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Nature (London), ISSN 1476-4687, 07/2012, Volume 487, Issue 7408, pp. 477 - 481
Journal Article
Cell (Cambridge), ISSN 0092-8674, 05/2020, Volume 181, Issue 4, pp. 905 - 913.e7
Journal Article
Circulation (New York, N.Y.), ISSN 1524-4539, 08/2010, Volume 122, Issue 7, pp. 717 - 728
Journal Article
Nature (London), ISSN 1476-4687, 03/2020, Volume 581, Issue 7807, pp. 221 - 224
The crystal structure of the receptor-binding domain of the SARS-CoV-2 spike in complex with human ACE2, compared with the receptor-binding domain of SARS-CoV,... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Chiroptera - virology | Pandemics | Receptors, Virus - metabolism | Coronavirus Infections - drug therapy | Disease Reservoirs - virology | Humans | Pneumonia, Viral - drug therapy | Crystallography, X-Ray | Zoonoses - virology | Coronavirus Infections - transmission | Pneumonia, Viral - transmission | Coronavirus Infections - epidemiology | Pneumonia, Viral - epidemiology | Betacoronavirus - chemistry | Zoonoses - epidemiology | Peptidyl-Dipeptidase A - metabolism | Protein Domains | Protein Stability | Binding Sites | Coronavirus - isolation & purification | Spike Glycoprotein, Coronavirus - genetics | Spike Glycoprotein, Coronavirus - metabolism | Betacoronavirus - drug effects | Crystallization | Models, Molecular | China - epidemiology | Betacoronavirus - metabolism | SARS Virus - chemistry | Zoonoses - transmission | Animals | Peptidyl-Dipeptidase A - chemistry | Receptors, Virus - chemistry | Coronavirus - chemistry | Coronavirus Infections - virology | Protein Binding | Eutheria - virology | Pneumonia, Viral - virology | Spike Glycoprotein, Coronavirus - chemistry | Analysis | Angiotensin converting enzyme | Crystals | Coronaviruses | Structure | Radioligand assay | Membrane proteins | Epidemics | Enzymes | Severe acute respiratory syndrome | China | Health aspects | Binding | Target recognition | Spike protein | Pathogenesis | Viral diseases | Viruses | Angiotensin-converting enzyme 2--ACE2 | Severe acute respiratory syndrome coronavirus 2 | COVID-19 | Proteins | Receptors | Disease transmission | Hydrogen bonds | Peptidyl-dipeptidase A | Infectivity | Angiotensin | Host range | Crystal structure | Index Medicus | X-ray crystallography | SARS-CoV-2 | angiotensin-converting enzyme 2 | receptor-binding motif | SARS-CoV | receptor-binding domain
Journal Article
Journal Article
PloS one, ISSN 1932-6203, 12/2018, Volume 13, Issue 12, pp. e0208854 - e0208854
Journal Article