Role and therapeutic implications of protein glycosylation in neuroinflammation

Chondroitinase ABC promotes functional recovery after spinal cord injury

Bradbury, E. J., Moon, L. D. F., Popat, R. J., King, V. R., Bennett, G. S., Patel, P. N., Fawcett, J. W., & McMahon, S. B. (2002) · Nature · doi:10.1038/416636a · Cited by 2,357 · see citing works

The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity

Zhu, C., Anderson, A. C., Schubart, A., Xiong, H., Imitola, J., Khoury, S. J., Zheng, X. X., Strom, T. B., & Kuchroo, V. K. (2005) · Nature Immunology · doi:10.1038/ni1271 · Cited by 2,057 · see citing works

Siglecs and their roles in the immune system

Crocker, P. R., Paulson, J. C., & Varki, A. P. (2007) · Nature reviews. Immunology · doi:10.1038/nri2056 · Cited by 2,032 · see citing works

Neuroinflammation in Parkinson’s disease: A target for neuroprotection?

Hirsch, E. C., & Hunot, S. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70062-6 · Cited by 1,984 · see citing works

IMMUNOBIOLOGY : the immunesystem in health and disease

Janeway, C. A. (1994) · Cited by 1,775 · see citing works

Neuroinflammation: The Devil Is in the Details

DiSabato, D. J., Quan, N., & Godbout, J. P. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13607 · Cited by 1,640 · see citing works

Glycosylation and the Immune System

Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A., & Dwek, R. A. (2001) · Science · doi:10.1126/science.291.5512.2370 · Cited by 1,588 · see citing works

Siglec-mediated regulation of immune cell function in disease

Macauley, M. S., Crocker, P. R., & Paulson, J. C. (2014) · Nature Reviews Immunology · doi:10.1038/nri3737 · Cited by 1,098 · see citing works

Current understanding of Alzheimer’s disease diagnosis and treatment

Weller, J., & Budson, A. (2018) · F1000Research · doi:10.12688/f1000research.14506.1 · Cited by 1,083 · see citing works

Neuroinflammation in Parkinson's disease and its potential as therapeutic target

Wang, Q., Liu, Y., & Zhou, J. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0042-0 · Cited by 884 · see citing works

Review: microglia of the aged brain: primed to be activated and resistant to regulation

Norden, D. M., & Godbout, J. P. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2012.01306.x · Cited by 792 · see citing works

Neuroinflammation as a common feature of neurodegenerative disorders

Guzman-Martinez, L., Maccioni, R. B., Andrade, V., Navarrete, L. P., Pastor, M. G., & Ramos-Escobar, N. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01008 · Cited by 702 · see citing works

The role of selectins in inflammation and disease

Ley, K. F. (2003) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(03)00071-6 · Cited by 683 · see citing works

Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death

Toscano, M. A., Bianco, G. A., Ilarregui, J. M., Croci, D. O., Correale, J., Hernandez, J. D., Zwirner, N. W., Poirier, F., Riley, E. M., Baum, L. G., et al. (2007) · Nature Immunology · doi:10.1038/ni1482 · Cited by 653 · see citing works

Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation

Yuzwa, S. A., Shan, X., Macauley, M. S., Clark, T., Skorobogatko, Y., Vosseller, K., & Vocadlo, D. J. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.797 · Cited by 611 · see citing works

Traumatic Brain Injury

Galgano, M. A., Toshkezi, G., Qiu, X., Russell, T., Chin, L. S., & Zhao, L. (2017) · Cell Transplantation · doi:10.1177/0963689717714102 · Cited by 588 · see citing works

Glycans and neural cell interactions

KLEENE, R. B., & Schachner, M. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1349 · Cited by 518 · see citing works

The clinical impact of glycobiology: targeting selectins, Siglecs and mammalian glycans

Smith, B. A. H., & Bertozzi, C. R. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-00093-1 · Cited by 504 · see citing works

Tumor necrosis factor

Chu, W. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.10.014 · Cited by 503 · see citing works

A Novel Mechanism of Carbohydrate Recognition by the C-type Lectins DC-SIGN and DC-SIGNR

