• Refine your search:
  • 
    Keyword
  • 
    Creator / Publisher:
    
    • Alexander-Katz, Alfredo (3)
    • Fallah, Mohammad A. (3)
    • Huck, Volker (3)
    • Mess, Christian (3)
    • Obser, Tobias (3)
    • Schneider, Matthias F. (3)
    • Schneider, Stefan W. (3)
    • Schneppenheim, Reinhard (3)
    • Massachusetts Institute of Technology. Department of Materials Science and Engineering (1)
  • 
    Year:
    
    • 2020 (3)
  • 
    Medium
  • 
    Type
  • 
    BLLDB-Access

Search in the Catalogues and Directories

All fields Title Creator / Publisher Keyword Year AND OR AND NOT All fields Title Creator / Publisher Keyword Year AND OR AND NOT All fields Title Creator / Publisher Keyword Year AND OR AND NOT All fields Title Creator / Publisher Keyword Year AND OR AND NOT All fields Title Creator / Publisher Keyword Year Sort by creator [A → Z]' creator [Z → A]' publishing year ↑ (asc)' publishing year ↓ (desc)' title [A → Z]' title [Z → A]' Simple Search Hits 1 – 3 of 3 1 Platelet adhesion and aggregate formation controlled by immobilised and soluble VWF Schneider, Matthias F.; Fallah, Mohammad A.; Mess, Christian; Obser, Tobias; Schneppenheim, Reinhard; Alexander-Katz, Alfredo; Schneider, Stefan W.; Huck, Volker In: BioMed Central (2020) Abstract: Background It has been demonstrated that von Willebrand factor (VWF) mediated platelet-endothelium and platelet-platelet interactions are shear dependent. The VWF’s mobility under dynamic conditions (e.g. flow) is pivotal to platelet adhesion and VWF-mediated aggregate formation in the cascade of VWF-platelet interactions in haemostasis. Results Combining microfluidic tools with fluorescence and reflection interference contrast microscopy (RICM), here we show, that specific deletions in the A-domains of the biopolymer VWF affect both, adhesion and aggregation properties independently. Intuitively, the deletion of the A1-domain led to a significant decrease in both adhesion and aggregate formation of platelets. Nevertheless, the deletion of the A2-domain revealed a completely different picture, with a significant increase in formation of rolling aggregates (gain of function). We predict that the A2-domain effectively ‘masks’ the potential between the platelet glycoprotein (GP) Ib and the VWF A1-domain. Furthermore, the deletion of the A3-domain led to no significant variation in either of the two functional characteristics. Conclusions These data demonstrate that the macroscopic functional properties i.e. adhesion and aggregate formation cannot simply be assigned to the properties of one particular domain, but have to be explained by cooperative phenomena. The absence or presence of molecular entities likewise affects the properties (thermodynamic phenomenology) of its neighbours, therefore altering the macromolecular function. URL: https://hdl.handle.net/1721.1/127675 BASE Hide details 2 Platelet adhesion and aggregate formation controlled by immobilised and soluble VWF Schneider, Matthias F.; Fallah, Mohammad A.; Mess, Christian... In: BMC Molecular and Cell Biology ; 21 (2020). - 64. - BioMed Central. - eISSN 2661-8850 (2020) BASE Show details 3 Platelet adhesion and aggregate formation controlled by immobilised and soluble VWF Schneider, Matthias F.; Fallah, Mohammad A.; Mess, Christian... In: BMC Mol Cell Biol (2020) BASE Show details

Mobile view All Catalogues UB Frankfurt Linguistik 0 IDS Mannheim 0 OLC Linguistik 0 UB Frankfurt Retrokatalog 0 DNB Subject Category Language 0 Institut für Empirische Sprachwissenschaft 0 Leibniz-Centre General Linguistics (ZAS) 0 Bibliographies BLLDB 0 BDSL 0 IDS Bibliografie zur deutschen Grammatik 0 IDS Bibliografie zur Gesprächsforschung 0 IDS Konnektoren im Deutschen 0 IDS Präpositionen im Deutschen 0 IDS OBELEX meta 0 MPI-SHH Linguistics Collection 0 MPI for Psycholinguistics 0 Linked Open Data catalogues Annohub 0 Online resources Link directory 0 Journal directory 0 Database directory 0 Dictionary directory 0 Open access documents BASE 3 Linguistik-Repository 0 IDS Publikationsserver 0 Online dissertations 0 Language Description Heritage 0