Selective covalent targeting of SARS-CoV-2 main protease by enantiopure chlorofluoroacetamide

The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (M pro ) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 M pro inhibi...

Full description

Saved in:
Bibliographic Details
Published inChemical science (Cambridge) Vol. 13; no. 10; pp. 3027 - 3034
Main Authors Yamane, Daiki, Onitsuka, Satsuki, Re, Suyong, Isogai, Hikaru, Hamada, Rui, Hiramoto, Tadanari, Kawanishi, Eiji, Mizuguchi, Kenji, Shindo, Naoya, Ojida, Akio
Format Journal Article
LanguageEnglish
Published CAMBRIDGE Royal Soc Chemistry 09.03.2022
Royal Society of Chemistry
The Royal Society of Chemistry
Subjects
Chemistry
Chemistry, Multidisciplinary
Chirality
Coronaviruses
Covalence
COVID-19
Inhibitors
Physical Sciences
Protease
Reaction kinetics
Science & Technology
Selectivity
Severe acute respiratory syndrome coronavirus 2
Stereoisomerism
Viral diseases
Warheads
DISCOVERY
INHIBITORS
Online AccessGet full text

Cover

Abstract The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (M pro ) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 M pro inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of M pro . Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 M pro . Among the four stereoisomers, ( R , R )-18 exhibited a markedly higher inhibitory activity against M pro than the other isomers. Reaction kinetics and computational docking studies suggest that the R configuration of the CFA warhead is crucial for the rapid covalent inhibition of M pro . Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors.
AbstractList The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (M pro ) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 M pro inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of M pro . Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 M pro . Among the four stereoisomers, ( R , R )-18 exhibited a markedly higher inhibitory activity against M pro than the other isomers. Reaction kinetics and computational docking studies suggest that the R configuration of the CFA warhead is crucial for the rapid covalent inhibition of M pro . Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors.
The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (M-pro) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 M-pro inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of M-pro. Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 M-pro. Among the four stereoisomers, (R,R)-18 exhibited a markedly higher inhibitory activity against M-pro than the other isomers. Reaction kinetics and computational docking studies suggest that the R configuration of the CFA warhead is crucial for the rapid covalent inhibition of M-pro. Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors.
The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (M pro ) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 M pro inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of M pro . Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 M pro . Among the four stereoisomers, ( R , R )-18 exhibited a markedly higher inhibitory activity against M pro than the other isomers. Reaction kinetics and computational docking studies suggest that the R configuration of the CFA warhead is crucial for the rapid covalent inhibition of M pro . Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors. Chlorofluoroacetamide (CFA) was used as the warhead for covalent targeting of SARS-CoV-2 M pro . The chirality at CFA showed marked influence on inhibitory activity, suggesting stereospecific activation of CFA for cysteine modification in the protein.
The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (Mpro) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 Mpro inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of Mpro. Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 Mpro. Among the four stereoisomers, (R,R)-18 exhibited a markedly higher inhibitory activity against Mpro than the other isomers. Reaction kinetics and computational docking studies suggest that the R configuration of the CFA warhead is crucial for the rapid covalent inhibition of Mpro. Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors.The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (Mpro) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 Mpro inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of Mpro. Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 Mpro. Among the four stereoisomers, (R,R)-18 exhibited a markedly higher inhibitory activity against Mpro than the other isomers. Reaction kinetics and computational docking studies suggest that the R configuration of the CFA warhead is crucial for the rapid covalent inhibition of Mpro. Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors.
The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (Mpro) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 Mpro inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of Mpro. Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 Mpro. Among the four stereoisomers, (R,R)-18 exhibited a markedly higher inhibitory activity against Mpro than the other isomers. Reaction kinetics and computational docking studies suggest that the R configuration of the CFA warhead is crucial for the rapid covalent inhibition of Mpro. Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors.
The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The main protease (M ) is a promising target for COVID-19 treatment. Here, we report an irreversible SARS-CoV-2 M inhibitor possessing chlorofluoroacetamide (CFA) as a warhead for the covalent modification of M . Ugi multicomponent reaction using chlorofluoroacetic acid enabled the rapid synthesis of dipeptidic CFA derivatives that identified 18 as a potent inhibitor of SARS-CoV-2 M . Among the four stereoisomers, ( , )-18 exhibited a markedly higher inhibitory activity against M than the other isomers. Reaction kinetics and computational docking studies suggest that the configuration of the CFA warhead is crucial for the rapid covalent inhibition of M . Our findings highlight the prominent influence of the CFA chirality on the covalent modification of proteinous cysteines and provide the basis for improving the potency and selectivity of CFA-based covalent inhibitors.
