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Advanced Glycoproteomics Research
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Advanced Glycoproteomics Research

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 May 2024) | Viewed by 886

Special Issue Editor

Dr. Yang Zhang

E-Mail Website
Guest Editor
Institutes of Biomedical Sciences, Fudan University, 138 Yixueyuan Road, Shanghai 200032, China
Interests: bioinformatics; proteomics; genomics; system biology; glycosylation

Special Issue Information

Dear Colleagues, 

Glycosylation, a modification that occurs on amino acids, is a highly prevalent post-translational modification in cells. Glycosylation plays important biological functions, particularly in glycoproteins on the cell membrane, such as the immunoglobulin superfamily and integrin receptors, which are responsible for cell signaling and communication. Mass spectrometry is a high-throughput technique that can be used to identify glycoproteins and can even achieve site-specific glycan structures. Characterizing glycoproteins in biological samples using high-throughput approaches, including subsequent biochemical validation, is a cutting-edge direction for deciphering the biological functions of site-specific glycosylation.

Dr. Yang Zhang
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • glycosylation
  • glycoproteomics
  • site-specific glycan structures
  • glycan function
  • biochemical validation

Published Papers (1 paper)

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Research

11 pages, 3759 KiB  
Article
Bidirectional Two-Sample Mendelian Randomization Study of Immunoglobulin G N-Glycosylation and Senescence-Associated Secretory Phenotype
by Haotian Wang, Di Liu, Xiaoni Meng, Wenxin Sun, Cancan Li, Huimin Lu, Deqiang Zheng, Lijuan Wu, Shengzhi Sun and Youxin Wang
Int. J. Mol. Sci. 2024, 25(12), 6337; https://doi.org/10.3390/ijms25126337 - 7 Jun 2024
Viewed by 555
Abstract
Observational studies revealed changes in Immunoglobulin G (IgG) N-glycosylation during the aging process. However, it lacks causal insights and remains unclear in which direction causal relationships exist. The two-sample bidirectional Mendelian randomization (MR) design was adopted to explore causal associations between IgG N-glycans [...] Read more.
Observational studies revealed changes in Immunoglobulin G (IgG) N-glycosylation during the aging process. However, it lacks causal insights and remains unclear in which direction causal relationships exist. The two-sample bidirectional Mendelian randomization (MR) design was adopted to explore causal associations between IgG N-glycans and the senescence-associated secretory phenotype (SASP). Inverse variance weighted (IVW) and Wald ratio methods were used as the main analyses, supplemented by sensitivity analyses. Forward MR analyses revealed causal associations between the glycan peak (GP) and SASP, including GP6 (odds ratio [OR] = 0.428, 95% confidence interval [CI] = 0.189–0.969) and GP17 (OR = 0.709, 95%CI = 0.504–0.995) with growth/differentiation factor 15 (GDF15), GP19 with an advanced glycosylation end-product-specific receptor (RAGE) (OR = 2.142, 95%  CI  = 1.384–3.316), and GP15 with matrix metalloproteinase 2 (MMP2) (OR = 1.136, 95%  CI =1.008–1.282). The reverse MR indicated that genetic liability to RAGE was associated with increased levels of GP17 (OR = 1.125, 95%  CI  = 1.003–1.261) and GP24 (OR = 1.222, 95%  CI  = 1.046–1.428), while pulmonary and activation-regulated chemokines (PARC) exhibited causal associations with GP10 (OR = 1.269, 95%  CI  = 1.048–1.537) and GP15 (OR = 1.297, 95%  CI = 1.072–1.570). The findings provided suggested evidence on the bidirectional causality between IgG N-glycans and SASP, which might reveal potential regulatory mechanisms. Full article
(This article belongs to the Special Issue Advanced Glycoproteomics Research)
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