Protein sialylation

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1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands 2Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, The Netherlands (2)
Chinese Academy of Sciences Shanghai Institute of Materia Medica (2)
1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands 2Netherlands Proteomics Center, Padualaan 8, 3584 CH, Utrecht, The Netherlands (1)
1Department of Chemistry and Sarafan Chem-H, Stanford University, Stanford, CA 94305, USA 2Howard Hughes Medical Institute, Stanford, CA 94305, USA (1)
1School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, USA. Email: lingjun.li@wisc.edu 2Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53705, USA. (1)
ARC Centre of Excellence in Synthetic Biology, Macquarie University (1)
Associate professor at Macquarie University, Sydney, Australia Visiting professor at Institute for Glyco-core Research (iGCORE), Nagoya Univeristy, Aichi, Japan (1)
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Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and Technology, N0. 1037 Luoyudong Road, Hongshan District, Wuhan 430074 (1)
Department of Cellular and Molecular Medicine Translational Glycobiology Institute Herbert Wertheim College of Medicine Florida International University Miami, FL, USA (1)
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Department of chemistry and biochemistry, Texas Tech University, Lubbock, Texas, USA, 79413. (1)
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Division of Hematology & Medical Oncology, Oregon Health & Science University, Portland, OR. (1)
Experimental Pathology and Therapeutics Group, IPO Porto Research Center (CI-IPOP), Portuguese Oncology Institute (IPO Porto), 4200-072 Porto, Portugal (1)
George State University (1)
GlycoProteomics Laboratory, Department of Parasitology, ICB, University of São Paulo, Sao Paulo, Brazil (1)

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Serum protein N-glycosylation changes in multiple myeloma

BACKGROUND: Multiple myeloma is characterized by clonal proliferation of malignant plasma cells in the bone marrow that produce monoclonal immunoglobulins. N-glycosylation changes of these monoclonal immunoglobulins have been reported in multiple myeloma, but previous studies on...

2022-04-27 | MTBLS676 | MetaboLights

Protein Sialylation Remodels Chromatin Architecture

PRJNA718724 | ENA

Inherited defect in ST6GalNAc1 reveals roles of sialylation in intestinal homeostasis

PRJNA762059 | ENA

Stable Protein Sialylation in Physcomitrella.

Not available

S-EPMC7775405 | biostudies-literature

Identifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry

Precise assignment of sialylation linkages at the glycopeptide level is of importance in bottom-up glycoproteomics, and is also an indispensable step to understand the function of glycoproteins in pathogen-host interactions and cancer progression. Even though some efforts have been dedicated to the ...

ORGANISM(S): Homo sapiens (Human)

2020-04-21 | PXD016151 | Pride

Engineering of complex protein sialylation in plants.

Not available

S-EPMC5003249 | biostudies-literature

Inherited defect in ST6GalNAc1 reveals roles of sialylation in intestinal homeostasis

PRJNA761456 | ENA

Inherited defect in ST6GalNAc1 reveals roles of sialylation in intestinal homeostasis

PRJNA761457 | ENA

Inherited defect in ST6GalNAc1 reveals roles of sialylation in intestinal homeostasis

Chronic inflammatory bowel disease (IBD) causes disability, suffering and risk of colon cancer in over 30 million people globally. Here, we investigate 3 kindreds of IBD with mutations in the N-acetylgalactosamide alpha-2,6-sialyltransferase 1/ST6GALNAC1 (ST6) glycosyltransferase gene that is unique...

ORGANISM(S): Mus musculus

2022-03-16 | GSE183821 | GEO

In planta protein sialylation through overexpression of the respective mammalian pathway.

Not available

S-EPMC2871460 | biostudies-literature

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BACKGROUND: Multiple myeloma is characterized by clonal proliferation of malignant plasma cells in the bone marrow that produce monoclonal immunoglobulins. N-glycosylation changes of these monoclonal immunoglobulins have been reported in multiple myeloma, but previous studies on...

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