Author Re, Suyong
Isogai, Hikaru
Hamada, Rui
Ojida, Akio
Onitsuka, Satsuki
Yamane, Daiki
Hiramoto, Tadanari
Kawanishi, Eiji
Shindo, Naoya
Mizuguchi, Kenji
Author_xml – sequence: 1
  givenname: Daiki
  surname: Yamane
  fullname: Yamane, Daiki
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
– sequence: 2
  givenname: Satsuki
  surname: Onitsuka
  fullname: Onitsuka, Satsuki
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
– sequence: 3
  givenname: Suyong
  surname: Re
  fullname: Re, Suyong
  organization: Artificial Intelligence Center for Health and Biomedical Research, National Institute of Biomedical Innovation, Health and Nutrition, 7-6-8 Saito-Asagi, Ibaraki, Osaka 567-0085, Japan
– sequence: 4
  givenname: Hikaru
  surname: Isogai
  fullname: Isogai, Hikaru
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
– sequence: 5
  givenname: Rui
  surname: Hamada
  fullname: Hamada, Rui
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
– sequence: 6
  givenname: Tadanari
  surname: Hiramoto
  fullname: Hiramoto, Tadanari
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
– sequence: 7
  givenname: Eiji
  orcidid: 0000-0002-4220-6328
  surname: Kawanishi
  fullname: Kawanishi, Eiji
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
– sequence: 8
  givenname: Kenji
  surname: Mizuguchi
  fullname: Mizuguchi, Kenji
  organization: Artificial Intelligence Center for Health and Biomedical Research, National Institute of Biomedical Innovation, Health and Nutrition, 7-6-8 Saito-Asagi, Ibaraki, Osaka 567-0085, Japan, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
– sequence: 9
  givenname: Naoya
  orcidid: 0000-0002-2374-9896
  surname: Shindo
  fullname: Shindo, Naoya
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
– sequence: 10
  givenname: Akio
  orcidid: 0000-0002-9440-8167
  surname: Ojida
  fullname: Ojida, Akio
  organization: Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/35432850$$D View this record in MEDLINE/PubMed
BookMark eNqNkl1rFDEUhoO02A974w-QAW-kMpqPSSa5Ecr40UJBcNU7GTKZM9uUmWSbZFb6782y62qLF-YiCeR5X845b07QgfMOEHpO8BuCmXr7niwaLLgSzRN0THFFSsGZOtjfKT5CZzHe4rwYI5zWT9ER4xWjkuNj9GMBI5hk11AYv9YjuFQkHZaQrFsWfigWF18WZeO_l7SYtHXFKvgEOkLR3RfgtEvWr-aQ1TejD34Y57xrA0lPtodn6HDQY4Sz3XmKvn388LW5LK8_f7pqLq5LU2GRSsZ6JVlfSSXlMPRYEG2qWstOAVcDJ7QzAlgna9NLwUUtie5w1w-S4U5o3bNT9G7ru5q7CXqTuwh6bFfBTjrct17b9uGLszft0q9bqTBXqs4Gr3YGwd_NEFM72WhgHLUDP8eWbgbJqBIqoy8fobd-Di63lylW85pjQjP14u-K9qX8nnwGXm-Bn9D5IRoLzsAey2HVOdOa8U1uJNPy_-nGJp1jcY2fXcrS863UBB9jgGEvI7jdfKH2zxfKMH4Em51ZHpsd_yX5BSQ6xkw
CitedBy_id crossref_primary_10_1002_mco2_151
crossref_primary_10_1021_acs_jmedchem_3c00737
crossref_primary_10_1021_acs_jmedchem_3c01825
crossref_primary_10_3390_ph15081021
crossref_primary_10_1021_acs_orglett_2c03547
crossref_primary_10_1080_14756366_2025_2460045
crossref_primary_10_3390_biom13091339
crossref_primary_10_1039_D4MD00707G
crossref_primary_10_1021_acs_jmedchem_2c01005
crossref_primary_10_1016_j_beha_2022_101373
crossref_primary_10_1039_D4RA03368J
crossref_primary_10_1039_D2QO00810F
crossref_primary_10_5059_yukigoseikyokaishi_82_50
crossref_primary_10_1021_acsomega_2c07259
crossref_primary_10_1038_s42004_024_01104_7
crossref_primary_10_1002_ptr_7651
crossref_primary_10_1016_j_rechem_2024_101428
crossref_primary_10_1021_acs_jmedchem_2c01081
crossref_primary_10_3390_futurepharmacol3010006
crossref_primary_10_1039_D3SC06441G
crossref_primary_10_1039_D4OB00924J
crossref_primary_10_1016_j_ejmech_2023_115772
crossref_primary_10_1002_cmdc_202300315
crossref_primary_10_1016_j_ejmech_2023_115667
Cites_doi 10.1038/s41586-020-2223-y
10.1021/acs.jmedchem.1c00616
10.1016/j.bbrc.2004.04.098
10.1016/S0040-4020(01)82831-3
10.1126/science.abb3405
10.1002/cmdc.202000924
10.1021/acsmedchemlett.9b00574
10.1126/science.abl4784
10.1016/j.cell.2020.09.044
10.1126/science.abf1611
10.1021/ci9002393
10.1038/s41589-020-00689-z
10.1021/acs.jmedchem.0c02258
10.1021/acs.jmedchem.1c00509
10.1055/s-1984-30987
10.1126/science.abb4489
10.1002/cmdc.201700356
10.1248/cpb.c20-00547
10.1016/j.chembiol.2021.05.018
10.1021/tx400301q
10.1038/s41586-020-2008-3
10.1021/acs.jmedchem.0c00606
10.1038/s41586-020-2012-7
10.1038/s41467-021-20900-6
10.1016/j.drudis.2020.01.015
10.1038/nrd3410
10.1002/anie.202016961
10.1038/s41589-018-0204-3
10.1021/acs.jmedchem.0c01140
10.1021/acs.jmedchem.1c00665
10.1021/jacs.1c08060
10.1039/B711844A
10.1038/nrd.2018.21
10.1038/s41579-021-00573-0
10.1016/j.virusres.2015.05.018
10.1021/acs.jmedchem.0c01063
10.1038/s41467-020-19662-4
10.1126/science.1085658
10.1021/jm301580n
10.1021/acsinfecdis.9b00012
10.1039/b711844a
ContentType Journal Article
Copyright This journal is © The Royal Society of Chemistry.
