메뉴 건너뛰기




Volumn 6, Issue 4, 2011, Pages 393-398

Identification of proteins interacting with lactate dehydrogenase in claw muscle of the porcelain crab Petrolisthes cinctipes

Author keywords

Glycolysis; Lactate dehydrogenase; Metabolon; Protein protein interactions; Stability

Indexed keywords

CYTOSKELETON PROTEIN; GLYCOLYTIC ENZYME; HEMOCYANIN; LACTATE DEHYDROGENASE; MUSCLE PROTEIN;

EID: 80755153605     PISSN: 1744117X     EISSN: 18780407     Source Type: Journal    
DOI: 10.1016/j.cbd.2011.09.002     Document Type: Article
Times cited : (4)

References (33)
  • 1
    • 0023334744 scopus 로고
    • Thermal denaturation of bacteriophage T4 lysozyme at neutral pH
    • W. Becktel, and W. Baase Thermal denaturation of bacteriophage T4 lysozyme at neutral pH Biopolymers 26 1987 619 623
    • (1987) Biopolymers , vol.26 , pp. 619-623
    • Becktel, W.1    Baase, W.2
  • 2
    • 0027828164 scopus 로고
    • Immobilized enzymes as tools for the demonstration of metabolon formation. A short overview
    • S. Beeckmans, E. Van Driessche, and L. Kanarek Immobilized enzymes as tools for the demonstration of metabolon formation. A short overview J. Mol. Recogn. 6 1993 195 204
    • (1993) J. Mol. Recogn. , vol.6 , pp. 195-204
    • Beeckmans, S.1    Van Driessche, E.2    Kanarek, L.3
  • 4
    • 55749086024 scopus 로고    scopus 로고
    • Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice
    • M.E. Campanella, H. Chu, N.J. Wandersee, L.L. Peters, N. Mohandas, D.M. Gilligan, and P.S. Low Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice Blood 112 2008 3900 3906
    • (2008) Blood , vol.112 , pp. 3900-3906
    • Campanella, M.E.1    Chu, H.2    Wandersee, N.J.3    Peters, L.L.4    Mohandas, N.5    Gilligan, D.M.6    Low, P.S.7
  • 5
    • 35548974795 scopus 로고    scopus 로고
    • Activity, Stability and Structural Studies of Lactate Dehydrogenases Adapted to Extreme Thermal Environments
    • DOI 10.1016/j.jmb.2007.09.049, PII S0022283607012375
    • N. Coquelle, E. Fioravanti, M. Weik, F. Vellieux, and D. Madern Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments J. Mol. Biol. 374 2007 547 562 (Pubitemid 350007659)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.2 , pp. 547-562
    • Coquelle, N.1    Fioravanti, E.2    Weik, M.3    Vellieux, F.4    Madern, D.5
  • 6
    • 0025384606 scopus 로고
    • SDS-PAGE analysis of protein and lipopolysaccharide of extracellular vesicules and sarkosyl-insoluble membranes from bacteroides gingivalis
    • M. Deslauiers, D. ni Eidhin, L. Lamonde, and C. Mouton SDS-PAGE analysis of protein and lipopolysaccharide of extracellular vesicules and sarkosyl-insoluble membranes from bacteroides gingivalis Oral Microbiol. Immunol. 5 1990 1 7
    • (1990) Oral Microbiol. Immunol. , vol.5 , pp. 1-7
    • Deslauiers, M.1    Ni Eidhin, D.2    Lamonde, L.3    Mouton, C.4
  • 7
    • 0030857260 scopus 로고    scopus 로고
    • 4-LDHS)
    • P. Fields, and G.N. Somero Amino acid sequence differences cannot fully explain interspecific variation in thermal sensitivities of gobiid fish A4-lactate dehydrogenases (A4-LDHs) J. Exp. Biol. 200 1997 1839 1850 (Pubitemid 27288851)
    • (1997) Journal of Experimental Biology , vol.200 , Issue.13 , pp. 1839-1850
    • Fields, P.A.1    Somero, G.N.2
  • 8
    • 0034825983 scopus 로고    scopus 로고
    • 4-lactate dehydrogenase orthologs from warm-adapted and cold-adapted marine fishes
    • DOI 10.1046/j.1432-1327.2001.02374.x
