Evidence map›Paper›PMID 10388753›Full record

ArticleBiophysical journal1999

Conformational changes of the in situ nuclear pore complex.

H Wang, D E Clapham

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Modeling of the mechano-chemical behaviour of the nuclear pore complex: current research and perspectives.Integrative biology : quantitative biosciences from nano to macro · 2016
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Calcium signaling in synapse-to-nucleus communication.Cold Spring Harbor perspectives in biology · 2011
    Review
  12. Review
  13. Mitogen activated protein kinase at the nuclear pore complex.Journal of cellular and molecular medicine · 2011
    Article
  14. Signaling from the secretory granule to the nucleus: Uhmk1 and PAM.Molecular endocrinology (Baltimore, Md.) · 2010
    Article
  15. Review
  16. Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  17. An historical perspective on cell mechanics.Pflugers Archiv : European journal of physiology · 2008
    Article
  18. Review
  19. Biology and biophysics of the nuclear pore complex and its components.International review of cell and molecular biology · 2008
    Review
  20. Review
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.

H WangHoward Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115 USA.
D E Clapham
Howard Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By bridging the double membrane separating the cell nucleus and cytoplasm, nuclear pore complexes (NPCs) are crucial pathways for the exchange of ions, proteins, and RNA between these two cellular compartments. A structure in the central lumen of the NPC, called the nuclear transport protein, central granule, or nuclear plug, appeared to gate diffusion of intermediate-sized molecules (10-40 kDa) across the nuclear membranes. Visualization of the NPC required drying and fixation of the specimen for electron and atomic force microscopy (AFM), a requirement that has raised doubts about the physiological relevance of the observation. Here we present AFM images of the outer nuclear membranes and NPCs of Xenopus laevis oocytes under more physiological conditions. Measured under a variety of Ca2+ depletion conditions, the central granule appeared to occupy and occlude the lumen of the pore in >80% of NPCs compared to <10% in controls. In a few instances images were obtained of the same NPCs as the solution was changed from control saline to store depletion conditions, and finally to store repletion conditions. We conclude that the central lumen of the nuclear pore complex undergoes a conformational change in response to depletion of nuclear cisternal Ca2+ levels.

Indexed as

Protein ConformationAdenosine TriphosphateAnimalsCalciumDiffusionEgtazic AcidInositol 1,4,5-TrisphosphateMicroscopy, Atomic ForceNuclear EnvelopeNuclear ProteinsOocytesXenopus1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acidAdenosine TriphosphateCalciumEgtazic AcidInositol 1,4,5-TrisphosphateNuclear Proteins

Identifiers

PMID10388753
PMCPMC1300325
OpenAlexW2019234354

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.