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


10.1016/j.celrep.2021.109892

http://scihub22266oqcxt.onion/10.1016/j.celrep.2021.109892
suck pdf from google scholar
34672947!8501228!34672947
unlimited free pdf from europmc34672947    free
PDF from PMC    free
html from PMC    free
PDF vom PMID34672947 :   free

suck abstract from ncbi

pmid34672947
Nephropedia Template TP

gab.com Text

Twit Text FOAVip

Twit Text #

English Wikipedia


  • Mechanistic insights into COVID-19 by global analysis of the SARS-CoV-2 3CL(pro) substrate degradome #MMPMID34672947
  • Pablos I; Machado Y; de Jesus HCR; Mohamud Y; Kappelhoff R; Lindskog C; Vlok M; Bell PA; Butler GS; Grin PM; Cao QT; Nguyen JP; Solis N; Abbina S; Rut W; Vederas JC; Szekely L; Szakos A; Drag M; Kizhakkedathu JN; Mossman K; Hirota JA; Jan E; Luo H; Banerjee A; Overall CM
  • Cell Rep 2021[Oct]; 37 (4): 109892 PMID34672947show ga
  • The main viral protease (3CL(pro)) is indispensable for SARS-CoV-2 replication. We delineate the human protein substrate landscape of 3CL(pro) by TAILS substrate-targeted N-terminomics. We identify more than 100 substrates in human lung and kidney cells supported by analyses of SARS-CoV-2-infected cells. Enzyme kinetics and molecular docking simulations of 3CL(pro) engaging substrates reveal how noncanonical cleavage sites, which diverge from SARS-CoV, guide substrate specificity. Cleaving the interactors of essential effector proteins, effectively stranding them from their binding partners, amplifies the consequences of proteolysis. We show that 3CL(pro) targets the Hippo pathway, including inactivation of MAP4K5, and key effectors of transcription, mRNA processing, and translation. We demonstrate that Spike glycoprotein directly binds galectin-8, with galectin-8 cleavage disengaging CALCOCO2/NDP52 to decouple antiviral-autophagy. Indeed, in post-mortem COVID-19 lung samples, NDP52 rarely colocalizes with galectin-8, unlike in healthy lungs. The 3CL(pro) substrate degradome establishes a foundational substrate atlas to accelerate exploration of SARS-CoV-2 pathology and drug design.
  • |*COVID-19[MESH]
  • |Coronavirus 3C Proteases/*metabolism[MESH]
  • |Humans[MESH]
  • |SARS-CoV-2/*metabolism[MESH]
  • |Substrate Specificity[MESH]


  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    109892 4.37 2021