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Special Issue "CZE/LC-MS-based Proteomics"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Analytical Chemistry".

Deadline for manuscript submissions: 31 August 2019

Special Issue Editor

Guest Editor
Dr. Zhenbin Zhang

Department of chemistry and biochemistry, University of Notre Dame, Notre Dame, IN 46556-5670, USA
Website | E-Mail
Interests: study of proteome using liquid chromatogray (LC) and capillary zone electrophoresis-mass spectrometry (CZE-MS); developing microreactors and novel sample preparation methods for proteomics; single cell proteomics

Special Issue Information

Dear Colleagues,

Mass spectrometry (MS)-based proteomics has established itself as an indispensable technology to interpret the information encoded in genomes. Its plays a critical role in molecular and cellular biology, as well as systems biology, due to its ability to identify and, increasingly, precisely quantifying thousands of proteins from complex samples. Although it has achieved tremendous recent success, MS-based proteomics still faces various technical challenges. The Special Issue of Molecules, entitled “Capillary Zone Electrophoresis/Liquid Chromatography(CZE/LC)-MS-Based Proteomics”, welcomes original papers and comprehensive reviews focused on, but not limited, to the improvement of techniques related to CZE/LC-MS-based proteomics, such as novel methods for sample preparation, novel separation techniques, advancements in mass spectrometers, improved methods (software) for data acquisition and analyses, and the applications of MS-based proteomics techniques, such as the study of post-translational modifications (PTMs, e.g., phosphoproteomics, glycoproteomics, etc.) or protein–protein interactions, clinical diagnoses, host cell protein analyses, as well as single-cell proteomics. Please refer to the list of keywords for further topics.

Dr. Zhenbin 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 papers will be 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. Molecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). 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

  • Bottom up proteomics
  • Top down proteomics
  • Sample preparation
  • CZE/LC-MS
  • Post-translational modifications (e.g., phosphoproteomics, glycoproteomics, etc.)
  • Protein-protein interactions
  • Clinical diagnosis
  • Single cell proteomics
  • Data analysis tools for proteomics

Published Papers (1 paper)

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Research

Open AccessArticle Phosphoproteomics of Retinoblastoma: A Pilot Study Identifies Aberrant Kinases
Molecules 2018, 23(6), 1454; https://doi.org/10.3390/molecules23061454
Received: 18 April 2018 / Revised: 31 May 2018 / Accepted: 7 June 2018 / Published: 15 June 2018
PDF Full-text (3396 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Retinoblastoma is a malignant tumour of the retina which most often occurs in children. Earlier studies on retinoblastoma have concentrated on the identification of key players in the disease and have not provided information on activated/inhibited signalling pathways. The dysregulation of protein phosphorylation
[...] Read more.
Retinoblastoma is a malignant tumour of the retina which most often occurs in children. Earlier studies on retinoblastoma have concentrated on the identification of key players in the disease and have not provided information on activated/inhibited signalling pathways. The dysregulation of protein phosphorylation in cancer provides clues about the affected signalling cascades in cancer. Phosphoproteomics is an ideal tool for the study of phosphorylation changes in proteins. Hence, global phosphoproteomics of retinoblastoma (RB) was carried out to identify signalling events associated with this cancer. Over 350 proteins showed differential phosphorylation in RB compared to control retina. Our study identified stress response proteins to be hyperphosphorylated in RB which included H2A histone family member X (H2AFX) and sirtuin 1. In particular, Ser140 of H2AFX also known as gamma-H2AX was found to be hyperphosphorylated in retinoblastoma, which indicated the activation of DNA damage response pathways. We also observed the activation of anti-apoptosis in retinoblastoma compared to control. These observations showed the activation of survival pathways in retinoblastoma. The identification of hyperphosphorylated protein kinases including Bromodomain containing 4 (BRD4), Lysine deficient protein kinase 1 (WNK1), and Cyclin-dependent kinase 1 (CDK1) in RB opens new avenues for the treatment of RB. These kinases can be considered as probable therapeutic targets for RB, as small-molecule inhibitors for some of these kinases are already in clinical trials for the treatment other cancers. Full article
(This article belongs to the Special Issue CZE/LC-MS-based Proteomics)
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