메뉴 건너뛰기




Volumn 400, Issue 3, 2010, Pages 447-451

Characterization of caged compounds binding to proteins by NMR spectroscopy

Author keywords

Annexin A6; Caged ligands; Creatine kinase; Fourier transform infrared spectroscopy; NMR spectroscopy

Indexed keywords

CALPHOBINDIN II; CREATINE KINASE; CREATINE KINASE MM; LIGAND; NUCLEOTIDE; ADENOSINE TRIPHOSPHATE; GUANOSINE 5'-O-(3-THIOTRIPHOSPHATE) P-3-(1-(4,5-DIMETHOXY-2-NITROPHENYL)ETHYL) ESTER; GUANOSINE TRIPHOSPHATE; P(3)-1-(2-NITRO)PHENYLETHYLADENOSINE 5'-TRIPHOSPHATE; PROTEIN BINDING;

EID: 77956891988     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.08.104     Document Type: Article
Times cited : (3)

References (43)
  • 1
    • 34547638628 scopus 로고    scopus 로고
    • Caged compounds: photorelease technology for control of cellular chemistry and physiology
    • Ellis-Davies G.C.R. Caged compounds: photorelease technology for control of cellular chemistry and physiology. Nat. Methods 2007, 4:619-628.
    • (2007) Nat. Methods , vol.4 , pp. 619-628
    • Ellis-Davies, G.C.R.1
  • 2
    • 0020016226 scopus 로고
    • Physiological and pharmacological manipulations with light flashes
    • Lester H.A., Nerbonne J.M. Physiological and pharmacological manipulations with light flashes. Annu. Rev. Biophys. Bioeng. 1982, 11:151-175.
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 151-175
    • Lester, H.A.1    Nerbonne, J.M.2
  • 3
    • 0025359827 scopus 로고
    • Photochemical manipulation of divalent cation levels
    • Kaplan J.H. Photochemical manipulation of divalent cation levels. Annu. Rev. Physiol. 1990, 52:897-914.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 897-914
    • Kaplan, J.H.1
  • 4
    • 0017867017 scopus 로고
    • Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts
    • Kaplan J.H., Forbush B., Hoffman J.F. Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts. Biochemistry 1978, 17:1929-1935.
    • (1978) Biochemistry , vol.17 , pp. 1929-1935
    • Kaplan, J.H.1    Forbush, B.2    Hoffman, J.F.3
  • 5
    • 33748797724 scopus 로고    scopus 로고
    • Controlled release of DNA/polyamine complex by photoirradiation of a solid phase presenting o-nitrobenzyl ether tethered spermine or polyethyleneimine
    • Kim M.S., Diamond S.L. Controlled release of DNA/polyamine complex by photoirradiation of a solid phase presenting o-nitrobenzyl ether tethered spermine or polyethyleneimine. Bioorg. Med. Chem. Lett. 2006, 16:5572-5575.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 5572-5575
    • Kim, M.S.1    Diamond, S.L.2
  • 6
    • 35048824748 scopus 로고    scopus 로고
    • Optically triggered release of DNA from multivalent dendrons by degrading and charge-switching multivalency
    • Kostiainen M.A., Smith D.K., Ikkala O. Optically triggered release of DNA from multivalent dendrons by degrading and charge-switching multivalency. Angew. Chem. Int. Ed. Engl. 2007, 46:7600-7604.
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 7600-7604
    • Kostiainen, M.A.1    Smith, D.K.2    Ikkala, O.3
  • 7
    • 33744801096 scopus 로고    scopus 로고
    • Formulation of photocleavable liposomes and the mechanism of their content release
    • Chandra B., Subramaniam R., Mallik S., Srivastava D.K. Formulation of photocleavable liposomes and the mechanism of their content release. Org. Biomol. Chem. 2006, 4:1730-1740.
