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


10.1002/prot.26205

http://scihub22266oqcxt.onion/10.1002/prot.26205
suck pdf from google scholar
34369011!8441931!34369011
unlimited free pdf from europmc34369011    free
PDF from PMC    free
html from PMC    free

suck abstract from ncbi


Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
pmid34369011      Proteins 2022 ; 90 (1): 176-185
Nephropedia Template TP

gab.com Text

Twit Text FOAVip

Twit Text #

English Wikipedia


  • A distinct ssDNA/RNA binding interface in the Nsp9 protein from SARS-CoV-2 #MMPMID34369011
  • El-Kamand S; Du Plessis MD; Breen N; Johnson L; Beard S; Kwan AH; Richard DJ; Cubeddu L; Gamsjaeger R
  • Proteins 2022[Jan]; 90 (1): 176-185 PMID34369011show ga
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel, highly infectious RNA virus that belongs to the coronavirus family. Replication of the viral genome is a fundamental step in the virus life cycle and SARS-CoV-2 non-structural protein 9 (Nsp9) is shown to be essential for virus replication through its ability to bind RNA in the closely related SARS-CoV-1 strain. Two recent studies revealing the three-dimensional structure of Nsp9 from SARS-CoV-2 have demonstrated a high degree of similarity between Nsp9 proteins within the coronavirus family. However, the binding affinity to RNA is very low which, until now, has prevented the determination of the structural details of this interaction. In this study, we have utilized nuclear magnetic resonance spectroscopy (NMR) in combination with surface biolayer interferometry (BLI) to reveal a distinct binding interface for both ssDNA and RNA that is different to the one proposed in the recently solved SARS-CoV-2 replication and transcription complex (RTC) structure. Based on these data, we have proposed a structural model of a Nsp9-RNA complex, shedding light on the molecular details of these important interactions.
  • |Binding Sites[MESH]
  • |DNA, Single-Stranded/*metabolism[MESH]
  • |Interferometry[MESH]
  • |Magnetic Resonance Spectroscopy[MESH]
  • |Models, Molecular[MESH]
  • |Protein Conformation[MESH]
  • |Protein Multimerization[MESH]
  • |RNA[MESH]
  • |RNA-Binding Proteins/*chemistry/*metabolism[MESH]
  • |Solutions[MESH]


  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    Linkout box