Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.bpj.2014.11.006 http://scihub22266oqcxt.onion/10.1016/j.bpj.2014.11.006 C4269765!4269765!25517163     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2014 ; 107 (12): 2982-92 Nephropedia Template TP {{tp|p=25517163|t=2014. Exploring the Stability Limits of Actin and Its Suprastructures |pdf=|usr=}}{{25517163}} gab.com Text Exploring the Stability Limits of Actin and Its Suprastructures JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25517163 #FOAvip Actin is the main component of the microfilament system in eukaryotic cells and can be found in distinct morphological states. Global (G)-actin is able to assemble into highly organized, supramolecular cellular structures known as filamentous (F)-actin and bundled (B)-actin. To evaluate the structure and stability of G-, F-, and B-actin over a wide range of temperatures and pressures, we used Fourier transform infrared spectroscopy in combination with differential scanning and pressure perturbation calorimetry, small-angle x-ray scattering, laser confocal scanning microscopy, and transmission electron microscopy. Our analysis was designed to provide new (to our knowledge) insights into the stabilizing forces of actin self-assembly and to reveal the stability of the actin polymorphs, including in conditions encountered in extreme environments. In addition, we sought to explain the limited pressure stability of actin self-assembly observed in vivo. G-actin is not only the least temperature-stable but also the least pressure-stable actin species. Under abyssal conditions, where temperatures as low as 1?4°C and pressures up to 1 kbar are reached, G-actin is hardly stable. However, the supramolecular assemblies of actin are stable enough to withstand the extreme conditions usually encountered on Earth. Beyond ?3?4 kbar, filamentous structures disassemble, and beyond ?4 kbar, complete dissociation of F-actin structures is observed. Between ?1 and 2 kbar, some disordering of actin assemblies commences, in agreement with in vivo observations. The limited pressure stability of the monomeric building block seems to be responsible for the suppression of actin assembly in the kbar pressure range. Twit Text FOAVip Exploring the Stability Limits of Actin and Its Suprastructures ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25517163 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25517163 #FOAvip English Wikipedia <ref>{{Cite pmid|25517163}}</ref> Exploring the Stability Limits of Actin and Its Suprastructures #MMPMID25517163 Rosin C; Erlkamp M; Ecken J; Raunser S; Winter R Biophys J 2014[Dec]; 107 (12): 2982-92 PMID25517163show ga Actin is the main component of the microfilament system in eukaryotic cells and can be found in distinct morphological states. Global (G)-actin is able to assemble into highly organized, supramolecular cellular structures known as filamentous (F)-actin and bundled (B)-actin. To evaluate the structure and stability of G-, F-, and B-actin over a wide range of temperatures and pressures, we used Fourier transform infrared spectroscopy in combination with differential scanning and pressure perturbation calorimetry, small-angle x-ray scattering, laser confocal scanning microscopy, and transmission electron microscopy. Our analysis was designed to provide new (to our knowledge) insights into the stabilizing forces of actin self-assembly and to reveal the stability of the actin polymorphs, including in conditions encountered in extreme environments. In addition, we sought to explain the limited pressure stability of actin self-assembly observed in vivo. G-actin is not only the least temperature-stable but also the least pressure-stable actin species. Under abyssal conditions, where temperatures as low as 1?4°C and pressures up to 1 kbar are reached, G-actin is hardly stable. However, the supramolecular assemblies of actin are stable enough to withstand the extreme conditions usually encountered on Earth. Beyond ?3?4 kbar, filamentous structures disassemble, and beyond ?4 kbar, complete dissociation of F-actin structures is observed. Between ?1 and 2 kbar, some disordering of actin assemblies commences, in agreement with in vivo observations. The limited pressure stability of the monomeric building block seems to be responsible for the suppression of actin assembly in the kbar pressure range. äExploring the Stability Limits of Actin and Its Suprastructures (epmc).pdf DeepDyve Pubget Overpricing