Mitchell, D. A., Fadden, A. J., & Drickamer, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104565200 · Cited by 502 · see citing works

Extracellular matrix of the central nervous system: from neglect to challenge

Zimmermann, D. R., & Dours-Zimmermann, M. T. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0485-9 · Cited by 465 · see citing works

Microglia-secreted Galectin-3 acts as a toll-like receptor 4 ligand and contributes to microglial activation

Burguillos, M. A., Svensson, M., Schulte, T., Boza-Serrano, A., Garcia-Quintanilla, A., Kavanagh, E., Santiago, M., Viceconte, N., Oliva-Martin, M. J., Osman, A. M., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.02.012 · Cited by 365 · see citing works

Galectin-1 Deactivates Classically Activated Microglia and Protects from Inflammation-Induced Neurodegeneration

Starossom, S. C., Mascanfroni, I. D., Imitola, J., Cao, L., Raddassi, K., Hernandez, S. F., Bassil, R., Croci, D. O., Cerliani, J. P., Delacour, D., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.05.023 · Cited by 356 · see citing works

Inflammation and neurodegenerative diseases

Griffin, W. S. T. (2006) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.2.470s · Cited by 351 · see citing works

pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification

Liu, M., Zeng, W., Fang, P., Cao, W., Liu, C., Yan, G., Zhang, Y., Peng, C., Wu, J.-Q., Zhang, X.-J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00535-2 · Cited by 316 · see citing works

Re-expression of PSA-NCAM by demyelinated axons: an inhibitor of remyelination in multiple sclerosis?

Charles, P. (2002) · Brain · doi:10.1093/brain/awf216 · Cited by 289 · see citing works

Huntington's DiseasePreprint

Finkbeiner, S. M. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007476 · Cited by 260 · see citing works

Galectin-3 is required for the microglia-mediated brain inflammation in a model of Huntington’s disease

Siew, J. J., Chen, H., Chen, H., Chen, H.-L., Chen, C., Soong, B., Wu, Y., Chang, C., Chan, Y., Lin, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11441-0 · Cited by 224 · see citing works

Glycosylation and Integrin Regulation in Cancer

Marsico, G., Russo, L., Quondamatteo, F., & Pandit, A. S. (2018) · Trends in cancer · doi:10.1016/j.trecan.2018.05.009 · Cited by 204 · see citing works

Innate Immunity and Neuroinflammation

Shastri, A., Bonifati, D. M., & Kishore, U. (2013) · Mediators of Inflammation · doi:10.1155/2013/342931 · Cited by 201 · see citing works

Insights into Neuroinflammation in Parkinson’s Disease: From Biomarkers to Anti-Inflammatory Based Therapies

Rocha, N. P., de Miranda, A. S., & Teixeira, A. L. (2015) · BioMed Research International · doi:10.1155/2015/628192 · Cited by 200 · see citing works

The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?

Hergesheimer, R. C., Chami, A. A., de Assis, D. R., Vourc’h, P., Andres, C. R., Corcia, P., Lanznaster, D., & Blasco, H. (2019) · Brain · doi:10.1093/brain/awz078 · Cited by 198 · see citing works

Alleviation of Neurotoxicity by Microglial Human Siglec-11

Wang, Y., & Neumann, H. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3940-09.2010 · Cited by 190 · see citing works

Neuroinflammation and protein pathology in Parkinson’s disease dementia

Kouli, A., Camacho, M., Allinson, K. S. J., & Williams‐Gray, C. H. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01083-5 · Cited by 187 · see citing works

Definition of complete spinal cord injury

Waters, R. L., Adkins, R. H., & Yakura, J. S. (1991) · Spinal Cord · doi:10.1038/sc.1991.85 · Cited by 185 · see citing works

Genetics and the environment converge to dysregulate N-glycosylation in multiple sclerosis

Mkhikian, H., Grigorian, A., Li, C. F., Chen, H.-L., Newton, B. L., Zhou, R. W., Beeton, C., Torossian, S., Tatarian, G. G., Lee, S.-U., et al. (2011) · Nature Communications · doi:10.1038/ncomms1333 · Cited by 174 · see citing works

