Evidence map›Paper›PMID 7787089›Full record

ReviewBiophysical journal1995

Determinants of motor polarity in the kinesin proteins.

S A Endow

Open access · greenAbstract readReview
In one paragraph

Review in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

1 author at 1 institution in 1 country.

S A EndowDepartment of Microbiology, Duke University Medical Center, Durham, North Carolina 27710, USA.
Duke University Hospital · US

Funding

CHROMOSOME MOVEMENT IN MEIOSIS AND MITOSISR01GM046225 · NIGMS · DUKE UNIVERSITY · PI ENDOW, SHARYN A. · 1991 to 2011
$3.5M
NIGMS NIH HHS R01 GM046225
6 · The paper itself

Abstract

Many of the proteins that are members of the kinesin family of microtubule motor proteins are plus-end motors; however, a few of the kinesin proteins have now been found to be minus-end microtubule motors. Overall structural features of the proteins can be used to identify further kinesins that are likely to be minus-end motors. Structural or biochemical differences that may serve as the basis of the "reversed" polarity of a unique subset of the kinesin proteins are discussed.

Indexed as

Adenosine TriphosphateAnimalsBiophysical PhenomenaBiophysicsHydrolysisIn Vitro TechniquesKinesinsMicrotubulesModels, BiologicalMolecular StructureMovementTubulinAdenosine TriphosphateKinesinsTubulin

Identifiers

PMID7787089
PMCPMC1281944
OpenAlexW1468280468

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.