Evidence map›Paper›PMID 9247647›Full record

ArticleMolecular biology of the cell1997

Immunochemical analysis of kinesin light chain function.

D L Stenoien, S T Brady

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 144 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Biological functions and potential therapeutic applications of huntingtin-associated protein 1: progress and prospects.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Tau and Axonal Transport Misregulation in Tauopathies.Advances in experimental medicine and biology · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

D L StenoienDepartment of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas 75235-9111, USA.
S T Brady
The University of Texas Southwestern Medical Center · US

Funding

MOLECULAR MECHANISMS OF AXONAL TRANSPORTR01NS023868 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BRADY, SCOTT THOMAS · 1986 to 2010
$3.7M
PROPERTIES OF AXONAL TUBULIN RELATED TO NEURONAL GROWTHR01NS023320 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BRADY, SCOTT THOMAS · 1985 to 2003
$1.0M
Molecular Mechanisms of Axonal TransportR56NS023868 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS · 2011 to 2011
$554k
NIA NIH HHS NAG2-962/AG12646NINDS NIH HHS NS23320NINDS NIH HHS NS23868
6 · The paper itself

Abstract

The kinesin heterotetramer consists of two heavy and two light chains. Kinesin light chains have been proposed to act in binding motor protein to cargo, but evidence for this has been indirect. A library of monoclonal antibodies directed against conserved epitopes throughout the kinesin light chain sequence were used to map light chain functional architecture and to assess physiological functions of these domains. Immunocytochemistry with all antibodies showed a punctate pattern that was detergent soluble. A monoclonal antibody (KLC-All) made against a highly conserved epitope in the tandem repeat domain of light chains inhibited fast axonal transport in isolated axoplasm by decreasing both the number and velocity of vesicles moving, whereas an antibody against a conserved amino terminus epitope had no effect. KLC-All was equally effective at inhibiting both anterograde and retrograde transport. Neither antibody inhibited microtubule-binding or ATPase activity in vitro. KLC-All was unique among antibodies tested in releasing kinesin from purified membrane vesicles, suggesting a mechanism of action for inhibition of axonal transport. These results provide further evidence that conventional kinesin is a motor for fast axonal transport and demonstrate that kinesin light chains play an important role in kinesin interaction with membranes.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsAntibodies, MonoclonalAntibody SpecificityAxonsBiological TransportCattleConserved SequenceDecapodiformesEpitopesFluorescent Antibody Technique, DirectKinesinsMammalsMiceMicrotubule-Associated ProteinsAdenosine TriphosphatasesAntibodies, MonoclonalEpitopesKinesinsMicrotubule-Associated Proteins

Identifiers

PMID9247647
PMCPMC276118
OpenAlexW2103461242

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.