Fu X - Search Results

1

Periplasmic proteins of Escherichia coli are highly resistant to aggregation: reappraisal for roles of molecular chaperones in periplasm.

Liu Y, Fu X, Shen J, Zhang H, Hong W, Chang Z. Liu Y, et al. Among authors: fu x. Biochem Biophys Res Commun. 2004 Apr 9;316(3):795-801. doi: 10.1016/j.bbrc.2004.02.125. Biochem Biophys Res Commun. 2004. PMID: 15033470

2

Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones.

Fu X, Li W, Mao Q, Chang Z. Fu X, et al. Biochem Biophys Res Commun. 2003 Aug 29;308(3):627-35. doi: 10.1016/s0006-291x(03)01450-5. Biochem Biophys Res Commun. 2003. PMID: 12914797

3

Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation.

Fu X, Liu C, Liu Y, Feng X, Gu L, Chen X, Chang Z. Fu X, et al. Biochem Biophys Res Commun. 2003 Oct 17;310(2):412-20. doi: 10.1016/j.bbrc.2003.09.027. Biochem Biophys Res Commun. 2003. PMID: 14521926

4

Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis.

Fu X, Chang Z. Fu X, et al. Biochem Biophys Res Commun. 2004 Apr 2;316(2):291-9. doi: 10.1016/j.bbrc.2004.02.053. Biochem Biophys Res Commun. 2004. PMID: 15020216

5

4,4'-Dianilino-1,1'-binaphthyl-5,5'-sulfonate, a novel molecule having chaperone-like activity.

Fu X, Zhang X, Chang Z. Fu X, et al. Biochem Biophys Res Commun. 2005 Apr 15;329(3):1087-93. doi: 10.1016/j.bbrc.2005.01.164. Biochem Biophys Res Commun. 2005. PMID: 15752765

6

The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: dissociation of oligomers is a prerequisite.

Zhang H, Fu X, Jiao W, Zhang X, Liu C, Chang Z. Zhang H, et al. Among authors: fu x. Biochem Biophys Res Commun. 2005 May 20;330(4):1055-61. doi: 10.1016/j.bbrc.2005.03.092. Biochem Biophys Res Commun. 2005. PMID: 15823550

7

Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: evidences for a two-step substrate-binding mechanism.

Fu X, Chang Z. Fu X, et al. Biochem Biophys Res Commun. 2006 Oct 13;349(1):167-71. doi: 10.1016/j.bbrc.2006.08.036. Epub 2006 Aug 15. Biochem Biophys Res Commun. 2006. PMID: 16930542

Our previous study showed an overlapping nature of the sites for both hydrophobic probe 1,1'-Bi(4-anilino)naphthalene-5,5'-disulfonic acid (bis-ANS) binding and substrate binding in Mycobacterium tuberculosis Hsp16.3 [X. Fu, H. Zhang, X. Zhang, Y. Cao, W. Jia …

Our previous study showed an overlapping nature of the sites for both hydrophobic probe 1,1'-Bi(4-anilino)naphthalene-5,5'-disulfonic acid ( …

8

The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein Hsp16.3 occurs via a stepwise mechanism.

Feng X, Huang S, Fu X, Abulimiti A, Chang Z. Feng X, et al. Among authors: fu x. Biochem J. 2002 Apr 15;363(Pt 2):329-34. doi: 10.1042/0264-6021:3630329. Biochem J. 2002. PMID: 11931661 Free PMC article.

9

Inter-subunit cross-linking suppressed the dynamic oligomeric dissociation of Mycobacterium tuberculosis Hsp16.3 and reduced its chaperone activity.

Fu X, Jiao W, Abulimiti A, Chang Z. Fu X, et al. Biochemistry (Mosc). 2004 May;69(5):552-7. doi: 10.1023/b:biry.0000029854.86015.61. Biochemistry (Mosc). 2004. PMID: 15193130

10

Chaperone-like activity of beta-casein.

Zhang X, Fu X, Zhang H, Liu C, Jiao W, Chang Z. Zhang X, et al. Among authors: fu x. Int J Biochem Cell Biol. 2005 Jun;37(6):1232-40. doi: 10.1016/j.biocel.2004.12.004. Epub 2005 Jan 19. Int J Biochem Cell Biol. 2005. PMID: 15778087

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