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


10.1021/acs.jpcb.2c01254

http://scihub22266oqcxt.onion/10.1021/acs.jpcb.2c01254
suck pdf from google scholar
35580331!9186263!35580331
unlimited free pdf from europmc35580331    free
PDF from PMC    free
html from PMC    free

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

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

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
pmid35580331      J+Phys+Chem+B 2022 ; 126 (20): 3648-3658
Nephropedia Template TP

gab.com Text

Twit Text FOAVip

Twit Text #

English Wikipedia


  • Effect of an Amyloidogenic SARS-COV-2 Protein Fragment on alpha-Synuclein Monomers and Fibrils #MMPMID35580331
  • Jana AK; Lander CW; Chesney AD; Hansmann UHE
  • J Phys Chem B 2022[May]; 126 (20): 3648-3658 PMID35580331show ga
  • Aggregates of alpha-synuclein are thought to be the disease-causing agent in Parkinson's disease. Various case studies have hinted at a correlation between COVID-19 and the onset of Parkinson's disease. For this reason, we use molecular dynamics simulations to study whether amyloidogenic regions in SARS-COV-2 proteins can initiate and modulate aggregation of alpha-synuclein. As an example, we choose the nine-residue fragment SFYVYSRVK (SK9), located on the C-terminal of the envelope protein of SARS-COV-2. We probe how the presence of SK9 affects the conformational ensemble of alpha-synuclein monomers and the stability of two resolved fibril polymorphs. We find that the viral protein fragment SK9 may alter alpha-synuclein amyloid formation by shifting the ensemble toward aggregation-prone and preferentially rod-like fibril seeding conformations. However, SK9 has only a small effect on the stability of pre-existing or newly formed fibrils. A potential mechanism and key residues for potential virus-induced amyloid formation are described.
  • |*Amyloidogenic Proteins/chemistry/metabolism[MESH]
  • |*Coronavirus Envelope Proteins/chemistry/metabolism[MESH]
  • |*Parkinson Disease/metabolism[MESH]
  • |*Peptide Fragments/chemistry/metabolism[MESH]
  • |*alpha-Synuclein/chemistry/metabolism[MESH]
  • |COVID-19/virology[MESH]
  • |Humans[MESH]


  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    Linkout box