Chang Z - 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: 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

2

Probing the roles of the only universally conserved leucine residue (Leu122) in the oligomerization and chaperone-like activity of Mycobacterium tuberculosis small heat shock protein Hsp16.3.

Dai H, Mao Q, Yang H, Huang S, Chang Z. Dai H, et al. Among authors: chang z. J Protein Chem. 2000 May;19(4):319-26. doi: 10.1023/a:1007003631120. J Protein Chem. 2000. PMID: 11043937

3

Site-directed mutation on the only universally conserved residue Leu122 of small heat shock protein Hsp16.3.

Mao Q, Chang Z. Mao Q, et al. Among authors: chang z. Biochem Biophys Res Commun. 2001 Dec 21;289(5):1257-61. doi: 10.1006/bbrc.2001.6062. Biochem Biophys Res Commun. 2001. PMID: 11741330

4

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.

5

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

6

Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants.

Abulimiti A, Qiu X, Chen J, Liu Y, Chang Z. Abulimiti A, et al. Among authors: chang z. Biochem Biophys Res Commun. 2003 May 23;305(1):87-93. doi: 10.1016/s0006-291x(03)00685-5. Biochem Biophys Res Commun. 2003. PMID: 12732200

7

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

8

Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer.

Chen Y, Lu YJ, Wang HW, Quan S, Chang Z, Sui SF. Chen Y, et al. Among authors: chang z. Biochem Biophys Res Commun. 2003 Oct 17;310(2):360-6. doi: 10.1016/j.bbrc.2003.09.026. Biochem Biophys Res Commun. 2003. PMID: 14521918

9

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

10

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

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My Custom Filters

Publication date

Text availability

Article attribute

Article type

Article Language

Species

Sex

Age

Other

3,239 results

Search Page

Filters