine 1-phosphate lyase enzyme assay using a BODIPY-labeled substrate. Biochem Biophys Res Commun 380 (2009) 366-370
    • (2009) Biochem Biophys Res Commun , vol.380 , pp. 366-370
    • Bandhuvula, P.1    Li, Z.G.2    Bittman, R.3    Saba JD4
  • 19
    • 34250311282 scopus 로고    scopus 로고
    • Synthesis of a novel ceramide analogue and its use in a high-throughput fluorogenic assay for ceramidases
    • Bedia C., Casas J., Garcia V., Levade T., and Fabriàs G. Synthesis of a novel ceramide analogue and its use in a high-throughput fluorogenic assay for ceramidases. ChemBioChem 8 (2007) 642-648
    • (2007) ChemBioChem , vol.8 , pp. 642-648
    • Bedia, C.1    Casas, J.2    Garcia, V.3    Levade, T.4    Fabriàs, G.5
  • 20
    • 65549171632 scopus 로고    scopus 로고
    • Synthesis of a fluorogenic analogue of sphingosine-1-phosphate and its use to determine sphingosine-1-phosphate lyase activity
    • Bedia C., Camacho L., Casas J., Abad J.L., Delgado A., Van Veldhoven P.R., and Fabrias G. Synthesis of a fluorogenic analogue of sphingosine-1-phosphate and its use to determine sphingosine-1-phosphate lyase activity. ChemBioChem 10 (2009) 820-822
    • (2009) ChemBioChem , vol.10 , pp. 820-822
    • Bedia, C.1    Camacho, L.2    Casas, J.3    Abad, J.L.4    Delgado, A.5    Van Veldhoven, P.R.6    Fabrias, G.7
  • 21
    • 13844276672 scopus 로고    scopus 로고
    • Site-specific labeling of proteins with small molecules in live cells
    • Chen I., and Ting A.Y. Site-specific labeling of proteins with small molecules in live cells. Curr Opin Biotechnol 16 (2005) 35-40
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 35-40
    • Chen, I.1    Ting, A.Y.2
  • 22
    • 44449096254 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization
    • GPCRs are examined using an engineered snap-tag, allowing for studies of receptor oligomerization. This should be a generally applicable method for studying receptor clustering.
    • Maurel D., Comps-Agrar L., Brock C., Rives M.L., Bourrier E., Ayoub M.A., Bazin H., Tinel N., Durroux T., Prézeau L., et al. Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization. Nat Methods 5 (2008) 561-567. GPCRs are examined using an engineered snap-tag, allowing for studies of receptor oligomerization. This should be a generally applicable method for studying receptor clustering.
    • (2008) Nat Methods , vol.5 , pp. 561-567
    • Maurel, D.1    Comps-Agrar, L.2    Brock, C.3    Rives, M.L.4    Bourrier, E.5    Ayoub, M.A.6    Bazin, H.7    Tinel, N.8    Durroux, T.9    Prézeau, L.10
  • 23
    • 23444448243 scopus 로고    scopus 로고
    • Adding value to fusion proteins through covalent labelling
    • Gronemeyer T., Godin G., and Johnsson K. Adding value to fusion proteins through covalent labelling. Curr Opin Biotechnol 16 (2005) 453-458
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 453-458
    • Gronemeyer, T.1    Godin, G.2    Johnsson, K.3
  • 24
    • 13444261101 scopus 로고    scopus 로고
    • Selective chemical labeling of proteins in living cells
    • Miller L.W., and Cornish V.W. Selective chemical labeling of proteins in living cells. Curr Opin Chem Biol 9 (2005) 56-61
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 56-61
    • Miller, L.W.1    Cornish, V.W.2
  • 25
    • 35549004067 scopus 로고    scopus 로고
    • Specific and covalent labeling of a membrane protein with organic fluorochromes and quantum dots
    • An engineered label is introduced into LFA-1 and the receptor localization is observed during lymphocyte migration.
