메뉴 건너뛰기




Volumn 4, Issue 4, 2008, Pages 491-498

Modulation of ligand binding affinity of tumorigenic carbonic anhydrase XII upon interaction with cationic CdTe quantum dots

Author keywords

Carbonic anhydrase; CdTe quantum dots; Energy transfer; Fluorescence spectroscopy; Tumor

Indexed keywords

BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; CADMIUM ALLOYS; CADMIUM COMPOUNDS; ENERGY TRANSFER; ENZYME ACTIVITY; ENZYMES; FLOW INTERACTIONS; FLUORESCENCE; LIGANDS; MODULATION; OPTICAL WAVEGUIDES; QUANTUM ELECTRONICS; SELF ASSEMBLY; TUMORS;

EID: 58149311051     PISSN: 15507033     EISSN: 15507041     Source Type: Journal    
DOI: 10.1166/jbn.2008.009     Document Type: Article
Times cited : (7)

References (23)
  • 1
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - a key regulatory factor in tumour growth
    • A. L. Harris, Hypoxia - a key regulatory factor in tumour growth. Nat. Rev. Cancer 2, 38 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 38
    • Harris, A.L.1
  • 3
    • 2542601328 scopus 로고    scopus 로고
    • Hypoxia inducible carbonic anhydrase IX, marker of tumour hypoxia, survival pathway and therapy target
    • C. Potter and A. L. Harris, Hypoxia inducible carbonic anhydrase IX, marker of tumour hypoxia, survival pathway and therapy target. Cell Cycle 3, 164 (2004).
    • (2004) Cell Cycle , vol.3 , pp. 164
    • Potter, C.1    Harris, A.L.2
  • 5
    • 0032514685 scopus 로고    scopus 로고
    • Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes
    • S. V. Ivanov, I. Kuzmin, M. H. Wei, S. Pack, L. Geil, B. E. Johnson, E. J. Stanbridge, and M. I. Lerman, Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes. Proc. Natl. Acad. Sci. USA 95, 12596 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12596
    • Ivanov, S.V.1    Kuzmin, I.2    Wei, M.H.3    Pack, S.4    Geil, L.5    Johnson, B.E.6    Stanbridge, E.J.7    Lerman, M.I.8
  • 7
    • 0035859892 scopus 로고    scopus 로고
    • Crystal structure of the dimeric extracellular domain of human carbonic anhydrase xii, a bitopic membrane protein overexpressed in certain cancer tumor cells
    • D.A. Whittington, A. Waheed, B. Ulmasov, G. N. Shah, J. H. Grubb, W. S. Sly, and D. W. Christianson, Crystal structure of the dimeric extracellular domain of human carbonic anhydrase xii, a bitopic membrane protein overexpressed in certain cancer tumor cells. Proc. Natl. Acad. Sci. USA 98, 9545 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9545
    • Whittington, D.A.1    Waheed, A.2    Ulmasov, B.3    Shah, G.N.4    Grubb, J.H.5    Sly, W.S.6    Christianson, D.W.7
  • 8
    • 42449158610 scopus 로고    scopus 로고
    • Nanoparticle fluorescence based technology for biological applications
    • W. Chen, Nanoparticle fluorescence based technology for biological applications. J. Nanosci. Nanotechnol. 8, 1019 (2008).
    • (2008) J. Nanosci. Nanotechnol , vol.8 , pp. 1019
    • Chen, W.1
  • 12
    • 33646706119 scopus 로고    scopus 로고
    • Synthesis and characterization of CdTe nanoparticles stabilized by cysteamine
    • Y. Qin, X. Yang, and J. Yu, Synthesis and characterization of CdTe nanoparticles stabilized by cysteamine. Chinese J. Inorg. Chem. 22, 851 (2006).
    • (2006) Chinese J. Inorg. Chem , vol.22 , pp. 851
    • Qin, Y.1    Yang, X.2    Yu, J.3
  • 13
    • 58149298425 scopus 로고    scopus 로고
    • J. Sambrook, E. F. Fritsch, and T. Maniatis eds, Cold Spring Harbor Laboratory Press, Plainview, NY
    • J. Sambrook, E. F. Fritsch, and T. Maniatis (eds.), Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Plainview, NY (2000), Vol. 1.
    • (2000) Molecular Cloning: A Laboratory Manual , vol.1
