Structure and topology of the linkers in the conserved lepidosaur β-keratin chain with four 34-residue repeats support an interfilament role for the central linker
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Published:2020-10
Issue:1
Volume:212
Page:107599
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ISSN:1047-8477
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Container-title:Journal of Structural Biology
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language:en
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Short-container-title:Journal of Structural Biology
Subject
Structural Biology
Reference34 articles.
1. Self-tensioning aquatic caddisfly silk: Ca2+-dependent structure, strength, and liquid cycle hysteresis;Ashton;Biomacromology,2013
2. The results of X-ray diffraction studies on keratin fibers;Bear;Ann. N.Y. Acad. Sci.,1951
3. Spidroins from the Brazilian spider Nephilengys cruentata (Aranae: Nephilidae);Bittencourt;Comp. Biochem. Physiol. Part B,2007
4. The molecular organization of the beta-sheet region in corneous beta-proteins (beta-keratins) of sauropsids explains it stability and polymerization into filaments;Calvaresi;J. Struct. Biol.,2016
5. Forty keratin-associated β-proteins (β-proteins) form the hard layers of scales, claws, adhesive pads in the green anole lizard, Anolis carolinensis;Dalla Valle;J. Exp. Zool.,2010
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