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10.1016/j.cell.2020.09.033 http://scihub22266oqcxt.onion/10.1016/j.cell.2020.09.033 32970989!7489987!32970989     free     free     free 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       Cell 2020 ; 183 (4): 1043-1057.e15 Nephropedia Template TP {{tp|p=32970989|t=2020. SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 |pdf=|usr=}}{{32970989}} gab.com Text SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=32970989 #FOAvip We show that SARS-CoV-2 spike protein interacts with both cellular heparan sulfate and angiotensin-converting enzyme 2 (ACE2) through its receptor-binding domain (RBD). Docking studies suggest a heparin/heparan sulfate-binding site adjacent to the ACE2-binding site. Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold. Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2. On cells, spike protein binding depends on both heparan sulfate and ACE2. Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. We suggest a model in which viral attachment and infection involves heparan sulfate-dependent enhancement of binding to ACE2. Manipulation of heparan sulfate or inhibition of viral adhesion by exogenous heparin presents new therapeutic opportunities. Twit Text FOAVip SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=32970989 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32970989 #FOAvip English Wikipedia <ref>{{Cite pmid|32970989}}</ref> SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 #MMPMID32970989 Clausen TM; Sandoval DR; Spliid CB; Pihl J; Perrett HR; Painter CD; Narayanan A; Majowicz SA; Kwong EM; McVicar RN; Thacker BE; Glass CA; Yang Z; Torres JL; Golden GJ; Bartels PL; Porell RN; Garretson AF; Laubach L; Feldman J; Yin X; Pu Y; Hauser BM; Caradonna TM; Kellman BP; Martino C; Gordts PLSM; Chanda SK; Schmidt AG; Godula K; Leibel SL; Jose J; Corbett KD; Ward AB; Carlin AF; Esko JD Cell 2020[Nov]; 183 (4): 1043-1057.e15 PMID32970989show ga We show that SARS-CoV-2 spike protein interacts with both cellular heparan sulfate and angiotensin-converting enzyme 2 (ACE2) through its receptor-binding domain (RBD). Docking studies suggest a heparin/heparan sulfate-binding site adjacent to the ACE2-binding site. Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold. Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2. On cells, spike protein binding depends on both heparan sulfate and ACE2. Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. We suggest a model in which viral attachment and infection involves heparan sulfate-dependent enhancement of binding to ACE2. Manipulation of heparan sulfate or inhibition of viral adhesion by exogenous heparin presents new therapeutic opportunities. |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Betacoronavirus/isolation & purification/*physiology[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Cell Line[MESH] |Coronavirus Infections/pathology/virology[MESH] |Heparin/chemistry/metabolism[MESH] |Heparitin Sulfate/chemistry/*metabolism[MESH] |Humans[MESH] |Kidney/metabolism[MESH] |Lung/metabolism[MESH] |Molecular Dynamics Simulation[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/chemistry/*metabolism[MESH] |Pneumonia, Viral/pathology/virology[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Recombinant Proteins/biosynthesis/chemistry/isolation & purification[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/chemistry/genetics/*metabolism[MESH]SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 (epmc).pdf DeepDyve Pubget Overpricing