메뉴 건너뛰기




Volumn 272, Issue 8, 2005, Pages 2076-2084

Hyperthermal stability of neuroglobin and cytoglobin

Author keywords

Cytoglobin; Disulfide bond; Ligand kinetics; Neuroglobin; Protein melting temperature

Indexed keywords

CYSTEINE; CYTOGLOBIN; GLOBIN; HISTIDINE; NEUROGLOBIN; UNCLASSIFIED DRUG;

EID: 17444369738     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04635.x     Document Type: Article
Times cited : (50)

References (31)
  • 2
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T, Ebner B, Weich B & Hankeln T (2002) Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol Biol Evol 19, 416-421.
    • (2002) Mol Biol Evol , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 3
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexa-coordinate hemoglobin
    • Trent JT III & Hargrove MS (2002) A ubiquitously expressed human hexa-coordinate hemoglobin. J Biol Chem 277, 19538-19545.
    • (2002) J Biol Chem , vol.277 , pp. 19538-19545
    • Trent III, J.T.1    Hargrove, M.S.2
  • 5
    • 0037449744 scopus 로고    scopus 로고
    • How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina
    • Schmidt M, Giessl A, Laufs T, Hankein T, Wolfrum U & Burmester T (2003) How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina. J Biol Chem 278, 1932-1935.
    • (2003) J Biol Chem , vol.278 , pp. 1932-1935
    • Schmidt, M.1    Giessl, A.2    Laufs, T.3    Hankein, T.4    Wolfrum, U.5    Burmester, T.6
  • 11
    • 3042727978 scopus 로고    scopus 로고
    • Neuroglobin: A respiratory protein of the nervous system
    • Burmester T & Hankeln T (2004) Neuroglobin: a respiratory protein of the nervous system. News Physiol Sci 19, 110-113.
    • (2004) News Physiol Sci , vol.19 , pp. 110-113
    • Burmester, T.1    Hankeln, T.2
  • 12
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury
    • Sun Y, Jin K, Mao XO, Zhu Y & Greenberg DA (2001) Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury. Proc Natl Acad Sci USA 98, 15306-15311.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.O.3    Zhu, Y.4    Greenberg, D.A.5
  • 17
    • 0021658956 scopus 로고
    • Allostery without conformational change. A plausible model
    • Cooper A & Dryden DT (1984) Allostery without conformational change. A plausible model. Eur Biophys J 11, 103-109.
    • (1984) Eur Biophys J , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.2
  • 18
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan MK, Mukund S, Kietzin A, Adams MW & Rees DC (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267, 1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kietzin, A.3    Adams, M.W.4    Rees, D.C.5
  • 19
    • 0027209738 scopus 로고
    • Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser117 → Phe
    • Anderson DE, Hurley JH, Nicholson H, Baase WA & Matthews BW (1993) Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser117 → Phe. Protein Sci 2, 1285-1290.
    • (1993) Protein Sci , vol.2 , pp. 1285-1290
    • Anderson, D.E.1    Hurley, J.H.2    Nicholson, H.3    Baase, W.A.4    Matthews, B.W.5
  • 21
    • 0028774720 scopus 로고
    • The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum
    • Russell RJ, Hough DW, Danson MJ & Taylor GL (1994) The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum. Structure 2, 1157-1167.
    • (1994) Structure , vol.2 , pp. 1157-1167
    • Russell, R.J.1    Hough, D.W.2    Danson, M.J.3    Taylor, G.L.4
  • 22
    • 0027488713 scopus 로고
    • Stabilization of creatinase from Pseudomonas putida by random mutagenesis
    • Schumann J, Bohm G, Schumacher G, Rudolph R & Jaenicke R (1993) Stabilization of creatinase from Pseudomonas putida by random mutagenesis. Protein Sci 2, 1612-1620.
    • (1993) Protein Sci , vol.2 , pp. 1612-1620
    • Schumann, J.1    Bohm, G.2    Schumacher, G.3    Rudolph, R.4    Jaenicke, R.5
  • 23
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Angstroms resolution
    • Tanner JJ, Hecht RM & Krause KL (1996) Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Angstroms resolution. Biochemistry 35, 2597-2609.
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 25
    • 0029115963 scopus 로고
    • The optimization of protein-solvent interactions: Thermostability and the role of hydrophobic and electrostatic interactions
    • Spassov VZ, Karshikoff AD & Ladenstein R (1995) The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions. Protein Sci 4, 1516-1527.
    • (1995) Protein Sci , vol.4 , pp. 1516-1527
    • Spassov, V.Z.1    Karshikoff, A.D.2    Ladenstein, R.3
  • 26
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove MS & Olson JS (1996) The stability of holomyoglobin is determined by heme affinity. Biochemistry 35, 11310-11318.
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 27
    • 0021096641 scopus 로고
    • Comparative studies on thermostability of calmodulin, skeletal muscle troponin C and their tryptic fragments
    • Brzeska H, Venyaminov S, Grabarek Z & Drabikowski W (1983) Comparative studies on thermostability of calmodulin, skeletal muscle troponin C and their tryptic fragments. FEBS Let 153, 169-173.
    • (1983) FEBS Let , vol.153 , pp. 169-173
    • Brzeska, H.1    Venyaminov, S.2    Grabarek, Z.3    Drabikowski, W.4
  • 29
    • 4143067901 scopus 로고    scopus 로고
    • Neuroglobin and other hexa-coordinated hemoglobins show a weak temperature dependence of oxygen binding
    • Uzan J, Dewilde S, Burmester T, Hankeln T, Moens L, Hamdane D, Marden MC & Kiger L (2004) Neuroglobin and other hexa-coordinated hemoglobins show a weak temperature dependence of oxygen binding. Biophys J 2, 1196-1204.
    • (2004) Biophys J , vol.2 , pp. 1196-1204
    • Uzan, J.1    Dewilde, S.2    Burmester, T.3    Hankeln, T.4    Moens, L.5    Hamdane, D.6    Marden, M.C.7    Kiger, L.8
  • 30
    • 7244245630 scopus 로고    scopus 로고
    • Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance
    • Fago A, Hundahl C, Dewilde S, Gilany K, Moens L & Weber RE (2004) Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance. J Biol Chem 279, 44417-44126.
    • (2004) J Biol Chem , vol.279 , pp. 44417-44126
    • Fago, A.1    Hundahl, C.2    Dewilde, S.3    Gilany, K.4    Moens, L.5    Weber, R.E.6
  • 31
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM & Bolen DW (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.