ArticleJournal of cell science2011
Unique amino acid signatures that are evolutionarily conserved distinguish simple-type, epidermal and hair keratins.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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.
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Who cites it
33 citing papers in PubMed, 86 citations in OpenAlex.
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- Efficacy and Safety of a Drinkable Nutraceutical in Premenopausal Women with Telogen Effluvium: A 6-Month, Randomized, Multicenter, Double-Blind, Placebo-Controlled Study.Dermatology and therapy · 2026Article
- Convergent Evolution of Cysteine-Rich Keratins in Horny Teeth of Jawless Vertebrates and in Cornified Skin Appendages of Amniotes.Molecular biology and evolution · 2025Article
- Identification of Low-Complexity Domains by Compositional Signatures Reveals Class-Specific Frequencies and Functions Across the Domains of Life.PLoS computational biology · 2024Article
- Evolutionary origin of Hoxc13-dependent skin appendages in amphibians.Nature communications · 2024Article
- Production and characterization of human hair keratin bioplastic films with novel plasticizers.Scientific reports · 2024Article
- Considerations on amino acid patterns in the natural felid diet: a review.Frontiers in veterinary science · 2024Review
- Raman spectroscopy and mass spectrometry identifies a unique group of epidermal lipids in active discoid lupus erythematosus.Scientific reports · 2023Article
- Dermatophytosis caused by Nannizzia nana (Microsporum nanum): a comprehensive review on a novel pathogen.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Review
- Metabolomic Analysis and MRM Verification of Coarse and Fine Skin Tissues of Liaoning Cashmere Goat.Molecules (Basel, Switzerland) · 2022Article
- From Strain Stiffening to Softening-Rheological Characterization of Keratins 8 and 18 Networks Crosslinked via Electron Irradiation.Polymers · 2022Article
- Update of the keratin gene family: evolution, tissue-specific expression patterns, and relevance to clinical disorders.Human genomics · 2022Article
- A modern baseline for the paired isotopic analysis of skin and bone in terrestrial mammals.Royal Society open science · 2022Article
- Review
- De novo filament formation by human hair keratins K85 and K35 follows a filament development pattern distinct from cytokeratin filament networks.FEBS open bio · 2021Article
- Review
- Predictive Model of Nail Consistency Using Scanning Electron Microscopy with Energy-Dispersive X-Ray.Biology · 2021Article
- Structure of Keratin.Methods in molecular biology (Clifton, N.J.) · 2021Article
- From structural resilience to cell specification - Intermediate filaments as regulators of cell fate.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Review
- Genotype-phenotype analysis of LMNA-related diseases predicts phenotype-selective alterations in lamin phosphorylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
Keratins (Ks) consist of central α-helical rod domains that are flanked by non-α-helical head and tail domains. The cellular abundance of keratins, coupled with their selective cell expression patterns, suggests that they diversified to fulfill tissue-specific functions although the primary structure differences between them have not been comprehensively compared. We analyzed keratin sequences from many species: K1, K2, K5, K9, K10, K14 were studied as representatives of epidermal keratins, and compared with K7, K8, K18, K19, K20 and K31, K35, K81, K85, K86, which represent simple-type (single-layered or glandular) epithelial and hair keratins, respectively. We show that keratin domains have striking differences in their amino acids. There are many cysteines in hair keratins but only a small number in epidermal keratins and rare or none in simple-type keratins. The heads and/or tails of epidermal keratins are glycine and phenylalanine rich but alanine poor, whereas parallel domains of hair keratins are abundant in prolines, and those of simple-type epithelial keratins are enriched in acidic and/or basic residues. The observed differences between simple-type, epidermal and hair keratins are highly conserved throughout evolution. Cysteines and histidines, which are infrequent keratin amino acids, are involved in de novo mutations that are markedly overrepresented in keratins. Hence, keratins have evolutionarily conserved and domain-selectively enriched amino acids including glycine and phenylalanine (epidermal), cysteine and proline (hair), and basic and acidic (simple-type epithelial), which reflect unique functions related to structural flexibility, rigidity and solubility, respectively. Our findings also support the importance of human keratin 'mutation hotspot' residues and their wild-type counterparts.
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Registered trials
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