Browsing by Author "Ohashi, Tomoo"
Now showing items 1-8 of 8
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Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.
(The Journal of biological chemistry, 2011-11)The mechanism of fibronectin (FN) assembly and the self-association sites are still unclear and contradictory, although the N-terminal 70-kDa region ((I)1-9) is commonly accepted as one of the assembly sites. We previously ... -
Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants.
(Biochemistry, 2017-08-11)To study fibronectin (FN) conformation and assembly, we generated several deletion mutants: FNΔ(I)1-5, FNΔ(III)1-3, FNΔ(III)4-8, and FNΔ(III)11-14. A monomeric form, FNmono, which lacked the C-terminal dimerization region, ... -
High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.
(Acta crystallographica. Section F, Structural biology communications, 2020-02-05)Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial ... -
How the kinetochore couples microtubule force and centromere stretch to move chromosomes.
(Nature cell biology, 2016-04)The Ndc80 complex (Ndc80, Nuf2, Spc24 and Spc25) is a highly conserved kinetochore protein essential for end-on anchorage to spindle microtubule plus ends and for force generation coupled to plus-end polymerization ... -
Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
(The Journal of biological chemistry, 2011-07)Fibronectin (FN) is an extracellular matrix protein that is assembled into fibrils by cells during tissue morphogenesis and wound healing. FN matrix fibrils are highly elastic, but the mechanism of elasticity has been debated: ... -
Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.
(J Biol Chem, 2017-01-20)Globular proteins are not permanently folded but spontaneously unfold and refold on time scales that can span orders of magnitude for different proteins. A longstanding debate in the protein-folding field is whether unfolding ... -
Tenascin-C is an innate broad-spectrum, HIV-1-neutralizing protein in breast milk.
(Proceedings of the National Academy of Sciences of the United States of America, 2013-11)Achieving an AIDS-free generation will require elimination of postnatal transmission of HIV-1 while maintaining the nutritional and immunologic benefits of breastfeeding for infants in developing regions. Maternal/infant ... -
The structure of irisin reveals a novel intersubunit β-sheet fibronectin type III (FNIII) dimer: implications for receptor activation.
(The Journal of biological chemistry, 2013-11)Irisin was recently identified as a putative myokine that is induced by exercise. Studies suggest that it is produced by cleavage of the FNDC5 (fibronectin domain-containing protein 5) receptor; irisin corresponds to the ...
