Evidence map›Paper›PMID 35320434›Full record

ArticleJournal of biomolecular NMR2022

Caitlin M Quinn, Shiping Xu, Guangjin Hou, Qingqing Chen, Deepak Sail, R Andrew Byrd, Sharon Rozovsky

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

Article in Journal of biomolecular NMR, 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
–field-weighted citation impact, top 98% 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, 0 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 4 institutions in 2 countries.

Caitlin M QuinnDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Shiping XuDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Guangjin HouState Key Laboratory of Catalysis, National Laboratory for Clean Energy, 2011-Collaborative Innovation Center of Chemistry for Energy Materials, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Zhongshan Road 457, Dalian, 116023, China.
Qingqing ChenDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Deepak SailChemistry and Synthesis Center, National Heart Lung and Blood Institute, Bethesda, MD, USA.
R Andrew ByrdCenter for Cancer Research, National Cancer Institute, Frederick, MD, USA.
Sharon RozovskyDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA. rozovsky@udel.edu.ORCID http://orcid.org/0000-0003-4902-0777
University of Delaware · USDalian Institute of Chemical Physics · CNNational Cancer Institute · USNational Heart Lung and Blood Institute · US

Funding

This renovation project will create over 1455 sq. ft. of state- of-the-art reseaP20GM104316 · NIGMS · UNIVERSITY OF DELAWARE · PI FOX, JOSEPH M · 2014 to 2024
$26.8M
Pilot Research Subproject ProgramP30GM110758 · NIGMS · UNIVERSITY OF DELAWARE · PI PATEL, SANDEEP · 2014 to 2018
$5.8M
Methods DevelopmentZIABC011132 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$4.6M
Chemistry-Biology Interface Predoctoral Training Grant 2024-2029T32GM133395 · NIGMS · UNIVERSITY OF DELAWARE · PI Catherine Leimkuhler Grimes · 2019 to 2026
$3.7M
Molecular Design of Advanced BiomaterialsP20GM103541 · NIGMS · UNIVERSITY OF DELAWARE · PI POLENOVA, TATYANA · 2012 to 2012
$2.1M
national science foundation 1616178NIGMS NIH HHS P20 GM103541NIGMS NIH HHS P20 GM104316NIGMS NIH HHS P20GM104316NIGMS NIH HHS P30 GM110758NIGMS NIH HHS P30GM110758NIGMS NIH HHS T32 GM133395NIGMS NIH HHS T32-GM133395
6 · The paper itself

Abstract

Sulfur-containing sites in proteins are of great importance for both protein structure and function, including enzymatic catalysis, signaling pathways, and recognition of ligands and protein partners. Selenium-77 is an NMR active spin-1/2 nucleus that shares many physiochemical properties with sulfur and can be readily introduced into proteins at sulfur sites without significant perturbations to the protein structure. The sulfur-containing amino acid methionine is commonly found at protein-protein or protein-ligand binding sites. Its selenium-containing counterpart, selenomethionine, has a broad chemical shift dispersion useful for NMR-based studies of complex systems. Methods such as (

Indexed as

SeleniumLigandsNuclear Magnetic Resonance, BiomolecularProteinsSelenomethionineSulfurLigandsProteinsSeleniumSelenomethionineSulfur77SeGB1Selenium NMRSelenomethionine

Identifiers

PMID35320434
PMCPMC9195563
OpenAlexW4220954767

What OpenQuestion holds

Textmetadata
LicenceTDM
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.