Copyright Royal Society of Chemistry 2022
This journal is © The Royal Society of Chemistry 2022 The Royal Society of Chemistry
Copyright_xml – notice: This journal is © The Royal Society of Chemistry.
– notice: Copyright Royal Society of Chemistry 2022
– notice: This journal is © The Royal Society of Chemistry 2022 The Royal Society of Chemistry
DBID AAYXX
CITATION
17B
1KM
AHQBO
BLEPL
DTL
EGQ
NPM
7SR
8BQ
8FD
JG9
7X8
5PM
DOI 10.1039/D1SC06596C
DatabaseName CrossRef
Web of Knowledge
Index Chemicus
Web of Science - Science Citation Index Expanded - 2022
Web of Science Core Collection
Science Citation Index Expanded
Web of Science Primary (SCIE, SSCI & AHCI)
PubMed
Engineered Materials Abstracts
METADEX
Technology Research Database
Materials Research Database
MEDLINE - Academic
PubMed Central (Full Participant titles)
DatabaseTitle CrossRef
Web of Science
PubMed
Materials Research Database
Engineered Materials Abstracts
Technology Research Database
METADEX
MEDLINE - Academic
DatabaseTitleList CrossRef
Web of Science

MEDLINE - Academic
Materials Research Database
PubMed
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: 1KM
  name: Index Chemicus
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/woscc/search-with-editions?editions=WOS.IC
  sourceTypes:
    Enrichment Source
    Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
EISSN 2041-6539
EndPage 3034
ExternalDocumentID PMC8905997
35432850
000759673500001
10_1039_D1SC06596C
Genre Journal Article
GrantInformation_xml – fundername: Grants-in-Aid for Scientific Research; Ministry of Education, Culture, Sports, Science and Technology, Japan (MEXT); Japan Society for the Promotion of Science; Grants-in-Aid for Scientific Research (KAKENHI)
  grantid: 19H02854
– fundername: ''Chemistry for Multimolecular Crowding Biosystems" (JSPS KAKENHI)
  grantid: JP17H06349
– fundername: Sumitomo Foundation
– fundername: JSPS KAKENHI; Ministry of Education, Culture, Sports, Science and Technology, Japan (MEXT); Japan Society for the Promotion of Science; Grants-in-Aid for Scientific Research (KAKENHI)
  grantid: 19H02854
– fundername: AMED
  grantid: JP18am0101091; JP21ak0101121; JP20.0108519
– fundername: ;
  grantid: JP17H06349; JP18am0101091; 19H02854; JP21ak0101121; JP20fk0108519
GroupedDBID 0-7
0R~
53G
705
7~J
AAEMU
AAFWJ
AAIWI
AAJAE
AARTK
AAXHV
AAYXX
ABEMK
ABIQK
ABPDG
ABXOH
ACGFS
ACIWK
ADBBV
ADMRA
AEFDR
AENEX
AESAV
AFLYV
AFPKN
AGEGJ
AGRSR
AHGCF
AKBGW
ALMA_UNASSIGNED_HOLDINGS
ANUXI
AOIJS
APEMP
AUDPV
AZFZN
BCNDV
BLAPV
BSQNT
C6K
CITATION
D0L
EE0
EF-
F5P
GROUPED_DOAJ
H13
HYE
HZ~
H~N
O-G
O9-
OK1
PGMZT
R7C
R7D
RAOCF
RCNCU
RNS
RPM
RRC
RSCEA
RVUXY
SKA
SKF
SKH
SKJ
SKM
SKR
SKZ
SLC
SLF
SLH
17B
1KM
BLEPL
DTL
GROUPED_WOS_SCIENCE_CITATION_INDEX_EXPANDED
GROUPED_WOS_WEB_OF_SCIENCE
-JG
AGSTE
NPM
SMJ
7SR
8BQ
8FD
JG9
7X8
5PM
ID FETCH-LOGICAL-c406t-33d983d48988ffd061ac47a8b9e59f512bc6e3b87cd8656781ab0bdf830b6aad3
ISICitedReferencesCount 27
ISICitedReferencesURI https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=CitingArticles&UT=000759673500001
ISSN 2041-6520
IngestDate Thu Aug 21 18:27:48 EDT 2025
Mon Jul 21 09:42:51 EDT 2025
Fri Jul 25 02:26:17 EDT 2025
Thu Jan 02 22:34:44 EST 2025
Fri Aug 29 16:17:57 EDT 2025
Wed Aug 06 11:24:37 EDT 2025
Tue Jul 01 01:30:37 EDT 2025
Thu Apr 24 23:06:59 EDT 2025
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 10
Keywords DISCOVERY
INHIBITORS
Language English
License This journal is © The Royal Society of Chemistry.
