Evidence map›Paper›PMID 30114294›Full record

ArticlePloS one2018

Understanding the dynamics of keratin weakening and hydrolysis by proteases.

Laura Navone, Robert Speight

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Strategies of Recovery and Organic Recycling Used in Textile Waste Management.International journal of environmental research and public health · 2022
    Review
  14. Platyphylloside, a potential inhibitor from epicarp ofSaudi journal of biological sciences · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Article
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  20. 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

2 authors at 1 institution in 1 country.

Laura NavoneScience and Engineering Faculty, Queensland University of Technology, Brisbane, Queensland, Australia.ORCID 0000-0003-3672-3799
Robert SpeightScience and Engineering Faculty, Queensland University of Technology, Brisbane, Queensland, Australia.
Queensland University of Technology · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Keratin is the structural protein in hair, nails, feathers and horns. Keratin is recalcitrant, highly disulfide bonded and is generally inaccessible to common proteases. Only certain types of proteases, called keratinases, are able to cleave the peptide bonds within the keratin structure. Due to this outstanding activity, keratinases have potential application in industries such as livestock, cosmetics and pharmaceuticals. Yet, the process of enzymatic keratin degradation is poorly understood, affecting the development of industrial enzyme formulations that may require full or only partial modification or weakening. Here we investigate the dynamics of keratin weakening and hydrolysis, showing that the decrease in hair mechanical strength is associated with cuticle removal and damage to the cortex and complete breakdown is dependent on reducing agents. Proteases with keratinolytic activity were selected and applied to hair with degradation examined by mechanical, biochemical and microscopic techniques. The extent of keratin degradation was highly enhanced by the presence of reducing agents, principally sodium thioglycolate, exceeding 90% degradation within 16 h of enzymatic treatment. Application was extended to feathers showing that the findings are relevant to improving the use of keratinases in a variety of industries. Overall, the outcomes provide valuable insights into the keratin degradation process by enzymes for the optimization of cosmetic and pharmaceutical products and for livestock waste recycling among other important applications.

Indexed as

AnimalsCytoskeletonDisulfidesHairHydrolysisKeratinsMechanical PhenomenaPeptide HydrolasesProteolysisDisulfidesKeratinsPeptide Hydrolases

Identifiers

PMID30114294
PMCPMC6095591
OpenAlexW2885175055

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.