ReviewScience progress2009
Tubulin and its prokaryotic homologue FtsZ: a structural and functional comparison.
Review in Science progress, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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.
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.
Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator.PLoS genetics · 2024Article
- Understanding molecular mechanisms and predicting phenotypic effects of pathogenic tubulin mutations.PLoS computational biology · 2022Article
- Molecular Evolution of Tubulins in Diatoms.International journal of molecular sciences · 2022Article
- Characteristics, chemical compositions and biological activities of propolis from Al-Bahah, Saudi Arabia.Scientific reports · 2017Article
- Six subgroups and extensive recent duplications characterize the evolution of the eukaryotic tubulin protein family.Genome biology and evolution · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are one of the three primary constituents of the eukaryotic cytoskeleton and are constructed from the protein tubulin. FtsZ is a close structural homologue of tubulin within prokaryotes, and plays an important structural role during cell division. This article compares what is known about the structures that these two homologues are able to form in vivo and in vitro and examines the evidence that the water in the immediate vicinity of the structures, particularly in microtubules, may play an important role in their formation and stability. The article then examines evidence that this hydration layer might help our understanding of how the structures formed by tubulin and FtsZ are stabilised by associated proteins and selected cations. The article then considers recent studies of the charge distribution and dipole moments of tubulin and extends this work to include the electrostatic characteristics of FtsZ. There is then an examination of the ways in which the electrostatic similarities and differences between the two proteins might be related to the similarities and differences in the filamentary structures that they form.
Indexed as
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What OpenQuestion holds
Registered trials
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.