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Molecular packing in the feather keratin filament

https://doi.org/10.1016/j.jsb.2008.01.011

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/dvdy.21202openalex-snapshot

β‐keratins of differentiating epidermis of snake comprise glycine‐proline‐serine‐rich proteins with an avian‐like gene organization

inferredcites →https://doi.org/10.1002/j.1460-2075.1984.tb01779.xopenalex-snapshot

A comparison of genomic coding sequences for feather and scale keratins: structural and evolutionary implications.

inferredcites →https://doi.org/10.1002/jez.b.17openalex-snapshot

Origin of archosaurian integumentary appendages: The bristles of the wild turkey beard express feather‐type β keratins

inferredcites →https://doi.org/10.1002/pro.5560021004openalex-snapshot

Identification, classification, and analysis of beta‐bulges in proteins

inferredcites →https://doi.org/10.1006/jmbi.1993.1047openalex-snapshot

Left-handed Polyproline II Helices Commonly Occur in Globular Proteins

inferredcites →https://doi.org/10.1016/0006-3002(47)90170-4openalex-snapshot

X-ray studies of the distribution of protein chain types in the vertebrate epidermis

inferredcites →https://doi.org/10.1016/0022-2836(68)90014-4openalex-snapshot

“Cross-β” conformation in proteins

inferredcites →https://doi.org/10.1016/0022-2836(73)90022-3openalex-snapshot

Conformation of twisted β-pleated sheets in proteins

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A simple method for displaying the hydropathic character of a protein

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Analysis and prediction of the different types of β-turn in proteins

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Conformation of β-hairpins in protein structures

inferredcites →https://doi.org/10.1016/0022-2836(91)90721-hopenalex-snapshot

Influence of proline residues on protein conformation

inferredcites →https://doi.org/10.1016/0032-3861(71)90011-5openalex-snapshot

The structure of feather keratin

inferredcites →https://doi.org/10.1016/0141-8130(91)90037-uopenalex-snapshot

Glycine loops in proteins: their occurence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins

inferredcites →https://doi.org/10.1016/0141-8130(96)01129-4openalex-snapshot

The molecular structure of reptilian keratin

inferredcites →https://doi.org/10.1016/0167-4838(86)90182-2openalex-snapshot

The primary structure of feather keratins from duck (Anas platyrhynchos) and pigeon (Columba livia)

inferredcites →https://doi.org/10.1016/s0006-3495(79)85259-5openalex-snapshot

Prediction of beta-turns

inferredcites →https://doi.org/10.1016/s0022-5320(77)80038-5openalex-snapshot

The structure of chicken scale keratin

inferredcites →https://doi.org/10.1016/s0065-3233(08)60520-3openalex-snapshot

The Anatomy and Taxonomy of Protein Structure

inferredcites →https://doi.org/10.1021/bi00699a001openalex-snapshot

Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins

inferredcites →https://doi.org/10.1021/pr060626+openalex-snapshot

The Epidermis of Scales in Gecko Lizards Contains Multiple Forms of β-Keratins Including Basic Glycine-Proline-Serine-Rich Proteins

inferredcites →https://doi.org/10.1021/pr0702619openalex-snapshot

Hard (Beta-)Keratins in the Epidermis of Reptiles: Composition, Sequence, and Molecular Organization

inferredcites →https://doi.org/10.1038/130309b0openalex-snapshot

X-Ray Interpretation of the Molecular Structure of Feather Keratin

inferredcites →https://doi.org/10.1038/316170a0openalex-snapshot

β-Hairpin families in globular proteins

inferredcites →https://doi.org/10.1042/bj2400289openalex-snapshot

Four classes of β-hairpins in proteins

inferredcites →https://doi.org/10.1071/bi9730415openalex-snapshot

The Complete Amino Acid Sequence of a Feather Keratin From Emu (Dromaius Novae-Hollandiae)

inferredcites →https://doi.org/10.1071/bi9740369openalex-snapshot

Amino Acid Sequence of a Feather Keratin From Silver Gull (Larus novae-hollandiae) and Comparison with One from Emu (Dromaius novae-hollandiae)

inferredcites →https://doi.org/10.1073/pnas.052706099openalex-snapshot

Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation

inferredcites →https://doi.org/10.1073/pnas.37.5.251openalex-snapshot

The Pleated Sheet, A New Layer Configuration of Polypeptide Chains

inferredcites →https://doi.org/10.1073/pnas.74.10.4130openalex-snapshot

Structure of proteins: packing of alpha-helices and pleated sheets.