LinkModel OpenURL
LogoURL https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg
MergedId FETCHMERGED-LOGICAL-c406t-33d983d48988ffd061ac47a8b9e59f512bc6e3b87cd8656781ab0bdf830b6aad3
Notes KAKEN
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ORCID 0000-0002-4220-6328
0000-0002-2374-9896
0000-0002-9440-8167
0000-0003-3021-7078
OpenAccessLink http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=FullRecord&UT=000759673500001
PMID 35432850
PQID 2637575012
PQPubID 2047492
PageCount 8
ParticipantIDs webofscience_primary_000759673500001CitationCount
webofscience_primary_000759673500001
pubmed_primary_35432850
crossref_citationtrail_10_1039_D1SC06596C
crossref_primary_10_1039_D1SC06596C
pubmedcentral_primary_oai_pubmedcentral_nih_gov_8905997
proquest_journals_2637575012
proquest_miscellaneous_2652032969
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2022-03-09
PublicationDateYYYYMMDD 2022-03-09
PublicationDate_xml – month: 03
  year: 2022
  text: 2022-03-09
  day: 09
PublicationDecade 2020
PublicationPlace CAMBRIDGE
PublicationPlace_xml – name: CAMBRIDGE
– name: England
– name: Cambridge
PublicationTitle Chemical science (Cambridge)
PublicationTitleAbbrev CHEM SCI
PublicationTitleAlternate Chem Sci
PublicationYear 2022
Publisher Royal Soc Chemistry
Royal Society of Chemistry
The Royal Society of Chemistry
Publisher_xml – name: Royal Soc Chemistry
– name: Royal Society of Chemistry
– name: The Royal Society of Chemistry
References Bellucci (D1SC06596C/cit34/1) 1969; 25
Konno (D1SC06596C/cit19/1) 2021
Shindo (D1SC06596C/cit29/1) 2019; 15
Dai (D1SC06596C/cit15/1) 2021
Qiao (D1SC06596C/cit13/1) 2021; 371
Zaidman (D1SC06596C/cit24/1) 2021; 28
Zhang (D1SC06596C/cit11/1) 2020; 368
Owen (D1SC06596C/cit21/1) 2021; 374
Wu (D1SC06596C/cit1/1) 2020; 579
Singh (D1SC06596C/cit25/1) 2011; 10
Harvey (D1SC06596C/cit3/1) 2021; 19
Rut (D1SC06596C/cit8/1) 2021; 17
Pillaiyar (D1SC06596C/cit5/1) 2020; 25
O'Hagan (D1SC06596C/cit39/1) 2008; 37
Zhou (D1SC06596C/cit40/1) 2009; 49
Dai (D1SC06596C/cit12/1) 2020; 368
Jin (D1SC06596C/cit7/1) 2020; 582
Ferguson (D1SC06596C/cit26/1) 2018; 17
Kim (D1SC06596C/cit27/1) 2020; 183
Hoffman (D1SC06596C/cit16/1) 2020; 63
Zhou (D1SC06596C/cit2/1) 2020; 579
Breidenbach (D1SC06596C/cit20/1) 2021; 60
Miura (D1SC06596C/cit31/1) 2020; 68
Gil (D1SC06596C/cit4/1) 2020; 63
Tonge (D1SC06596C/cit36/1) 2019; 5
Cannalire (D1SC06596C/cit6/1) 2020
Hattori (D1SC06596C/cit17/1) 2021; 12
Sowaileh (D1SC06596C/cit33/1) 2017; 12
Wu (D1SC06596C/cit10/1) 2015; 208
Lee (D1SC06596C/cit37/1) 2020; 11
Bai (D1SC06596C/cit18/1) 2021
Anand (D1SC06596C/cit9/1) 2003; 300
Jacobs (D1SC06596C/cit22/1) 2013; 56
Sato (D1SC06596C/cit30/1) 2020; 11
Molines (D1SC06596C/cit35/1) 1984; 1984
Ma (D1SC06596C/cit38/1) 2021; 143
Dahal (D1SC06596C/cit28/1) 2013; 26
Kuo (D1SC06596C/cit32/1) 2004; 318
Kitamura (D1SC06596C/cit23/1) 2021
Yang (D1SC06596C/cit14/1) 2021; 16
Dahal, UP (WOS:000327225800015) 2013; 26
Breidenbach, J (WOS:000631784400001) 2021; 60
Kitamura, N (WOS:000797940600010) 2022; 65
Hoffman, RL (WOS:000592734300030) 2020; 63
Anand, K (WOS:000183459700056) 2003; 300
Tonge, PJ (WOS:000472120100003) 2019; 5
BELLUCCI, G (WOS:A1969D766200006) 1969; 25
Wu, F (CCC:000530151300006) 2020; 580
Miura, C (WOS:000584615300008) 2020; 68
Jacobs, J (WOS:000314205000014) 2013; 56
Qiao, JX (WOS:000636043400052) 2021; 371
Pillaiyar, T (WOS:000530687600006) 2020; 25
Jin, ZM (WOS:000537932300001) 2020; 582
Zhang, LL (WOS:000528513300041) 2020; 368
Singh, J (WOS:000289056000016) 2011; 10
Bai, B (WOS:000797940600013) 2022; 65
Lee, J (WOS:000595686500004) 2020; 11
Zhou, P. (000759673500001.2) 1000
Cannalire, R (WOS:000797940600002) 2022; 65
Dai, WH (WOS:000797940600005) 2022; 65
Kuo, CJ (WOS:000221776400010) 2004; 318
Ma, CL (WOS:000750799000006) 2021; 143
Hattori, S (WOS:000616785800002) 2021; 12
Shindo, N (WOS:000458824400013) 2019; 15
Kim, D (WOS:000588640900005) 2020; 183
Rut, W (WOS:000581588300001) 2021; 17
Dai, WH (WOS:000544017600040) 2020; 368
Yang, KS (WOS:000596948600001) 2021; 16
Zaidman, D (WOS:000733742800013) 2021; 28
Konno, S (WOS:000797940600014) 2022; 65
Wu, AD (WOS:000360951800008) 2015; 208
Sato, M (WOS:000541747800014) 2020; 11
Owen, DR (WOS:000736589300028) 2021; 374
Gil, C (WOS:000592734300012) 2020; 63
O'Hagan, D (WOS:000252411800006) 2008; 37
Harvey, WT (WOS:000656810800002) 2021; 19
Zhou, P (WOS:000271011500018) 2009; 49
Sowaileh, MF (WOS:000417407500001) 2017; 12
Molines, H. (000759673500001.35) 1984; 1984
Ferguson, FM (WOS:000431172600016) 2018; 17
References_xml – volume: 582
  start-page: 289
  year: 2020
  ident: D1SC06596C/cit7/1
  publication-title: Nature
  doi: 10.1038/s41586-020-2223-y
– year: 2021
  ident: D1SC06596C/cit18/1
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.1c00616
– volume: 318
  start-page: 862
  year: 2004
  ident: D1SC06596C/cit32/1
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2004.04.098
– volume: 25
  start-page: 2979
  year: 1969
  ident: D1SC06596C/cit34/1
  publication-title: Tetrahedron
  doi: 10.1016/S0040-4020(01)82831-3
– volume: 368
  start-page: 409
  year: 2020
  ident: D1SC06596C/cit11/1
  publication-title: Science
  doi: 10.1126/science.abb3405
– volume: 16
  start-page: 942
  year: 2021
  ident: D1SC06596C/cit14/1
  publication-title: ChemMedChem
  doi: 10.1002/cmdc.202000924
– volume: 11
  start-page: 1137
  year: 2020
  ident: D1SC06596C/cit30/1
  publication-title: ACS Med. Chem. Lett.
