Literature DB >> 12220543

Low stability for monomeric human chaperonin protein 10: interprotein interactions contribute majority of oligomer stability.

Jesse J Guidry1, Pernilla Wittung-Stafshede.   

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Year:  2002        PMID： 12220543     DOI： 10.1016/s0003-9861(02)00406-x

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN： 0003-9861            Impact factor:   4.013


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  5 in total

1.  Dissecting homo-heptamer thermodynamics by isothermal titration calorimetry: entropy-driven assembly of co-chaperonin protein 10.

Authors:  Kathryn Luke; David Apiyo; Pernilla Wittung-Stafshede
Journal:  Biophys J       Date:  2005-08-12       Impact factor: 4.033

2.  Monomer topology defines folding speed of heptamer.

Authors:  Neil Bascos; Jesse Guidry; Pernilla Wittung-Stafshede
Journal:  Protein Sci       Date:  2004-04-09       Impact factor: 6.725

3.  Location and flexibility of the unique C-terminal tail of Aquifex aeolicus co-chaperonin protein 10 as derived by cryo-electron microscopy and biophysical techniques.

Authors:  Dong-Hua Chen; Kathryn Luke; Junjie Zhang; Wah Chiu; Pernilla Wittung-Stafshede
Journal:  J Mol Biol       Date:  2008-06-17       Impact factor: 5.469

4.  Formation of high-order oligomers by a hyperthemostable Fe-superoxide dismutase (tcSOD).

Authors:  Sha Wang; Zhi-Yang Dong; Yong-Bin Yan
Journal:  PLoS One       Date:  2014-10-14       Impact factor: 3.240

5.  Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified.

Authors:  Jesse J Guidry; Frank Shewmaker; Karol Maskos; Samuel Landry; Pernilla Wittung-Stafshede
Journal:  BMC Biochem       Date:  2003-10-02       Impact factor: 4.059
  5 in total

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