Evidence map›Paper›PMID 31888987›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Braiding topology and the energy landscape of chromosome organization proteins.

Dana Krepel, Aram Davtyan, Nicholas P Schafer, Peter G Wolynes, José N Onuchic

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed, 24 citations in OpenAlex.

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  4. Motorized chain models of the ideal chromosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Dana KrepelCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005; danakrezus@rice.edu jonuchic@rice.edu.
Aram DavtyanCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005.
Nicholas P SchaferCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005.
Peter G WolynesCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005.ORCID 0000-0001-7975-9287
José N OnuchicCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005; danakrezus@rice.edu jonuchic@rice.edu.
Center for Theoretical Biological Physics · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assemblies of structural maintenance of chromosomes (SMC) proteins and kleisin subunits are essential to chromosome organization and segregation across all kingdoms of life. While structural data exist for parts of the SMC-kleisin complexes, complete structures of the entire complexes have yet to be determined, making mechanistic studies difficult. Using an integrative approach that combines crystallographic structural information about the globular subdomains, along with coevolutionary information and an energy landscape optimized force field (AWSEM), we predict atomic-scale structures for several tripartite SMC-kleisin complexes, including prokaryotic condensin, eukaryotic cohesin, and eukaryotic condensin. The molecular dynamics simulations of the SMC-kleisin protein complexes suggest that these complexes exist as a broad conformational ensemble that is made up of different topological isomers. The simulations suggest a critical role for the SMC coiled-coil regions, where the coils intertwine with various linking numbers. The twist and writhe of these braided coils are coupled with the motion of the SMC head domains, suggesting that the complexes may function as topological motors. Opening, closing, and translation along the DNA of the SMC-kleisin protein complexes would allow these motors to couple to the topology of DNA when DNA is entwined with the braided coils.

Indexed as

Molecular Dynamics SimulationBinding SitesChromosomal Proteins, Non-HistoneHumansKinesinsProtein BindingChromosomal Proteins, Non-HistoneKinesinschromosome organizationDNA topologyprotein topologySMC−kleisin complexes

Identifiers

PMID31888987
PMCPMC6983425
OpenAlexW2998208938

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.