Chang Z - Search Results

1

A novel mechanism for small heat shock proteins to function as molecular chaperones.

Zhang K, Ezemaduka AN, Wang Z, Hu H, Shi X, Liu C, Lu X, Fu X, Chang Z, Yin CC. Zhang K, et al. Among authors: chang z. Sci Rep. 2015 Mar 6;5:8811. doi: 10.1038/srep08811. Sci Rep. 2015. PMID: 25744691 Free PMC article.

2

The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity.

Yang H, Huang S, Dai H, Gong Y, Zheng C, Chang Z. Yang H, et al. Among authors: chang z. Protein Sci. 1999 Jan;8(1):174-9. doi: 10.1110/ps.8.1.174. Protein Sci. 1999. PMID: 10210195 Free PMC article.

Hsp16.3, the alpha-crystallin-related small heat shock protein of Mycobacterium tuberculosis that is maximally expressed during the stationary phase and is a major membrane protein, has been reported to form specific trimer-of-trimers structure and to act as an effective molecula …

Hsp16.3, the alpha-crystallin-related small heat shock protein of Mycobacterium tuberculosis that is maximally expressed during the stationa …

3

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: chang z. Biochem J. 2002 Apr 15;363(Pt 2):329-34. doi: 10.1042/0264-6021:3630329. Biochem J. 2002. PMID: 11931661 Free PMC article.

4

Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-assembled via trimer and hexamer intermediates.

Abulimiti A, Fu X, Gu L, Feng X, Chang Z. Abulimiti A, et al. Among authors: chang z. J Mol Biol. 2003 Feb 28;326(4):1013-23. doi: 10.1016/s0022-2836(03)00018-4. J Mol Biol. 2003. PMID: 12589750

5

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. Among authors: chang z. 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

6

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. Among authors: chang z. 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

7

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. Among authors: chang z. 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

8

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: chang z. 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

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. Among authors: chang z. Biochemistry (Mosc). 2004 May;69(5):552-7. doi: 10.1023/b:biry.0000029854.86015.61. Biochemistry (Mosc). 2004. PMID: 15193130

10

A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins.

Fu X, Zhang H, Zhang X, Cao Y, Jiao W, Liu C, Song Y, Abulimiti A, Chang Z. Fu X, et al. Among authors: chang z. J Biol Chem. 2005 Feb 25;280(8):6337-48. doi: 10.1074/jbc.M406319200. Epub 2004 Nov 15. J Biol Chem. 2005. PMID: 15545279 Free article.

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