NDLI: SWATH-MS Glycoproteomics Reveals Consequences of Defects in the Glycosylation Machinery.

Please wait, while we are loading the content...

Apolipoprotein E*4 (APOE*4) Genotype Is Associated with Altered Levels of Glutamate Signaling Proteins and Synaptic Coexpression Networks in the Prefrontal Cortex in Mild to Moderate Alzheimer Disease.

A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.

Proteomics in India: A Report on a Brainstorming Meeting at Hyderabad, India.

Characterization of Dynamic UbR-Proteasome Subcomplexes by In vivo Cross-linking (X) Assisted Bimolecular Tandem Affinity Purification (XBAP) and Label-free Quantitation.

Global Membrane Protein Interactome Analysis using In vivo Crosslinking and Mass Spectrometry-based Protein Correlation Profiling.

Multidimensional Proteomics Reveals a Role of UHRF2 in the Regulation of Epithelial-Mesenchymal Transition (EMT).

Identification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics*

The Metacaspase (Mca1p) Restricts O-glycosylation During Farnesol-induced Apoptosis in Candida albicans.

Uncovering a Dual Regulatory Role for Caspases During Endoplasmic Reticulum Stress-induced Cell Death.

Identification of Candidate Cyclin-dependent kinase 1 (Cdk1) Substrates in Mitosis by Quantitative Phosphoproteomics.

Proteomics-driven Antigen Discovery for Development of Vaccines Against Gonorrhea.

A Contra Capture Protein Array Platform for Studying Post-translationally Modified (PTM) Auto-antigenomes*

The Pathogenesis of the Demyelinating Form of Guillain-Barre Syndrome (GBS): Proteo-peptidomic and Immunological Profiling of Physiological Fluids.

Protein Markers Predict Survival in Glioma Patients.

Differential Neuroproteomic and Systems Biology Analysis of Spinal Cord Injury.

The Importance of Non-accessible Crosslinks and Solvent Accessible Surface Distance in Modeling Proteins with Restraints From Crosslinking Mass Spectrometry.

SWATH Mass Spectrometry Performance Using Extended Peptide MS/MS Assay Libraries.

Identification and Characterization of Potential Biomarkers by Quantitative Tissue Proteomics of Primary Lung Adenocarcinoma.

Quantitative Mass Spectrometry Reveals Changes in Histone H2B Variants as Cells Undergo Inorganic Arsenic-Mediated Cellular Transformation*

Mapping Proteoforms and Protein Complexes From King Cobra Venom Using Both Denaturing and Native Top-down Proteomics.

Year: 2016 Volume: 15 Issue: 6

Year: 2016 Volume: 15 Issue: 5

Year: 2016 Volume: 15 Issue: 4

Year: 2016 Volume: 15 Issue: 3

Year: 2016 Volume: 15 Issue: 2

Year: 2016 Volume: 15 Issue: 1

Year: 2015 Volume: 14

Year: 2014 Volume: 13

Year: 2013 Volume: 12

Year: 2012 Volume: 11

Year: 2011 Volume: 10

SWATH-MS Glycoproteomics Reveals Consequences of Defects in the Glycosylation Machinery.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zacchi, Lucia F. Schulz, Benjamin L.
Description	Country affiliation: Argentina Author Affiliation: Zacchi LF ( From the School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia); Schulz BL ( From the School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia)
Abstract	Glycan macro- and microheterogeneity have profound impacts on protein folding and function. This heterogeneity can be regulated by physiological or environmental factors. However, unregulated heterogeneity can lead to disease, and mutations in the glycosylation process cause a growing number of Congenital Disorders of Glycosylation. We systematically studied how mutations in the N-glycosylation pathway lead to defects in mature proteins using all viable Saccharomyces cerevisiae strains with deletions in genes encoding Endoplasmic Reticulum lumenal mannosyltransferases (Alg3, Alg9, and Alg12), glucosyltransferases (Alg6, Alg8, and Die2/Alg10), or oligosaccharyltransferase subunits (Ost3, Ost5, and Ost6). To measure the changes in glycan macro- and microheterogeneity in mature proteins caused by these mutations we developed a SWATH-mass spectrometry glycoproteomics workflow. We measured glycan structures and occupancy on mature cell wall glycoproteins, and relative protein abundance, in the different mutants. All mutants showed decreased glycan occupancy and altered cell wall proteomes compared with wild-type cells. Mutations in earlier mannosyltransferase or glucosyltransferase steps of glycan biosynthesis had stronger hypoglycosylation phenotypes, but glucosyltransferase defects were more severe. ER mannosyltransferase mutants displayed substantial global changes in glycan microheterogeneity consistent with truncations in the glycan transferred to protein in these strains. Although ER glucosyltransferase and oligosaccharyltransferase subunit mutants broadly showed no change in glycan structures, ost3Δ cells had shorter glycan structures at some sites, consistent with increased protein quality control mannosidase processing in this severely hypoglycosylating mutant. This method allows facile relative quantitative glycoproteomics, and our results provide insights into global regulation of site-specific glycosylation.
File Format	HTM / HTML
ISSN	15359476
e-ISSN	15359484
Journal	Molecular & Cellular Proteomics
Issue Number	7
Volume Number	15
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2016-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Proteomics
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

SWATH Mass Spectrometry Performance Using Extended Peptide MS/MS Assay Libraries.

Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs).

Large-scale quantitative glycoproteomics analysis of site-specific glycosylation occupancy.

Mass Spectrometry Based Glycoproteomics—From a Proteomics Perspective*

mzDB: A File Format Using Multiple Indexing Strategies for the Efficient Analysis of Large LC-MS/MS and SWATH-MS Data Sets*

Development of Immobilized Enzyme Reactors for the characterization of the glycosylation heterogeneity of a protein

Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2)

Opening a SWATH Window on Posttranslational Modifications: Automated Pursuit of Modified Peptides.

Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD.

SWATH-MS Glycoproteomics Reveals Consequences of Defects in the Glycosylation Machinery.

Similar Documents

SWATH Mass Spectrometry Performance Using Extended Peptide MS/MS Assay Libraries.

Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs).

Large-scale quantitative glycoproteomics analysis of site-specific glycosylation occupancy.

Mass Spectrometry Based Glycoproteomics—From a Proteomics Perspective*

mzDB: A File Format Using Multiple Indexing Strategies for the Efficient Analysis of Large LC-MS/MS and SWATH-MS Data Sets*

Development of Immobilized Enzyme Reactors for the characterization of the glycosylation heterogeneity of a protein

Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2)

Opening a SWATH Window on Posttranslational Modifications: Automated Pursuit of Modified Peptides.

Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD.

SWATH-MS Glycoproteomics Reveals Consequences of Defects in the Glycosylation Machinery.