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 1730-1740
    • Chandra, B.1    Subramaniam, R.2    Mallik, S.3    Srivastava, D.K.4
  • 8
    • 14544287702 scopus 로고    scopus 로고
    • Synthesis and photochemical properties of photoactivated antitumor prodrugs releasing 5-fluorouracil
    • Zhang Z., Hatta H., Ito T., Nishimoto S. Synthesis and photochemical properties of photoactivated antitumor prodrugs releasing 5-fluorouracil. Org. Biomol. Chem. 2005, 3:592-596.
    • (2005) Org. Biomol. Chem. , vol.3 , pp. 592-596
    • Zhang, Z.1    Hatta, H.2    Ito, T.3    Nishimoto, S.4
  • 9
    • 0037945575 scopus 로고    scopus 로고
    • Phototriggered delivery of hydrophobic carbonic anhydrase inhibitors
    • Kehayova P.D., Woodrell C.D., Dostal P.J., et al. Phototriggered delivery of hydrophobic carbonic anhydrase inhibitors. Photochem. Photobiol. Sci. 2002, 1:774-779.
    • (2002) Photochem. Photobiol. Sci. , vol.1 , pp. 774-779
    • Kehayova, P.D.1    Woodrell, C.D.2    Dostal, P.J.3
  • 10
    • 49649112436 scopus 로고    scopus 로고
    • Creatine and creatine kinase in health and disease-a bright future ahead?
    • Wyss M., Braissant O., Pischel I., et al. Creatine and creatine kinase in health and disease-a bright future ahead?. Subcell Biochem. 2007, 46:309-334.
    • (2007) Subcell Biochem. , vol.46 , pp. 309-334
    • Wyss, M.1    Braissant, O.2    Pischel, I.3
  • 11
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: linking Ca2+ signalling to membrane dynamics
    • Gerke V., Creutz C.E., Moss S.E. Annexins: linking Ca2+ signalling to membrane dynamics. Nat. Rev. Mol. Cell Biol. 2005, 6:449-461.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 12
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M., Meyer B. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J. Am. Chem. Soc. 2001, 123:6108-6117.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 14
    • 34548093336 scopus 로고    scopus 로고
    • Effect of temperature in Saturation Transfer Difference NMR experiments
    • Groves P., Kövér K.E., André S., et al. Effect of temperature in Saturation Transfer Difference NMR experiments. Magn. Reson. Chem. 2007, 45:745-748.
    • (2007) Magn. Reson. Chem. , vol.45 , pp. 745-748
    • Groves, P.1    Kövér, K.E.2    André, S.3
  • 16
    • 0028212764 scopus 로고
    • Evolution of phosphagen kinase. Primary structure of glycocyamine kinase and arginine kinase from invertebrates
    • Suzuki T., Furukohri T. Evolution of phosphagen kinase. Primary structure of glycocyamine kinase and arginine kinase from invertebrates. J. Mol. Biol. 1994, 237:353-357.
    • (1994) J. Mol. Biol. , vol.237 , pp. 353-357
    • Suzuki, T.1    Furukohri, T.2
  • 17
    • 0035052706 scopus 로고    scopus 로고
    • Evolution and physiological roles of phosphagen systems
    • Ellington W.R. Evolution and physiological roles of phosphagen systems. Annu. Rev. Physiol. 2001, 63:289-325.
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 289-325
    • Ellington, W.R.1
  • 18
    • 77956904558 scopus 로고
    • Creatine kinase (Adenosine 5'-triphosphate-creatine phosphotransferase)
    • Academic Press, New York
    • Watts D.C. Creatine kinase (Adenosine 5'-triphosphate-creatine phosphotransferase). The Enzymes 1973, vol. 8:383-455. Academic Press, New York.
