Evidence map›Paper›PMID 31170242›Full record

ArticlePloS one2019

Interactions of nuclear transport factors and surface-conjugated FG nucleoporins: Insights and limitations.

Ryo Hayama, Mirco Sorci, John J Keating Iv, Lee M Hecht, Joel L Plawsky, Georges Belfort, Brian T Chait, Michael P Rout

Abstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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

8 authors.

Ryo HayamaLaboratory of Cellular and Structural Biology, the Rockefeller University, New York, NY, United States of America.ORCID 0000-0001-8706-213X
Mirco SorciDepartment of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States of America.
John J Keating IvDepartment of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States of America.
Lee M HechtLaboratory of Cellular and Structural Biology, the Rockefeller University, New York, NY, United States of America.
Joel L PlawskyDepartment of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States of America.
Georges BelfortDepartment of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States of America.
Brian T ChaitLaboratory of Mass Spectrometry and Gaseous Chemistry, the Rockefeller University, New York, NY, United States of America.
Michael P RoutLaboratory of Cellular and Structural Biology, the Rockefeller University, New York, NY, United States of America.ORCID 0000-0003-2010-706X

Funding

TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2014 to 2023
$18.8M
National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
Structure-Function Mapping of the Nuclear Pore Complex-RenewalR01GM112108 · NIGMS · ROCKEFELLER UNIVERSITY · PI JOHN D. AITCHISON, MICHAEL P ROUT · 2015 to 2026
$9.1M
The dynamic mechanism of nuclear transport visualized at the atomic scaleR01GM117212 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI COWBURN, DAVID · 2016 to 2023
$3.7M
NIGMS NIH HHS P41 GM103314NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM112108NIGMS NIH HHS R01 GM117212
6 · The paper itself

Abstract

Protein-protein interactions are central to biological processes. In vitro methods to examine protein-protein interactions are generally categorized into two classes: in-solution and surface-based methods. Here, using the multivalent interactions between nucleocytoplasmic transport factors and intrinsically disordered FG repeat containing nuclear pore complex proteins as a model system, we examined the utility of three surface-based methods: atomic force microscopy, quartz crystal microbalance with dissipation, and surface plasmon resonance. Although results were comparable to those of previous reports, the apparent effect of mass transport limitations was demonstrated. Additional experiments with a loss-of-interaction FG repeat mutant variant demonstrated that the binding events that take place on surfaces can be unexpectedly complex, suggesting particular care must be exercised in interpretation of such data.

Indexed as

Repetitive Sequences, Nucleic AcidActive Transport, Cell NucleusAmino Acid Sequencebeta KaryopherinsCell NucleusMutationNuclear Pore Complex ProteinsProtein BindingQuartz Crystal Microbalance Techniquesbeta KaryopherinsNuclear Pore Complex Proteins

Identifiers

PMID31170242
PMCPMC6553764

What OpenQuestion holds

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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.