메뉴 건너뛰기




Volumn 143, Issue 2, 2006, Pages 228-233

Functional characterization of parvalbumin from the Arctic cod (Boreogadus saida): Similarity in calcium affinity among parvalbumins from polar teleosts

Author keywords

Calcium affinity; Calcium binding protein; EF hand protein; Muscle; Parvalbumin; Teleost fish; Temperature

Indexed keywords

CALCIUM; PARVALBUMIN;

EID: 32044440802     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2005.11.020     Document Type: Article
Times cited : (14)

References (22)
  • 1
    • 0141654004 scopus 로고    scopus 로고
    • Impact of proline residues on parvalbumin stability
    • S. Agah, J.D. Larson, and M.T. Henzl Impact of proline residues on parvalbumin stability Biochemistry 42 2003 10886 10895
    • (2003) Biochemistry , vol.42 , pp. 10886-10895
    • Agah, S.1    Larson, J.D.2    Henzl, M.T.3
  • 4
    • 0033570025 scopus 로고    scopus 로고
    • Metal-ion affinity and specificity in EF-hand proteins: Coordination geometry and domain plasticity in parvalbumin
    • M.S. Cates, M.B. Berry, E.L. Ho, Q. Li, J.D. Potter, and G.N. Phillips Jr. Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin Structure 7 1999 1269 1278
    • (1999) Structure , vol.7 , pp. 1269-1278
    • Cates, M.S.1    Berry, M.B.2    Ho, E.L.3    Li, Q.4    Potter, J.D.5    Phillips Jr., G.N.6
  • 5
    • 0036192876 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium and magnesium binding to parvalbumin
    • M.S. Cates, M.L. Teodoro, and G.N. Phillips Jr. Molecular mechanisms of calcium and magnesium binding to parvalbumin Biophys. J. 82 2002 1133 1146
    • (2002) Biophys. J. , vol.82 , pp. 1133-1146
    • Cates, M.S.1    Teodoro, M.L.2    Phillips Jr., G.N.3
  • 6
    • 0033568444 scopus 로고    scopus 로고
    • Remodeling of the AB site of rat parvalbumin and oncomodulin into a canonical EF-hand
    • J.A. Cox, I. Durussel, D.J. Scott, and M.W. Berchtold Remodeling of the AB site of rat parvalbumin and oncomodulin into a canonical EF-hand Eur. J. Biochem. 264 1999 790 799
    • (1999) Eur. J. Biochem. , vol.264 , pp. 790-799
    • Cox, J.A.1    Durussel, I.2    Scott, D.J.3    Berchtold, M.W.4
  • 7
    • 0029670819 scopus 로고    scopus 로고
    • Kinetic tuning of the EF-hand calcium binding motif: The gateway residue independently adjusts (i) barrier height and (ii) equilibrium
    • S.K. Drake, and J.J. Falke Kinetic tuning of the EF-hand calcium binding motif: the gateway residue independently adjusts (i) barrier height and (ii) equilibrium Biochemistry 35 1996 1753 1760
    • (1996) Biochemistry , vol.35 , pp. 1753-1760
    • Drake, S.K.1    Falke, J.J.2
  • 8
    • 0028221324 scopus 로고
    • Calcium and magnesium binding to rat parvalbumin
    • M. Eberhard, and P. Erne Calcium and magnesium binding to rat parvalbumin Eur. J. Biochem. 222 1994 21 26
    • (1994) Eur. J. Biochem. , vol.222 , pp. 21-26
    • Eberhard, M.1    Erne, P.2
  • 9
    • 14644413494 scopus 로고    scopus 로고
    • Temperature sensitivity of calcium binding for parvalbumins from Antarctic and temperate zone teleost fishes
    • J.R. Erickson, B.D. Sidell, and T.S. Moerland Temperature sensitivity of calcium binding for parvalbumins from Antarctic and temperate zone teleost fishes Comp. Biochem. Physiol. A 140 2005 179 185
    • (2005) Comp. Biochem. Physiol. a , vol.140 , pp. 179-185
    • Erickson, J.R.1    Sidell, B.D.2    Moerland, T.S.3
  • 10
    • 0027945446 scopus 로고
    • Molecular tuning of ion binding to calcium signaling proteins
    • J.J. Falke, S.K. Drake, A.L. Hazard, and O.B. Peersen Molecular tuning of ion binding to calcium signaling proteins Q. Rev. Biophys. 27 1994 219 290
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 219-290
    • Falke, J.J.1    Drake, S.K.2    Hazard, A.L.3    Peersen, O.B.4
  • 12
    • 0021733359 scopus 로고