    • (1973) The Enzymes , vol.8 , pp. 383-455
    • Watts, D.C.1
  • 19
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • Bessman S.P., Carpenter C.L. The creatine-creatine phosphate energy shuttle. Ann. Rev. Biochem. 1985, 54:831-862.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 831-862
    • Bessman, S.P.1    Carpenter, C.L.2
  • 20
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis
    • Wallimann T., Wyss M., Brdiczka D., et al. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis. Biochem. J. 1992, 281:21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3
  • 21
    • 0002721248 scopus 로고
    • Comparisons of creatine kinase primary structures
    • Babbitt P.C., Kenyon G.L., Kuntz I.D., et al. Comparisons of creatine kinase primary structures. J. Prot. Chem. 1986, 5:1-14.
    • (1986) J. Prot. Chem. , vol.5 , pp. 1-14
    • Babbitt, P.C.1    Kenyon, G.L.2    Kuntz, I.D.3
  • 22
    • 0024299193 scopus 로고    scopus 로고
    • Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework
    • Hossle J.P., Schlegel J., Wegmann G., et al. Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework. Biochem. Biophys. Res. Commun. 1998, 151:408-416.
    • (1998) Biochem. Biophys. Res. Commun. , vol.151 , pp. 408-416
    • Hossle, J.P.1    Schlegel, J.2    Wegmann, G.3
  • 23
    • 0015598038 scopus 로고
    • A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase
    • Turner D.C., Wallimann T., Eppenberger H.M. A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase. Proc. Natl. Acad. Sci. USA 1973, 70:702-705.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 702-705
    • Turner, D.C.1    Wallimann, T.2    Eppenberger, H.M.3
  • 24
    • 0001440934 scopus 로고
    • Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences
    • Pickering L., Pang H., Biemann K., et al. Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences. Proc. Natl. Acad. Sci. USA 1985, 82:2310-2314.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2310-2314
    • Pickering, L.1    Pang, H.2    Biemann, K.3
  • 25
    • 0029820647 scopus 로고    scopus 로고
    • Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study
    • Raimbault C., Buchet R., Vial C. Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study. Eur. J. Biochem. 1996, 240:134-142.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 134-142
    • Raimbault, C.1    Buchet, R.2    Vial, C.3
  • 26
    • 0034622590 scopus 로고    scopus 로고
    • Magnesium-adenosine diphosphate binding sites in wild-type creatine kinase and in mutants: role of aromatic residues probed by Raman and infrared spectroscopies
    • Hagemann H., Marcillat O., Buchet R., Vial C. Magnesium-adenosine diphosphate binding sites in wild-type creatine kinase and in mutants: role of aromatic residues probed by Raman and infrared spectroscopies. Biochemistry 2000, 39:9251-9256.
    • (2000) Biochemistry , vol.39 , pp. 9251-9256
    • Hagemann, H.1    Marcillat, O.2    Buchet, R.3    Vial, C.4
  • 27
    • 0031045929 scopus 로고    scopus 로고
    • Conformational changes of arginine kinase induced by photochemical release of nucleotides from caged nucleotides-an infrared difference-spectroscopy investigation
    • Raimbault C., Besson F., Buchet R. Conformational changes of arginine kinase induced by photochemical release of nucleotides from caged nucleotides-an infrared difference-spectroscopy investigation. Eur. J. Biochem. 1997, 244:343-351.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 343-351
    • Raimbault, C.1    Besson, F.2    Buchet, R.3
  • 28
    • 0035814912 scopus 로고    scopus 로고
    • Structural changes of mitochondrial creatine kinase upon binding of ADP, ATP, or Pi, observed by reaction-induced infrared difference spectra
    • Granjon T., Vacheron M.-J., Vial C., Buchet R. Structural changes of mitochondrial creatine kinase upon binding of ADP, ATP, or Pi, observed by reaction-induced infrared difference spectra. Biochemistry 2001, 40:2988-2994.
