Evidence map›Paper›PMID 29610398›Full record

ReviewCold Spring Harbor perspectives in biology2018

Types I and II Keratin Intermediate Filaments.

Justin T Jacob, Pierre A Coulombe, Raymond Kwan, M Bishr Omary

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing 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

134 citing papers in PubMed, 258 citations in OpenAlex.

  1. Article
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  9. An updated guide to hair follicle stem cell markers and changes in their expression with aging.JID innovations : skin science from molecules to population health · 2026
    Review
  10. Comparative analysis of wavelength-specific UV stress granule formation.bioRxiv : the preprint server for biology · 2026
    Article
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  14. Review
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74 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

4 authors at 3 institutions in 1 country.

Justin T JacobDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland 21205.
Pierre A CoulombeDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland 21205.
Raymond KwanDepartments of Molecular & Integrative Physiology and Medicine, University of Michigan, Ann Arbor, Michigan 48109.
M Bishr OmaryDepartments of Molecular & Integrative Physiology and Medicine, University of Michigan, Ann Arbor, Michigan 48109.
Johns Hopkins University · USMichigan Medicine · USVA Ann Arbor Healthcare System · US

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Non-Canonical Functions of Keratin Proteins in SkinR01AR044232 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COULOMBE, PIERRE · 1996 to 2020
$8.6M
TYPE II KERATIN GENES /PROTEINS IN COMPLEX EPITHELIAR01AR042047 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COULOMBE, PIERRE · 1995 to 2018
$7.1M
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
Keratins as novel determinants of tumor biologyR01CA160255 · NCI · JOHNS HOPKINS UNIVERSITY · PI COULOMBE, PIERRE · 2011 to 2017
$1.9M
Role of keratin intermediate filaments in skin epithelial architecture and homeostasisR56AR042047 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COULOMBE, PIERRE · 2020 to 2020
$429k
Genetic and molecular effects on hepatocyte nucleocytoplasm protein aggregationR56DK052951 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OMARY, BISHR · 2012 to 2012
$179k
NCI NIH HHS R01 CA160255NCI NIH HHS T32 CA009110NIAMS NIH HHS R01 AR042047NIAMS NIH HHS R01 AR044232NIAMS NIH HHS R56 AR042047NIDDK NIH HHS R01 DK047918NIDDK NIH HHS R01 DK052951NIDDK NIH HHS R56 DK052951
6 · The paper itself

Abstract

Keratins-types I and II-are the intermediate-filament-forming proteins expressed in epithelial cells. They are encoded by 54 evolutionarily conserved genes (28 type I, 26 type II) and regulated in a pairwise and tissue type-, differentiation-, and context-dependent manner. Here, we review how keratins serve multiple homeostatic and stress-triggered mechanical and nonmechanical functions, including maintenance of cellular integrity, regulation of cell growth and migration, and protection from apoptosis. These functions are tightly regulated by posttranslational modifications and keratin-associated proteins. Genetically determined alterations in keratin-coding sequences underlie highly penetrant and rare disorders whose pathophysiology reflects cell fragility or altered tissue homeostasis. Furthermore, keratin mutation or misregulation represents risk factors or genetic modifiers for several additional acute and chronic diseases.

Indexed as

ApoptosisCell MovementCell ProliferationHomeostasisKeratins, Type IKeratins, Type IIProtein Processing, Post-TranslationalStress, PhysiologicalKeratins, Type IKeratins, Type II

Identifiers

PMID29610398
PMCPMC5880164
OpenAlexW2795986011

What OpenQuestion holds

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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.