Paper · 1443554
A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase F in 18O-labeled water.
Gonzalez J and 6 others. Anal Biochem, 1992. Cited by 92 papers, by iCite.
11 sourcespapers-2026-11-12-0.1.0
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ConductScience Library. A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase F in 18O-labeled water. Papers, record 1443554. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/1443554
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Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase F in 18O-labeled water.
- PubMed
Topics16
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Amidohydrolases | Major topic |
| Asparagine | Major topic |
| Carbohydrates | Major topic |
| Glycoproteins | Major topic |
| alpha-Amylases | Major topic |
| Amino Acid Sequence | |
| Bacillus | |
| Carbohydrate Sequence | |
| Chromatography, High Pressure Liquid | |
| Electrophoresis, Polyacrylamide Gel | |
| Glycosylation | |
| Molecular Sequence Data | |
| Oxygen Isotopes | |
| Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase | |
| Recombinant Proteins | |
| Spectrometry, Mass, Fast Atom Bombardment |
Source PubMed
Grants0
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Trials0
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Comments and corrections0
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References0
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Cited by24
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 92 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 42,395,976 | Site-Specific Analysis of Bone Morphogenetic Protein Receptor Type 2 N‑Glycosylation Reveals High Heterogeneity at Site Involved in Ligand Binding. | ACS Omega | 2026 | https://conductscience.org/library/papers/42395976 | PubMed |
| 36,948,700 | DeGlyPHER: Highly sensitive site-specific analysis of N-linked glycans on proteins. | Methods Enzymol | 2023 | https://conductscience.org/library/papers/36948700 | PubMed |
| 35,712,026 | The antibody-binding Fc gamma receptor IIIa / CD16a is N-glycosylated with high occupancy at all five sites. | Curr Res Immunol | 2022 | https://conductscience.org/library/papers/35712026 | PubMed |
| 35,163,546 | Strategies for Proteome-Wide Quantification of Glycosylation Macro- and Micro-Heterogeneity. | Int J Mol Sci | 2022 | https://conductscience.org/library/papers/35163546 | PubMed |
| 34,869,209 | Site-Specific Glycosylation Patterns of the SARS-CoV-2 Spike Protein Derived From Recombinant Protein and Viral WA1 and D614G Strains. | Front Chem | 2021 | https://conductscience.org/library/papers/34869209 | PubMed |
| 32,350,911 | Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships. | Mass Spectrom Rev | 2020 | https://conductscience.org/library/papers/32350911 | PubMed |
| 29,769,321 | Lectin-mediated binding and sialoglycans of porcine surfactant protein D synergistically neutralize influenza A virus. | J Biol Chem | 2018 | https://conductscience.org/library/papers/29769321 | PubMed |
| 27,960,262 | Chemical Glycoproteomics. | Chem Rev | 2016 | https://conductscience.org/library/papers/27960262 | PubMed |
| 27,491,298 | N-linked glycosite profiling and use of Skyline as a platform for characterization and relative quantification of glycans in differentiating xylem of Populus trichocarpa. | Anal Bioanal Chem | 2017 | https://conductscience.org/library/papers/27491298 | PubMed |
| 26,901,320 | Liver-Enriched Gene 1, a Glycosylated Secretory Protein, Binds to FGFR and Mediates an Anti-stress Pathway to Protect Liver Development in Zebrafish. | PLoS Genet | 2016 | https://conductscience.org/library/papers/26901320 | PubMed |
1 to 10 of 24
See all 24 cited byGenes1
The genes the Gene search release ties to the paper: Swiss-Prot's references first, then PubTator's text mining.
| Gene | NCBI Gene ID | Linked by | In Genes |
|---|---|---|---|
| NGLY1 | 55,768 | PubTator's text mining | https://conductscience.org/library/genes/55768 |
Source NCBI Gene
Drugs0
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Data0
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- Trials
- 2026-11-12
- Gene search
- 2026-11-11
- Pipelines
- 2026-09-18
Sources 11
- ChEMBL, through Open TargetsCC BY-SA 3.0
- ClinicalTrials.govNo license stated
- HGNCCC0
- iCiteCC BY 4.0
- NCBI GenePublic domain (US government)
- NIH RePORTER's grant and paper linksPublic domain
- Open TargetsCC0 1.0
- PMC's ID filePublic domain (US government)
- PubMedNLM's terms
- PubTator 3Public domain
- UniProtCC BY 4.0
Each source's terms
- ChEMBL, through Open TargetsCC BY-SA 3.0, for the parts from ChEMBL. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
- ClinicalTrials.govnone stated
- HGNCCC0: https://www.genenames.org/about/license/
- iCiteCC BY 4.0
- NCBI GeneNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
- NIH RePORTER's grant and paper linksPublic domain (NIH RePORTER)
- Open TargetsCC0 1.0. Open Targets asks that users cite its latest paper: Buniello et al. 2025, Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery, Nucleic Acids Research 53(D1):D1467, PMID 39657122. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
- PMC's ID fileNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
- PubMedNLM's terms
- PubTator 3Public domain
- UniProtCC BY 4.0. UniProt's licence file: "All databases and documents in the UniProt FTP directory may be copied and redistributed freely, without advance permission, provided that this copyright statement is reproduced with each copy." UniProt asks that users cite its latest paper: The UniProt Consortium, UniProt: the Universal Protein Knowledgebase in 2025, Nucleic Acids Research 53:D609-D617, https://doi.org/10.1093/nar/gkae1010. Read on 9 Nov 2026 at https://www.uniprot.org/help/license
ClinicalTrials.gov's data carry an international copyright outside the United States: https://clinicaltrials.gov/about-site/terms-conditions.
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