inferredcites →https://doi.org/10.1083/jcb.13.1.1openalex-snapshot

AN ELECTRON MICROSCOPE STUDY OF THE FINE STRUCTURE OF FEATHER KERATIN

inferredcites →https://doi.org/10.1093/bioinformatics/16.4.404openalex-snapshot

The PSIPRED protein structure prediction server

inferredcites →https://doi.org/10.1111/j.1432-1033.1976.tb10660.xopenalex-snapshot

The Keratin Chains of Avian Scale Tissue

inferredcites →https://doi.org/10.1111/j.1432-1033.1976.tb10918.xopenalex-snapshot

The Structural Basis for the Heterogeneity of Chick Down Feather Keratin

inferredcites →https://doi.org/10.1111/j.1749-6632.1951.tb31964.xopenalex-snapshot

THE RESULTS OF X‐RAY DIFFRACTION STUDIES ON KERATIN FIBERS

inferredcites →https://doi.org/10.1146/annurev.bi.47.070178.001343openalex-snapshot

Empirical Predictions of Protein Conformation

inferredcites →https://doi.org/10.5860/choice.43-1577openalex-snapshot

Proteins: structure and function

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Tensile deformation and failure of North American porcupine quills

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Robert Donald Bruce Fraser 1924–2019

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Feather keratin gene polymorphism (F-KER) in domestic pigeons

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Investigation on the mechanical genes of “rigidity-flexibility balance” composite materials similar to feather shaft by SR-CT in-situ experiments

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β-Sheet alignment in intact feathers revealed by polarization-resolved second harmonic generation (SHG) and coherent Raman imaging

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Genetic and Molecular Basis of Feather Diversity in Birds

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The feather’s multi-functional structure across nano to macro scales inspires hierarchical design

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Microscopic and immunohistochemical analyses of the claw of the nesting dinosaur, Citipati osmolskae

inferred← citeshttps://doi.org/10.1099/jmm.0.000982openalex-snapshot

Host- and pathogen-dependent susceptibility and predisposition to dermatophytosis

inferred← citeshttps://doi.org/10.1101/2024.09.08.611866openalex-snapshot

Feather keratin in Pavo cristatus : A tentative structure

inferred← citeshttps://doi.org/10.1111/asj.12093openalex-snapshot

Properties of alkaline‐hydrolyzed waterfowl feather keratin

inferred← citeshttps://doi.org/10.1111/j.1469-7580.2008.01030.xopenalex-snapshot

Beta‐keratins of turtle shell are glycine‐proline‐tyrosine rich proteins similar to those of crocodilians and birds

inferred← citeshttps://doi.org/10.1111/j.1469-7580.2009.01045.xopenalex-snapshot

Evolution of hard proteins in the sauropsid integument in relation to the cornification of skin derivatives in amniotes

inferred← citeshttps://doi.org/10.1111/j.1469-7580.2009.01066.xopenalex-snapshot

Structure and functions of keratin proteins in simple, stratified, keratinized and cornified epithelia

inferred← citeshttps://doi.org/10.1111/j.1469-7580.2009.01192.xopenalex-snapshot

Isolation of a new class of cysteine–glycine–proline‐rich beta‐proteins (beta‐keratins) and their expression in snake epidermis

inferred← citeshttps://doi.org/10.1111/myc.12876openalex-snapshot

The host range of dermatophytes, it is at all possible? Phenotypic evaluation of the keratinolytic activity of Trichophyton verrucosum clinical isolates

inferred← citeshttps://doi.org/10.11606/d.9.2013.tde-11092013-150522openalex-snapshot

