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.

suck abstract from ncbi


10.1039/c4cp05883f

http://scihub22266oqcxt.onion/10.1039/c4cp05883f
suck pdf from google scholar
C4464955!4464955 !25665896
unlimited free pdf from europmc25665896
    free
PDF from PMC    free
html from PMC    free

Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25665896 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215

suck abstract from ncbi


Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25665896 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117
pmid25665896
      Phys+Chem+Chem+Phys 2015 ; 17 (24 ): 15561-8
Nephropedia Template TP

gab.com Text

Twit Text FOAVip

Twit Text #

English Wikipedia


  • Biophysics of ?-synuclein induced membrane remodelling #MMPMID25665896
  • Shi Z ; Sachs JN ; Rhoades E ; Baumgart T
  • Phys Chem Chem Phys 2015[Jun]; 17 (24 ): 15561-8 PMID25665896 show ga
  • ?-Synuclein is an intrinsically disordered protein whose aggregation is a hallmark of Parkinson's disease. In neurons, ?-synuclein is thought to play important roles in mediating both endo- and exocytosis of synaptic vesicles through interactions with either the lipid bilayer or other proteins. Upon membrane binding, the N-terminus of ?-synuclein forms a helical structure and inserts into the hydrophobic region of the outer membrane leaflet. However, membrane structural changes induced by ?-synuclein are still largely unclear. Here we report a substantial membrane area expansion induced by the binding of ?-synuclein monomers. This measurement is accomplished by observing the increase of membrane area during the binding of ?-synuclein to pipette-aspirated giant vesicles. The extent of membrane area expansion correlates linearly with the density of ?-synuclein on the membrane, revealing a constant area increase induced by the binding per ?-synuclein molecule. The area expansion per synuclein is found to exhibit a strong dependence on lipid composition, but is independent of membrane tension and vesicle size. Fragmentation or tubulation of the membrane follows the membrane expansion process. However, contrary to BAR domain proteins, no distinct tubulation-transition density can apparently be identified for ?-synuclein, suggesting a more complex membrane curvature generation mechanism. Consideration of ?-synuclein's membrane binding free energy and biophysical properties of the lipid bilayer leads us to conclude that membrane expansion by ?-synuclein results in thinning of the bilayer. These membrane thinning and tubulation effects may underlie ?-synuclein's role in mediating cell trafficking processes such as endo- and exocytosis.
  • |Biophysical Phenomena [MESH]
  • |Lipid Bilayers/chemistry/*metabolism [MESH]


  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    Linkout box