    • Parvalbumin, an intracellular calcium-binding protein; Distribution, properties, and possible roles in mammalian cells
    • C.W. Heizmann Parvalbumin, an intracellular calcium-binding protein; distribution, properties, and possible roles in mammalian cells Experientia 40 1984 910 921
    • (1984) Experientia , vol.40 , pp. 910-921
    • Heizmann, C.W.1
  • 13
    • 0030896384 scopus 로고    scopus 로고
    • Evolution of lactate dehydrogenase-A homologs of barracuda fishes (genus Sphyraena) from different thermal environments: Differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site
    • L.Z. Holland, M. McFall-Ngai, and G.N. Somero Evolution of lactate dehydrogenase-A homologs of barracuda fishes (genus Sphyraena) from different thermal environments: differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site Biochemistry 36 1997 3207 3215
    • (1997) Biochemistry , vol.36 , pp. 3207-3215
    • Holland, L.Z.1    McFall-Ngai, M.2    Somero, G.N.3
  • 14
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • R.H. Kretsinger, and C.E. Nockolds Carp muscle calcium-binding protein. II. Structure determination and general description J. Biol. Chem. 248 1973 3313 3326
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 15
    • 0030973268 scopus 로고    scopus 로고
    • Conformational effects of calcium release from parvalbumin: Comparison of computational simulations with spectroscopic investigations
    • M. Laberge, W.W. Wright, K. Sudhakar, P.A. Liebman, and J.M. Vanderkooi Conformational effects of calcium release from parvalbumin: comparison of computational simulations with spectroscopic investigations Biochemistry 36 1997 5363 5371
    • (1997) Biochemistry , vol.36 , pp. 5363-5371
    • Laberge, M.1    Wright, W.W.2    Sudhakar, K.3    Liebman, P.A.4    Vanderkooi, J.M.5
  • 16
    • 0030939677 scopus 로고    scopus 로고
    • The isolation of parvalbumin isoforms from the tail muscle of the American alligator (Alligator mississipiensis)
    • E.L. Laney, J. Shabanowitz, G. King, D.F. Hunt, and D.J. Nelson The isolation of parvalbumin isoforms from the tail muscle of the American alligator (Alligator mississipiensis) J. Inorg. Biochem. 66 1997 67 76
    • (1997) J. Inorg. Biochem. , vol.66 , pp. 67-76
    • Laney, E.L.1    Shabanowitz, J.2    King, G.3    Hunt, D.F.4    Nelson, D.J.5
  • 17
    • 0029052550 scopus 로고
    • Increase of skeletal muscle relaxation speed by direct injection of parvalbumin cDNA
    • M. Muntener, L. Kaser, J. Weber, and M.W. Berchtold Increase of skeletal muscle relaxation speed by direct injection of parvalbumin cDNA Proc. Natl. Acad. Sci. U. S. A. 92 1995 6504 6508
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6504-6508
    • Muntener, M.1    Kaser, L.2    Weber, J.3    Berchtold, M.W.4
  • 20
    • 0030371176 scopus 로고    scopus 로고
    • Role of parvalbumin in skeletal muscle relaxation
    • J.A. Rall Role of parvalbumin in skeletal muscle relaxation News Physiol. Sci. 11 1996 249 255
    • (1996) News Physiol. Sci. , vol.11 , pp. 249-255
    • Rall, J.A.1
  • 21
    • 0028949615 scopus 로고
    • Proteins and temperature
    • G.N. Somero Proteins and temperature Annu. Rev. Physiol. 57 1995 43 68
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 22
    • 0035501710 scopus 로고    scopus 로고
    • Structure of rat parvalbumin with deleted AB domain: Implications for the evolution of EF-hand calcium-binding proteins and possible physiological relevance
    • M. Thepaut, M. Strub, A. Cave, J. Baneres, M.W. Berchtold, C. Dumas, and A. Padilla Structure of rat parvalbumin with deleted AB domain: implications for the evolution of EF-hand calcium-binding proteins and possible physiological relevance Proteins 45 2001 117 128
    • (2001) Proteins , vol.45 , pp. 117-128
    • Thepaut, M.1    Strub, M.2    Cave, A.3    Baneres, J.4    Berchtold, M.W.5    Dumas, C.6    Padilla, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.