39630-68-7Relevant articles and documents
THE INHIBITION OF GLUTAMATE DEHYDROGENASE BY DERIVATIVES OF ISOPHTHALIC ACID
Cunliffe, Denise,Leason, Mark,Parkin, Donald,Lea, Peter J.
, p. 1357 - 1360 (1983)
A range of compounds, structurally related to glutamate, have been tested as inhibitors of pea leaf glutamate dehydrogenase assayed in either direction.Only 5-N-substituted derivatives of aminoisophthalic acid completely inhibited the enzyme when tested at concentrations equal to either those of 2-oxoglutarate or glutamate.A minimum of three carbon atoms attached linearly to the amino group was required for maximum inhibition, inhibition was removed if there was any substitution on the first carbon.The 5-N-substituted derivatives also inhibited yeast (to a greater extent) and bovine liver (to a lesser extent) glutamate dehydrogenases.Key Word Index - Pisum sativum; Leguminoseae; yeast; bovine; glutamate dehydrogenase inhibition; isophthalic acid derivatives.
Nano composite of polynucleotide and gold nano rod, and preparation method and applications thereof
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Paragraph 0029; 0030; 0031, (2017/08/31)
The invention discloses a nano composite of polynucleotide and gold nano rod, and a preparation method and applications thereof. The surface of a nano gold rod is modified by a polynucleotide carrier compound, which is modified by lipoic acid having high
In-situ generation of differential sensors that fingerprint kinases and the cellular response to their expression
Zamora-Olivares, Diana,Kaoud, Tamer S.,Dalby, Kevin N.,Anslyn, Eric V.
supporting information, p. 14814 - 14820 (2013/10/22)
Mitogen-activated protein (MAP) kinases are responsible for many cellular functions, and their malfunction manifests itself in several human diseases. Usually, monitoring the phosphorylation states of MAP kinases in vitro requires the preparation and puri