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Journal Abstract Search

129 related items for PubMed ID: 10491151

  • 1. A stable cold folding intermediate of rabbit muscle D-glyceraldehyde 3-phosphate dehydrogenase.
    Zhang NX, Wang C.
    Eur J Biochem; 1999 Sep; 264(3):1002-8. PubMed ID: 10491151
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  • 3. GroEL-assisted dehydrogenase folding mediated by coenzyme is ATP-independent.
    Zhang S, Li J, Wang CC.
    Biochem Biophys Res Commun; 2001 Jul 13; 285(2):277-82. PubMed ID: 11444838
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  • 4. GroEL and protein disulfide isomerase each binds with folding intermediates of D-glyceraldehyde-3-phosphate dehydrogenase released from complexes formed with the other.
    Zhang N, Li J, Wang C.
    J Protein Chem; 2000 Oct 13; 19(7):569-74. PubMed ID: 11233170
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  • 6. Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase.
    Chen YH, He RQ, Liu Y, Liu Y, Xue ZG.
    Biochem J; 2000 Oct 01; 351(Pt 1):233-40. PubMed ID: 10998366
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  • 7. Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme.
    Polyakova OV, Roitel O, Asryants RA, Poliakov AA, Branlant G, Muronetz VI.
    Protein Sci; 2005 Apr 01; 14(4):921-8. PubMed ID: 15741339
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  • 9. Unfolded, oxidized, and thermoinactivated forms of glyceraldehyde-3-phosphate dehydrogenase interact with the chaperonin GroEL in different ways.
    Naletova IN, Muronetz VI, Schmalhausen EV.
    Biochim Biophys Acta; 2006 Apr 01; 1764(4):831-8. PubMed ID: 16551514
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  • 13. Folding intermediates of hyperthermophilic D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima are trapped at low temperature.
    Schultes V, Jaenicke R.
    FEBS Lett; 1991 Sep 23; 290(1-2):235-8. PubMed ID: 1915883
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  • 15. Effect of alpha-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase.
    Khanova HA, Markossian KA, Kleimenov SY, Levitsky DI, Chebotareva NA, Golub NV, Asryants RA, Muronetz VI, Saso L, Yudin IK, Muranov KO, Ostrovsky MA, Kurganov BI.
    Biophys Chem; 2007 Feb 23; 125(2-3):521-31. PubMed ID: 17229514
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  • 16. The low-temperature folding intermediate of hyperthermophilic D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima shows a native-like cooperative unfolding transition.
    Rehaber V, Jaenicke R.
    FEBS Lett; 1993 Feb 08; 317(1-2):163-6. PubMed ID: 8428625
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  • 17. Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures.
    Naletova I, Schmalhausen E, Kharitonov A, Katrukha A, Saso L, Caprioli A, Muronetz V.
    Biochim Biophys Acta; 2008 Dec 08; 1784(12):2052-8. PubMed ID: 18725330
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  • 18. The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation.
    Bhattacharyya AM, Horowitz PM.
    J Biol Chem; 2001 Aug 03; 276(31):28739-43. PubMed ID: 11397797
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  • 20. [The non-functioning chaperonin GroEL stimulates protein aggregation].
    Naletov IN, Shmal'gauzen EV, Shalova IN, Pleten' AP, Tsiriul'nikov K, Ertl' T, Muronets VI.
    Biomed Khim; 2006 Aug 03; 52(5):518-24. PubMed ID: 17180927
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