ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
A new crystal form of human diamine oxidase.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Diamine Oxidase and Gastrointestinal Diseases.Biomolecules · 2026Review
- Recognition-Element-Driven Rapid Detection of Biogenic Amines in Foods: From Molecular Recognition to On-Site Sensing.Foods (Basel, Switzerland) · 2026Review
- Standardization of a colorimetric technique for determination of enzymatic activity of diamine oxidase (DAO) and its application in patients with clinical diagnosis of histamine intolerance.The World Allergy Organization journal · 2020Article
- Human Copper-Containing Amine Oxidases in Drug Design and Development.Molecules (Basel, Switzerland) · 2020Review
- Conformational Design and Characterisation of a Truncated Diamine Oxidase fromHigh-throughput · 2018Article
- Oligomannosidic glycans at Asn-110 are essential for secretion of human diamine oxidase.The Journal of biological chemistry · 2018Article
- Human copper-dependent amine oxidases.Archives of biochemistry and biophysics · 2014Review
- A new crystal form of human vascular adhesion protein 1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
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 at 3 institutions in 2 countries.
Funding
Abstract
Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1-3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P2(1)2(1)2(1) with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 A resolution in space group C222(1) with one molecule in the asymmetric unit is reported.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.