Evidence map›Paper›PMID 16227433›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Functions and dysfunctions of the nuclear lamin Ig-fold domain in nuclear assembly, growth, and Emery-Dreifuss muscular dystrophy.

Dale K Shumaker, Reynold I Lopez-Soler, Stephen A Adam, Harald Herrmann, Robert D Moir, Timothy P Spann, Robert D Goldman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. From lamins to lamina: a structural perspective.Histochemistry and cell biology · 2013
    Review
  18. Article
  19. Article
  20. Nuclear lamins.Cold Spring Harbor perspectives in biology · 2010
    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

7 authors at 2 institutions in 2 countries.

Dale K ShumakerDepartment of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA.
Reynold I Lopez-Soler
Stephen A Adam
Harald Herrmann
Robert D Moir
Timothy P Spann
Robert D Goldman
Northwestern University · USHeidelberg University · DE

Funding

INTERMEDIATE FILAMENTS IN NORMAL AND TRANSFORMED CELLSR01CA031760 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 1985 to 2013
$4.9M
TRAINING PROGRAM IN ONCOGENESIS &DEVELOPMENT BIOLOGYT32CA080621 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI EKLUND, ELIZABETH ANN · 2001 to 2018
$4.1M
MINORITY PREDOCTORAL TRAINING PROGRAMF31GM020083 · NIGMS · NORTHWESTERN UNIVERSITY · PI LOPEZ-SOLER, REYNOLD I · 1999 to 2002
$66k
NCI NIH HHS CA 31760NCI NIH HHS R01 CA031760NCI NIH HHS T32 CA080621NCI NIH HHS T32 CA 80621NIGMS NIH HHS 5F31 GM 20083-03NIGMS NIH HHS F31 GM020083
6 · The paper itself

Abstract

The non-alpha-helical C terminus of Xenopus lamin B3 (LB3T) inhibits the polymerization of lamin B3 in vitro and prevents the assembly of nuclei in Xenopus egg interphase extracts. To more precisely define the functions of LB3T in nuclear assembly, we have expressed subdomains of LB3T and determined their effects on nuclear assembly in Xenopus extracts. The results demonstrate that the Ig-fold motif (LB3T-Ig) is sufficient to inhibit lamin polymerization in vitro. Addition of the LB3T-Ig to egg extracts before the introduction of chromatin prevents chromatin decondensation and the assembly of the lamina, membranes, and pore complexes comprising the nuclear envelope. When added to assembled nuclei, LB3T-Ig prevents the further incorporation of lamin B3 into the endogenous lamina and blocks nuclear growth. The introduction of a point mutation in LB3T-Ig (R454W; LB3T-IgRW), known to cause Emery-Dreifuss muscular dystrophy when present in lamin A, does not inhibit lamin polymerization, chromatin decondensation, or nuclear assembly and growth. These results shed light on the specific alterations in lamin functions attributable to a known muscular dystrophy mutation and provide an experimental framework for revealing the effects of other mutations causing a wide range of laminopathies.

Indexed as

Protein FoldingAnimalsCell NucleusHumansLamin Type BMuscular Dystrophy, Emery-DreifussNuclear EnvelopePoint MutationPolymersProtein Structure, TertiaryXenopusLamin Type BPolymers

Identifiers

PMID16227433
PMCPMC1255737
OpenAlexW2071225961

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.