Evidence map›Paper›PMID 36385993›Full record

ArticleFrontiers in chemistry2022

Identification and characterization of alternative sites and molecular probes for SARS-CoV-2 target proteins.

Suhasini M Iyengar, Kelly K Barnsley, Hoang Yen Vu, Ian Jef A Bongalonta, Alyssa S Herrod, Jasmine A Scott, Mary Jo Ondrechen

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 51% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Suhasini M IyengarDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States.
Kelly K BarnsleyDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States.
Hoang Yen VuDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States.
Ian Jef A BongalontaDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States.
Alyssa S HerrodDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States.
Jasmine A ScottDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States.
Mary Jo OndrechenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, United States.
Northeastern University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three protein targets from SARS-CoV-2, the viral pathogen that causes COVID-19, are studied: the main protease, the 2'-O-RNA methyltransferase, and the nucleocapsid (N) protein. For the main protease, the nucleophilicity of the catalytic cysteine C145 is enabled by coupling to three histidine residues, H163 and H164 and catalytic dyad partner H41. These electrostatic couplings enable significant population of the deprotonated state of C145. For the RNA methyltransferase, the catalytic lysine K6968 that serves as a Brønsted base has significant population of its deprotonated state

Indexed as

coupled amino acidsmain proteaseNucleocapsidPOOLRNA methyltransferaseSARS-CoV-2secondary sites

Identifiers

PMID36385993
PMCPMC9659918
OpenAlexW4307746311

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.