Evidence map›Paper›PMID 23499021›Full record

ArticleStructure (London, England : 1993)2013

Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex.

Parthasarathy Sampathkumar, Seung Joong Kim, Paula Upla, William J Rice, Jeremy Phillips, Benjamin L Timney, Ursula Pieper, Jeffrey B Bonanno, Javier Fernandez-Martinez, Zhanna Hakhverdyan and 9 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  3. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Synthesis and Biological Evaluation of BODIPY-PF-543.Molecules (Basel, Switzerland) · 2019
    Article
  11. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review
  12. Article
  13. Evolutionary divergence of the nuclear pore complex from fungi to metazoans.Protein science : a publication of the Protein Society · 2019
    Article
  14. Article
  15. Review
  16. Identification of the NovelG3 (Bethesda, Md.) · 2018
    Article
  17. Review
  18. Article
  19. Article
  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

19 authors at 9 institutions in 1 country.

Parthasarathy SampathkumarDepartment of Biochemistry, Ullmann Building, Room 409, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Seung Joong Kim
Paula Upla
William J Rice
Jeremy Phillips
Benjamin L Timney
Ursula Pieper
Jeffrey B Bonanno
Javier Fernandez-Martinez
Zhanna Hakhverdyan
Natalia E Ketaren
Tsutomu Matsui
Thomas M Weiss
David L Stokes
J Michael Sauder
Stephen K Burley
Andrej Sali
Michael P Rout
Steven C Almo
Rockefeller University · USAlbert Einstein College of Medicine · USUniversity of California, San Francisco · USNew York Structural Biology Center · USStanford Synchrotron Radiation Lightsource · USEli Lilly (United States) · USNew York University · USQB3 · USRutgers, The State University of New Jersey · US

Funding

SUBPROJECT 5U54GM074945 · NIGMS · SGX PHARMACEUTICALS, INC. · PI BURLEY, STEPHEN KEVIN · 2005 to 2009
$46.2M
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
The NYSGRC: A Large Scale Center for PSI:BiologyU54GM094662 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI FISER, ANDRAS · 2010 to 2014
$32.6M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
New Tools for Exploring the Dynamic Interactome (Renewal)U54GM103511 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2012 to 2013
$6.2M
IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
Virtual Gating Machines for Protein PurificationR01GM071329 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2004 to 2013
$4.6M
Nucleocytoplasmic transport: a target for cellular controlU01GM098256 · NIGMS · ROCKEFELLER UNIVERSITY · PI AITCHISON, JOHN D., ROUT, MICHAEL P · 2011 to 2014
$3.0M
DISSECTING THE MOLECULAR MACHINERY OF NUCLEAR TRANSPORTR01GM062427 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2001 to 2010
$2.7M
RES FACIL CONSTRUCTION: HALLUCINOGENSC06RR017528 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI COWBURN, DAVID · 2002 to 2002
$2.0M
NCIPC CDC HHS C06 RR017528-01-CEMNCRR NIH HHS C06 RR017528NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NIBIB NIH HHS P30 EB009998NIBIB NIH HHS P30-EB-009998NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM062427NIGMS NIH HHS R01 GM071329NIGMS NIH HHS R01 GM083960NIGMS NIH HHS U01 GM098256NIGMS NIH HHS U54 GM074945NIGMS NIH HHS U54 GM094662NIGMS NIH HHS U54 GM103511
6 · The paper itself

Abstract

The nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure composed of the nuclear ring, cytoplasmic ring, a membrane ring, and two inner rings. Nup192 is a major component of the NPC's inner ring. We report the crystal structure of Saccharomyces cerevisiae Nup192 residues 2-960 [ScNup192(2-960)], which adopts an α-helical fold with three domains (i.e., D1, D2, and D3). Small angle X-ray scattering and electron microscopy (EM) studies reveal that ScNup192(2-960) could undergo long-range transition between "open" and "closed" conformations. We obtained a structural model of full-length ScNup192 based on EM, the structure of ScNup192(2-960), and homology modeling. Evolutionary analyses using the ScNup192(2-960) structure suggest that NPCs and vesicle-coating complexes are descended from a common membrane-coating ancestral complex. We show that suppression of Nup192 expression leads to compromised nuclear transport and hypothesize a role for Nup192 in modulating the permeability of the NPC central channel.

Indexed as

Evolution, MolecularModels, MolecularProtein ConformationActive Transport, Cell NucleusCrystallizationMicroscopy, ElectronNuclear PoreNuclear Pore Complex ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsScattering, Small AngleNuclear Pore Complex ProteinsNUP192 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID23499021
PMCPMC3755625
OpenAlexW2129095181

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.