Extração, caracterização e modificação química da queratina extraída das penas de frango

inferred← citeshttps://doi.org/10.1177/17581559211072656openalex-snapshot

Keratinolytic bacteria from the feathers of wild Dark-eyed Juncos ( Junco hyemalis )

inferred← citeshttps://doi.org/10.1186/1471-2148-10-148openalex-snapshot

Genomic organization and molecular phylogenies of the beta (β) keratin multigene family in the chicken (Gallus gallus) and zebra finch (Taeniopygia guttata): implications for feather evolution

inferred← citeshttps://doi.org/10.1186/gb-2013-14-3-r28openalex-snapshot

The western painted turtle genome, a model for the evolution of extreme physiological adaptations in a slowly evolving lineage

inferred← citeshttps://doi.org/10.1201/9781315373713-6openalex-snapshot

Films and Coatings from Animal Protein

inferred← citeshttps://doi.org/10.12688/f1000research.157679.1openalex-snapshot

Feather keratin in Pavo cristatus: A tentative structure

inferred← citeshttps://doi.org/10.1371/journal.pone.0065849openalex-snapshot

A New Helical Crossed-Fibre Structure of β-Keratin in Flight Feathers and Its Biomechanical Implications

inferred← citeshttps://doi.org/10.1371/journal.pone.0157699openalex-snapshot

Keratin Durability Has Implications for the Fossil Record: Results from a 10 Year Feather Degradation Experiment

inferred← citeshttps://doi.org/10.1371/journal.pone.0167789openalex-snapshot

Immunolocalization of a Histidine-Rich Epidermal Differentiation Protein in the Chicken Supports the Hypothesis of an Evolutionary Developmental Link between the Embryonic Subperiderm and Feather Barbs and Barbules

inferred← citeshttps://doi.org/10.1371/journal.pone.0202608openalex-snapshot

Understanding the dynamics of keratin weakening and hydrolysis by proteases

inferred← citeshttps://doi.org/10.1371/journal.pone.0206569openalex-snapshot

Preservation potential of keratin in deep time

inferred← citeshttps://doi.org/10.1371/journal.pone.0312679openalex-snapshot

High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis

inferred← citeshttps://doi.org/10.1515/biolog-2015-0031openalex-snapshot

Prokaryotic expression and characterization of a keratinolytic protease from Aspergillus niger

inferred← citeshttps://doi.org/10.1520/jte20190475openalex-snapshot

Study on the Interlocking Mechanism of Barbules of an Eagle Feather and the Corresponding Microstructures to Reconstitute Their Integrity

inferred← citeshttps://doi.org/10.1557/mrc.2013.2openalex-snapshot

An ancient method-inspired route for fast fabrication of ‘PbS bird feathers’

inferred← citeshttps://doi.org/10.3109/07388551.2013.794768openalex-snapshot

A current assessment on the production of bacterial keratinases

inferred← citeshttps://doi.org/10.32604/cmes.2021.015426openalex-snapshot

Micro Hierarchical Structure and Mechanical Property of Sparrow Hawk (Accipiter nisus) Feather Shaf

inferred← citeshttps://doi.org/10.32604/jrm.2024.056251openalex-snapshot

Synthesis and Properties of Biomimetic Self-Assembling Structures from Poultry Feather Keratin

inferred← citeshttps://doi.org/10.32634/0869-8155-2021-344-1-30-38openalex-snapshot

Proteases in the diet of monogastric animals

inferred← citeshttps://doi.org/10.32657/10356/146707openalex-snapshot

Understanding the biochemical properties of human hair keratins : self-assembly potential and cell response

inferred← citeshttps://doi.org/10.3389/fbioe.2020.00071openalex-snapshot

Fusarium oxysporum and Aspergillus sp. as Keratinase Producers Using Swine Hair From Agroindustrial Residues

inferred← citeshttps://doi.org/10.3389/fmicb.2021.674345openalex-snapshot

Structure, Application, and Biochemistry of Microbial Keratinases

inferred← citeshttps://doi.org/10.3389/fmicb.2022.918262openalex-snapshot

Perspectives on Converting Keratin-Containing Wastes Into Biofertilizers for Sustainable Agriculture

inferred← citeshttps://doi.org/10.3390/ani15030457openalex-snapshot

Skin Appendage Proteins of Tetrapods: Building Blocks of Claws, Feathers, Hair and Other Cornified Epithelial Structures

inferred← citeshttps://doi.org/10.3390/app112412163openalex-snapshot

From Feather to Adsorbent: Keratin Extraction, Chemical Modification, and Fe(III) Removal from Aqueous Solution