    • (2001) Biochemistry , vol.40 , pp. 2988-2994
    • Granjon, T.1    Vacheron, M.-J.2    Vial, C.3    Buchet, R.4
  • 29
    • 0035916253 scopus 로고    scopus 로고
    • Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms
    • Zscherp C., Barth A. Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms. Biochemistry 2001, 40:1875-1883.
    • (2001) Biochemistry , vol.40 , pp. 1875-1883
    • Zscherp, C.1    Barth, A.2
  • 30
    • 0030943060 scopus 로고    scopus 로고
    • Interaction of annexins IV and VI with ATP. An alternative mechanism by which a cellular function of these calcium- and membrane-binding proteins is regulated
    • Bandorowicz-Pikula J., Awasthi Y.C. Interaction of annexins IV and VI with ATP. An alternative mechanism by which a cellular function of these calcium- and membrane-binding proteins is regulated. FEBS Lett. 1997, 409:300-306.
    • (1997) FEBS Lett. , vol.409 , pp. 300-306
    • Bandorowicz-Pikula, J.1    Awasthi, Y.C.2
  • 31
    • 0031463513 scopus 로고    scopus 로고
    • The relationship between the binding of ATP and calcium to annexin IV. Effect of nucleotide on the calcium-dependent interaction of annexin with phosphatidylserine
    • Bandorowicz-Pikula J., Wrzosek A., Makowski P., Pikula S. The relationship between the binding of ATP and calcium to annexin IV. Effect of nucleotide on the calcium-dependent interaction of annexin with phosphatidylserine. Mol. Membr. Biol. 1997, 14:179-186.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 179-186
    • Bandorowicz-Pikula, J.1    Wrzosek, A.2    Makowski, P.3    Pikula, S.4
  • 32
    • 0032703759 scopus 로고    scopus 로고
    • Annexin VI interacts with adenine nucleotides and their analogs
    • Danieluk M., Pikula S., Bandorowicz-Pikula J. Annexin VI interacts with adenine nucleotides and their analogs. Biochimie 1999, 81:717-726.
    • (1999) Biochimie , vol.81 , pp. 717-726
    • Danieluk, M.1    Pikula, S.2    Bandorowicz-Pikula, J.3
  • 33
    • 0033527404 scopus 로고    scopus 로고
    • ATP-Binding site of annexin VI characterized by photochemical release of nucleotide and infrared difference spectroscopy
    • Bandorowicz-Pikula J., Wrzosek A., Danieluk M., et al. ATP-Binding site of annexin VI characterized by photochemical release of nucleotide and infrared difference spectroscopy. Biochem. Biophys. Res. Commun. 1999, 263:775-779.
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 775-779
    • Bandorowicz-Pikula, J.1    Wrzosek, A.2    Danieluk, M.3
  • 34
    • 0036229987 scopus 로고    scopus 로고
    • GTP-induced membrane binding and ion channel activity of annexin VI: is annexin VI a GTP biosensor?
    • Kirilenko A., Golczak M., Pikula S., et al. GTP-induced membrane binding and ion channel activity of annexin VI: is annexin VI a GTP biosensor?. Biophys. J. 2002, 82:2737-2745.
    • (2002) Biophys. J. , vol.82 , pp. 2737-2745
    • Kirilenko, A.1    Golczak, M.2    Pikula, S.3
  • 35
    • 0041664870 scopus 로고    scopus 로고
    • A putative consensus sequence for the nucleotide-binding site of annexin A6
    • Bandorowicz-Pikula J., Kirilenko A., van Deursen R., et al. A putative consensus sequence for the nucleotide-binding site of annexin A6. Biochemistry 2003, 42:9137-9146.
    • (2003) Biochemistry , vol.42 , pp. 9137-9146
    • Bandorowicz-Pikula, J.1    Kirilenko, A.2    van Deursen, R.3
  • 36
    • 33645954276 scopus 로고    scopus 로고
    • Effects of mutagenesis of W343 in human annexin A6 isoform 1 on its interaction with GTP: nucleotide-induced oligomer formation and ion channel activity
    • Kirilenko A., Pikula S., Bandorowicz-Pikula J. Effects of mutagenesis of W343 in human annexin A6 isoform 1 on its interaction with GTP: nucleotide-induced oligomer formation and ion channel activity. Biochemistry 2006, 45:4965-4973.
