0000000001293485
AUTHOR
Outi Heikkinen
Fitnessurheilijoiden blogit : body fitness kulttuurisena ilmiönä
Tutkimuksessa tarkastellaan body fitness-lajia kulttuurisena ilmiönä fitnessurheilijoiden blogeja aineistona käyttäen. Tavoitteena on luoda kuvaus siitä, mitä tekijöitä lajin alakulttuuriin kuuluu. Lisäksi tavoitteena on selvittää, mihin fitnessblogia käytetään osana lajin harjoittamista. Tutkimusaineisto koostuu kolmen body fitness -lajissa kilpailevan naisen kirjoittamista blogiteksteistä. Ajanjakso, jolta aineisto on kerätty, on lähes vuoden mittainen. Se alkaa jokaisen bloggaajan osalta kilpailupäätöksen julkistamisajankohdasta ja päättyy kuukausi käytyjen kilpailujen jälkeen. Tutkimus on laadullinen tapaustutkimus. Tutkimuksen tieteenfilosofiset lähtökohdat pohjautuvat hermeneutiikkaan…
Molecular basis of filamin a-filGAP interaction and its impairment in congenital disorders associated with filamin a mutations
Background Mutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans. Methodology/Principal Findings We determined the structure of the 23rd Ig repeat of FLNa (IgFLNa23) that interacts with FilGAP, a Rac-specific GTPase-activating protein and regulator of cell polarity and movement, and the effect of the three disease-related mutations on this interaction. A combination of NMR structural analysis and in silico modeling revealed the structural interface details between the C and D β-strands of the IgFLNa23 and the C-terminal 32 residues of FilGAP. Mutagenesis of the predicted key interface residues confirmed the b…
Atomic Structures of Two Novel Immunoglobulin-like Domain Pairs in the Actin Cross-linking Protein Filamin
Filamins are actin filament cross-linking proteins composed of an N-terminal actin-binding domain and 24 immunoglobulin-like domains (IgFLNs). Filamins interact with numerous proteins, including the cytoplasmic domains of plasma membrane signaling and cell adhesion receptors. Thereby filamins mechanically and functionally link the cell membrane to the cytoskeleton. Most of the interactions have been mapped to the C-terminal IgFLNs 16–24. Similarly, as with the previously known compact domain pair of IgFLNa20–21, the two-domain fragments IgFLNa16–17 and IgFLNa18–19 were more compact in small angle x-ray scattering analysis than would be expected for two independent domains. Solution state NM…
Molecular Basis of Filamin A-FilGAP Interaction and Its Impairment in Congenital Disorders Associated with Filamin A Mutations
Background: Mutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans. Methodology/Principal Findings: We determined the structure of the 23rd Ig repeat of FLNa (IgFLNa23) that interacts with FilGAP, a Rac-specific GTPase-activating protein and regulator of cell polarity and movement, and the effect of the three disease-related mutations on this interaction. A combination of NMR structural analysis and in silico modeling revealed the structural interface details between the C and D b-strands of the IgFLNa23 and the C-terminal 32 residues of FilGAP. Mutagenesis of the predicted key interface residues confirmed the…