  doi: 10.1021/acsmedchemlett.9b00574
– volume: 374
  start-page: 1586
  year: 2021
  ident: D1SC06596C/cit21/1
  publication-title: Science
  doi: 10.1126/science.abl4784
– volume: 183
  start-page: 850
  year: 2020
  ident: D1SC06596C/cit27/1
  publication-title: Cell
  doi: 10.1016/j.cell.2020.09.044
– volume: 371
  start-page: 1374
  year: 2021
  ident: D1SC06596C/cit13/1
  publication-title: Science
  doi: 10.1126/science.abf1611
– volume: 49
  start-page: 2344
  year: 2009
  ident: D1SC06596C/cit40/1
  publication-title: J. Chem. Inf. Model.
  doi: 10.1021/ci9002393
– volume: 17
  start-page: 222
  year: 2021
  ident: D1SC06596C/cit8/1
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/s41589-020-00689-z
– year: 2021
  ident: D1SC06596C/cit15/1
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.0c02258
– year: 2021
  ident: D1SC06596C/cit23/1
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.1c00509
– volume: 1984
  start-page: 838
  year: 1984
  ident: D1SC06596C/cit35/1
  publication-title: Synthesis
  doi: 10.1055/s-1984-30987
– volume: 368
  start-page: 1331
  year: 2020
  ident: D1SC06596C/cit12/1
  publication-title: Science
  doi: 10.1126/science.abb4489
– volume: 12
  start-page: 1481
  year: 2017
  ident: D1SC06596C/cit33/1
  publication-title: ChemMedChem
  doi: 10.1002/cmdc.201700356
– volume: 68
  start-page: 1074
  year: 2020
  ident: D1SC06596C/cit31/1
  publication-title: Chem. Pharm. Bull.
  doi: 10.1248/cpb.c20-00547
– volume: 28
  start-page: 1795
  year: 2021
  ident: D1SC06596C/cit24/1
  publication-title: Cell Chem. Biol.
  doi: 10.1016/j.chembiol.2021.05.018
– volume: 26
  start-page: 1739
  year: 2013
  ident: D1SC06596C/cit28/1
  publication-title: Chem. Res. Toxicol.
  doi: 10.1021/tx400301q
– volume: 579
  start-page: 265
  year: 2020
  ident: D1SC06596C/cit1/1
  publication-title: Nature
  doi: 10.1038/s41586-020-2008-3
– volume: 63
  start-page: 12359
  year: 2020
  ident: D1SC06596C/cit4/1
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.0c00606
– volume: 579
  start-page: 270
  year: 2020
  ident: D1SC06596C/cit2/1
  publication-title: Nature
  doi: 10.1038/s41586-020-2012-7
– volume: 12
  start-page: 668
  year: 2021
  ident: D1SC06596C/cit17/1
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-021-20900-6
– volume: 25
  start-page: 668
  year: 2020
  ident: D1SC06596C/cit5/1
  publication-title: Drug Discovery Today
  doi: 10.1016/j.drudis.2020.01.015
– volume: 10
  start-page: 307
  year: 2011
  ident: D1SC06596C/cit25/1
  publication-title: Nat. Rev. Drug Discov
  doi: 10.1038/nrd3410
– volume: 60
  start-page: 10423
  year: 2021
  ident: D1SC06596C/cit20/1
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.202016961
– volume: 15
  start-page: 250
  year: 2019
  ident: D1SC06596C/cit29/1
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/s41589-018-0204-3
– year: 2020
  ident: D1SC06596C/cit6/1
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.0c01140
– year: 2021
  ident: D1SC06596C/cit19/1
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.1c00665
– volume: 143
  start-page: 20697
  year: 2021
  ident: D1SC06596C/cit38/1
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/jacs.1c08060
– volume: 37
  start-page: 308
  year: 2008
  ident: D1SC06596C/cit39/1
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/B711844A
– volume: 17
  start-page: 353
  year: 2018
  ident: D1SC06596C/cit26/1
  publication-title: Nat. Rev. Drug Discovery
  doi: 10.1038/nrd.2018.21
– volume: 19
  start-page: 409
  year: 2021
  ident: D1SC06596C/cit3/1
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/s41579-021-00573-0
– volume: 208
  start-page: 56
  year: 2015
  ident: D1SC06596C/cit10/1
  publication-title: Virus Res.
