Academic literature on the topic 'Glycoproteome'

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Journal articles on the topic "Glycoproteome"

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Schulze, Stefan, Friedhelm Pfeiffer, Benjamin A. Garcia, and Mechthild Pohlschroder. "Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea." PLOS Biology 19, no. 6 (2021): e3001277. http://dx.doi.org/10.1371/journal.pbio.3001277.

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Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic dataset
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Yang, Lijun, Jie Liu, Hua Li, et al. "A fully integrated sample preparation strategy for highly sensitive intact glycoproteomics." Analyst 147, no. 5 (2022): 794–98. http://dx.doi.org/10.1039/d1an02166d.

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A fully integrated spintip-based glycoproteomic technology, termed Intact GlycoSISPROT, was developed for highly sensitive intact glycoproteome analysis with low microgram to nanogram level protein samples.
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Lu, Haojie, Ying Zhang, and Pengyuan Yang. "Advancements in mass spectrometry-based glycoproteomics and glycomics." National Science Review 3, no. 3 (2016): 345–64. http://dx.doi.org/10.1093/nsr/nww019.

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Abstract Protein N-glycosylation plays a crucial role in a considerable number of important biological processes. Research studies on glycoproteomes and glycomes have already characterized many glycoproteins and glycans associated with cell development, life cycle, and disease progression. Mass spectrometry (MS) is the most powerful tool for identifying biomolecules including glycoproteins and glycans, however, utilizing MS-based approaches to identify glycoproteomes and glycomes is challenging due to the technical difficulties associated with glycosylation analysis. In this review, we summari
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Mertz, Joseph L., Shisheng Sun, Bojiao Yin, et al. "Comparison of Three Glycoproteomic Methods for the Analysis of the Secretome of CHO Cells Treated with 1,3,4-O-Bu3ManNAc." Bioengineering 7, no. 4 (2020): 144. http://dx.doi.org/10.3390/bioengineering7040144.

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Comprehensive analysis of the glycoproteome is critical due to the importance of glycosylation to many aspects of protein function. The tremendous complexity of this post-translational modification, however, makes it difficult to adequately characterize the glycoproteome using any single method. To overcome this pitfall, in this report we compared three glycoproteomic analysis methods; first the recently developed N-linked glycans and glycosite-containing peptides (NGAG) chemoenzymatic method, second, solid-phase extraction of N-linked glycoproteins (SPEG), and third, hydrophilic interaction l
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Vivekanandan-Giri, Anuradha, Jessica L. Slocum, Carolyn L. Buller, et al. "Urine Glycoprotein Profile Reveals Novel Markers for Chronic Kidney Disease." International Journal of Proteomics 2011 (October 10, 2011): 1–18. http://dx.doi.org/10.1155/2011/214715.

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Chronic kidney disease (CKD) is a significant public health problem, and progression to end-stage renal disease leads to dramatic increases in morbidity and mortality. The mechanisms underlying progression of disease are poorly defined, and current noninvasive markers incompletely correlate with disease progression. Therefore, there is a great need for discovering novel markers for CKD. We utilized a glycoproteomic profiling approach to test the hypothesis that the urinary glycoproteome profile from subjects with CKD would be distinct from healthy controls. N-linked glycoproteins were isolated
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Sharma, Ashok, James Cox, Joshua Glass, et al. "Serum Glycoproteomic Alterations in Patients with Diabetic Retinopathy." Proteomes 8, no. 3 (2020): 25. http://dx.doi.org/10.3390/proteomes8030025.

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The precise molecular mechanisms of diabetic retinopathy (DR) pathogenesis are unclear, and treatment options are limited. There is an urgent need to discover and develop novel therapeutic targets for the treatment of this disease. Glycosylation is a post-translational modification that plays a critical role in determining protein structure, function, and stability. Recent studies have found that serum glycoproteomic changes are associated with the presence or progression of several inflammatory diseases. However, very little is known about the glycoproteomic changes associated with DR. In thi
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Nilsson, Jonas, Adnan Halim, Ammi Grahn, and Göran Larson. "Targeting the glycoproteome." Glycoconjugate Journal 30, no. 2 (2012): 119–36. http://dx.doi.org/10.1007/s10719-012-9438-6.

