Evidence map›Paper›PMID 35323112›Full record

ArticleeLife2022

The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein.

Hisham M Dokainish, Suyong Re, Takaharu Mori, Chigusa Kobayashi, Jaewoon Jung, Yuji Sugita

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

41 citing papers in PubMed, 74 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

Hisham M DokainishTheoretical Molecular Science Laboratory, RIKEN Cluster for Pioneering Research, Wako, Japan.ORCID 0000-0002-4387-4790
Suyong ReArtificial Intelligence Center for Health and Biomedical Research, National Institutes of Biomedical Innovation, Health and Nutrition, Osaka, Japan.ORCID 0000-0002-3752-6554
Takaharu MoriTheoretical Molecular Science Laboratory, RIKEN Cluster for Pioneering Research, Wako, Japan.ORCID 0000-0002-8717-2926
Chigusa KobayashiComputational Biophysics Research Team, RIKEN Center for Computational Science, Kobe, Japan.ORCID 0000-0002-5603-4619
Jaewoon JungTheoretical Molecular Science Laboratory, RIKEN Cluster for Pioneering Research, Wako, Japan.ORCID 0000-0002-2285-4432
Yuji SugitaTheoretical Molecular Science Laboratory, RIKEN Cluster for Pioneering Research, Wako, Japan.ORCID 0000-0001-9738-9216
Pioneer (United States) · USNational Institute of Biomedical Innovation, Health and Nutrition · JPRIKEN Center for Computational Science · JP

Funding

HPCI System Research project hp200028HPCI System Research project hp200135HPCI System Research project hp200153HPCI System Research project hp210107HPCI System Research project hp210177Ministry of Education, Culture, Sports, Science and Technology 19H05645Ministry of Education, Culture, Sports, Science and Technology 19K06532Ministry of Education, Culture, Sports, Science and Technology 19K12229Ministry of Education, Culture, Sports, Science and Technology 20K15737Ministry of Education, Culture, Sports, Science and Technology 21H05157Ministry of Education, Culture, Sports, Science and Technology 21H05249Ministry of Education, Culture, Sports, Science and Technology FLAGSHIP 2020 projectMinistry of Education, Culture, Sports, Science and Technology JPMXP1020200101Ministry of Education, Culture, Sports, Science and Technology JPMXP1020200201Ministry of Education, Culture, Sports, Science and Technology Priority Issue on Post-K computerMinistry of Education, Culture, Sports, Science and Technology Program for Promoting Researches on the Supercomputer FugakuRIKEN Dynamic Structural Biology/Glycolipidologue Initiative/Biology of Intracellular Environments
6 · The paper itself

Abstract

Spike (S) protein is the primary antigenic target for neutralization and vaccine development for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It decorates the virus surface and undergoes large motions of its receptor binding domains (RBDs) to enter the host cell. Here, we observe Down, one-Up, one-Open, and two-Up-like structures in enhanced molecular dynamics simulations, and characterize the transition pathways via inter-domain interactions. Transient salt-bridges between RBD

Indexed as

Spike Glycoprotein, CoronavirusCOVID-19Cryoelectron MicroscopyHumansProtein DomainsSARS-CoV-2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2biochemistrychemical biologyconformational transitioncryptic pocketsenhanced samplinghumanmolecular biophysicsSARS-CoV-2spike proteinstructural biology

Identifiers

PMID35323112
PMCPMC8963885
OpenAlexW4226110365

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.