Evidence map›Paper›PMID 20138783›Full record

ArticleJournal of the American Society for Mass Spectrometry2010

Amino acid influence on copper binding to peptides: cysteine versus arginine.

Zhaoxiang Wu, Francisco A Fernandez-Lima, David H Russell

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 51 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

3 authors at 1 institution in 1 country.

Zhaoxiang WuDepartment of Chemistry, Texas A and M University, College Station, Texas 77843, USA.
Francisco A Fernandez-Lima
David H Russell
Texas A&M University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and theoretical calculations [density functional theory (DFT)] were utilized to investigate the influence of cysteine side chain on Cu(+) binding to peptides and how Cu(+) ions competitively interact with cysteine (-SH/SO(3)H) versus arginine. Results from theoretical and experimental (fragmentation reactions) studies on [M + Cu](+) and [M + 2Cu - H](+) ions suggest that cysteine side chains (-SH) and cysteic acid (-SO(3)H) are important Cu(+) ligands. For example, we show that Cu(+) ions are competitively coordinated to the -SH or SO(3)H groups; however, we also present evidence that the proton of the SH/SO(3)H group is mobile and can be transferred to the arginine guanidine group. For [M + 2Cu - H](+) ions, deprotonation of the -SH/SO(3)H group is energetically more favorable than that of the carboxyl group, and the resulting thiolate/sulfonate group plays an important role in the coordination structure of [M + 2Cu - H](+) ions, as well as the fragmentation patterns.

Indexed as

Models, ChemicalArginineComputer SimulationCopperCysteinePeptidesSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationArginineCopperCysteinePeptides

Identifiers

PMID20138783
OpenAlexW2071041701

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.