Evidence map›Paper›PMID 21455237›Full record

ReviewNature reviews. Drug discovery2011

The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis.

James Leiper, Manasi Nandi

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Drug discovery, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed, 1 pooled it
8.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

78 citing papers in PubMed, 1 synthesis or guideline pooled it, 171 citations in OpenAlex.

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18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

James LeiperMRC Clinical Sciences Centre, Faculty of Medicine, Imperial College London, Hammersmith Hospital Campus, Du Cane Road, London W120NN, UK. james.leiper@csc.mrc.ac.uk
Manasi Nandi
Hammersmith Hospital · GBKing's College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E527098/1British Heart FoundationMedical Research Council MC_U120097118Wellcome Trust
6 · The paper itself

Abstract

Asymmetric dimethylarginine (ADMA)--a naturally occurring amino acid that is a product of protein breakdown--is released into the cytoplasm following the post-translational methylation of arginine residues within proteins and the subsequent proteolysis of these arginine-methylated proteins. ADMA inhibits all three isoforms of nitric oxide synthase and therefore has the potential to produce diverse biological effects, particularly in the cardiovascular system. In addition to its renal clearance, endogenously produced ADMA is metabolized to L-citrulline and dimethylamine by the dimethylarginine dimethylaminohydrolase (DDAH) enzymes. Pharmacological modification of DDAH has therefore been proposed as a mechanism for manipulating endogenous ADMA concentrations and regulating the production of nitric oxide in situations where alterations in nitric oxide signalling have been shown to contribute to pathophysiology. This review describes the biology of ADMA and the potential therapeutic utility of manipulating DDAH activity.

Indexed as

Drug Delivery SystemsAmidohydrolasesAnimalsArginineCytoplasmHumansMethylationNitric OxideNitric Oxide SynthaseProtein IsoformsProtein Processing, Post-TranslationalAmidohydrolasesArgininedimethylargininaseNitric OxideNitric Oxide SynthaseN,N-dimethylarginineProtein Isoforms

Identifiers

PMID21455237
OpenAlexW2067251916

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.