Evidence map›Paper›PMID 23973083›Full record

ArticleMethods in cell biology2013

Structure-function analysis of yeast tubulin.

Anna Luchniak, Yusuke Fukuda, Mohan L Gupta

Abstract read
In one paragraph

Article in Methods in cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Synthesis,RSC medicinal chemistry · 2024
    Article
  2. The Amazing Evolutionary Complexity of Eukaryotic Tubulins: Lessons fromFrontiers in cell and developmental biology · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. 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

3 authors at 1 institution in 1 country.

Anna LuchniakDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Yusuke Fukuda
Mohan L Gupta
University of Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Differential regulationR01GM094313 · NIGMS · UNIVERSITY OF CHICAGO · PI GUPTA, MOHAN · 2011 to 2015
$1.4M
NIGMS NIH HHS R01 GM094313NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Microtubules play essential roles in a wide variety of cellular processes including cell division, motility, and vesicular transport. Microtubule function depends on the polymerization dynamics of tubulin and specific interactions between tubulin and diverse microtubule-associated proteins. To date, investigation of the structural and functional properties of tubulin and tubulin mutants has been limited by the inability to obtain functional protein from overexpression systems, and by the heterogeneous mixture of tubulin isotypes typically isolated from higher eukaryotes. The budding yeast, Saccharomyces cerevisiae, has emerged as a leading system for tubulin structure-function analysis. Yeast cells encode a single beta-tubulin gene and can be engineered to express just one of two alpha isotypes. Moreover, yeast allows site-directed modification of tubulin genes at the endogenous loci expressed under the native promoter and regulatory elements. These advantageous features provide a homogeneous and controlled environment for analysis of the functional consequences of specific mutations. Here, we present the techniques to generate site-specific tubulin mutations in diploid and haploid cells, assess the ability of the mutated protein to support cell viability, measure overall microtubule stability, and define changes in the specific parameters of microtubule dynamic instability. We also outline strategies to determine whether mutations disrupt interactions with microtubule-associated proteins. Microtubule-based functions in yeast are well defined, which allows the observed changes in microtubule properties to be related to the role of microtubules in specific cellular processes.

Indexed as

Bacterial ProteinsCell SurvivalLuminescent ProteinsMicrotubule-Associated ProteinsPromoter Regions, GeneticProtein IsoformsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipBacterial ProteinsLuminescent ProteinsMicrotubule-Associated ProteinsProtein IsoformsSaccharomyces cerevisiae ProteinsTub1 protein, S cerevisiaeTub2 protein, S cerevisiaeyellow fluorescent protein, BacteriaMicrotubule dynamicsMicrotubule structureMicrotubule structure–functionMutant tubulinTubulinTubulin mutationsTubulin structureTubulin structure–functionYeast tubulin

Identifiers

PMID23973083
PMCPMC4084847
OpenAlexW85231079

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.