Evidence map›Paper›PMID 30557666›Full record

ArticleJournal of proteomics2019

Comprehensive identification of protein disulfide bonds with pepsin/trypsin digestion, Orbitrap HCD and Spectrum Identification Machine.

Chuanlong Cui, Tong Liu, Tong Chen, Johanna Lu, Ian Casaren, Diogo Borges Lima, Paulo Costa Carvalho, Annie Beuve, Hong Li

Abstract read
In one paragraph

Article in Journal of proteomics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
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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

9 authors.

Chuanlong CuiCenter for Advanced Proteomics Research and Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School and Cancer Institute of New Jersey, Newark, NJ 07103, USA.
Tong LiuCenter for Advanced Proteomics Research and Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School and Cancer Institute of New Jersey, Newark, NJ 07103, USA.
Tong ChenCenter for Advanced Proteomics Research and Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School and Cancer Institute of New Jersey, Newark, NJ 07103, USA.
Johanna LuCenter for Advanced Proteomics Research and Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School and Cancer Institute of New Jersey, Newark, NJ 07103, USA.
Ian CasarenCenter for Advanced Proteomics Research and Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School and Cancer Institute of New Jersey, Newark, NJ 07103, USA.
Diogo Borges LimaMass Spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, Paris, France.
Paulo Costa CarvalhoLaboratory for Structural and Computational Proteomics, Carlos Chagas Institute, Fiocruz Paraná, Brazil.
Annie BeuveDepartment of Pharmacology, Physiology and Neuroscience, Rutgers University - New Jersey Medical School, Newark, NJ 07103, USA.
Hong LiCenter for Advanced Proteomics Research and Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School and Cancer Institute of New Jersey, Newark, NJ 07103, USA. Electronic address: liho2@rutgers.edu.

Funding

Rutgers Mass Spectrometry Core for Integrative Neuroscience ResearchP30NS046593 · NINDS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI LOBEL, PETER · 2004 to 2018
$9.9M
Regulation of Soluble Guanylyl Cyclase, the NO-ReceptorR01GM067640 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI BEUVE, ANNIE V · 2003 to 2021
$5.8M
NO signaling by a Soluble Guanylyl Cyclase-Thioredoxin transnitrosation complexR01GM112415 · NIGMS · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI BEUVE, ANNIE V · 2015 to 2023
$3.5M
Orbitrap Fusion Lumos Tribrid MS System for Proteomics Research at Rutgers Newark CampusS10OD025047 · OD · RBHS-NEW JERSEY MEDICAL SCHOOL · PI LI, HONG · 2018 to 2018
$1.1M
NIGMS NIH HHS R01 GM067640NIGMS NIH HHS R01 GM112415NIH HHS S10 OD025047NINDS NIH HHS P30 NS046593
6 · The paper itself

Abstract

Disulfide bonds (SS) are post-translational modifications important for the proper folding and stabilization of many cellular proteins with therapeutic uses, including antibodies and other biologics. With budding advances of biologics and biosimilars, there is a mounting need for a robust method for accurate identification of SS. Even though several mass spectrometry methods have emerged for this task, their practical use rests on the broad effectiveness of both sample preparation methods and bioinformatics tools. Here we present a new protocol tailored toward mapping SS; it uses readily available reagents, instruments, and software. For sample preparation, a 4-h pepsin digestion at pH 1.3 followed by an overnight trypsin digestion at pH 6.5 can maximize the release of SS-containing peptides from non-reduced proteins, while minimizing SS scrambling. For LC/MS/MS analysis, SS-containing peptides can be efficiently fragmented with HCD in a Q Exactive Orbitrap mass spectrometer, preserving SS for subsequent identification. Our bioinformatics protocol describes how we tailored our freely downloadable and easy-to-use software, Spectrum Identification Machine for Cross-Linked Peptides (SIM-XL), to minimize false identification and facilitate manual validation of SS-peptide mass spectra. To substantiate this optimized method, we've comprehensively identified 14 out of 17 known SS in BSA. SIGNIFICANCE: Comprehensive and accurate identification of SS in proteins is critical for elucidating protein structures and functions. Yet, it is far from routine to accomplish this task in many analytical or core laboratories. Numerous published methods require complex sample preparation methods, specialized mass spectrometers and cumbersome or proprietary software tools, thus cannot be easily implemented in unspecialized laboratories. Here, we describe a robust and rapid SS mapping approach that utilizes readily available reagents, instruments, and software; it can be easily implemented in any analytical core laboratories, and tested for its impact on the research community.

Indexed as

Mass SpectrometryAnimalsCattleChickensDisulfidesPepsin APeptidesTrypsinDisulfidesPepsin APeptidesTrypsinHCDPepsinProtein disulfide bondSIM-XLTandem mass spectrometryTrypsin

Identifiers

PMID30557666
PMCPMC6414265

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Registered trials

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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.