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Ashley Auerbach
Researcher at University of Minnesota
Publications - 9
Citations - 5619
Ashley Auerbach is an academic researcher from University of Minnesota. The author has contributed to research in topics: Coronavirus & Medicine. The author has an hindex of 4, co-authored 4 publications receiving 3546 citations.
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Journal ArticleDOI
Structural basis of receptor recognition by SARS-CoV-2.
Jian Shang,Gang Ye,Ke Shi,Yushun Wan,Chuming Luo,Hideki Aihara,Qibin Geng,Ashley Auerbach,Fang Li +8 more
TL;DR: This study determines the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2 and sheds light on the structural features that increase its binding affinity to ACE2.
Journal ArticleDOI
Cell entry mechanisms of SARS-CoV-2.
TL;DR: Key cell entry mechanisms of SARS-CoV-2 that potentially contribute to the immune evasion, cell infectivity, and wide spread of the virus are identified using biochemical and pseudovirus entry assays and the potency and evasiveness are highlighted.
Journal ArticleDOI
Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.
Jian Shang,Yushun Wan,Chang Liu,Boyd Yount,Kendra Gully,Yang Yang,Ashley Auerbach,Guiqing Peng,Ralph S. Baric,Fang Li +9 more
TL;DR: The cryo-EM structure of mouse hepatitis coronavirus spike complexed with mouse CEACAM1a is determined and a new role of receptor binding in MHV entry is revealed: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes.
Posted ContentDOI
Structural basis for receptor recognition by the novel coronavirus from Wuhan
Jian Shang,Gang Ye,Ke Shi,Yushun Wan,Chuming Luo,Hideki Aihara,Qibin Geng,Ashley Auerbach,Fang Li +8 more
TL;DR: The crystal structure of 2019-nCoV receptor-binding domain (RBD) (engineered to facilitate crystallization) in complex of human ACE2 is determined, revealing the molecular mechanisms of the animal-to-human transmission of the novel SARS-like coronavirus.
Journal ArticleDOI
APOBEC3B drives PKR-mediated translation shutdown and protects stress granules in response to viral infection
Lavanya Manjunath,Sunwoo Oh,Pedro Ortega,Alexis Bouin,Elodie Bournique,Ambrocio Sanchez,Pia M. Martensen,Ashley Auerbach,Jordan T. Becker,Marcus M. Seldin,Reuben S. Harris,Bert L. Semler,Rémi Buisson +12 more
TL;DR: In this paper , APOBEC3B forms a complex with PABPC1 to stimulate PKR and counterbalances the PKR-suppressing activity of ADAR1 in response to infection by many types of viruses.