    • P.A. Fields, B.D. Wahlstrand, and G.N. Somero Intrinsic versus extrinsic stabilization of enzymes: the interaction of solutes and temperature on A4-lactate dehydrogenase orthologs from warm-adapted and cold-adapted marine fishes Eur. J. Biochem. 268 2001 4497 4505 (Pubitemid 32862859)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.16 , pp. 4497-4505
    • Fields, P.A.1    Wahlstrand, B.D.2    Somero, G.N.3
  • 9
    • 0036022336 scopus 로고    scopus 로고
    • 4-lactate dehydrogenases: Identical primary structures produce subtly different conformations
    • P.A. Fields, Y.-S. Kim, J.F. Carpenter, and G.N. Somero Temperature adaptation in Gillichthys (Teleost: Gobiidae) A4-lactate dehydrogenases: identical primary structures produce subtly different conformations J. Exp. Biol. 205 2002 1293 1303 (Pubitemid 34853765)
    • (2002) Journal of Experimental Biology , vol.205 , Issue.9 , pp. 1293-1303
    • Fields, P.A.1    Kim, Y.-S.2    Carpenter, J.F.3    Somero, G.N.4
  • 10
    • 0023831539 scopus 로고
    • The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase
    • P.S. Freemont, B. Dunbar, and L.A. Fothergill-Gilmore The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase Biochem. J. 249 1988 779 788 (Pubitemid 18042797)
    • (1988) Biochemical Journal , vol.249 , Issue.3 , pp. 779-788
    • Freemont, P.S.1    Dunbar, B.2    Fothergill-Gilmore, L.A.3
  • 11
    • 0030991485 scopus 로고    scopus 로고
    • Detachment of glycolytic enzymes from cytoskeleton of melanoma cells induced by calmodulin antagonists
    • DOI 10.1016/S0014-2999(97)83051-8, PII S0014299997000848
    • L. Glass-Marmor, and R. Beitner Detachment of glycolytic enzymes from cytoskeleton of melanoma cells induced by calmodulin antagonists Eur. J. Pharmacol. 328 1997 241 248 (Pubitemid 27263363)
    • (1997) European Journal of Pharmacology , vol.328 , Issue.2-3 , pp. 241-248
    • Glass-Marmor, L.1    Beitner, R.2
  • 12
    • 0345440101 scopus 로고    scopus 로고
    • A potential role of the cytoskeleton of Saccharamyces cerevisiae in a functional organization of glycolytic enzymes
    • DOI 10.1002/(SICI)1097-0061(199911)15:15<1619::AID-YEA487>3.0.CO;2- R
    • R. Goetz, E. Schlueter, G. Shoham, and F.K. Zimmermann A potential role of the cytoskeleton of Saccharomyces cerevisiae in a functional organization of glycolytic enzymes Yeast 15 1999 1619 1629 (Pubitemid 29537390)
    • (1999) Yeast , vol.15 , Issue.15 , pp. 1619-1629
    • Gotz, R.1    Schluter, E.2    Shoham, G.3    Zimmermann, F.K.4
  • 14
    • 68549107626 scopus 로고    scopus 로고
    • A cytoskeletal tropomyosin can compromise the structural integrity of skeletal muscle
    • A.J. Kee, P.W. Gunning, and E.C. Hardeman A cytoskeletal tropomyosin can compromise the structural integrity of skeletal muscle Cell Motil. Cytoskel. 66 2009 710 720
    • (2009) Cell Motil. Cytoskel. , vol.66 , pp. 710-720
    • Kee, A.J.1    Gunning, P.W.2    Hardeman, E.C.3
  • 15
    • 0029841451 scopus 로고    scopus 로고
    • Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism
    • DOI 10.1002/(SICI)1099-0844(199612)14:4<237::AID-CBF698>3.0.CO;2-Q
    • H. Knull, and A.P. Minton Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism Cell Biochem. Funct. 14 1996 237 248 (Pubitemid 26402151)
    • (1996) Cell Biochemistry and Function , vol.14 , Issue.4 , pp. 237-248
    • Knull, H.1    Minton, A.P.2
  • 16
    • 67349219399 scopus 로고    scopus 로고
    • Phosphoglycerate mutase in mammalian striated muscles: Subcellular localization and binding partners
