Evidence map›Paper›PMID 28835994›Full record

ReviewCurrent genetics2018

A new twist in the coil: functions of the coiled-coil domain of structural maintenance of chromosome (SMC) proteins.

Avi Matityahu, Itay Onn

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Cohesin organization, dynamics, and subdomain functions revealed by genetic suppressor screening.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Article
  7. Cohesin ATPase activities regulate DNA binding and coiled-coil configuration.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. It's all in the numbers: Cohesin stoichiometry.Frontiers in molecular biosciences · 2022
    Review
  9. Review
  10. Review
  11. Functions ofBiomedicines · 2021
    Article
  12. Article
  13. Article
  14. Braiding topology and the energy landscape of chromosome organization proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. A Rubisco-binding protein is required for normal pyrenoid number and starch sheath morphology inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Review
  18. Review
  19. 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 at 1 institution in 1 country.

Avi MatityahuFaculty of Medicine in the Galilee, Bar-Ilan University, 8 Henrietta Szold St., P.O. Box 1589, 1311502, Safed, Israel.
Itay OnnFaculty of Medicine in the Galilee, Bar-Ilan University, 8 Henrietta Szold St., P.O. Box 1589, 1311502, Safed, Israel. Itay.Onn@biu.ac.il.ORCID http://orcid.org/0000-0002-7689-5520
Bar-Ilan University · IL

Funding

Israel Cancer Association 20170111Israel Science Foundation 1099/16
6 · The paper itself

Abstract

The higher-order organization of chromosomes ensures their stability and functionality. However, the molecular mechanism by which higher order structure is established is poorly understood. Dissecting the activity of the relevant proteins provides information essential for achieving a comprehensive understanding of chromosome structure. Proteins of the structural maintenance of chromosome (SMC) family of ATPases are the core of evolutionary conserved complexes. SMC complexes are involved in regulating genome dynamics and in maintaining genome stability. The structure of all SMC proteins resembles an elongated rod that contains a central coiled-coil domain, a common protein structural motif in which two α-helices twist together. In recent years, the imperative role of the coiled-coil domain to SMC protein activity and regulation has become evident. Here, we discuss recent advances in the function of the SMC coiled coils. We describe the structure of the coiled-coil domain of SMC proteins, modifications and interactions that are mediated by it. Furthermore, we assess the role of the coiled-coil domain in conformational switches of SMC proteins, and in determining the architecture of the SMC dimer. Finally, we review the interplay between mutations in the coiled-coil domain and human disorders. We suggest that distinctive properties of coiled coils of different SMC proteins contribute to their distinct functions. The discussion clarifies the mechanisms underlying the activity of SMC proteins, and advocates future studies to elucidate the function of the SMC coiled coil domain.

Indexed as

Protein Interaction Domains and MotifsChromosomal Proteins, Non-HistoneGene Expression RegulationHumansMultigene FamilyMutationProtein BindingSignal TransductionStructure-Activity RelationshipChromosomal Proteins, Non-HistoneChromosome structureCohesinCoiled-coil domainCondensinSMC5/6Structural maintenance of chromosome (SMC) proteins

Identifiers

PMID28835994
OpenAlexW2750207165

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.