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1 t is controlled by a delicate apparatus, the byssus.
2 we their tenacity to a holdfast known as the byssus, a fibrous extracellular structure that ends dist
3 empt to better understand the zebra mussel's byssus activity, a cDNA microarray (ZMB) including 716 g
6 apfp-1 is an interfacial linker between the byssus and soft tissue, that is, the DOPA-containing dom
7 was localized at the interface between stiff byssus and the soft tissue by immunochemical staining an
9 findings demonstrated that the zebra mussel byssus cDNA microarray is an efficient tool for the stud
11 oxyphenyl-L-alanine) (diDOPA) cross-links in byssus has raised questions about the relationship of th
13 bers and foamlike adhesive plaques in mussel byssus is robust despite the strikingly dissimilar conne
17 arkable ability to attach their holdfast, or byssus, opportunistically to a variety of substrata that
18 alanine (Dopa)-containing proteins of mussel byssus play a critical role in wet adhesion and have ins
19 Recent experiments on permeabilized anterior byssus retractor muscle (ABRM) of Mytilus edulis have sh
21 periments on thick filaments of the anterior byssus retractor muscle of Mytilus and the telson-levato
23 f isolated thick filaments from the anterior byssus retractor muscle of the blue mussel Mytilus eduli
27 ed by proteins during maturation of a mussel byssus secretion, we have developed a simple method to c
28 l forces far exceed the measured strength of byssus threads and their attachment to the environment.
29 t the heterogeneous material distribution in byssus threads has a critical role in decreasing the eff
33 protein family known as fp-1 provides mussel byssus with a protective outer coating and has drawn muc
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