The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition

Michael Dominic Sacco; Yanmei Hu; Maura Verenice Gongora; Flora Meilleur; Michael Trent Kemp; Xiujun Zhang; Jun Wang; Yu Chen

doi:10.1038/s41422-022-00640-y

The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition

Michael Dominic Sacco, Yanmei Hu, Maura Verenice Gongora, Flora Meilleur, Michael Trent Kemp, Xiujun Zhang, Jun Wang, Yu Chen

Research output: Contribution to journal › Letter › peer-review

95 Scopus citations

Original language	English (US)
Pages (from-to)	498-500
Number of pages	3
Journal	Cell Research
Volume	32
Issue number	5
DOIs	https://doi.org/10.1038/s41422-022-00640-y
State	Published - May 2022
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

Access to Document

10.1038/s41422-022-00640-y

Cite this

@article{733f99fabd4641f9ac5c7d41361c388e,

title = "The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition",

author = "Sacco, {Michael Dominic} and Yanmei Hu and Gongora, {Maura Verenice} and Flora Meilleur and Kemp, {Michael Trent} and Xiujun Zhang and Jun Wang and Yu Chen",

note = "Funding Information: X-ray data were collected at the X-ray facility supported by the Spallation Neutron Source (Oak Ridge National Laboratory), a DOE Office of Science User Facility. This research was supported by the National Institutes of Health (NIH) (grants AI147325, AI157046, and AI158775) to J.W. We thank Eric M Lewandowski for reviewing this paper. ",

year = "2022",

month = may,

doi = "10.1038/s41422-022-00640-y",

language = "English (US)",

volume = "32",

pages = "498--500",

journal = "Cell Research",

issn = "1001-0602",

publisher = "Springer Nature",

number = "5",

}

TY - JOUR

T1 - The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition

AU - Sacco, Michael Dominic

AU - Hu, Yanmei

AU - Gongora, Maura Verenice

AU - Meilleur, Flora

AU - Kemp, Michael Trent

AU - Zhang, Xiujun

AU - Wang, Jun

AU - Chen, Yu

N1 - Funding Information: X-ray data were collected at the X-ray facility supported by the Spallation Neutron Source (Oak Ridge National Laboratory), a DOE Office of Science User Facility. This research was supported by the National Institutes of Health (NIH) (grants AI147325, AI157046, and AI158775) to J.W. We thank Eric M Lewandowski for reviewing this paper.

PY - 2022/5

Y1 - 2022/5

UR - http://www.scopus.com/inward/record.url?scp=85126330616&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85126330616&partnerID=8YFLogxK

U2 - 10.1038/s41422-022-00640-y

DO - 10.1038/s41422-022-00640-y

M3 - Letter

C2 - 35292745

AN - SCOPUS:85126330616

SN - 1001-0602

VL - 32

SP - 498

EP - 500

JO - Cell Research

JF - Cell Research

IS - 5

ER -

The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this