Evidence map›Paper›PMID 33333016›Full record

ArticleMolecular cell2021

Dissecting the Structural Dynamics of the Nuclear Pore Complex.

Zhanna Hakhverdyan, Kelly R Molloy, Sarah Keegan, Thurston Herricks, Dante M Lepore, Mary Munson, Roman I Subbotin, David Fenyö, John D Aitchison, Javier Fernandez-Martinez and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
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  4. A multiomics atlas of theScience advances · 2026
    Article
  5. Review
  6. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  7. Article
  8. Review
  9. Article
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  14. Review
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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

12 authors at 4 institutions in 1 country.

Zhanna HakhverdyanLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10065, USA.
Kelly R MolloyLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA.
Sarah KeeganInstitute for Systems Genetics and Department of Biochemistry and Molecular Pharmacology, NYU Grossman School of Medicine, New York, NY 10016, USA.
Thurston HerricksCenter for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, WA 98101, USA.
Dante M LeporeDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Mary MunsonDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Roman I SubbotinLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA.
David FenyöInstitute for Systems Genetics and Department of Biochemistry and Molecular Pharmacology, NYU Grossman School of Medicine, New York, NY 10016, USA.
John D AitchisonCenter for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, WA 98101, USA; Departments of Pediatrics and Biochemistry, University of Washington, Seattle, WA 98101, USA.
Javier Fernandez-MartinezLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10065, USA. Electronic address: jfernandez@rockefeller.edu.
Brian T ChaitLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA. Electronic address: chait@rockefeller.edu.
Michael P RoutLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10065, USA. Electronic address: rout@rockefeller.edu.
Rockefeller University · USInfectious Disease Research Institute · USInstitute for Systems Biology · USUniversity of Massachusetts Chan Medical School · US

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
Structure and Function of the Exocyst ComplexR01GM068803 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MUNSON, MARY · 2005 to 2021
$7.4M
New Tools for Exploring the Dynamic Interactome (Renewal)U54GM103511 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2012 to 2013
$6.2M
Site Specific Immunophenotyping Assays of COVID19 Patients to Align with NIAID National StudyR01AI141953 · NIAID · INSTITUTE FOR SYSTEMS BIOLOGY · PI BALIGA, NITIN S · 2019 to 2023
$5.7M
NIAID NIH HHS R01 AI141953NIGMS NIH HHS P41 GM103314NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM068803NIGMS NIH HHS R01 GM112108NIGMS NIH HHS U54 GM103511
6 · The paper itself

Abstract

Cellular processes are largely carried out by macromolecular assemblies, most of which are dynamic, having components that are in constant flux. One such assembly is the nuclear pore complex (NPC), an ∼50 MDa assembly comprised of ∼30 different proteins called Nups that mediates selective macromolecular transport between the nucleus and cytoplasm. We developed a proteomics method to provide a comprehensive picture of the yeast NPC component dynamics. We discovered that, although all Nups display uniformly slow turnover, their exchange rates vary considerably. Surprisingly, this exchange rate was relatively unrelated to each Nup's position, accessibility, or role in transport but correlated with its structural role; scaffold-forming Nups exchange slowly, whereas flexible connector Nups threading throughout the NPC architecture exchange more rapidly. Targeted perturbations in the NPC structure revealed a dynamic resilience to damage. Our approach opens a new window into macromolecular assembly dynamics.

Indexed as

Nuclear PoreNuclear Pore Complex ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteinsassemblydynamicsexchangenuclear pore complexnucleoporinquantitative proteomicsturnover

Identifiers

PMID33333016
PMCPMC8121378
OpenAlexW3112736594

What OpenQuestion holds

Textmetadata
LicenceTDM
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.