| 1 |
Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism
Fu XM, Chang ZY
Biochemical and Biophysical Research Communications, 349(1), 167, 2006 |
| 2 |
Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis
Fu XM, Chang ZY
Biochemical and Biophysical Research Communications, 316(2), 291, 2004 |
| 3 |
Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer
Chen Y, Lu YJ, Wang HW, Quan S, Chang ZY, Sui SF
Biochemical and Biophysical Research Communications, 310(2), 360, 2003 |
| 4 |
Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation
Fu XM, Liu C, Liu Y, Feng XG, Lu LC, Chen XY, Chang ZY
Biochemical and Biophysical Research Communications, 310(2), 412, 2003 |
| 5 |
Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants
Abulimiti A, Qiu XL, Chen J, Liu Y, Chang ZY
Biochemical and Biophysical Research Communications, 305(1), 87, 2003 |
| 6 |
Preheat treatment for Mycobacterium tuberculosis Hsp16.3: Correlation between a structural phase change at 60 degrees C and a dramatic increase in chaperone-like activity
Mao QL, Ke DX, Feng XG, Chang ZY
Biochemical and Biophysical Research Communications, 284(4), 942, 2001 |
