Literature DB >> 4906846

Aspartate transcarbamylase. A study by transient nuclear magnetic resonance of the binding of succinate to the native enzyme and its catalytic subunit.

B D Sykes, P G Schmidt, G R Stark.   

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Year:  1970        PMID： 4906846

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  4 in total

1.  1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.

Authors:  R E Cohen; M Takama; H K Schachman
Journal:  Proc Natl Acad Sci U S A       Date:  1992-12-15       Impact factor: 11.205

2.  Substrate anchoring and the catalytic power of enzymes.

Authors:  J Reuben
Journal:  Proc Natl Acad Sci U S A       Date:  1971-03       Impact factor: 11.205

3.  Proton magnetic resonance studies of cholinergic ligand binding to the acetylcholine receptor in its membrane environment.

Authors:  J Miller; V Witzemann; U Quast; M A Raftery
Journal:  Proc Natl Acad Sci U S A       Date:  1979-08       Impact factor: 11.205

4.  The active site of staphylococcal nuclease: paramagnetic relaxation of bound nucleotide inhibitor nuclei by lanthanide ions.

Authors:  B Furie; J H Griffin; R J Feldmann; E A Sokoloski; A N Schechter
Journal:  Proc Natl Acad Sci U S A       Date:  1974-07       Impact factor: 11.205
  4 in total

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