Evidence map›Paper›PMID 32008172›Full record

ArticleJournal of biomolecular NMR2020

Mass spectrometry assisted arginine side chains assignment of NMR resonances in natural abundance proteins.

Jingjing Lu, Fengmei Zhou, Wanhui Liu, Fei Yu

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

4 authors.

Jingjing LuSchool of Pharmacy, Key Laboratory of Molecular Pharmacology and Drug Evaluation (Yantai University), Ministry of Education, Collaborative Innovation Center of Advanced Drug Delivery System and Biotech Drugs in Universities of Shandong, Yantai University, Yantai, China.
Fengmei ZhouState Key Laboratory of Long-Acting and Targeting Drug Delivery Technologies, Shandong Luye Pharmaceutical Co. Ltd., Yantai, China.
Wanhui LiuSchool of Pharmacy, Key Laboratory of Molecular Pharmacology and Drug Evaluation (Yantai University), Ministry of Education, Collaborative Innovation Center of Advanced Drug Delivery System and Biotech Drugs in Universities of Shandong, Yantai University, Yantai, China.
Fei YuSchool of Pharmacy, Key Laboratory of Molecular Pharmacology and Drug Evaluation (Yantai University), Ministry of Education, Collaborative Innovation Center of Advanced Drug Delivery System and Biotech Drugs in Universities of Shandong, Yantai University, Yantai, China. yufei@luye.com.ORCID http://orcid.org/0000-0001-7068-7360

Funding

National Natural Science Foundation of China No. 81773679
6 · The paper itself

Abstract

Arginine side chains play critical roles in many protein-ligand interactions and enzyme catalysis. Unambiguous resonance assignment is a prerequisite for the nuclear magnetic resonance (NMR) spectroscopy studies of arginine side chains dynamics and hydrogen exchange properties from which one can expect to elucidate in more detail the roles of arginine residues in protein structure and function. Here we present a new mass spectrometry (MS)-based method for assigning the side-chain resonances of arginine residues in 2D

Indexed as

Isotope LabelingMass SpectrometryNuclear Magnetic Resonance, BiomolecularArginineChromatography, LiquidHumansUbiquitinArginineUbiquitinArginineGuanidino groupsLC–MSNMRSide chainsUbiquitin

Identifiers

PMID32008172

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.