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Phung, Toan K., Cassandra L. Pegg, and Benjamin L. Schulz. "GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis." Beilstein Journal of Organic Chemistry 16 (September 1, 2020): 2127–35. http://dx.doi.org/10.3762/bjoc.16.180.

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Mass spectrometry glycoproteomics is rapidly maturing, allowing unprecedented insights into the diversity and functions of protein glycosylation. However, quantitative glycoproteomics remains challenging. We developed GlypNirO, an automated software pipeline which integrates the complementary outputs of Byonic and Proteome Discoverer to allow high-throughput automated quantitative glycoproteomic data analysis. The output of GlypNirO is clearly structured, allowing manual interrogation, and is also appropriate for input into diverse statistical workflows. We used GlypNirO to analyse a published
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Chernykh, Anastasia, Rebeca Kawahara, and Morten Thaysen-Andersen. "Towards structure-focused glycoproteomics." Biochemical Society Transactions 49, no. 1 (2021): 161–86. http://dx.doi.org/10.1042/bst20200222.

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Facilitated by advances in the separation sciences, mass spectrometry and informatics, glycoproteomics, the analysis of intact glycopeptides at scale, has recently matured enabling new insights into the complex glycoproteome. While diverse quantitative glycoproteomics strategies capable of mapping monosaccharide compositions of N- and O-linked glycans to discrete sites of proteins within complex biological mixtures with considerable sensitivity, quantitative accuracy and coverage have become available, developments supporting the advancement of structure-focused glycoproteomics, a recognised f
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Liu, Jing, Fangjun Wang, Hui Lin, et al. "Monolithic Capillary Column Based Glycoproteomic Reactor for High-Sensitive Analysis of N-Glycoproteome." Analytical Chemistry 85, no. 5 (2013): 2847–52. http://dx.doi.org/10.1021/ac400315n.

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Dissertations / Theses on the topic "Glycoproteome"

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Zielinska, Dorota. "Unveiling the eukaryotic N-glycoproteome." Diss., Ludwig-Maximilians-Universität München, 2011. http://nbn-resolving.de/urn:nbn:de:bvb:19-166063.

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Zielinska, Dorota [Verfasser], and Matthias [Akademischer Betreuer] Mann. "Unveiling the eukaryotic N-glycoproteome / Dorota Zielinska. Betreuer: Matthias Mann." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2011. http://d-nb.info/1047543605/34.

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Huang, Peiwu. "Method development and application for spatial proteome and glycoproteome profiling." HKBU Institutional Repository, 2020. https://repository.hkbu.edu.hk/etd_oa/788.

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Tissues are heterogeneous ecosystems comprised of various cell types. For example, in tumor tissues, malignant cancer cells are surround by various non-malignant stromal cells. Proteins, especially N-linked glycoproteins, are key players in tumor microenvironment and respond to many extracellular stimuli for involving and regulating intercellular signaling. Understanding the human proteome and glycoproteome in heterogeneous tissues with spatial resolution are meaningful for exploring intercellular signaling networks and discovering protein biomarkers for various diseases, such as cancer. In th
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Murrey, Heather Elizabeth Dougherty Dennis A. Hsieh-Wilson Linda C. "Identification and characterization of the plasticity-relevant fucose-alpha(1-2)galactose glycoproteome from mouse brain /." Diss., Pasadena, Calif. : Caltech, 2009. http://resolver.caltech.edu/CaltechETD:etd-12182008-145714.

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Kalxdorf, Mathias [Verfasser]. "Mass spectrometric methods for measuring dynamic processes, drug-induced effects and target engagement on the cell surface glycoproteome / Mathias Kalxdorf." Halle, 2018. http://d-nb.info/1166140695/34.

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Ji, Yanlong [Verfasser], Volker [Gutachter] Dötsch, and Thomas [Gutachter] Oellerich. "Quantitative N-glycoproteome, phosphoproteome and ubiquitinome analyses for studying B-cell receptor signaling in B-cell lymphoma / Yanlong Ji ; Gutachter: Volker Dötsch, Thomas Oellerich." Frankfurt am Main : Universitätsbibliothek Johann Christian Senckenberg, 2021. http://d-nb.info/1234680874/34.

