Site-Specific N-Glycoproteomic Analysis Reveals Upregulated Sialylation and Core Fucosylation during Transient Regeneration Loss in Neonatal Mouse Hearts

2020 ◽  
Vol 19 (8) ◽  
pp. 3191-3200 ◽  
Author(s):  
Jun Li ◽  
Li Jia ◽  
Zhifang Hao ◽  
Yintai Xu ◽  
Jiechen Shen ◽  
...  
Keyword(s):  
Neonatal Mouse ◽  
Site Specific ◽  
Core Fucosylation

scholarly journals Label-free relative quantification of alpha-2-macroglobulin site-specific core-fucosylation in pancreatic cancer by LC-MS/MS

2013 ◽  
pp. n/a-n/a ◽  
Author(s):  
Zhenxin Lin ◽  
Haidi Yin ◽  
Andy Lo ◽  
Mack T. Ruffin ◽  
Michelle A. Anderson ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Relative Quantification ◽  
Label Free ◽  
Site Specific ◽  
Free Relative ◽  
Core Fucosylation

scholarly journals Mass-Selected Site-Specific Core-Fucosylation of Serum Proteins in Hepatocellular Carcinoma

2015 ◽  
Vol 14 (11) ◽  
pp. 4876-4884 ◽  
Author(s):  
Haidi Yin ◽  
Zhijing Tan ◽  
Jing Wu ◽  
Jianhui Zhu ◽  
Kerby A. Shedden ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Serum Proteins ◽  
Site Specific ◽  
Core Fucosylation

scholarly journals Mass-Selected Site-Specific Core-Fucosylation of Ceruloplasmin in Alcohol-Related Hepatocellular Carcinoma

2014 ◽  
Vol 13 (6) ◽  
pp. 2887-2896 ◽  
Author(s):  
Haidi Yin ◽  
Zhenxin Lin ◽  
Song Nie ◽  
Jing Wu ◽  
Zhijing Tan ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Site Specific ◽  
Core Fucosylation

scholarly journals Site-specific glycoproteomic analysis revealing increased core-fucosylation on FOLR1 enhances folate uptake capacity of HCC cells to promote EMT

Theranostics ◽  
2021 ◽  
Vol 11 (14) ◽  
pp. 6905-6921
Author(s):  
Li Jia ◽  
Jun Li ◽  
Pengfei Li ◽  
Didi Liu ◽  
Jing Li ◽  
...  
Keyword(s):  
Uptake Capacity ◽  
Site Specific ◽  
Core Fucosylation ◽  
Hcc Cells

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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