Evidence map›Paper›PMID 19674973›Full record

ArticleThe Journal of biological chemistry2009

Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element.

James R R Whittle, Thomas U Schwartz

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review
  11. Article
  12. Evolutionary divergence of the nuclear pore complex from fungi to metazoans.Protein science : a publication of the Protein Society · 2019
    Article
  13. Review
  14. Article
  15. Review
  16. The Structure Inventory of the Nuclear Pore Complex.Journal of molecular biology · 2016
    Review
  17. Article
  18. Article
  19. Review
  20. 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

2 authors.

James R R WhittleDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
Thomas U SchwartzDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139. Electronic address: tus@mit.edu.

Funding

High Resolution Assembly Structure of The Nuclear Pore ComplexR01GM077537 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2007 to 2019
$4.3M
NIGMS NIH HHS GM77537NIGMS NIH HHS R01 GM077537
6 · The paper itself

Abstract

The nuclear pore complex (NPC) constitutes one of the largest protein assemblies in the eukaryotic cell and forms the exclusive gateway to the nucleus. The stable, approximately 15-20-MDa scaffold ring of the NPC is built from two multiprotein complexes arranged around a central 8-fold axis. Here we present crystal structures of two large architectural units, yNup170(979-1502) and hNup107(658-925) x hNup133(517-1156), each a constituent of one of the two multiprotein complexes. Conservation of domain arrangement and of tertiary structure suggests that Nup157/170 and Nup133 derived from a common ancestor. Together with the previously established ancestral coatomer element (ACE1), these two elements constitute the major alpha-helical building blocks of the NPC scaffold and define its branched, lattice-like architecture, similar to vesicle coats like COPII. We hypothesize that the extant NPC evolved early during eukaryotic evolution from a rudimentary structure composed of several identical copies of a few ancestral elements, later diversified and specified by gene duplication.

Indexed as

Evolution, MolecularAmino Acid SequenceCrystallography, X-RayHumansMinor Histocompatibility AntigensModels, MolecularMolecular Sequence DataMultiprotein ComplexesNuclear PoreNuclear Pore Complex ProteinsProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidMinor Histocompatibility AntigensMultiprotein ComplexesNuclear Pore Complex ProteinsNUP107 protein, humanNUP133 protein, humanNUP157 protein, S cerevisiaeNUP170 protein, S cerevisiaeNUP84 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID19674973
PMCPMC2788893

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.