  doi: 10.1016/j.virusres.2015.05.018
– volume: 63
  start-page: 12725
  year: 2020
  ident: D1SC06596C/cit16/1
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.0c01063
– volume: 11
  start-page: 5877
  year: 2020
  ident: D1SC06596C/cit37/1
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-020-19662-4
– volume: 300
  start-page: 1763
  year: 2003
  ident: D1SC06596C/cit9/1
  publication-title: Science
  doi: 10.1126/science.1085658
– volume: 56
  start-page: 534
  year: 2013
  ident: D1SC06596C/cit22/1
  publication-title: J. Med. Chem.
  doi: 10.1021/jm301580n
– volume: 5
  start-page: 796
  year: 2019
  ident: D1SC06596C/cit36/1
  publication-title: ACS Infect. Dis.
  doi: 10.1021/acsinfecdis.9b00012
– volume: 15
  start-page: 250
  year: 2019
  ident: WOS:000458824400013
  article-title: Selective and reversible modification of kinase cysteines with chlorofluoroacetamides
  publication-title: NATURE CHEMICAL BIOLOGY
  doi: 10.1038/s41589-018-0204-3
– volume: 17
  start-page: 353
  year: 2018
  ident: WOS:000431172600016
  article-title: Kinase inhibitors: the road ahead
  publication-title: NATURE REVIEWS DRUG DISCOVERY
  doi: 10.1038/nrd.2018.21
– year: 1000
  ident: 000759673500001.2
– volume: 10
  start-page: 307
  year: 2011
  ident: WOS:000289056000016
  article-title: The resurgence of covalent drugs
  publication-title: NATURE REVIEWS DRUG DISCOVERY
  doi: 10.1038/nrd3410
– volume: 12
  start-page: ARTN 668
  year: 2021
  ident: WOS:000616785800002
  article-title: A small molecule compound with an indole moiety inhibits the main protease of SARS-CoV-2 and blocks virus replication
  publication-title: NATURE COMMUNICATIONS
  doi: 10.1038/s41467-021-20900-6
– volume: 183
  start-page: 850
  year: 2020
  ident: WOS:000588640900005
  article-title: Targeting KRAS(G12C): From Inhibitory Mechanism to Modulation of Antitumor Effects in Patients
  publication-title: CELL
  doi: 10.1016/j.cell.2020.09.044
– volume: 318
  start-page: 862
  year: 2004
  ident: WOS:000221776400010
  article-title: Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate
  publication-title: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  doi: 10.1016/j.bbrc.2004.04.098
– volume: 143
  start-page: 20697
  year: 2021
  ident: WOS:000750799000006
  article-title: Discovery of Di- and Trihaloacetamides as Covalent SARS-CoV-2 Main Protease Inhibitors with High Target Specificity
  publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
  doi: 10.1021/jacs.1c08060
– volume: 12
  start-page: 1481
  year: 2017
  ident: WOS:000417407500001
  article-title: Application of the Pentafluorosulfanyl Group as a Bioisosteric Replacement
  publication-title: CHEMMEDCHEM
  doi: 10.1002/cmdc.201700356
– volume: 65
  start-page: 2848
  year: 2022
  ident: WOS:000797940600010
  article-title: Expedited Approach toward the Rational Design of Noncovalent SARS-CoV-2 Main Protease Inhibitors
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/acs.jmedchem.1c00509
– volume: 65
  start-page: 2716
  year: 2022
  ident: WOS:000797940600002
  article-title: Targeting SARS-CoV-2 Proteases and Polymerase for COVID-19 Treatment: State of the Art and Future Opportunities
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/acs.jmedchem.0c01140
– volume: 63
  start-page: 12725
  year: 2020
  ident: WOS:000592734300030
  article-title: Discovery of Ketone-Based Covalent Inhibitors of Coronavirus 3CL Proteases for the Potential Therapeutic Treatment of COVID-19
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/acs.jmedchem.0c01063
– volume: 17
  start-page: 222
  year: 2021
  ident: WOS:000581588300001
  article-title: SARS-CoV-2 Mpro inhibitors and activity-based probes for patient-sample imaging
  publication-title: NATURE CHEMICAL BIOLOGY
  doi: 10.1038/s41589-020-00689-z
– volume: 68
  start-page: 1074
  year: 2020
  ident: WOS:000584615300008
  article-title: Fragment-Based Discovery of Irreversible Covalent Inhibitors of Cysteine Proteases Using Chlorofluoroacetamide Library
  publication-title: CHEMICAL & PHARMACEUTICAL BULLETIN
  doi: 10.1248/cpb.c20-00547
– volume: 371
  start-page: 1374
  year: 2021
  ident: WOS:000636043400052
  article-title: SARS-CoV-2 M-pro inhibitors with antiviral activity in a transgenic mouse model
  publication-title: SCIENCE
  doi: 10.1126/science.abf1611
– volume: 368
  start-page: 409
  year: 2020
  ident: WOS:000528513300041
  article-title: Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors
  publication-title: SCIENCE
  doi: 10.1126/science.abb3405
– volume: 49
  start-page: 2344
  year: 2009
  ident: WOS:000271011500018
  article-title: Fluorine Bonding - How Does It Work In Protein-Ligand Interactions?
