Evidence map›Paper›PMID 12835758›Full record

ArticleEMBO reports2003

Dimerization properties of a Xenopus laevis kinesin-II carboxy-terminal stalk fragment.

Valeria De Marco, Ario De Marco, Kenneth N Goldie, John J Correia, Andreas Hoenger

Abstract read
In one paragraph

Article in EMBO reports, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. How kinesin-2 forms a stalk.Molecular biology of the cell · 2011
    Article
  8. Article
  9. 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

5 authors.

Valeria De MarcoEuropean Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Ario De Marco
Kenneth N Goldie
John J Correia
Andreas Hoenger

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have analysed the structural and physical properties of the carboxy-terminal stalk region of a kinesin-II, Xenopus kinesin-like protein 3A/B (Xklp3A/B), which we showed to be essential for heterodimerization in a previous work (De Marco et al., 2001). We expressed the corresponding A-stalk and B-stalk fragments and investigated their modes of interaction by analytical ultracentrifugation (AUC), circular dichroism spectroscopy, denaturation assays and electron microscopy. Co-expression of the A-stalk and B-stalk produced the properly folded, hetero-dimeric coiled coil at high yields. The dimeric nature of the complex was confirmed by AUC. We also found that the isolated A-stalk fragment forms a stable helix by itself and shows a significant tendency towards homodimer and higher-order complex formation. In the absence of the corresponding A-stalk fragment, the isolated B-stalk fragment remains partially unfolded, which suggests that the A-stalk provides a template structure for the B-stalk in order to recompose the complete heterodimeric coiled coil.

Indexed as

Amino Acid SequenceAnimalsCalcium-Binding ProteinsCircular DichroismDimerizationKinesinsMolecular Sequence DataMuscle ProteinsPeptide FragmentsProtein ConformationProtein FoldingUltracentrifugationXenopus laevisXenopus ProteinsCalcium-Binding ProteinsKIF3A protein, Xenopuskinesin-IIKinesinsMuscle ProteinsPeptide FragmentsXenopus ProteinsXKLP3 protein, Xenopus

Identifiers

PMID12835758
PMCPMC1326323

What OpenQuestion holds

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Registered trials

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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.