    • W. Kowalski, A. Gizak, and D. Rakus Phosphoglycerate mutase in mammalian striated muscles: subcellular localization and binding partners FEBS Lett. 583 2009 1841 1845
    • (2009) FEBS Lett. , vol.583 , pp. 1841-1845
    • Kowalski, W.1    Gizak, A.2    Rakus, D.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • U.K. Laemmli Cleavage of structural proteins during assembly of head of bacteriophage-T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 79960692993 scopus 로고    scopus 로고
    • Quantitation of protein-protein interactions by thermal stability shift analysis
    • 10.1002/pro.674
    • C.J. Layton, and H.W. Hellinga Quantitation of protein-protein interactions by thermal stability shift analysis Protein Sci. 20 2011 1439 1450 10.1002/pro.674
    • (2011) Protein Sci. , vol.20 , pp. 1439-1450
    • Layton, C.J.1    Hellinga, H.W.2
  • 19
    • 0026580080 scopus 로고
    • Microenvironmental factors and the binding of glycolytic enzymes to contractile filaments
    • C. Masters Microenvironmental factors and the binding of glycolytic enzymes to contractile filaments Int. J. Biochem. 24 1992 405 410
    • (1992) Int. J. Biochem. , vol.24 , pp. 405-410
    • Masters, C.1
  • 20
    • 0030882879 scopus 로고    scopus 로고
    • Glucose catabolism in cancer cells. The type II hexokinase promoter contains functionally active response elements for the tumor suppressor p53
    • DOI 10.1074/jbc.272.36.22776
    • S.P. Mathupala, C. Heese, and P.L. Pedersen Glucose catabolism in cancer cells. The type II hexokinase promoter contains functionally active response elements for the tumor suppressor p53 J. Biol. Chem. 272 1997 22776 22780 (Pubitemid 27386097)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.36 , pp. 22776-22780
    • Mathupala, S.P.1    Heese, C.2    Pedersen, P.L.3
  • 21
    • 0025853524 scopus 로고
    • Molecular structure of the human muscle-specific enolase gene (ENO3)
    • M. Peshavaria Molecular structure of the human muscle-specific enolase gene (ENO3) Biochem. J. 275 1991 427 433
    • (1991) Biochem. J. , vol.275 , pp. 427-433
    • Peshavaria, M.1
  • 22
    • 33745711847 scopus 로고    scopus 로고
    • Identification of phytochrome-interacting protein candidates in Arabidopsis thaliana by co-immunoprecipitation coupled with MALDI-TOF MS
    • DOI 10.1002/pmic.200500222
    • B. Phee, D.H. Shin, J. Cho, S. Kim, J. Kim, Y. Lee, J. Jeon, S.H. Bhoo, and T. Hahn Identification of phytochrome-interacting protein candidates in arabidopsis thaliana by co-immunoprecipitation coupled with MALDI-TOF MS Proteomics 6 2006 3671 3680 (Pubitemid 44000194)
    • (2006) Proteomics , vol.6 , Issue.12 , pp. 3671-3680
    • Phee, B.-K.1    Shin, D.H.2    Cho, J.-H.3    Kim, S.-H.4    Kim, J.-I.I.5    Lee, Y.-H.6    Jeon, J.-S.7    Bhoo, S.H.8    Hahn, T.-R.9
  • 23
    • 0023644515 scopus 로고
    • Further Characterization of the Krebs tricarboxylic acid cycle metabolon
    • B.J. Robinson, L. Inman, B. Sumegi, and P.A. Srere Further Characterization of the Krebs tricarboxylic acid cycle metabolon J. Biol. Chem. 262 1986 1786 1790
    • (1986) J. Biol. Chem. , vol.262 , pp. 1786-1790
    • Robinson, B.J.1    Inman, L.2    Sumegi, B.3    Srere, P.A.4
  • 24
    • 33847070047 scopus 로고    scopus 로고
    • Correlation of trimethylamine oxide and habitat depth within and among species of teleost fish: An analysis of causation