Neuronal expression of CD22: Novel mechanism for inhibiting microglial proinflammatory cytokine production

Mott, R. T., Ait‐Ghezala, G., Town, T., Mori, T., Vendrame, M., Zeng, J., Ehrhart, J. C., MULLAN, M. J., & Tan, J. (2004) · Glia · doi:10.1002/glia.20009 · Cited by 171 · see citing works

Huntington disease: A single-gene degenerative disorder of the striatum

Nopoulos, P. C. (2016) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2016.18.1/pnopoulos · Cited by 161 · see citing works

The N-glycosylation of immunoglobulin G as a novel biomarker of Parkinson's disease

Russell, A. C., Šimurina, M., Garcia, M., Novokmet, M., Wang, Y., Rudan, I., Campbell, H. J., Lauc, G., Thomas, M. G., & Wang, W. (2017) · Glycobiology · doi:10.1093/glycob/cwx022 · Cited by 147 · see citing works

A randomized, controlled, delayed start trial of GM1 ganglioside in treated Parkinson's disease patients

Schneider, J. S., Gollomp, S. M., Sendek, S., Colcher, A., Cambi, F., & Du, W. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.10.024 · Cited by 143 · see citing works

Glucosamine exerts a neuroprotective effect via suppression of inflammation in rat brain ischemia/reperfusion injury

Hwang, S., Shin, J., Hwang, J., Kim, S., Shin, J., Oh, E., Oh, S., Kim, J., Lee, J., & Han, I. (2010) · Glia · doi:10.1002/glia.21058 · Cited by 138 · see citing works

Markers of neuroinflammation associated with Alzheimer’s disease pathology in older adults

Popp, J., Oikonomidi, A., Tautvydaitė, D., Dayon, L., Bacher, M., Migliavacca, E., Henry, H., Kirkland, R., Severin, I., Wojcik, J., et al. (2017) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2017.01.020 · Cited by 136 · see citing works

Targeting Mannose-Binding Lectin Confers Long-Lasting Protection With a Surprisingly Wide Therapeutic Window in Cerebral Ischemia

Orsini, F., Villa, P., Parrella, S., Zangari, R., Zanier, E. R., Gesuete, R., Stravalaci, M., Fumagalli, S., Ottria, R., Reina, J. J., et al. (2012) · Circulation · doi:10.1161/circulationaha.112.103051 · Cited by 133 · see citing works

The role of protein N-glycosylation in neural transmission

Scott, H. A., & Panin, V. M. (2014) · Glycobiology · doi:10.1093/glycob/cwu015 · Cited by 132 · see citing works

Systemic Blockade of Sialylation in Mice with a Global Inhibitor of Sialyltransferases

Macauley, M. S., Arlian, B. M., Rillahan, C. D., Pang, P.-C., Bortell, N., Marcondes, M. C. G., Haslam, S. M., Dell, A., & Paulson, J. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.606517 · Cited by 129 · see citing works

Role of Oligodendrocyte Dysfunction in Demyelination, Remyelination and Neurodegeneration in Multiple Sclerosis

Dulamea, A. O. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-47861-6_7 · Cited by 128 · see citing works

Regulation of B Cell Functions by the Sialic Acid-Binding Receptors Siglec-G and CD22

Jellusova, J., & Nitschke, L. (2011) · Front. Immun. · doi:10.3389/fimmu.2011.00096 · Cited by 127 · see citing works

Thiamet G mediates neuroprotection in experimental stroke by modulating microglia/macrophage polarization and inhibiting NF-κB p65 signaling

He, Y., Ma, X., Li, D., & Hao, J. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16679671 · Cited by 127 · see citing works

Interplay Between Age and Neuroinflammation in Multiple Sclerosis: Effects on Motor and Cognitive Functions

Musella, A., Gentile, A., Rizzo, F. R., Vito, F. D., Fresegna, D., Bullitta, S., Vanni, V., Guadalupi, L., Bassi, M. S., Buttari, F., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00238 · Cited by 121 · see citing works