    • Bonasio R., Carman C.V., Kim E., Sage P.T., Love K.R., Mempel T.R., Springer T.A., and Von Andrian U.H. Specific and covalent labeling of a membrane protein with organic fluorochromes and quantum dots. Proc Natl Acad Sci U S A 104 (2007) 14753-14758. An engineered label is introduced into LFA-1 and the receptor localization is observed during lymphocyte migration.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14753-14758
    • Bonasio, R.1    Carman, C.V.2    Kim, E.3    Sage, P.T.4    Love, K.R.5    Mempel, T.R.6    Springer, T.A.7    Von Andrian, U.H.8
  • 27
    • 34347368946 scopus 로고    scopus 로고
    • Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases
    • Zhou Z., Cironi P., Lin A.J., Xu Y., Hrvatin S., Golan D.E., Silver P.A., Walsh C.T., and Yin J. Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases. ACS Chem Biol 2 (2007) 337-346
    • (2007) ACS Chem Biol , vol.2 , pp. 337-346
    • Zhou, Z.1    Cironi, P.2    Lin, A.J.3    Xu, Y.4    Hrvatin, S.5    Golan, D.E.6    Silver, P.A.7    Walsh, C.T.8    Yin, J.9
  • 28
    • 33745293709 scopus 로고    scopus 로고
    • Post-translational covalent labeling reveals heterogeneous mobility of individual G protein-coupled receptors in living cells
    • Prummer M., Meyer B.H., Franzini R., Segura J.M., George N., Johnsson K., and Vogel H. Post-translational covalent labeling reveals heterogeneous mobility of individual G protein-coupled receptors in living cells. ChemBioChem 7 (2006) 908-911
    • (2006) ChemBioChem , vol.7 , pp. 908-911
    • Prummer, M.1    Meyer, B.H.2    Franzini, R.3    Segura, J.M.4    George, N.5    Johnsson, K.6    Vogel, H.7
  • 29
    • 33646038598 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells
    • Lin C.W., and Ting A.Y. Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. J Am Chem Soc 128 (2006) 4542-4543
    • (2006) J Am Chem Soc , vol.128 , pp. 4542-4543
    • Lin, C.W.1    Ting, A.Y.2
  • 30
    • 61849124088 scopus 로고    scopus 로고
    • Expansion of the sortase-mediated labeling method for site-specific N-terminal labeling of cell surface proteins on living cells
    • Yamamoto T., and Nagamune T. Expansion of the sortase-mediated labeling method for site-specific N-terminal labeling of cell surface proteins on living cells. Chem Commun 9 (2009) 1022-1024
    • (2009) Chem Commun , vol.9 , pp. 1022-1024
    • Yamamoto, T.1    Nagamune, T.2
  • 32
    • 34248993985 scopus 로고    scopus 로고
    • Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins
    • Chen I., Choi Y.A., and Ting A.Y. Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins. J Am Chem Soc 129 (2007) 6619-6625
    • (2007) J Am Chem Soc , vol.129 , pp. 6619-6625
    • Chen, I.1    Choi, Y.A.2    Ting, A.Y.3
  • 33
    • 67650555677 scopus 로고    scopus 로고
    • Phosphopantetheinyl transferase catalyzed site-specific protein labeling with ADP conjugated chemical probes
    • Zou Y., and Yin J. Phosphopantetheinyl transferase catalyzed site-specific protein labeling with ADP conjugated chemical probes. J Am Chem Soc 131 (2009) 7548-7549
    • (2009) J Am Chem Soc , vol.131 , pp. 7548-7549
    • Zou, Y.1    Yin, J.2
  • 34
    • 49249125507 scopus 로고    scopus 로고
    • Covalent fluorescence labeling of his-tagged proteins on the surface of living cells
    • A short His-tag is used to label proteins in live cells using photocrosslinking.
    • Hintersteiner M., Weidemann T., Kimmerlin T., Filiz N., Buehler C., and Auer M. Covalent fluorescence labeling of his-tagged proteins on the surface of living cells. ChemBioChem 9 (2008) 1391-1395. A short His-tag is used to label proteins in live cells using photocrosslinking.
    • (2008) ChemBioChem , vol.9 , pp. 1391-1395
    • Hintersteiner, M.1    Weidemann, T.2    Kimmerlin, T.3    Filiz, N.4    Buehler, C.5    Auer, M.6
  • 36
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications
    • Adams S.R., Campbell R.E., Gross L.A., Martin B.R., Walkup G.K., Yao Y., Llopis J., and Tsien R.Y. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J Am Chem Soc 124 (2002) 6063-6076
    • (2002) J Am Chem Soc , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 37
    • 60549094701 scopus 로고    scopus 로고
    • Specific biarsenical labeling of cell surface proteins allows fluorescent-and biotin-tagging of amyloid precursor protein and prion proteins
    • A modified FlAsH labeling protocol was introduced which allows for improved labeling of membrane proteins.