  publication-title: JOURNAL OF CHEMICAL INFORMATION AND MODELING
  doi: 10.1021/ci9002393
– volume: 1984
  start-page: 838
  year: 1984
  ident: 000759673500001.35
  publication-title: Synthesis
– volume: 26
  start-page: 1739
  year: 2013
  ident: WOS:000327225800015
  article-title: Benchmarking in Vitro Covalent Binding Burden As a Tool To Assess Potential Toxicity Caused by Nonspecific Covalent Binding of Covalent Drugs
  publication-title: CHEMICAL RESEARCH IN TOXICOLOGY
  doi: 10.1021/tx400301q
– volume: 300
  start-page: 1763
  year: 2003
  ident: WOS:000183459700056
  article-title: Coronavirus main proteinase (3CLpro) structure:: Basis for design of anti-SARS drugs
  publication-title: SCIENCE
– volume: 25
  start-page: 2979
  year: 1969
  ident: WOS:A1969D766200006
  article-title: PREPARATION OF OPTICALLY ACTIVE CHLOROFLUOROACETIC ACID AND CHLOROFLUOROETHANOL
  publication-title: TETRAHEDRON
– volume: 374
  start-page: 1586
  year: 2021
  ident: WOS:000736589300028
  article-title: An oral SARS-CoV-2 Mpro inhibitor clinical candidate for the treatment of COVID-19
  publication-title: SCIENCE
  doi: 10.1126/science.abl4784
– volume: 5
  start-page: 796
  year: 2019
  ident: WOS:000472120100003
  article-title: Quantifying the Interactions between Biomolecules: Guidelines for Assay Design and Data Analysis
  publication-title: ACS INFECTIOUS DISEASES
  doi: 10.1021/acsinfecdis.9b00012
– volume: 208
  start-page: 56
  year: 2015
  ident: WOS:000360951800008
  article-title: Prediction and biochemical analysis of putative cleavage sites of the 3C-like protease of Middle East respiratory syndrome coronavirus
  publication-title: VIRUS RESEARCH
  doi: 10.1016/j.virusres.2015.05.018
– volume: 28
  start-page: 1795
  year: 2021
  ident: WOS:000733742800013
  article-title: An automatic pipeline for the design of irreversible derivatives identifies a potent SARS-CoV-2 Mpro inhibitor
  publication-title: CELL CHEMICAL BIOLOGY
  doi: 10.1016/j.chembiol.2021.05.018
– volume: 16
  start-page: 942
  year: 2021
  ident: WOS:000596948600001
  article-title: A Quick Route to Multiple Highly Potent SARS-CoV-2 Main Protease Inhibitors**
  publication-title: CHEMMEDCHEM
  doi: 10.1002/cmdc.202000924
– volume: 582
  start-page: 289
  year: 2020
  ident: WOS:000537932300001
  article-title: Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors
  publication-title: NATURE
  doi: 10.1038/s41586-020-2223-y
– volume: 11
  start-page: ARTN 5877
  year: 2020
  ident: WOS:000595686500004
  article-title: Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
  publication-title: NATURE COMMUNICATIONS
  doi: 10.1038/s41467-020-19662-4
– volume: 25
  start-page: 668
  year: 2020
  ident: WOS:000530687600006
  article-title: Recent discovery and development of inhibitors targeting coronaviruses
  publication-title: DRUG DISCOVERY TODAY
  doi: 10.1016/j.drudis.2020.01.015
– volume: 63
  start-page: 12359
  year: 2020
  ident: WOS:000592734300012
  article-title: COVID-19: Drug Targets and Potential Treatments
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/acs.jmedchem.0c00606
– volume: 368
  start-page: 1331
  year: 2020
  ident: WOS:000544017600040
  article-title: Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease
  publication-title: SCIENCE
  doi: 10.1126/science.abb4489
– volume: 65
  start-page: 2905
  year: 2022
  ident: WOS:000797940600013
  article-title: Peptidomimetic α-Acyloxymethylketone Warheads with Six-Membered Lactam P1 Glutamine Mimic: SARS-CoV-2 3CL Protease Inhibition, Coronavirus Antiviral Activity, and in Vitro Biological Stability
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/acs.jmedchem.1c00616
– volume: 60
  start-page: 10423
  year: 2021
  ident: WOS:000631784400001
  article-title: Targeting the Main Protease of SARS-CoV-2: From the Establishment of High Throughput Screening to the Design of Tailored Inhibitors
  publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
  doi: 10.1002/anie.202016961
– volume: 11
  start-page: 1137
  year: 2020
  ident: WOS:000541747800014
  article-title: Selective Covalent Targeting of Mutated EGFR(T790M) with Chlorofluoroacetamide-Pyrimidines
  publication-title: ACS MEDICINAL CHEMISTRY LETTERS
  doi: 10.1021/acsmedchemlett.9b00574
– volume: 580
  start-page: E7
  year: 2020
  ident: CCC:000530151300006
  article-title: A new coronavirus associated with human respiratory disease in China (vol 579, pg 265, 2020)
  publication-title: NATURE
– volume: 19
  start-page: 409
  year: 2021
  ident: WOS:000656810800002
  article-title: SARS-CoV-2 variants, spike mutations and immune escape
  publication-title: NATURE REVIEWS MICROBIOLOGY
  doi: 10.1038/s41579-021-00573-0
– volume: 37
  start-page: 308
  year: 2008
  ident: WOS:000252411800006
  article-title: Understanding organofluorine chemistry. An introduction to the C-F bond
  publication-title: CHEMICAL SOCIETY REVIEWS
  doi: 10.1039/b711844a
– volume: 56
  start-page: 534
  year: 2013
  ident: WOS:000314205000014
  article-title: Discovery, Synthesis, And Structure-Based Optimization of a Series of N-(tert-Butyl)-2-(N-arylamido)-2-(pyridin-3-yl) Acetamides (ML188) as Potent Noncovalent Small Molecule Inhibitors of the Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) 3CL Protease
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/jm301580n
– volume: 65
  start-page: 2794
  year: 2022
  ident: WOS:000797940600005
  article-title: Design, Synthesis, and Biological Evaluation of Peptidomimetic Aldehydes as Broad-Spectrum Inhibitors against Enterovirus and SARS-CoV-2
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/acs.jmedchem.0c02258
– volume: 65
  start-page: 2926
  year: 2022
  ident: WOS:000797940600014
  article-title: 3CL Protease Inhibitors with an Electrophilic Arylketone Moiety as Anti-SARS-CoV-2 Agents
  publication-title: JOURNAL OF MEDICINAL CHEMISTRY
  doi: 10.1021/acs.jmedchem.1c00665
SSID ssj0000331527
Score 2.4775515
Snippet The coronavirus disease 2019 (COVID-19) pandemic has necessitated the development of antiviral agents against severe acute respiratory syndrome coronavirus 2...
