Evidence map›Paper›PMID 16012187›Full record

ReviewJournal of molecular neuroscience : MN2005

How proteins come together in the plasma membrane and function in macromolecular assemblies: focus on receptor mosaics.

Luigi F Agnati, Diego Guidolin, Susanna Genedani, Sergi Ferré, Albertino Bigiani, Amina S Woods, Kjell Fuxe

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular neuroscience : MN, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. On the key role played by altered protein conformation in Parkinson's disease.Journal of neural transmission (Vienna, Austria : 1996) · 2008
    Review
  9. Intramembrane receptor-receptor interactions: a novel principle in molecular medicine.Journal of neural transmission (Vienna, Austria : 1996) · 2007
    Review
  10. Article
  11. Review
  12. Article
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

7 authors at 4 institutions in 3 countries.

Luigi F AgnatiDepartment of Biomedical Sciences, Section of Physiology, University of Modena and Reggio Emilia, 41100 Modena, Italy. luigiagnati@tin.it
Diego Guidolin
Susanna Genedani
Sergi Ferré
Albertino Bigiani
Amina S Woods
Kjell Fuxe
University of Modena and Reggio Emilia · ITNational Institute on Drug Abuse · USKarolinska Institutet · SEUniversity of Padua · IT

Funding

Neurotransmitter Receptor Heteromers in the Striatal Spine ModuleZIADA000493 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI FERRE, SERGI · 2009 to 2025
$35.6M
Drugs On Learned & Spontaneous Behavior Of Experimental AnimalsZIADA000003 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI SHAHAM, YAVIN · 2009 to 2017
$6.8M
EFFECTS OF DRUGS ON SCHEDULE-CONTROLLED BEHAVIOR OF EXPERIMENTAL ANIMALSZ01DA000003 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI GOLDBERG, STEVEN R · 1991 to 2008
$2.8M
Neurotransmitter Receptor Heteromers in the Striatal Spine ModuleZ01DA000493 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI GOLDBERG, STEVEN R · 2006 to 2008
$691k
6 · The paper itself

Abstract

Some theoretical aspects on structure and function of proteins have been discussed previously. Proteins form multimeric complexes, as they have the capability of binding other proteins (Lego property) resulting in multimeric complexes capable of emergent functions. Multimeric proteins might have either a genomic or a postgenomic origin. Proteins spanning the plasma membrane have been analyzed by considering the effects of the microenvironment in which the protein is embedded. In particular, the different effects of the hydrophilic (extracellular and intracellular) versus the lipophilic (intramembrane) environment have been considered. These aspects have been discussed in the framework of membrane microdomains, in particular, the so-called rafts. In alpha-helix proteins the individual peptide dipoles align to produce a macrodipole crossing the entire membrane. This macrodipole has its positive (extracellular) pole at the N-terminal end of the helix and its negative (intracellular) pole at the C-terminal end. This arrangement has been analyzed in the framework of the counter-ion atmosphere, that is, the formation of a cloud of small ions bearing an opposite charge. Excitable cells reverse their resting potential during the all-or-none action potentials. Hence, the extracellular side of the plasma membrane becomes negative with respect to the intracellular side. This change of polarization affects also the direction and magnitude of the alpha-helix dipole in view of the fact that there is a displacement of the counter ions. The oscillation in the intensity of the dipole caused by the action potentials opens the possibility of an interaction among dipoles by electromagnetic waves.

Indexed as

AnimalsCalorimetryCell MembraneMacromolecular SubstancesMembrane ProteinsProtein Structure, SecondaryReceptors, G-Protein-CoupledStatic ElectricityMacromolecular SubstancesMembrane ProteinsReceptors, G-Protein-Coupled

Identifiers

PMID16012187
OpenAlexW2326840425

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.