111 related articles for article (PubMed ID: 11509563)
41. Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system.
Kubo Y; Tsunehiro T; Nishikawa S; Nakai M; Ikeda E; Toh-e A; Morishima N; Shibata T; Endo T
J Mol Biol; 1999 Feb; 286(2):447-64. PubMed ID: 9973563
[TBL] [Abstract][Full Text] [Related]
42. Nucleolar protein B23 has molecular chaperone activities.
Szebeni A; Olson MO
Protein Sci; 1999 Apr; 8(4):905-12. PubMed ID: 10211837
[TBL] [Abstract][Full Text] [Related]
43. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.
Goloubinoff P; Mogk A; Zvi AP; Tomoyasu T; Bukau B
Proc Natl Acad Sci U S A; 1999 Nov; 96(24):13732-7. PubMed ID: 10570141
[TBL] [Abstract][Full Text] [Related]
44. Structural and functional consequences of chaperone site deletion in αA-crystallin.
Santhoshkumar P; Karmakar S; Sharma KK
Biochim Biophys Acta; 2016 Nov; 1864(11):1529-38. PubMed ID: 27524665
[TBL] [Abstract][Full Text] [Related]
45. Appraisal of casein's inhibitory effects on aggregation accompanying carbonic anhydrase refolding and heat-induced ovalbumin fibrillogenesis.
Khodarahmi R; Beyrami M; Soori H
Arch Biochem Biophys; 2008 Sep; 477(1):67-76. PubMed ID: 18485276
[TBL] [Abstract][Full Text] [Related]
46. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.
Veinger L; Diamant S; Buchner J; Goloubinoff P
J Biol Chem; 1998 May; 273(18):11032-7. PubMed ID: 9556585
[TBL] [Abstract][Full Text] [Related]
47. Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation.
Goenka S; Raman B; Ramakrishna T; Rao CM
Biochem J; 2001 Nov; 359(Pt 3):547-56. PubMed ID: 11672428
[TBL] [Abstract][Full Text] [Related]
48. Some properties of human small heat shock protein Hsp20 (HspB6).
Bukach OV; Seit-Nebi AS; Marston SB; Gusev NB
Eur J Biochem; 2004 Jan; 271(2):291-302. PubMed ID: 14717697
[TBL] [Abstract][Full Text] [Related]
49. A peptide sequence-YSGVCHTDLHAWHGDWPLPVK [40-60]-in yeast alcohol dehydrogenase prevents the aggregation of denatured substrate proteins.
Bhattacharyya J; Santhoshkumar P; Sharma KK
Biochem Biophys Res Commun; 2003 Jul; 307(1):1-7. PubMed ID: 12849973
[TBL] [Abstract][Full Text] [Related]
50. 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; 351(Pt 1):233-40. PubMed ID: 10998366
[TBL] [Abstract][Full Text] [Related]
51. Mechanism of thermal aggregation of yeast alcohol dehydrogenase I: role of intramolecular chaperone.
Markossian KA; Golub NV; Khanova HA; Levitsky DI; Poliansky NB; Muranov KO; Kurganov BI
Biochim Biophys Acta; 2008 Sep; 1784(9):1286-93. PubMed ID: 18515108
[TBL] [Abstract][Full Text] [Related]
52. Artificial chaperone-assisted refolding of chemically denatured alpha-amylase.
Yazdanparast R; Khodagholi F; Khodarahmi R
Int J Biol Macromol; 2005 Jun; 35(5):257-63. PubMed ID: 15862864
[TBL] [Abstract][Full Text] [Related]
53. Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule.
Guagliardi A; Cerchia L; Rossi M
J Biol Chem; 1995 Nov; 270(47):28126-32. PubMed ID: 7499301
[TBL] [Abstract][Full Text] [Related]
54. A Novel Method for Assessing the Chaperone Activity of Proteins.
Hristozova N; Tompa P; Kovacs D
PLoS One; 2016; 11(8):e0161970. PubMed ID: 27564234
[TBL] [Abstract][Full Text] [Related]
55. Artificial chaperone-assisted refolding of GuHCl-denatured alpha-amylase at low temperature: refolding versus aggregation.
Khodagholi F; Yazdanparast R
Protein J; 2005 Jul; 24(5):303-13. PubMed ID: 16284728
[TBL] [Abstract][Full Text] [Related]
56. Alpha casein micelles show not only molecular chaperone-like aggregation inhibition properties but also protein refolding activity from the denatured state.
Sakono M; Motomura K; Maruyama T; Kamiya N; Goto M
Biochem Biophys Res Commun; 2011 Jan; 404(1):494-7. PubMed ID: 21144837
[TBL] [Abstract][Full Text] [Related]
57. Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro.
Hartman DJ; Surin BP; Dixon NE; Hoogenraad NJ; Høj PB
Proc Natl Acad Sci U S A; 1993 Mar; 90(6):2276-80. PubMed ID: 8096339
[TBL] [Abstract][Full Text] [Related]
58. Chaperone-like properties of lysophospholipids.
Kern R; Joseleau-Petit D; Chattopadhyay MK; Richarme G
Biochem Biophys Res Commun; 2001 Dec; 289(5):1268-74. PubMed ID: 11741332
[TBL] [Abstract][Full Text] [Related]
59. Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity.
Zahn R; Perrett S; Fersht AR
J Mol Biol; 1996 Aug; 261(1):43-61. PubMed ID: 8760501
[TBL] [Abstract][Full Text] [Related]
60. Molecular cloning of a novel chaperone-like protein induced by rhabdovirus infection with sequence similarity to the bacterial extracellular solute-binding protein family 5.
Cho WJ; Yoon WJ; Moon CH; Cha SJ; Song H; Cho HR; Jang SJ; Chung DK; Jeong CS; Park JW
J Biol Chem; 2002 Nov; 277(44):41489-96. PubMed ID: 12183466
[TBL] [Abstract][Full Text] [Related]
[Previous] [Next] [New Search]