    • Taguchi Y., Shi Z.D., Ruddy B., Dorward D.W., Greene L., and Baron G.S. Specific biarsenical labeling of cell surface proteins allows fluorescent-and biotin-tagging of amyloid precursor protein and prion proteins. Mol Biol Cell 20 (2009) 233-244. A modified FlAsH labeling protocol was introduced which allows for improved labeling of membrane proteins.
    • (2009) Mol Biol Cell , vol.20 , pp. 233-244
    • Taguchi, Y.1    Shi, Z.D.2    Ruddy, B.3    Dorward, D.W.4    Greene, L.5    Baron, G.S.6
  • 38
    • 58849164442 scopus 로고    scopus 로고
    • Single-molecule imaging of a fluorescent unnatural amino acid incorporated into nicotinic receptors
    • Pantoja R., Rodriguez E.A., Dibas M.I., Dougherty D.A., and Lester H.A. Single-molecule imaging of a fluorescent unnatural amino acid incorporated into nicotinic receptors. Biophys J 96 (2009) 226-237
    • (2009) Biophys J , vol.96 , pp. 226-237
    • Pantoja, R.1    Rodriguez, E.A.2    Dibas, M.I.3    Dougherty, D.A.4    Lester, H.A.5
  • 40
    • 34250810262 scopus 로고    scopus 로고
    • Fluorescent epibatidine agonists for neuronal and muscle-type nicotinic acetylcholine receptors
    • Single particle tracking of a fluorescent ligand analog is performed on nAChR in live cells.
    • Grandl J., Sakr E., Kotzyba-Hibert F., Krieger F., Bertrand S., Bertrand D., Vogel H., Goeldner M., and Hovius R. Fluorescent epibatidine agonists for neuronal and muscle-type nicotinic acetylcholine receptors. Angew Chem, Int Ed Engl 46 (2007) 3505-3508. Single particle tracking of a fluorescent ligand analog is performed on nAChR in live cells.
    • (2007) Angew Chem, Int Ed Engl , vol.46 , pp. 3505-3508
    • Grandl, J.1    Sakr, E.2    Kotzyba-Hibert, F.3    Krieger, F.4    Bertrand, S.5    Bertrand, D.6    Vogel, H.7    Goeldner, M.8    Hovius, R.9
  • 43
    • 33847407887 scopus 로고    scopus 로고
    • Probing orientations of single fluorescent labels on a peptide reversibly binding to the human delta-opioid receptor
    • Opioid receptor binding in live cells was studied by single molecule microscopy using a synthetic ligand-fluorophore conjugate.
    • Tokimoto T., Bethea T.R.C., Zhou M., Ghosh I., and Wirth M.J. Probing orientations of single fluorescent labels on a peptide reversibly binding to the human delta-opioid receptor. Appl Spectrosc 61 (2007) 130-137. Opioid receptor binding in live cells was studied by single molecule microscopy using a synthetic ligand-fluorophore conjugate.
    • (2007) Appl Spectrosc , vol.61 , pp. 130-137
    • Tokimoto, T.1    Bethea, T.R.C.2    Zhou, M.3    Ghosh, I.4    Wirth, M.J.5
  • 44
    • 63849308514 scopus 로고    scopus 로고
    • Fluorescent ligands of the bradykinin B receptors: pharmacologic characterization and application to the study of agonist-induced receptor translocation and cell surface receptor expression
    • Bawolak M.T., Gera L., Morissette G., Bouthillier J., Stewart J.M., Gobeil L.A., Lodge R., Adam A., and Marceau F. Fluorescent ligands of the bradykinin B receptors: pharmacologic characterization and application to the study of agonist-induced receptor translocation and cell surface receptor expression. J Pharmacol Exp Ther 329 (2009) 159-168
    • (2009) J Pharmacol Exp Ther , vol.329 , pp. 159-168
    • Bawolak, M.T.1    Gera, L.2    Morissette, G.3    Bouthillier, J.4    Stewart, J.M.5    Gobeil, L.A.6    Lodge, R.7    Adam, A.8    Marceau, F.9
  • 46
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase-new roles for an old actor
    • Soreq H., and Seidman S. Acetylcholinesterase-new roles for an old actor. Nat Rev Neurosci 2 (2001) 294-302
    • (2001) Nat Rev Neurosci , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 48
    • 0033816854 scopus 로고    scopus 로고
    • Ecto-enzymes: physiology meets pathology
