Evidence map›Paper›PMID 23663963›Full record

ReviewProgress in molecular biology and translational science2013

Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.

Hafumi Nishi, Kosuke Hashimoto, Thomas Madej, Anna R Panchenko

Abstract readReview
In one paragraph

Review in Progress in molecular biology and translational science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
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  4. International journal of molecular sciences · 2024
    Article
  5. Article
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  10. Structural and functional insights into the unique CBS-CP12 fusion protein family in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014
    Review
  15. Article
  16. 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

4 authors.

Hafumi NishiNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, USA.
Kosuke Hashimoto
Thomas Madej
Anna R Panchenko

Funding

Protein-protein binding: regulation and effect of disease mutationsZIALM090313 · NLM · NATIONAL LIBRARY OF MEDICINE · PI PANCHENKO, ANNA · 2013 to 2018
$5.2M
Intramural NIH HHS Z99 CL999999Intramural NIH HHS Z99 HL999999Intramural NIH HHS Z99 LM999999Intramural NIH HHS Z99 MH999999
6 · The paper itself

Abstract

Protein homooligomers afford several important benefits for the cell; they mediate and regulate gene expression, activity of many enzymes, ion channels, receptors, and cell-cell adhesion processes. The evolutionary and physical mechanisms of oligomer formation are very diverse and are not well understood. Certain homooligomeric states may be conserved within protein subfamilies and between different subfamilies, therefore providing the specificity to particular substrates while minimizing interactions with unwanted partners. In addition, transitions between different oligomeric states may regulate protein activity and support the switch between different pathways. In this chapter, we summarize the biological importance of homooligomeric assemblies, physicochemical properties of their interfaces, experimental methods for their identification, their evolution, and role in human diseases.

Indexed as

Evolution, MolecularProtein MultimerizationAnimalsComputational BiologyDiseaseHumansModels, MolecularProtein Structure, Quaternary

Identifiers

PMID23663963
PMCPMC3786560

What OpenQuestion holds

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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.