Evidence map›Paper›PMID 29256606›Full record

ReviewBiochemistry2018

Phase Transitioning the Centrosome into a Microtubule Nucleator.

Michael J Rale, Rachel S Kadzik, Sabine Petry

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Cep57 regulates human centrosomes through multivalent interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Protein phase separation: A novel therapy for cancer?British journal of pharmacology · 2020
    Review
  20. Review
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

3 authors at 1 institution in 1 country.

Michael J RaleDepartment of Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.ORCID 0000-0003-1426-6611
Rachel S KadzikDepartment of Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
Sabine PetryDepartment of Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.ORCID 0000-0002-8537-9763
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Building the Chromosome Segregation Machinery from ScratchDP2GM123493 · NIGMS · PRINCETON UNIVERSITY · PI PETRY, SABINE · 2016 to 2016
$2.4M
Determining the molecular mechanism of localizing and activating the gamma-tubulin ring complex (gamma-TuRC) at the centrosomeF32GM119195 · NIGMS · PRINCETON UNIVERSITY · PI KADZIK, RACHEL S · 2016 to 2017
$103k
Howard Hughes Medical InstituteNIGMS NIH HHS DP2 GM123493NIGMS NIH HHS F32 GM119195NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

Centrosomes are self-assembling, micron-scale, nonmembrane bound organelles that nucleate microtubules (MTs) and organize the microtubule cytoskeleton of the cell. They orchestrate critical cellular processes such as ciliary-based motility, vesicle trafficking, and cell division. Much is known about the role of the centrosome in these contexts, but we have a less comprehensive understanding of how the centrosome assembles and generates microtubules. Studies over the past 10 years have fundamentally shifted our view of these processes. Subdiffraction imaging has probed the amorphous haze of material surrounding the core of the centrosome revealing a complex, hierarchically organized structure whose composition and size changes profoundly during the transition from interphase to mitosis. New biophysical insights into protein phase transitions, where a diffuse protein spontaneously separates into a locally concentrated, nonmembrane bounded compartment, have provided a fresh perspective into how the centrosome might rapidly condense from diffuse cytoplasmic components. In this Perspective, we focus on recent findings that identify several centrosomal proteins that undergo phase transitions. We discuss how to reconcile these results with the current model of the underlying organization of proteins in the centrosome. Furthermore, we reflect on how these findings impact our understanding of how the centrosome undergoes self-assembly and promotes MT nucleation.

Indexed as

Models, BiologicalAnimalsBiochemistryCell Cycle ProteinsCentrosomeHumansInterphaseMicrotubule-Associated ProteinsMicrotubule-Organizing CenterMicrotubulesMitosisPhase TransitionProtein MultimerizationProtein TransportCell Cycle ProteinsMicrotubule-Associated Proteins

Identifiers

PMID29256606
PMCPMC6193265
OpenAlexW2778830888

What OpenQuestion holds

Textmetadata
LicenceTDM
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.