Evidence map›Paper›PMID 26238325›Full record

ArticleJournal of the American Society for Mass Spectrometry2015

Identification of Two Novel Modifications at Tryptophan Residues.

Shuzhen Zheng, Kai Zhang, Shanshan Tian, Xiwen He, Yukui Zhang

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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3 · Its place in the literature

Who cites it

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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

5 authors.

Shuzhen ZhengDepartment of Chemistry, Nankai University, Tianjin, 300071, People's Republic of China.
Kai ZhangDepartment of Chemistry, Nankai University, Tianjin, 300071, People's Republic of China. zhangkai@nankai.edu.cn.
Shanshan TianDepartment of Biochemistry and Molecular Biology & Tianjin Key Laboratory of Medical Epigenetics, Tianjin Medical University, Tianjin, 300070, People's Republic of China.
Xiwen HeDepartment of Chemistry, Nankai University, Tianjin, 300071, People's Republic of China.
Yukui ZhangDepartment of Chemistry, Nankai University, Tianjin, 300071, People's Republic of China. ykzhang@dicp.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein post-translational modifications (PTMs) play important roles in cellular physiology. Mass spectrometry (MS) has been developed into a powerful tool to identify all possible protein modifications. Herein, we describe our efforts to deduce the structures of two unknown modifications at tryptophan (Trp) residues (W + 92 Da and W + 108 Da). The two modifications were further confirmed by aligning the MS/MS fragmentation of synthetic peptide with in-vivo peptide identified. Finally, the mimic experiment elucidated how two Trp modifications occur. This study, therefore, expands current knowledge of Trp modifications.

Indexed as

Protein Processing, Post-TranslationalProteomicsTandem Mass SpectrometryTryptophanTryptophanMass spectrometryPost-translational modificationsProteomicsTryptophan modifications

Identifiers

PMID26238325

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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.