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Article

Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.

Biochemistry - 19 May 2009

Ohashi Tomoo, Augustus Anne Marie, Erickson Harold P

Abstract excerpt

We previously reported that the fibronectin (FN) type III domains of FN may unfold to interact with anastellin and form FN aggregates. In the present study, we have focused on the interaction between anastellin and the third FN type III domain (III3), which is a key anastellin binding site on FN. Anastellin binding to III3 was monitored by 8-anilino-1-naphthalene sulfonate (ANS) fluorescence. ANS binding to...

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Identifiers

PMID: 19320499
DOI: 10.1021/bi900001g
PMCID: PMC2680933

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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