Evidence map›Paper›PMID 11134075›Full record

ArticleThe Journal of cell biology2000

In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding.

H Wang, D A Parry, L N Jones, W W Idler, L N Marekov, P M Steinert

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 96 citations in OpenAlex.

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  15. Identification of reptilian genes encoding hair keratin-like proteins suggests a new scenario for the evolutionary origin of hair.Proceedings of the National Academy of Sciences of the United States of America · 2008
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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

6 authors at 4 institutions in 3 countries.

H WangLaboratory of Skin Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
D A Parry
L N Jones
W W Idler
L N Marekov
P M Steinert
National Institutes of Health · USCommonwealth Scientific and Industrial Research Organisation · AUMassey University · NZNational Institute of Arthritis and Musculoskeletal and Skin Diseases · US

Funding

STRUCTURAL FEATURES OF KERATIN AND RELATED INTERMEDIATE FILAMENTSZ01AR041084 · NIAMS · ARTHRITIS, MUSCULOSKELETAL, SKIN DIS · PI STEVEN, ALASDAIR C. · 1990 to 2004
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6 · The paper itself

Abstract

Intermediate filaments (IF) have been recognized as ubiquitous components of the cytoskeletons of eukaryotic cells for 25 yr. Historically, the first IF proteins to be characterized were those from wool in the 1960s, when they were defined as low sulfur keratins derived from "microfibrils." These proteins are now known as the type Ia/type IIa trichocyte keratins that constitute keratin IF of several hardened epithelial cell types. However, to date, of the entire class of >40 IF proteins, the trichocyte keratins remain the only ones for which efficient in vitro assembly remains unavailable. In this paper, we describe the assembly of expressed mouse type Ia and type IIa trichocyte keratins into IF in high yield. In cross-linking experiments, we document that the alignments of molecules within reduced trichocyte IF are the same as in type Ib/IIb cytokeratins. However, when oxidized in vitro, several intermolecular disulfide bonds form and the molecular alignments rearrange into the pattern shown earlier by x-ray diffraction analyses of intact wool. We suggest the realignments occur because the disulfide bonds confer substantially increased stability to trichocyte keratin IF. Our data suggest a novel role for disulfide bond cross linking in stabilization of these IF and the tissues containing them.

Indexed as

Amino Acid SequenceAnimalsCell DifferentiationChromatography, High Pressure LiquidDisulfidesHumansIntermediate FilamentsKeratinsLeast-Squares AnalysisMiceMicroscopy, ElectronMolecular Sequence DataOxidation-ReductionProtein Structure, QuaternaryProtein Structure, TertiarySequence AlignmentDisulfidesKeratins

Identifiers

PMID11134075
PMCPMC2150680
OpenAlexW2126507158

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.