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Weaver, Danielle. "N-linked glycosylation in Campylobacter jejuni and Campylobacter fetus and N-linked glycans as targets for antibody-based detection." Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/nlinked-glycosylation-in-campylobacter-jejuni-and-campylobacter-fetus-and-nlinked-glycans-as-targets-for-antibodybased-detection(2b739b0d-84a3-47cc-af7a-d915b4caf37c).html.

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Campylobacter spp., especially C. jejuni and C. coli, are the leading cause of bacterial gastroenteritis in Europe. There is a recognised need to develop detection tools which can be performed on farms to facilitate reducing the presence of Campylobacter in poultry. A similar application could be beneficial for detection of C. fetus, a veterinary pathogen which causes significant economic loss in the cattle industry. Campylobacter species perform protein N-linked glycosylation and in C. jejuni at least 150 proteins, many of which are surface-exposed, may be modified. Therefore, the first porti
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Wu, Gang. "Glycomic and glycoproteomic studies of immune disorders." Thesis, Imperial College London, 2014. http://hdl.handle.net/10044/1/42776.

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Sugar oligomers which are linked to proteins and lipids play important roles in a large number of biological processes. These sugars are referred to as glycans. In the immune system, almost all key proteins are glycosylated. Glycans regulate the migration, recognition, activation, and apoptosis of immune cells, as well as the activities of antibodies. Owing to glycan complexity, the study of glycosylation is challenging. Mass spectrometry (MS) is a state-of-the-art technology which is ideally suited to investigating glycosylation, because of its ultra-high sensitivity and resolution, as well a
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Cotton, Sofia Ribeiro. "Glycoproteomic characterization of advanced bladder cancer towards novel therapies." Master's thesis, Universidade de Aveiro, 2016. http://hdl.handle.net/10773/17366.

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Mestrado em Biologia Molecular e Celular<br>A heterogenidade da natureza molecular dos tumores de bexiga tem dificultado o estabelecimento de abordagens no campo da medicina de precisão, revelando-se a necessidade de terapias mais eficientes e novas ferramentas de detecção não-invasivas. Contudo, têm-se denotado um desenvolvimento no estudo da carcinogénese de bexiga e na progressão do tumor, acompanhado de profundas alterações na glicosilação de proteínas que, dada a sua superfície celular e a natureza secretada, apresenta um potencial elevado na melhoria da gestão da doença. Segundo
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Estrella, Ruby Poblete Graduate School of Biomedical Engineering Faculty of Engineering UNSW. "A glycoproteomic approach to the structural characterization of acidic glycoproteins." Publisher:University of New South Wales. Graduate School of Biomedical Engineering, 2009. http://handle.unsw.edu.au/1959.4/43562.

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Glycoproteins, and their subset proteoglycans, are an important group of molecules in joint tissues, providing crucial functions such as cartilage structural integrity and lubrication at cartilage surfaces. The functionality of these glycoproteins is attributable to their oligosaccharide components, however surprisingly little is known about their fine structural details. With the use of glycoproteomic methods, this thesis presents the development and incorporation of mass spectrometric, biochemical and immunological methods to elucidate glycoprotein structures in synovial fluids, chondroc
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Books on the topic "Glycoproteome"

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Hamburg, Universität, ed. Synthese und Konformationsanalyse von Oligosaccharidsequenzen der N-Glycoproteine. 1986.

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Rauwald, Wolfgang. Synthese von L-Serin-verknüpften Oligosaccharidsequenzen der O-Glycoproteine. 1986.

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Reck, Folkert. Synthese von modifizierten Oligosaccharid-Sequenzen der N-Glycoproteine als Substrate oder Inhibitoren für die N-Acetylglucosaminyltransferase I. 1991.

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Book chapters on the topic "Glycoproteome"

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Hanisch, Franz-Georg, and Stefan Müller. "Approaches to the O-Glycoproteome." In The Proteomics Protocols Handbook. Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-890-0:439.

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Pan, Sheng. "Quantitative Glycoproteomics for N-Glycoproteome Profiling." In Shotgun Proteomics. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0685-7_25.

