These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

109 related articles for article (PubMed ID: 16212548)

  • 1. Chaperone-like activity of Mycobacterium tuberculosis Hsp16.3 does not require its intact (native) structures.
    Chen X; Fu X; Ma Y; Chang Z
    Biochemistry (Mosc); 2005 Aug; 70(8):913-9. PubMed ID: 16212548
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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
    J Biol Chem; 2005 Feb; 280(8):6337-48. PubMed ID: 15545279
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity.
    Gu L; Abulimiti A; Li W; Chang Z
    J Mol Biol; 2002 May; 319(2):517-26. PubMed ID: 12051925
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Site-directed mutation on the only universally conserved residue Leu122 of small heat shock protein Hsp16.3.
    Mao Q; Chang Z
    Biochem Biophys Res Commun; 2001 Dec; 289(5):1257-61. PubMed ID: 11741330
    [TBL] [Abstract][Full Text] [Related]  

  • 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
    Biochem Biophys Res Commun; 2003 Aug; 308(3):627-35. PubMed ID: 12914797
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3.
    Panda AK; Chakraborty A; Nandi SK; Biswas A
    Proteins; 2020 Jun; 88(6):759-774. PubMed ID: 31860142
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis.
    Fu X; Chang Z
    Biochem Biophys Res Commun; 2004 Apr; 316(2):291-9. PubMed ID: 15020216
    [TBL] [Abstract][Full Text] [Related]  

  • 8. The C-terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function.
    Panda AK; Chakraborty A; Nandi SK; Kaushik A; Biswas A
    FEBS J; 2017 Jan; 284(2):277-300. PubMed ID: 27885799
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Lysine acetylation of Hsp16.3: Effect on its structure, chaperone function and influence towards the growth of Mycobacterium tuberculosis.
    Barik S; Panda AK; Biswas VK; Das S; Chakraborty A; Beura S; Modak R; Raghav SK; Kar RK; Biswas A
    Int J Biol Macromol; 2024 May; 268(Pt 2):131763. PubMed ID: 38657928
    [TBL] [Abstract][Full Text] [Related]  

  • 10. 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
    J Mol Biol; 2003 Feb; 326(4):1013-23. PubMed ID: 12589750
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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
    Biochemistry (Mosc); 2004 May; 69(5):552-7. PubMed ID: 15193130
    [TBL] [Abstract][Full Text] [Related]  

  • 12. 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
    Biochem Biophys Res Commun; 2003 Oct; 310(2):412-20. PubMed ID: 14521926
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Alpha-crystallin promotes assembly of a trimeric form of Mycobacterium tuberculosis Hsp16.3 in a cell free system.
    Abulimiti A; Chang Z
    Biochemistry (Mosc); 2003 Mar; 68(3):269-74. PubMed ID: 12733968
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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
    J Protein Chem; 2000 May; 19(4):319-26. PubMed ID: 11043937
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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
    Biochem Biophys Res Commun; 2006 Oct; 349(1):167-71. PubMed ID: 16930542
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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
    Biochem J; 2002 Apr; 363(Pt 2):329-34. PubMed ID: 11931661
    [TBL] [Abstract][Full Text] [Related]  

  • 17. 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
    Biochem Biophys Res Commun; 2005 May; 330(4):1055-61. PubMed ID: 15823550
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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 Q; Ke D; Feng X; Chang Z
    Biochem Biophys Res Commun; 2001 Jun; 284(4):942-7. PubMed ID: 11409884
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Identification of a highly conserved pro-gly doublet in non-animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3.
    Fu X; Chang Z
    Biochemistry (Mosc); 2006; 71 Suppl 1():S83-90. PubMed ID: 16487074
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Site-directed mutations within the core "alpha-crystallin" domain of the small heat-shock protein, human alphaB-crystallin, decrease molecular chaperone functions.
    Muchowski PJ; Wu GJ; Liang JJ; Adman ET; Clark JI
    J Mol Biol; 1999 Jun; 289(2):397-411. PubMed ID: 10366513
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 6.