Evidence map›Paper›PMID 30455356›Full record

ArticleThe Journal of biological chemistry2019

Mapping multivalency in the CLIP-170-EB1 microtubule plus-end complex.

Yaodong Chen, Ping Wang, Kevin C Slep

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
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  4. Review
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  14. Interactions by Disorder - A Matter of Context.Frontiers in molecular biosciences · 2020
    Review
  15. 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.

Yaodong ChenFrom the Key Laboratory of Resources Biology and Biotechnology in Western China, Ministry of Education, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, China.
Ping Wangthe Department of Neurology, University of North Carolina, Chapel Hill, North Carolina 27599.
Kevin C Slepthe Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599-3280, and kslep@bio.unc.edu.ORCID 0000-0003-2365-6080

Funding

Molecular Mechanisms of Cytoskeletal RegulatorsR01GM094415 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROGERS, STEPHEN, SLEP, KEVIN C · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM094415
6 · The paper itself

Abstract

Cytoplasmic linker protein 170 (CLIP-170) is a microtubule plus-end factor that links vesicles to microtubules and recruits the dynein-dynactin complex to microtubule plus ends. CLIP-170 plus-end localization is end binding 1 (EB1)-dependent. CLIP-170 contains two N-terminal cytoskeleton-associated protein glycine-rich (CAP-Gly) domains flanked by serine-rich regions. The CAP-Gly domains are known EB1-binding domains, and the serine-rich regions have also been implicated in CLIP-170's microtubule plus-end localization mechanism. However, the determinants in these serine-rich regions have not been identified. Here we elucidated multiple EB1-binding modules in the CLIP-170 N-terminal region. Using isothermal titration calorimetry and size-exclusion chromatography, we mapped and biophysically characterized these EB1-binding modules, including the two CAP-Gly domains, a bridging S

Indexed as

Amino Acid MotifsHumansMicrotubule-Associated ProteinsMultiprotein ComplexesNeoplasm ProteinsProtein DomainsTubulincytoplasmic linker protein 170MAPRE1 protein, humanMicrotubule-Associated ProteinsMultiprotein ComplexesNeoplasm ProteinsTubulinCAP-GlyCLIP-170cytoskeletonEB1isothermal titration calorimetry (ITC)microtubulemicrotubule-associated protein (MAP)protein–protein interactionSXIPtubulin

Identifiers

PMID30455356
PMCPMC6341378

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.