Evidence map›Paper›PMID 26795469›Full record

ArticleMethods in enzymology2016

Assays for Posttranslational Modifications of Intermediate Filament Proteins.

Natasha T Snider, M Bishr Omary

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. LncPTEN1, a long non-coding RNA generated fromNon-coding RNA research · 2025
    Article
  2. Article
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  8. Deimination, Intermediate Filaments and Associated Proteins.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Article
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  13. Review
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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 2 institutions in 1 country.

Natasha T SniderDepartment of Cell Biology and Physiology, University of North Carolina, Chapel Hill, North Carolina, USA. Electronic address: ntsnider@med.unc.edu.
M Bishr OmaryDepartment of Molecular & Integrative Physiology, Department of Medicine, University of Michigan, Ann Arbor, Michigan, USA; VA Ann Arbor Healthcare System, Ann Arbor, Michigan, USA.
University of North Carolina at Chapel Hill · USVA Ann Arbor Healthcare System · US

Funding

University of Michigan Center for Gastrointestinal ResearchP30DK034933 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OWYANG, CHUNG · 1986 to 2021
$22.5M
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
Role of cellular metabolism in keratin variant-mediated liver disease progressionR03DK102450 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SNIDER, NATASHA T · 2014 to 2015
$154k
NIDDK NIH HHS DK093776NIDDK NIH HHS DK102450NIDDK NIH HHS DK34933NIDDK NIH HHS DK47918NIDDK NIH HHS DK52951NIDDK NIH HHS K01 DK093776NIDDK NIH HHS P30 DK034933NIDDK NIH HHS R01 DK047918NIDDK NIH HHS R01 DK052951NIDDK NIH HHS R03 DK102450NIDDK NIH HHS R56 DK052951
6 · The paper itself

Abstract

Intermediate filament (IF) proteins are known to be regulated by a number of posttranslational modifications (PTMs). Phosphorylation is the best-studied IF PTM, whereas ubiquitination, sumoylation, acetylation, glycosylation, ADP-ribosylation, farnesylation, and transamidation are less understood in functional terms but are known to regulate specific IFs under various contexts. The number and diversity of IF PTMs is certain to grow along with rapid advances in proteomic technologies. Therefore, the need for a greater understanding of the implications of PTMs to the structure, organization, and function of the IF cytoskeleton has become more apparent with the increased availability of data from global profiling studies of normal and diseased specimens. This chapter will provide information on established methods for the isolation and monitoring of IF PTMs along with the key reagents that are necessary to carry out these experiments.

Indexed as

AcetylationAnimalsBiological AssayGlycosylationHumansIntermediate Filament ProteinsPhosphorylationProtein Processing, Post-TranslationalProteomicsUbiquitinationIntermediate Filament ProteinsAcetylationCytoskeletonFarnesylationGlycosylationIntermediate filamentsKeratinsPhosphorylationPosttranslational modificationsSumoylationTransamidation

Identifiers

PMID26795469
PMCPMC4855289
OpenAlexW2115998034

What OpenQuestion holds

Textmetadata
LicenceTDM
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.