Evidence map›Paper›PMID 19371079›Full record

ReviewBiochemistry2009

Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases.

Dale E Edmondson, Claudia Binda, Jin Wang, Anup K Upadhyay, Andrea Mattevi

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
26.4field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 293 citations in OpenAlex.

  1. Review
  2. Prenylcysteine Oxidase 1 Deficiency Protects the Cardiac Muscle Cell Line HL-1 Against Ischaemic/Hypoxic Stress.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Peripheral catecholamine systems: an evolutionary perspective.American journal of physiology. Regulatory, integrative and comparative physiology · 2025
    Review
  7. Article
  8. Article
  9. Type A monoamine oxidase; its unique role in mood, behavior and neurodegeneration.Journal of neural transmission (Vienna, Austria : 1996) · 2025
    Review
  10. Article
  11. Article
  12. Synthesis of 1,2,4-Oxadiazin-5(6Molecules (Basel, Switzerland) · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Heterocycle-containing tranylcypromine derivatives endowed with high anti-LSD1 activity.Journal of enzyme inhibition and medicinal chemistry · 2022
    Article
  20. Article

27 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

5 authors at 2 institutions in 2 countries.

Dale E EdmondsonDepartment of Biochemistry, Emory University, Atlanta, Georgia 30322, USA. deedmon@emory.edu
Claudia Binda
Jin Wang
Anup K Upadhyay
Andrea Mattevi
Emory University · USUniversity of Pavia · IT

Funding

COVALENT FLAVIN COENZYMES IN FLAVOENZYME CATALYSISR01GM029433 · NIGMS · EMORY UNIVERSITY · PI EDMONDSON, DALE E. · 1985 to 2013
$4.6M
NIGMS NIH HHS GM-29433NIGMS NIH HHS R01 GM029433
6 · The paper itself

Abstract

The past decade has brought major advances in our knowledge of the structures and mechanisms of MAO A and MAO B, which are pharmacological targets for specific inhibitors. In both enzymes, crystallographic and biochemical data show their respective C-terminal transmembrane helices anchor the enzymes to the outer mitochondrial membrane. Pulsed EPR data show both enzymes are dimeric in their membrane-bound forms with agreement between distances measured in their crystalline forms. Distances measured between active site-directed spin-labels in membrane preparations show excellent agreement with those estimated from crystallographic data. Our knowledge of requirements for development of specific reversible MAO B inhibitors is in a fairly mature status. Less is known regarding the structural requirements for highly specific reversible MAO A inhibitors. In spite of their 70% level of sequence identity and similarities of C(alpha) folds, the two enzymes exhibit significant functional and structural differences that can be exploited in the ultimate goal of the development of highly specific inhibitors. This review summarizes the current structural and mechanistic information available that can be utilized in the development of future highly specific neuroprotectants and cardioprotectants.

Indexed as

Allyl CompoundsAnimalsButylaminesCell MembraneCrystallography, X-RayHumansKineticsMitochondriaModels, ChemicalModels, MolecularMolecular ConformationMonoamine OxidaseProtein ConformationProtein Structure, TertiaryRatsAllyl CompoundsButylaminesmofegilineMonoamine Oxidase

Identifiers

PMID19371079
PMCPMC2710584
OpenAlexW2006911538

What OpenQuestion holds

Textmetadata
LicenceTDM
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.