2001
DOI: 10.1080/11263500112331350760
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Variation in isomeric products of a phosphodiesterase from the chloroplasts ofPhaseolus vulgarisin response to cations

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Cited by 4 publications
(1 citation statement)
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“…Plant PDEs degrading cGMP are elusive, as earlier bioinformatic searches failed to identify homologs of animal PDEs. However, PDE activity has been detected in crude protein extracts from different plant species in the 1970s [ 176 ] and partially purified PDE from chloroplasts of Phaseolus vulgaris displayed enzymatic activity in the presence of cAMP and cGMP [ 177 ]. A novel cGMP-activated PDE encoded by an ancient gene not represented in animals, is encoded in Arabidopsis by PDE1 [ 178 ], and more plant PDEs remain to be discovered and characterized.…”
Section: Nanodomains Surrounding Moonlighting Kinasesmentioning
confidence: 99%
“…Plant PDEs degrading cGMP are elusive, as earlier bioinformatic searches failed to identify homologs of animal PDEs. However, PDE activity has been detected in crude protein extracts from different plant species in the 1970s [ 176 ] and partially purified PDE from chloroplasts of Phaseolus vulgaris displayed enzymatic activity in the presence of cAMP and cGMP [ 177 ]. A novel cGMP-activated PDE encoded by an ancient gene not represented in animals, is encoded in Arabidopsis by PDE1 [ 178 ], and more plant PDEs remain to be discovered and characterized.…”
Section: Nanodomains Surrounding Moonlighting Kinasesmentioning
confidence: 99%