inferred← citeshttps://doi.org/10.3390/biology11050670openalex-snapshot

Chemistry and Analysis of Organic Compounds in Dinosaurs

inferred← citeshttps://doi.org/10.3390/genes12040591openalex-snapshot

Structures of the ß-Keratin Filaments and Keratin Intermediate Filaments in the Epidermal Appendages of Birds and Reptiles (Sauropsids)

inferred← citeshttps://doi.org/10.3390/ijms26094149openalex-snapshot

Antioxidant Peptide Production Using Keratin from Feather Waste: Effect of Extraction and Thiol Blocking Method

inferred← citeshttps://doi.org/10.3390/polym12010032openalex-snapshot

Keratin Associations with Synthetic, Biosynthetic and Natural Polymers: An Extensive Review

inferred← citeshttps://doi.org/10.3390/polym14020309openalex-snapshot

Anisotropic Composition and Mechanical Behavior of a Natural Thin-Walled Composite: Eagle Feather Shaft

inferred← citeshttps://doi.org/10.3390/polym14081601openalex-snapshot

Sustainable Applications of Animal Waste Proteins

inferred← citeshttps://doi.org/10.3390/polym15183701openalex-snapshot

Enhanced Biodegradability in Soil of Chicken Feather by Steam Explosion for Potential Application in Agricultural Biodegradable Plastics

inferred← citeshttps://doi.org/10.3390/su18189402openalex-snapshot

From Poultry Feather Waste to Keratin-Based Biomaterials: Advancing Circular Bioeconomy Through Sustainable By-Product Valorization

inferred← citeshttps://doi.org/10.36107/hfb.2025.i4.s275openalex-snapshot

The Use of Keratin Hydrolysate Obtained by Microbial Conversion of Chicken Feathers as Part of a Cosmetic Serum for Hair Care

inferred← citeshttps://doi.org/10.4028/www.scientific.net/amm.364.737openalex-snapshot

Two-Step Fabrication of Nano-PbS on Peacock Feathers Inspired by a Hair-Dyeing Method Used in Ancient Egypt

inferred← citeshttps://doi.org/10.4061/2011/487093openalex-snapshot

Production of Proteolytic Enzymes by a Keratin-Degrading Aspergillus niger

inferred← citeshttps://doi.org/10.4172/1948-5948.1000282openalex-snapshot

How Microbes helped solve a Complex Biomechanical Problem associated with Bird Flight

inferred← citeshttps://doi.org/10.5204/thesis.eprints.239502openalex-snapshot

Understanding enzyme-mediated keratin hydrolysis and evaluation of new keratin binding peptides

inferred← citeshttps://doi.org/10.5812/jjm.8896openalex-snapshot

Biodegradation of Hard Keratins by Two Bacillus Strains

inferred← citeshttps://doi.org/10.5821/dissertation-2117-95771openalex-snapshot

Valorización de residuos queratínicos para la obtención de materiales biocompuestos

inferred← citeshttps://doi.org/10.7287/peerj.12919v0.1/reviews/1openalex-snapshot

Peer Review #1 of "Analysis and comparison of protein secondary structures in the rachis of avian flight feathers (v0.1)"

inferred← citeshttps://doi.org/10.7287/peerj.12919v0.1/reviews/2openalex-snapshot

Peer Review #2 of "Analysis and comparison of protein secondary structures in the rachis of avian flight feathers (v0.1)"

inferred← citeshttps://doi.org/10.7287/peerj.12919v0.1/reviews/3openalex-snapshot

Peer Review #3 of "Analysis and comparison of protein secondary structures in the rachis of avian flight feathers (v0.1)"

inferred← citeshttps://doi.org/10.7287/peerj.12919v0.2/reviews/1openalex-snapshot

Peer Review #1 of "Analysis and comparison of protein secondary structures in the rachis of avian flight feathers (v0.2)"

inferred← citeshttps://doi.org/10.7287/peerj.12919v0.2/reviews/2openalex-snapshot

Peer Review #2 of "Analysis and comparison of protein secondary structures in the rachis of avian flight feathers (v0.2)"

inferred← citeshttps://doi.org/10.7717/peerj.12919openalex-snapshot

Analysis and comparison of protein secondary structures in the rachis of avian flight feathers

inferred← citeshttps://doi.org/10.7939/r39w09c65openalex-snapshot

Fabrication of feather keratin bio-based materials: Thermoplastics and tissue engineered scaffolds

Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.