ArticleACS omega2017
Modeling the Active Site of the Purple Acid Phosphatase Enzyme with Hetero-Dinuclear Mixed Valence M(II)-Fe(III) [M = Zn, Ni, Co, and Cu] Complexes Supported over a [N
Article in ACS omega, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Synthesis, structural characterization, and theoretical analysis of novel zinc(ii) schiff base complexes with halogen and hydrogen bonding interactions.RSC advances · 2024Article
- Purple acid phosphatase promoted hydrolysis of organophosphate pesticides in microalgae.Environmental science and ecotechnology · 2024Article
- Guanidine- and purine-functionalized ligands of FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Mechanistic Studies of Homo- and Heterodinuclear Zinc Phosphoesterase Mimics: What Has Been Learned?Frontiers in chemistry · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The active site of the purple acid phosphatase enzyme has been successfully modeled by a series of hetero-dinuclear M(II)-Fe(III) [M = Zn, Ni, Co, and Cu] type complexes of an unsymmetrical [N
Identifiers
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Registered trials
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