Evidence map›Paper›PMID 34929193›Full record

ArticleBiophysical journal2022

Negatively charged residues in the membrane ordering activity of SARS-CoV-1 and -2 fusion peptides.

Alex L Lai, Jack H Freed

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. SARS-CoV-2 FP1 Destabilizes Lipid Membranes and Facilitates Pore Formation.International journal of molecular sciences · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Alex L LaiDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York. Electronic address: ll564@cornell.edu.
Jack H FreedDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York. Electronic address: jhf3@cornell.edu.
Cornell University · US

Funding

TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
Electron Spin Relaxation in Model MembranesR01GM123779 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2017 to 2020
$2.1M
NIGMS NIH HHS P41 GM103521NIGMS NIH HHS R01 GM123779
6 · The paper itself

Abstract

Entry of coronaviruses into host cells is mediated by the viral spike protein. Previously, we identified the bona fide fusion peptides (FPs) for severe acute respiratory syndrome coronavirus ("SARS-1") and severe acute respiratory syndrome coronavirus-2 ("SARS-2") using electron spin resonance spectroscopy. We also found that their FPs induce membrane ordering in a Ca

Indexed as

COVID-19Membrane FusionHumansPeptidesSARS-CoV-2Spike Glycoprotein, CoronavirusViral Envelope ProteinsPeptidesSpike Glycoprotein, CoronavirusViral Envelope Proteins

Identifiers

PMID34929193
PMCPMC8683214
OpenAlexW4200181709

What OpenQuestion holds

Textmetadata
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.