    • (2006) Biochemistry , vol.45 , pp. 4965-4973
    • Kirilenko, A.1    Pikula, S.2    Bandorowicz-Pikula, J.3
  • 38
    • 43449106212 scopus 로고    scopus 로고
    • Calcium- and pH-dependent localization of annexin A6 isoforms in Balb/3T3 fibroblasts reflecting their potential participation in vesicular transport
    • Strzelecka-Kiliszek A., Buszewska M., Podszywalow-Bartnicka P., et al. Calcium- and pH-dependent localization of annexin A6 isoforms in Balb/3T3 fibroblasts reflecting their potential participation in vesicular transport. J. Cell. Biochem. 2008, 104:418-434.
    • (2008) J. Cell. Biochem. , vol.104 , pp. 418-434
    • Strzelecka-Kiliszek, A.1    Buszewska, M.2    Podszywalow-Bartnicka, P.3
  • 39
    • 0030741824 scopus 로고    scopus 로고
    • Fluorescence spectroscopic studies on interactions between liver annexin VI and nucleotides-a possible role for a tryptophan residue
    • Bandorowicz-Pikuła J., Wrzosek A., Pikuła S., Awasthi Y.C. Fluorescence spectroscopic studies on interactions between liver annexin VI and nucleotides-a possible role for a tryptophan residue. Eur. J. Biochem. 1997, 248:238-244.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 238-244
    • Bandorowicz-Pikuła, J.1    Wrzosek, A.2    Pikuła, S.3    Awasthi, Y.C.4
  • 40
    • 0031574062 scopus 로고    scopus 로고
    • Nucleotide binding sites in wild-type creatine kinase and in W227Y mutant probed by photochemical release of nucleotides and infrared difference spectroscopy
    • Raimbault C., Perraut C., Vial C., Buchet R. Nucleotide binding sites in wild-type creatine kinase and in W227Y mutant probed by photochemical release of nucleotides and infrared difference spectroscopy. Eur. J. Biochem. 1997, 250:773-782.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 773-782
    • Raimbault, C.1    Perraut, C.2    Vial, C.3    Buchet, R.4
  • 41
    • 0030789742 scopus 로고    scopus 로고
    • ADP-binding and ATP-binding sites in native and proteinase-K-digested creatine kinase, probed by reaction-induced difference infrared spectroscopy
    • Raimbault C., Leydier C., Vial C., Buchet R. ADP-binding and ATP-binding sites in native and proteinase-K-digested creatine kinase, probed by reaction-induced difference infrared spectroscopy. Eur. J. Biochem. 1997, 247:1197-1208.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1197-1208
    • Raimbault, C.1    Leydier, C.2    Vial, C.3    Buchet, R.4
  • 42
    • 31744435251 scopus 로고    scopus 로고
    • Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
    • Burz D.S., Dutta K., Cowburn D., Shekhtman A. Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR). Nat. Methods 2006, 3:91-93.
    • (2006) Nat. Methods , vol.3 , pp. 91-93
    • Burz, D.S.1    Dutta, K.2    Cowburn, D.3    Shekhtman, A.4
  • 43
    • 35048859971 scopus 로고    scopus 로고
    • 15N-group selective STD NMR experiment to study intermolecular interactions in heavily overlapped spectra
    • 15N-group selective STD NMR experiment to study intermolecular interactions in heavily overlapped spectra. J. Am. Chem. Soc. 2007, 129:11579-11582.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11579-11582
    • Kövér, K.E.1    Groves, P.2    Jiménez-Barbero, J.3    Batta, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.