Source Web of Science
SourceID pubmedcentral
proquest
pubmed
webofscience
crossref
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
StartPage 3027
SubjectTerms Chemistry
Chemistry, Multidisciplinary
Chirality
Coronaviruses
Covalence
COVID-19
Inhibitors
Physical Sciences
Protease
Reaction kinetics
Science & Technology
Selectivity
Severe acute respiratory syndrome coronavirus 2
Stereoisomerism
Viral diseases
Warheads
Title Selective covalent targeting of SARS-CoV-2 main protease by enantiopure chlorofluoroacetamide
URI http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=FullRecord&UT=000759673500001
https://www.ncbi.nlm.nih.gov/pubmed/35432850
https://www.proquest.com/docview/2637575012
https://www.proquest.com/docview/2652032969
https://pubmed.ncbi.nlm.nih.gov/PMC8905997
Volume 13
WOS 000759673500001
WOSCitedRecordID wos000759673500001
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwELdK9wAviG8CYwpiLwgFkjgfzuPUbarQGNLaTt0DimwnYVHXZlqTh_FX8CdzlzhOChUavESR7Sap72zfx-_uCNmXmRDUD5hl-0JaHsjUFqcC7VYRFS4Pg4RjoPCX02A88z7P_flg8LOHWqpK8VH-2BpX8j9UhTagK0bJ_gNl9UOhAe6BvnAFCsP1TjSe1EVsEPsjC3guuvUbZLeCMk8OzibWqDi33A9LntdgrBLdMShzpoiAyYtrdCDIS9Dai-yqKjC-Ki35Mk82cxi0aQXaKCD0_bbRXj1jwgVfKuzsIc8Xubbgwr6xrha8MUHjre46U9ig20IdoTWbFt-bKtnjfMFvqr5lApRahGZ1-19j_2jBpzW4RJWw6_Y41_YcK_DdxjWT9tuaHEd6k6Z9ZrR7Wy46XnvHNxzJ3tajwaaYWTVx1hJdyYHsDsDW6X_6NT6enZzE06P59B7ZcUHxcIdk5-x8Nr_QdjubUlUJWH97m_WWRp-6x2_KOX8oL9sxuL_JPbWMM31EHirlxDxoOO0xGaSrJ-S-ntCn5JvmOLPlOFNznFlkZsdxJnKc2XKcKW7NHseZWznuGZkdH01HY0sV6LAkyIGlRWkSMZrAumYsyxIQDbn0Qs5ElPpRBqKkkEEKKz-UCQO9IWQOF7ZIMkZtEXCe0OdkuCpW6Utiho4jUNhkIhVeageCc-FRFiSOnzrUcQ3yvp3OWKrs9VhE5SquURQ0ig-dyaie-pFB3umx103Olq2jdluqxGpNr2M3oCEoMDa-8K3uhklGNxosoKLCMUBz6kZBZJAXDRH1a6jvUZf5tkHCDfLqAZjNfbNnlV_WWd1ZhKmSQoPs9xlB_7AW7qMgpH7tkDOIc5dhIzVVmOCifPX3f_yaPOhW8S4ZljdV-gYk7lLs1ZaqPbUUfgH9K9w-
linkProvider Royal Society of Chemistry
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Selective+covalent+targeting+of+SARS-CoV-2+main+protease+by+enantiopure+chlorofluoroacetamide&rft.jtitle=Chemical+science+%28Cambridge%29&rft.au=Yamane%2C+Daiki&rft.au=Onitsuka%2C+Satsuki&rft.au=Re%2C+Suyong&rft.au=Isogai%2C+Hikaru&rft.date=2022-03-09&rft.pub=Royal+Society+of+Chemistry&rft.issn=2041-6520&rft.eissn=2041-6539&rft.volume=13&rft.issue=10&rft.spage=3027&rft.epage=3034&rft_id=info:doi/10.1039%2Fd1sc06596c&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2041-6520&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2041-6520&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2041-6520&client=summon