These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
161 related articles for article (PubMed ID: 12381854)
1. Alpha-crystallin and ATP facilitate the in vitro renaturation of xylanase: enhancement of refolding by metal ions. Nath D; Rawat U; Anish R; Rao M Protein Sci; 2002 Nov; 11(11):2727-34. PubMed ID: 12381854 [TBL] [Abstract][Full Text] [Related]
2. In vitro renaturation of alkaline family G/11 xylanase via a folding intermediate: alpha-crystallin facilitates refolding in an ATP-independent manner. Dutta T; Bhattacharjee A; Majumdar U; Ray SS; Sahoo R; Ghosh S Appl Biochem Biotechnol; 2010 Nov; 162(5):1238-48. PubMed ID: 20703955 [TBL] [Abstract][Full Text] [Related]
3. Artificial chaperone mediated refolding of xylanase from an alkalophilic thermophilic Bacillus sp. Implications for in vitro protein renaturation via a folding intermediate. Nath D; Rao M Eur J Biochem; 2001 Oct; 268(20):5471-8. PubMed ID: 11606210 [TBL] [Abstract][Full Text] [Related]
4. Fluorescence study on interactions of alpha-crystallin with the molten globule state of 1, 4-beta-D-glucan glucanohydrolase from Thermomonospora sp. induced by guanidine hydrochloride. Jagtap S; Rao M J Fluoresc; 2009 Nov; 19(6):967-73. PubMed ID: 19533311 [TBL] [Abstract][Full Text] [Related]
5. Illustration of HIV-1 protease folding through a molten-globule-like intermediate using an experimental model that implicates alpha-crystallin and calcium ions. Dash C; Sastry M; Rao M Biochemistry; 2005 Mar; 44(10):3725-34. PubMed ID: 15751949 [TBL] [Abstract][Full Text] [Related]
6. Acid-induced partly folded conformation resembling a molten globule state of xylanase from an alkalothermophilic Bacillus sp. Nath D; Rao M Biochem Biophys Res Commun; 2001 Nov; 288(5):1218-22. PubMed ID: 11700042 [TBL] [Abstract][Full Text] [Related]
7. Alpha-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: implications for preventing irreversible thermal denaturation. Tanksale A; Ghatge M; Deshpande V Protein Sci; 2002 Jul; 11(7):1720-8. PubMed ID: 12070325 [TBL] [Abstract][Full Text] [Related]
8. Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme. Rawat U; Rao M J Biol Chem; 1998 Apr; 273(16):9415-23. PubMed ID: 9545266 [TBL] [Abstract][Full Text] [Related]
9. Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. Biswas A; Das KP J Biol Chem; 2004 Oct; 279(41):42648-57. PubMed ID: 15292216 [TBL] [Abstract][Full Text] [Related]
10. Chaperone-like activity of alpha-crystallin and other small heat shock proteins. Ganea E Curr Protein Pept Sci; 2001 Sep; 2(3):205-25. PubMed ID: 12369933 [TBL] [Abstract][Full Text] [Related]
11. Effect of the chaperone-like alpha-crystallin on the refolding of lysozyme and ribonuclease A. Raman B; Ramakrishna T; Rao CM FEBS Lett; 1997 Oct; 416(3):369-72. PubMed ID: 9373187 [TBL] [Abstract][Full Text] [Related]
12. Structural perturbation of alpha-crystallin and its chaperone-like activity. Rao CM; Raman B; Ramakrishna T; Rajaraman K; Ghosh D; Datta S; Trivedi VD; Sukhaswami MB Int J Biol Macromol; 1998; 22(3-4):271-81. PubMed ID: 9650082 [TBL] [Abstract][Full Text] [Related]
13. alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner. Wang K; Spector A Eur J Biochem; 2000 Aug; 267(15):4705-12. PubMed ID: 10903503 [TBL] [Abstract][Full Text] [Related]
14. Detection and characterization of alpha-crystallin intermediate with maximal chaperone-like activity. Das BK; Liang JJ Biochem Biophys Res Commun; 1997 Jul; 236(2):370-4. PubMed ID: 9240443 [TBL] [Abstract][Full Text] [Related]
15. Proteostasis and the Regulation of Intra- and Extracellular Protein Aggregation by ATP-Independent Molecular Chaperones: Lens α-Crystallins and Milk Caseins. Carver JA; Ecroyd H; Truscott RJW; Thorn DC; Holt C Acc Chem Res; 2018 Mar; 51(3):745-752. PubMed ID: 29442498 [TBL] [Abstract][Full Text] [Related]
16. Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin. Srinivas V; Raman B; Rao KS; Ramakrishna T; Rao ChM Mol Vis; 2005 Apr; 11():249-55. PubMed ID: 15827547 [TBL] [Abstract][Full Text] [Related]
18. Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability. Gangadhariah MH; Wang B; Linetsky M; Henning C; Spanneberg R; Glomb MA; Nagaraj RH Biochim Biophys Acta; 2010 Apr; 1802(4):432-41. PubMed ID: 20085807 [TBL] [Abstract][Full Text] [Related]
19. Alpha-crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase. Marini I; Moschini R; Del Corso A; Mura U Cell Mol Life Sci; 2005 Mar; 62(5):599-605. PubMed ID: 15747064 [TBL] [Abstract][Full Text] [Related]
20. Alpha-crystallin assisted refolding of enzyme substrates: optimization of external parameters. Biswas A; Das KP Protein J; 2007 Jun; 26(4):247-55. PubMed ID: 17211683 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]