    • A.L. Samerotte, J.C. Drazen, G.L. Brand, B.A. Seibel, and P.H. Yancey Correlation of trimethylamine oxide and habitat depth within and among species of teleost fish: an analysis of causation Physiol. Biochem. Zool. 80 2007 197 208
    • (2007) Physiol. Biochem. Zool. , vol.80 , pp. 197-208
    • Samerotte, A.L.1    Drazen, J.C.2    Brand, G.L.3    Seibel, B.A.4    Yancey, P.H.5
  • 25
    • 0035746013 scopus 로고    scopus 로고
    • A comparative analysis of the evolutionary patterning and mechanistic bases of lactate dehydrogenase thermal stability in porcelain crabs, genus Petrolisthes
    • J.H. Stillman, and G.N. Somero A comparative analysis of the evolutionary patterning and mechanistic bases of lactate dehydrogenase thermal stability in porcelain crabs, genus Petrolisthes J. Exp. Biol. 204 2001 767 776 (Pubitemid 34861177)
    • (2001) Journal of Experimental Biology , vol.204 , Issue.4 , pp. 767-776
    • Stillman, J.H.1    Somero, G.N.2
  • 27
    • 0040777075 scopus 로고    scopus 로고
    • Model of a quinary structure between krebs TCA cycle enzymes: A model for the metabolon
    • DOI 10.1021/bi972011j
    • C. Velot, B.M. Mixon, M. Teige, and P.A. Srere Model of a quinary structure between Krebs TCA cycle enzymes: a model for the metabolon Biochemistry 36 1997 14271 14276 (Pubitemid 27509918)
    • (1997) Biochemistry , vol.36 , Issue.47 , pp. 14271-14276
    • Velot, C.1    Mixon, M.B.2    Teige, M.3    Srere, P.A.4
  • 29
    • 0026019452 scopus 로고
    • Differences in glycolytic capacity and hypoxia tolerance between hepatoma cells and hepatocytes
    • D.H. Wissemann, I. Anundi, W. Lauchart, R. Viebahn, and H. De Groot Differences in glycolytic capacity and hypoxia tolerance between hepatoma cells and hepatocytes Hepatology 13 1991 297 303
    • (1991) Hepatology , vol.13 , pp. 297-303
    • Wissemann, D.H.1    Anundi, I.2    Lauchart, W.3    Viebahn, R.4    De Groot, H.5
  • 30
    • 23044529588 scopus 로고    scopus 로고
    • Water stress, osmolytes and proteins
    • P.H. Yancey Water stress, osmolytes and proteins Am. Zool. 41 2001 699 709 (Pubitemid 33770242)
    • (2001) American Zoologist , vol.41 , Issue.4 , pp. 699-709
    • Yancey, P.H.1
  • 31
    • 24644450812 scopus 로고    scopus 로고
    • Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses
    • DOI 10.1242/jeb.01730
    • P.H. Yancey Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses J. Exp. Biol. 208 2005 2819 2830 (Pubitemid 41265173)
    • (2005) Journal of Experimental Biology , vol.208 , Issue.15 , pp. 2819-2830
    • Yancey, P.H.1
  • 32
    • 21644468585 scopus 로고    scopus 로고
    • Trimethylamine oxide, betaine and other osmolytes in deep-sea animals: Depth trends and effects on enzymes under hydrostatic pressure
    • P.H. Yancey, M.D. Rhea, K.M. Kemp, and D.M. Bailey Trimethylamine oxide, betaine and other osmolytes in deep-sea animals: depth trends and effects on enzymes under hydrostatic pressure Cell. Mol. Biol. 50 2004 371 376
    • (2004) Cell. Mol. Biol. , vol.50 , pp. 371-376
    • Yancey, P.H.1    Rhea, M.D.2    Kemp, K.M.3    Bailey, D.M.4
  • 33
    • 0033571682 scopus 로고    scopus 로고
    • Overexpression of hypoxia-inducible factor 1 alpha in commonhuman cancers and their metastases
    • H. Zhong, and A. De Marzo Overexpression of hypoxia-inducible factor 1 alpha in commonhuman cancers and their metastases Cancer Res. 59 1999 5830 5835
    • (1999) Cancer Res. , vol.59 , pp. 5830-5835
    • Zhong, H.1    De Marzo, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.