Literature DB >> 1170902

Conformational changes of glyceraldehyde-3-phosphate dehydrogenase observed using laser light-scattering spectroscopy.

R Gabler, N C Ford, E W Westhead.   

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Year:  1975        PMID： 1170902      PMCID： PMC1334777          DOI： 10.1016/S0006-3495(75)85851-6

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


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  6 in total

1.  A study of some of the physical properties of glyceraldehyde-3-phosphate dehydrogenase.

Authors:  J B FOX; W B DANDLIKER
Journal:  J Biol Chem       Date:  1956-01       Impact factor: 5.157

2.  The coenzyme content of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase.

Authors:  W B DANDLIKER; J B FOX
Journal:  J Biol Chem       Date:  1956-08       Impact factor: 5.157

3.  Reversible dissociation of tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase into dimers or monomers by adenosine triphosphate.

Authors:  S M Constantinides; W C Deal
Journal:  J Biol Chem       Date:  1969-10-25       Impact factor: 5.157

4.  Reversible dissociation of yeast glyceraldehyde 3-phosphate dehydrogenase by adenosine triphosphate.

Authors:  G M Stancel; W C Deal
Journal:  Biochemistry       Date:  1969-10       Impact factor: 3.162

5.  Metabolic control and structure of glycolytic enzymes. VII. Destabilization and inactivation of yeast glyceraldehyde 3-phosphate dehydrogenase by adenosine phosphates and chymotrypsin.

Authors:  S T Yang; W C Deal
Journal:  Biochemistry       Date:  1969-07       Impact factor: 3.162

6.  Studies of ribosomal diffusion coefficients using laser light-scattering spectroscopy.

Authors:  R Gabler; E W Westhead; N C Ford
Journal:  Biophys J       Date:  1974-07       Impact factor: 4.033
  6 in total

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