Evidence map›Paper›PMID 36320702›Full record

ArticleChemical science2022

Distinct core glycan and

David S Roberts, Morgan Mann, Brad H Li, Donguk Kim, Allan R Braiser, Song Jin, Ying Ge

Abstract read
In one paragraph

Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  8. Review
  9. Article
  10. Variations inBiomolecules · 2023
    Article
  11. Article
  12. Review
  13. Review
  14. Review
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.

David S RobertsDepartment of Chemistry, University of Wisconsin-Madison WI 53706 USA dsroberts@wisc.edu ying.ge@wisc.edu.ORCID https://orcid.org/0000-0002-0478-4987
Morgan MannDepartment of Medicine, School of Medicine and Public Health University of Wisconsin-Madison WI 53705 USA.ORCID https://orcid.org/0000-0001-6623-9522
Brad H LiDepartment of Cell and Regenerative Biology, University of Wisconsin-Madison WI 53705 USA.ORCID https://orcid.org/0000-0002-3664-0419
Donguk KimDepartment of Cell and Regenerative Biology, University of Wisconsin-Madison WI 53705 USA.ORCID https://orcid.org/0000-0003-1966-6710
Allan R BraiserDepartment of Medicine, School of Medicine and Public Health University of Wisconsin-Madison WI 53705 USA.
Song JinDepartment of Chemistry, University of Wisconsin-Madison WI 53706 USA dsroberts@wisc.edu ying.ge@wisc.edu.ORCID https://orcid.org/0000-0001-8693-7010
Ying GeDepartment of Chemistry, University of Wisconsin-Madison WI 53706 USA dsroberts@wisc.edu ying.ge@wisc.edu.ORCID https://orcid.org/0000-0001-5211-6812

Funding

Top Down Proteomics Of Myofilaments In Heart FailureR01HL096971 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2011 to 2021
$3.3M
Enabling Top-Down Proteomics through Materials Chemistry and NanotechnologyR01GM117058 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING, JIN, SONG · 2015 to 2023
$2.7M
Ultra High Resolution Mass Spectrometer for Biomedical ResearchS10OD018475 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2015 to 2015
$2.0M
MASH Explorer, a Comprehensive Software Environment for Top-Down ProteomicsR01GM125085 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2018 to 2021
$1.2M
NHLBI NIH HHS R01 HL096971NIGMS NIH HHS R01 GM117058NIGMS NIH HHS R01 GM125085NIH HHS S10 OD018475
6 · The paper itself

Abstract

The SARS-CoV-2 Omicron (B.1.1.529) variant possesses numerous spike (S) mutations particularly in the S receptor-binding domain (S-RBD) that significantly improve transmissibility and evasion of neutralizing antibodies. But exactly how the mutations in the Omicron variant enhance viral escape from immunological protection remains to be understood. The S-RBD remains the principal target for neutralizing antibodies and therapeutics, thus new structural insights into the Omicron S-RBD and characterization of the post-translational glycosylation changes can inform rational design of vaccines and therapeutics. Here we report the molecular variations and

Identifiers

PMID36320702
PMCPMC9491206

What Socratic 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 Socratic graph.