Evidence map›Paper›PMID 24556839›Full record

ReviewNature reviews. Molecular cell biology2014

Post-translational modifications of intermediate filament proteins: mechanisms and functions.

Natasha T Snider, M Bishr Omary

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 266 papers.

0numbers the graph read from it
0cells of the map it votes in
266citing papers in PubMed
24.0field-weighted citation impact, top 1% 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

266 citing papers in PubMed, 544 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Vimentin Intermediate Filaments: A Paradigm Shift From Static Structure to Dynamic Cytoplasmic Network.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. Vimentin Dynamics in Viral Infection: Shield or Sabotage?International journal of molecular sciences · 2025
    Review

206 more citing papers are in PubMed but not listed here.

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.

Natasha T SniderDepartments of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
M Bishr Omary1] Departments of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA. [2] Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA. [3] Veterans Affairs Ann Arbor Healthcare System, Ann Arbor, Michigan 48109, USA.
University of Michigan–Ann Arbor · US

Funding

Keratin Biology and Disease Aspects in Simple EpitheliaR01DK047918 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1995 to 2018
$6.6M
Regulation and Dynamics of Keratins in Digestive OrgansR01DK052951 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 1997 to 2015
$4.5M
Keratin sumoylation and its function during hepatocyte stress and liver diseaseK01DK093776 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SNIDER, NATASHA T · 2011 to 2015
$586k
Genetic and molecular effects on hepatocyte nucleocytoplasm protein aggregationR56DK052951 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 2012 to 2012
$179k
NIDDK NIH HHS DK093776NIDDK NIH HHS DK47918NIDDK NIH HHS DK52951NIDDK NIH HHS K01 DK093776NIDDK NIH HHS R01 DK047918NIDDK NIH HHS R01 DK052951NIDDK NIH HHS R56 DK052951
6 · The paper itself

Abstract

Intermediate filaments (IFs) are cytoskeletal and nucleoskeletal structures that provide mechanical and stress-coping resilience to cells, contribute to subcellular and tissue-specific biological functions, and facilitate intracellular communication. IFs, including nuclear lamins and those in the cytoplasm (keratins, vimentin, desmin, neurofilaments and glial fibrillary acidic protein, among others), are functionally regulated by post-translational modifications (PTMs). Proteomic advances highlight the enormous complexity and regulatory potential of IF protein PTMs, which include phosphorylation, glycosylation, sumoylation, acetylation and prenylation, with novel modifications becoming increasingly appreciated. Future studies will need to characterize their on-off mechanisms, crosstalk and utility as biomarkers and targets for diseases involving the IF cytoskeleton.

Indexed as

Models, BiologicalHumansIntermediate Filament ProteinsProtein Processing, Post-TranslationalIntermediate Filament Proteins

Identifiers

PMID24556839
PMCPMC4079540
OpenAlexW2008679290

What OpenQuestion holds

Textmetadata
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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.