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


10.1073/pnas.2112703118

http://scihub22266oqcxt.onion/10.1073/pnas.2112703118
suck pdf from google scholar
34782481!8640741!34782481
unlimited free pdf from europmc34782481    free
PDF from PMC    free
html from PMC    free

suck abstract from ncbi


Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
pmid34782481      Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (48): ä
Nephropedia Template TP

gab.com Text

Twit Text FOAVip

Twit Text #

English Wikipedia


  • Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein #MMPMID34782481
  • Tai L; Zhu G; Yang M; Cao L; Xing X; Yin G; Chan C; Qin C; Rao Z; Wang X; Sun F; Zhu Y
  • Proc Natl Acad Sci U S A 2021[Nov]; 118 (48): ä PMID34782481show ga
  • The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in beta-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.
  • |Amino Acid Motifs[MESH]
  • |Animals[MESH]
  • |Chlorocebus aethiops[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Electron Microscope Tomography[MESH]
  • |Glycosylation[MESH]
  • |Protein Domains[MESH]
  • |Protein Multimerization[MESH]
  • |SARS-CoV-2/*ultrastructure[MESH]
  • |Spike Glycoprotein, Coronavirus/*chemistry/metabolism[MESH]


  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    Linkout box