Absence of Neu5Gc and Presence of Anti-Neu5Gc Antibodies in Humans—An Evolutionary Perspective

Altman, M. O., & Gagneux, P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00789 · Cited by 112 · see citing works

CNS myelin induces regulatory functions of DC-SIGN–expressing, antigen-presenting cells via cognate interaction with MOG

García-Vallejo, J. J., Ilarregui, J. M., Kalay, H., Chamorro, S., Koning, N., Unger, W. W. J., Ambrosini, M., Montserrat, V., Fernandes, R. J., Bruijns, S. C. M., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20122192 · Cited by 109 · see citing works

CSF N-glycoproteomics for early diagnosis in Alzheimer's disease

Palmigiano, A., Barone, R., Sturiale, L., Sanfilippo, C., Bua, R. O., Romeo, D. A., Messina, A., Capuana, M. L., Maci, T., Le Pira, F., et al. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2015.10.006 · Cited by 107 · see citing works

N-Glycan Processing Deficiency Promotes Spontaneous Inflammatory Demyelination and Neurodegeneration

Lee, S.-U., Grigorian, A., Pawling, J., Chen, I., Gao, G., Mozaffar, T., McKerlie, C., & Demetriou, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704839200 · Cited by 107 · see citing works

Chronic upregulation of activated microglia immunoreactive for galectin-3/Mac-2 and nerve growth factor following diffuse axonal injury

Venkatesan, C., Chrzaszcz, M., Choi, N., & Wainwright, M. S. (2010) · Journal of Neuroinflammation · doi:10.1186/1742-2094-7-32 · Cited by 103 · see citing works

Rapid Trimming of Cell Surface Polysialic Acid (PolySia) by Exovesicular Sialidase Triggers Release of Preexisting Surface Neurotrophin

Sumida, M., Hane, M., Yabe, U., Shimoda, Y., Pearce, O. M. T., Kiso, M., Miyagi, T., Sawada, M., Varki, A. P., Kitajima, K., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.638759 · Cited by 102 · see citing works

O-GlcNAc regulation of autophagy and α-synuclein homeostasis; implications for Parkinson’s disease

Wani, W. Y., Ouyang, X., Benavides, G. A., Redmann, M., Cofield, S. S., Shacka, J. J., Chatham, J. C., Darley-Usmar, V. M., & Zhang, J. (2017) · Molecular Brain · doi:10.1186/s13041-017-0311-1 · Cited by 101 · see citing works

Protective effect of N-glycan bisecting GlcNAc residues on -amyloid production in Alzheimer's disease

Akasaka‐Manya, K., Manya, H., Sakurai, Y., Wójczyk, B. S., Kozutsumi, Y., Saito, Y., Taniguchi, N., Murayama, S., Spitalnik, S. L., & Endo, T. (2009) · Glycobiology · doi:10.1093/glycob/cwp152 · Cited by 100 · see citing works

Siglecs in Brain Function and Neurological Disorders

Siddiqui, S. S., Matar, R., Merheb, M., Hodeify, R., Vazhappilly, C. G., Marton, J., Shamsuddin, S. A., & Al Zouabi, H. (2019) · Cells · doi:10.3390/cells8101125 · Cited by 100 · see citing works

Alterations in sulfated chondroitin glycosaminoglycans following controlled cortical impact injury in mice

Yi, J., Katagiri, Y., Susarla, B., Figge, D., Symes, A. J., & Geller, H. M. (2012) · Journal of Comparative Neurology · doi:10.1002/cne.23156 · Cited by 93 · see citing works

Neuroinflammation in the peripheral nerve: Cause, modulator, or bystander in peripheral neuropathies?