  • 14
    • 14844345349 scopus 로고    scopus 로고
    • Molecular basis for the origin of differential spectral and binding profiles of dansylamide with human carbonic anhydrase I and II
    • A. L. Banerjee, S. Tobwala, B. Ganguly, S. Mallik, and D. K. Srivastava, Molecular basis for the origin of differential spectral and binding profiles of dansylamide with human carbonic anhydrase I and II. Biochemistry 44, 3673 (2005).
    • (2005) Biochemistry , vol.44 , pp. 3673
    • Banerjee, A.L.1    Tobwala, S.2    Ganguly, B.3    Mallik, S.4    Srivastava, D.K.5
  • 15
    • 0026319199 scopus 로고
    • Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Protein folding and association
    • A. Nicholls, K. A. Sharp, and B. Honig, Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281 (1991).
    • (1991) Proteins , vol.11 , pp. 281
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 16
    • 84957894255 scopus 로고
    • Electrometric and colorimetric determination of carbonic anhydrase
    • K. M. Wilbur and N. G. Anderson, Electrometric and colorimetric determination of carbonic anhydrase. J. Biol. Chem. 176, 147 (1948).
    • (1948) J. Biol. Chem , vol.176 , pp. 147
    • Wilbur, K.M.1    Anderson, N.G.2
  • 17
    • 0032502269 scopus 로고    scopus 로고
    • Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-coa, to medium-chain acyl-coenzyme-a dehydrogenase
    • L. Qin and D. K. Srivastava, Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-coa, to medium-chain acyl-coenzyme-a dehydrogenase. Biochemistry 37, 3499 (1998).
    • (1998) Biochemistry , vol.37 , pp. 3499
    • Qin, L.1    Srivastava, D.K.2
  • 18
    • 77953865084 scopus 로고    scopus 로고
    • J. R. Lakowicz ed, Springer, Hoboken
    • J. R. Lakowicz (ed.), Principles of Fluorescence Spectroscopy, Springer, Hoboken (1999), Vol. 1.
    • (1999) Principles of Fluorescence Spectroscopy , vol.1
  • 19
    • 0014217558 scopus 로고
    • Combination of bovine carbonic anhydrase with a fluorescent sulfonamide
    • R. F. Chen and J. C. Kernohan, Combination of bovine carbonic anhydrase with a fluorescent sulfonamide. J. Biol. Chem. 242, 5813 (1967).
    • (1967) J. Biol. Chem , vol.242 , pp. 5813
    • Chen, R.F.1    Kernohan, J.C.2
  • 20
    • 0028935889 scopus 로고
    • Structural basis of inhibitor affinity to variants of human carbonic anhydrase II
    • S. K. Nair, J. F. Krebs, D. W. Christianson, and C. A. Fierke, Structural basis of inhibitor affinity to variants of human carbonic anhydrase II. Biochemistry 34, 3981 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3981
    • Nair, S.K.1    Krebs, J.F.2    Christianson, D.W.3    Fierke, C.A.4
  • 21
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods
    • Y. S. N. Day, C. L. Baird, R. L. Rich, and D. G. Myszka, Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods. Protein Sci. 11, 1017 (2002).
    • (2002) Protein Sci , vol.11 , pp. 1017
    • Day, Y.S.N.1    Baird, C.L.2    Rich, R.L.3    Myszka, D.G.4
  • 22
    • 0025195942 scopus 로고
    • 2 to the active site of human carbonic anhydrase ii: A molecular dynamics study
    • 2 to the active site of human carbonic anhydrase ii: A molecular dynamics study. Proc. Natl. Acad. Sci. USA 87, 3675 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3675
    • Liang, J.Y.1    Lipscomb, W.N.2
  • 23
    • 0030849266 scopus 로고    scopus 로고
    • Structure and mechanism of carbonic anhydrase
    • S. Lindskog, Structure and mechanism of carbonic anhydrase. Pharmacol. Ther. 74, 1 (1997).
    • (1997) Pharmacol. Ther , vol.74 , pp. 1
    • Lindskog, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.