    • Goding J.W. Ecto-enzymes: physiology meets pathology. J Leukocyte Biol 67 (2000) 285-311
    • (2000) J Leukocyte Biol , vol.67 , pp. 285-311
    • Goding, J.W.1
  • 50
    • 56249093847 scopus 로고    scopus 로고
    • CD15 expression in human myeloid cell differentiation is regulated by sialidase activity
    • Gadhoum S.Z., and Sackstein R. CD15 expression in human myeloid cell differentiation is regulated by sialidase activity. Nat Chem Biol 4 (2008) 751-757
    • (2008) Nat Chem Biol , vol.4 , pp. 751-757
    • Gadhoum, S.Z.1    Sackstein, R.2
  • 51
    • 51449106611 scopus 로고    scopus 로고
    • Effect of sphingomyelinase-mediated generation of ceramide on aggregation of low-density lipoprotein
    • Walters M.J., and Wrenn S.P. Effect of sphingomyelinase-mediated generation of ceramide on aggregation of low-density lipoprotein. Langmuir 24 (2008) 9642-9647
    • (2008) Langmuir , vol.24 , pp. 9642-9647
    • Walters, M.J.1    Wrenn, S.P.2
  • 53
    • 43749107913 scopus 로고    scopus 로고
    • Application of activity-based probes to the study of enzymes involved in cancer progression
    • Paulick M.G., and Bogyo M. Application of activity-based probes to the study of enzymes involved in cancer progression. Curr Opin Genet Dev 18 (2008) 97-106
    • (2008) Curr Opin Genet Dev , vol.18 , pp. 97-106
    • Paulick, M.G.1    Bogyo, M.2
  • 54
    • 34548666006 scopus 로고    scopus 로고
    • Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes
    • Blum G., von Degenfeld G., Merchant M.J., Blau H.M., and Bogyo M. Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes. Nat Chem Biol 3 (2007) 668-677
    • (2007) Nat Chem Biol , vol.3 , pp. 668-677
    • Blum, G.1    von Degenfeld, G.2    Merchant, M.J.3    Blau, H.M.4    Bogyo, M.5
  • 55
    • 63049095880 scopus 로고    scopus 로고
    • Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation
    • Cavallo-Medved D., Rudy D., Blum G., Bogyo M., Caglic D., and Sloane B.F. Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation. Exp Cell Res 315 (2009) 1234-1246
    • (2009) Exp Cell Res , vol.315 , pp. 1234-1246
    • Cavallo-Medved, D.1    Rudy, D.2    Blum, G.3    Bogyo, M.4    Caglic, D.5    Sloane, B.F.6
  • 56
    • 33847269756 scopus 로고    scopus 로고
    • Biochemical analysis of ecto-nucleotide pyrophosphatase phosphodiesterase activity in brain membranes indicates involvement of NPP1 isoenzyme in extracellular hydrolysis of diadenosine polyphosphates in central nervous system
    • Asensio A.C., Rodriguez-Ferrer C.R., Castaneyra-Perdomo A., Oaknin S., and Rotllan P. Biochemical analysis of ecto-nucleotide pyrophosphatase phosphodiesterase activity in brain membranes indicates involvement of NPP1 isoenzyme in extracellular hydrolysis of diadenosine polyphosphates in central nervous system. Neurochem Int 50 (2007) 581-590
    • (2007) Neurochem Int , vol.50 , pp. 581-590
    • Asensio, A.C.1    Rodriguez-Ferrer, C.R.2    Castaneyra-Perdomo, A.3    Oaknin, S.4    Rotllan, P.5
  • 57
    • 58149520825 scopus 로고    scopus 로고
    • Linking phospholipase mobility to activity by single-molecule wide-field microscopy
    • An elegant application of single molecule imaging of phospholipase activity in model membranes.
    • Rocha S., Hutchison J.A., Peneva K., Herrmann A., Müllen K., Skjøt M., Jørgensen C.I., Svendsen A., De Schryver F.C., Hofkens J., et al. Linking phospholipase mobility to activity by single-molecule wide-field microscopy. ChemPhysChem 10 (2009) 151-161. An elegant application of single molecule imaging of phospholipase activity in model membranes.
    • (2009) ChemPhysChem , vol.10 , pp. 151-161
    • Rocha, S.1    Hutchison, J.A.2    Peneva, K.3    Herrmann, A.4    Müllen, K.5    Skjøt, M.6    Jørgensen, C.I.7    Svendsen, A.8    De Schryver, F.C.9    Hofkens, J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.