Literature DB >> 4770740

The use of absorption optics to measure dissociation of yeast enolase into enzymatically active monomers.

W H Holleman.   

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Year:  1973        PMID： 4770740     DOI： 10.1016/0005-2744(73)90115-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


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  6 in total

1.  Fluoride inhibition of enolase: crystal structure and thermodynamics.

Authors:  Jie Qin; Geqing Chai; John M Brewer; Leslie L Lovelace; Lukasz Lebioda
Journal:  Biochemistry       Date:  2006-01-24       Impact factor: 3.162

2.  Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit.

Authors:  Paul A Sims; Ann L Menefee; Todd M Larsen; Steven O Mansoorabadi; George H Reed
Journal:  J Mol Biol       Date:  2005-11-08       Impact factor: 5.469

3.  Dynamics and time-averaged chemical potential of proteins: importance in oligomer association.

Authors:  G Xu; G Weber
Journal:  Proc Natl Acad Sci U S A       Date:  1982-09       Impact factor: 11.205

4.  Purification and comparative characterization of an enolase from spinach.

Authors:  S Sinha; J M Brewer
Journal:  Plant Physiol       Date:  1984-04       Impact factor: 8.340

5.  Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate.

Authors:  Yunfei Wu; Chengliang Wang; Shenglong Lin; Minhao Wu; Lu Han; Changlin Tian; Xuan Zhang; Jianye Zang
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2015-11-26

6.  Dissociation of the octameric enolase from S. pyogenes--one interface stabilizes another.

Authors:  Farhad Karbassi; Veronica Quiros; Vijay Pancholi; Mary J Kornblatt
Journal:  PLoS One       Date:  2010-01-21       Impact factor: 3.240
  6 in total

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