Evidence map›Paper›PMID 34445785›Full record

ReviewInternational journal of molecular sciences2021

Modeling and Structure Determination of Homo-Oligomeric Proteins: An Overview of Challenges and Current Approaches.

Aljaž Gaber, Miha Pavšič

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Influence of heme and pH on the oligomeric states of Brucella melitensis bacterioferritin.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. Scotty: lattice coincidences in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. Article
  4. Article
  5. Democratizing protein language models with parameter-efficient fine-tuning.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Protein Oligomerization.International journal of molecular sciences · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. International journal of molecular sciences · 2022
    Article
  13. A Lumenal Loop Associated with Catalytic Asymmetry in Plant Vacuolar HInternational journal of molecular sciences · 2021
    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

2 authors.

Aljaž GaberDepartment of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, SI-1000 Ljubljana, Slovenia.ORCID 0000-0002-3744-3142
Miha PavšičDepartment of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, SI-1000 Ljubljana, Slovenia.ORCID 0000-0002-2230-1758

Funding

Javna Agencija za Raziskovalno Dejavnost RS P1-0140, P1-0207, Z1-2637, N1-0191
6 · The paper itself

Abstract

Protein homo-oligomerization is a very common phenomenon, and approximately half of proteins form homo-oligomeric assemblies composed of identical subunits. The vast majority of such assemblies possess internal symmetry which can be either exploited to help or poses challenges during structure determination. Moreover, aspects of symmetry are critical in the modeling of protein homo-oligomers either by docking or by homology-based approaches. Here, we first provide a brief overview of the nature of protein homo-oligomerization. Next, we describe how the symmetry of homo-oligomers is addressed by crystallographic and non-crystallographic symmetry operations, and how biologically relevant intermolecular interactions can be deciphered from the ordered array of molecules within protein crystals. Additionally, we describe the most important aspects of protein homo-oligomerization in structure determination by NMR. Finally, we give an overview of approaches aimed at modeling homo-oligomers using computational methods that specifically address their internal symmetry and allow the incorporation of other experimental data as spatial restraints to achieve higher model reliability.

Indexed as

AlgorithmsHumansModels, MolecularMolecular Docking SimulationProtein ConformationProtein MultimerizationProteinsReproducibility of ResultsProteinshomo-oligomersmodelingstructure determination

Identifiers

PMID34445785
PMCPMC8396596

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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.