Evidence map›Paper›PMID 10793159›Full record

ArticleMolecular biology of the cell2000

Structure-function relationships in yeast tubulins.

K L Richards, K R Anders, E Nogales, K Schwartz, K H Downing, D Botstein

Abstract readComparative Study
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. Article
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  9. Review
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  14. An electron microscopy journey in the study of microtubule structure and dynamics.Protein science : a publication of the Protein Society · 2015
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Structure-function analysis of yeast tubulin.Methods in cell biology · 2013
    Article
  20. 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

6 authors.

K L RichardsDepartment of Genetics, Stanford University School of Medicine, Stanford, California 94305, USA.
K R Anders
E Nogales
K Schwartz
K H Downing
D Botstein

Funding

Genetics of Functional Interactions in YeastR01GM046406 · NIGMS · STANFORD UNIVERSITY · PI BOTSTEIN, DAVID · 2001 to 2015
$9.5M
GENETICS OF FUNCTIONAL INTERACTIONS IN YEASTR37GM046406 · NIGMS · STANFORD UNIVERSITY · PI BOTSTEIN, DAVID · 1991 to 2000
$683k
NIGMS NIH HHS GM46406NIGMS NIH HHS R01 GM046406NIGMS NIH HHS R37 GM046406
6 · The paper itself

Abstract

A comprehensive set of clustered charged-to-alanine mutations was generated that systematically alter TUB1, the major alpha-tubulin gene of Saccharomyces cerevisiae. A variety of phenotypes were observed, including supersensitivity and resistance to the microtubule-destabilizing drug benomyl, lethality, and cold- and temperature-sensitive lethality. Many of the most benomyl-sensitive tub1 alleles were synthetically lethal in combination with tub3Delta, supporting the idea that benomyl supersensitivity is a rough measure of microtubule instability and/or insufficiency in the amount of alpha-tubulin. The systematic tub1 mutations were placed, along with the comparable set of tub2 mutations previously described, onto a model of the yeast alpha-beta-tubulin dimer based on the three-dimensional structure of bovine tubulin. The modeling revealed a potential site for binding of benomyl in the core of beta-tubulin. Residues whose mutation causes cold sensitivity were concentrated at the lateral and longitudinal interfaces between adjacent subunits. Residues that affect binding of the microtubule-binding protein Bim1p form a large patch across the exterior-facing surface of alpha-tubulin in the model. Finally, the positions of the mutations suggest that proximity to the alpha-beta interface may account for the finding of synthetic lethality of five viable tub1 alleles with the benomyl-resistant but otherwise entirely viable tub2-201 allele.

Indexed as

Saccharomyces cerevisiae ProteinsAnimalsBenomylBinding SitesCattleCell Cycle ProteinsCold TemperatureFungal ProteinsMicrotubule ProteinsMicrotubulesModels, MolecularMultigene FamilyMutationPhenotypeProtein ConformationSaccharomyces cerevisiaeBenomylBIM1 protein, S cerevisiaeCell Cycle ProteinsFungal ProteinsMicrotubule ProteinsSaccharomyces cerevisiae ProteinsTubulin

Identifiers

PMID10793159
PMCPMC14891

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.