Martini, R., & Willison, H. J. (2015) · Glia · doi:10.1002/glia.22899 · Cited by 92 · see citing works

N-Glycosylation in Regulation of the Nervous System

Scott, H. A., & Panin, V. M. (2014) · Advances in neurobiology · doi:10.1007/978-1-4939-1154-7_17 · Cited by 90 · see citing works

Sialoadhesin-Positive Macrophages Bind Regulatory T Cells, Negatively Controlling Their Expansion and Autoimmune Disease Progression

Wu, C., Rauch, U., Korpos, É., Song, J., Loser, K., Crocker, P. R., & Sorokin, L. M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804247 · Cited by 90 · see citing works

Chondroitinase treatment following spinal contusion injury increases migration of oligodendrocyte progenitor cells

Siebert, J. R., Stelzner, D. J., & Osterhout, D. J. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.05.002 · Cited by 89 · see citing works

Microglial Immunoreceptor Tyrosine-Based Activation and Inhibition Motif Signaling in Neuroinflammation

Linnartz, B., Wang, Y., & Neumann, H. (2010) · International Journal of Alzheimer's Disease · doi:10.4061/2010/587463 · Cited by 87 · see citing works

Glycoblotting method allows for rapid and efficient glycome profiling of human Alzheimer's disease brain, serum and cerebrospinal fluid towards potential biomarker discovery

Gizaw, S. T., Ohashi, T., Tanaka, M., Hinou, H., & Nishimura, S. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.03.009 · Cited by 86 · see citing works

Characteristics of α-Gal epitope, anti-Gal antibody, α1,3 galactosyltransferase and its clinical exploitation (Review)

HUAI, G., QI, P., YANG, H., & WANG, Y. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2397 · Cited by 82 · see citing works

Multiple sclerosis: new insights in pathogenesis and novel therapeutics.

Ontaneda, D., Hyland, M., & Cohen, J. A. (2012) · Annual Review of Medicine · doi:10.1146/annurev-med-042910-135833 · Cited by 81 · see citing works

In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease

Chen, Z., Yu, Q., Yu, Q., Johnson, J., Shipman, R. D., Zhong, X., Huang, J., Asthana, S., Carlsson, C. M., Okonkwo, O. C., et al. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100081 · Cited by 81 · see citing works

Towards structure-focused glycoproteomics

Chernykh, A., Kawahara, R., & Thaysen‐Andersen, M. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200222 · Cited by 80 · see citing works

Galectin-3: Roles in Neurodevelopment, Neuroinflammation, and Behavior

Srejovic, I. M., Selaković, D., Jovicic, N. U., Jakovljevic, V. L., Lukić, M. L., & Rosic, G. L. (2020) · Biomolecules · doi:10.3390/biom10050798 · Cited by 77 · see citing works

Loss of Branched O-Mannosyl Glycans in Astrocytes Accelerates Remyelination

Kanekiyo, K., Inamori, K., Kitazume, S., Sato, K., Maeda, J., Higuchi, M., Kizuka, Y., Korekane, H., Matsuo, I., Honke, K., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3137-12.2013 · Cited by 75 · see citing works

Lipolysaccharide-Induced Neuroinflammation Is Associated with Alzheimer-Like Amyloidogenic Axonal Pathology and Dendritic Degeneration in Rats

Deng, X., Li, M., Ai, W., He, L., Lu, D., Patrylo, P. R., Cai, H., Luo, X., Li, Z., & Yan, X. (2014) · Advances in Alzheimer s Disease · doi:10.4236/aad.2014.32009 · Cited by 75 · see citing works

Astrocyte galectin-9 potentiates microglial TNF secretion

Steelman, A. J., & Li, J. (2014) · Journal of Neuroinflammation · doi:10.1186/s12974-014-0144-0 · Cited by 75 · see citing works

Diminished O-GlcNAcylation in Alzheimer's disease is strongly correlated with mitochondrial anomalies

Pinho, T. S., Correia, S. C., Perry, G., Ambrósio, A. F., & Moreira, P. I. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.037 · Cited by 70 · see citing works

The sweet spot for biologics: recent advances in characterization of biotherapeutic glycoproteins

O’Flaherty, R., Trbojević‐Akmačić, I., Greville, G., Rudd, P. M., & Lauc, G. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1404907 · Cited by 64 · see citing works