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Campbell, Matthew P., Robyn A. Peterson, Elisabeth Gasteiger, Julien Mariethoz, Frederique Lisacek, and Nicolle H. Packer. "Navigating the Glycome Space and Connecting the Glycoproteome." In Protein Bioinformatics. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6783-4_7.

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Cao, Qichen, Qing Zhao, Xiaohong Qian, and Wantao Ying. "Identification of Core-Fucosylated Glycoproteome in Human Plasma." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7057-5_10.

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Santorelli, Lucia, Elisa Barigazzi, M. Pitto, and F. Raimondo. "Investigation of the N-Glycoproteome in the Urinary Exosomes: Technical Challenges." In Toxic Chemical and Biological Agents. Springer Netherlands, 2020. http://dx.doi.org/10.1007/978-94-024-2041-8_26.

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Kalxdorf, Mathias, Hans Christian Eberl, and Marcus Bantscheff. "Monitoring Dynamic Changes of the Cell Surface Glycoproteome by Quantitative Proteomics." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7201-2_3.

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Adav, Sunil S., and Siu Kwan Sze. "Simultaneous Enrichment of Plasma Extracellular Vesicles and Glycoproteome for Studying Disease Biomarkers." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7057-5_15.

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Chau, The Huong, Anastasia Chernykh, Julian Ugonotti, Benjamin L. Parker, Rebeca Kawahara, and Morten Thaysen-Andersen. "Glycomics-Assisted Glycoproteomics Enables Deep and Unbiased N-Glycoproteome Profiling of Complex Biological Specimens." In Methods in Molecular Biology. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2978-9_16.

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Krois, Daniel. "Glycokonjugate, Glycoproteine." In Organisch-chemische Methoden. Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-53013-9_5.

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Xiao, Haopeng, George X. Tang, Weixuan Chen, and Ronghu Wu. "A Boronic Acid-Based Enrichment for Site-Specific Identification of the N-glycoproteome Using MS-Based Proteomics." In Analysis of Post-Translational Modifications and Proteolysis in Neuroscience. Springer New York, 2015. http://dx.doi.org/10.1007/7657_2015_94.

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Conference papers on the topic "Glycoproteome"

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Flores, Ricardo J., Yiting Li, Serrine S. Lau, Eastwood Leung, Ching C. Lau, and Tsz-Kwong Man. "Abstract 5570: An affinity lectin chromatography approach to characterize N-linked glycoproteome in metastatic osteosarcoma." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5570.

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Arampatzidou, Maria, Majlinda Kullolli, and Sharon J. Pitteri. "Abstract 2489: Glycoproteomic analysis of breast cancer cell lines for biomarker discovery." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2489.

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Miyoshi, Eiji, Kanako Azuma, Shinji Takamatsu, et al. "Abstract 1407: Identification of sialylated glycoproteins in doxorubicin-treated hepatoma cells with glycoproteomic analyses." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1407.

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Block, Timothy M. "Abstract CN01-02: Glycoproteomic discovery of liver cancer biomarkers: Be careful how you use it!" In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Oct 22-25, 2011; Boston, MA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1940-6207.prev-11-cn01-02.

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Miyamoto, Suzanne, Ken Yoneda, Renee Ruhaak, Carol Stroble, Carlito B. Lebrilla, and David Gandara. "Abstract 4804: Glycoproteomic analysis of lung cancer malignant pleural effusions identify glycosylated proteins being produced by metastatic tumor cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4804.

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Lindpaintner, Klaus, Apoorva Srinivasan, Alan Mitchell, et al. "158 A novel, highly accurate liquid biopsy-based glycoproteomic predictor of checkpoint inhibitor treatment benefit in advanced non-small cell lung cancer." In SITC 37th Annual Meeting (SITC 2022) Abstracts. BMJ Publishing Group Ltd, 2022. http://dx.doi.org/10.1136/jitc-2022-sitc2022.0158.

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Ueda, Koji, Hidewaki Nakagawa, Naomi Saichi, Masaru Katsumata, Taka-Aki Sato, and Yusuke Nakamura. "Abstract 5568: Development of serum glycoproteomic profiling technology for the identification of pancreatic cancer biomarkers: simultaneous identification of glycosylation sites and site-specific quantification of glycan structure changes." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5568.

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