Understanding the Stepwise Synthesis of Glycolipids

Maccioni, H. J. F., Giraudo, C. G., & Daniotti, J. L. (2002) · Neurochemical Research · doi:10.1023/a:1020271932760 · Cited by 61 · see citing works

Microglial Lectins in Health and Neurological Diseases

Siew, J. J., & Chern, Y. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00158 · Cited by 61 · see citing works

A comprehensive glycome profiling of Huntington's disease transgenic mice

Gizaw, S. T., Koda, T., Amano, M., Kamimura, K., Ohashi, T., Hinou, H., & Nishimura, S. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.04.006 · Cited by 60 · see citing works

The N‐glycan profile in cortex and hippocampus is altered in Alzheimer disease

Gaunitz, S., Tjernberg, L. O., & Schedin‐Weiss, S. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15202 · Cited by 58 · see citing works

Glycan-dependent binding of galectin-1 to neuropilin-1 promotes axonal regeneration after spinal cord injury

Quintá, H. R., Pasquini, J. M., Rabinovich, G. A., & Pasquini, L. A. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.14 · Cited by 57 · see citing works

GM1 ganglioside in Parkinson's disease: Pilot study of effects on dopamine transporter binding

Schneider, J. S., Cambi, F., Gollomp, S. M., Kuwabara, H., Brašić, J. R., Leiby, B. E., Sendek, S., & Wong, D. F. (2015) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2015.06.028 · Cited by 55 · see citing works

Polysialic acid and Siglec-E orchestrate negative feedback regulation of microglia activation

Thiesler, H., Beimdiek, J., & Hildebrandt, H. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03601-z · Cited by 55 · see citing works

The role of N-Glycan modification of TNFR1 in inflammatory microglia activation

Han, L., Zhang, D., Tao, T., Sun, X., Liu, X., Zhu, G., Xu, Z., Zhu, L., Zhang, Y., Liu, W., et al. (2015) · Glycoconjugate Journal · doi:10.1007/s10719-015-9619-1 · Cited by 54 · see citing works

Serum N-Glycosylation in Parkinson’s Disease: A Novel Approach for Potential Alterations

Váradi, C., Nehéz, K., Hornyák, O., Viskolcz, B., & Bones, J. (2019) · Molecules · doi:10.3390/molecules24122220 · Cited by 53 · see citing works

Combination of serum and CSF neurofilament-light and neuroinflammatory biomarkers to evaluate ALS

Brodovitch, A., Boucraut, J., Delmont, É., Parlanti, A., Grapperon, A., Attarian, S., & Verschueren, A. (2021) · Scientific Reports · doi:10.1038/s41598-020-80370-6 · Cited by 53 · see citing works

Sialoadhesin promotes neuroinflammation‐related disease progression in two mouse models of CLN disease

Groh, J., Ribechini, E., Stadler, D., Schilling, T., Lutz, M. B., & Martini, R. (2016) · Glia · doi:10.1002/glia.22962 · Cited by 51 · see citing works

Polysialic acid on SynCAM 1 in NG2 cells and on neuropilin‐2 in microglia is confined to intracellular pools that are rapidly depleted upon stimulation

Werneburg, S., Mühlenhoff, M., Stangel, M., & Hildebrandt, H. (2015) · Glia · doi:10.1002/glia.22815 · Cited by 49 · see citing works

Glycomics: New Challenges and Opportunities in Regenerative Medicine

Russo, L., & Cipolla, L. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201602156 · Cited by 49 · see citing works

Excess APP O -glycosylation by GalNAc-T6 decreases Aβ production

Akasaka‐Manya, K., Kawamura, M., Tsumoto, H., Saito, Y., Tachida, Y., Kitazume, S., Hatsuta, H., Miura, Y., Hisanaga, S., Murayama, S., et al. (2016) · The Journal of Biochemistry · doi:10.1093/jb/mvw056 · Cited by 49 · see citing works

Nutritional Therapies in Congenital Disorders of Glycosylation (CDG)

Witters, P., Cassiman, D. M., & Morava, É. (2017) · Nutrients · doi:10.3390/nu9111222 · Cited by 48 · see citing works

Neoglucosylated Collagen Matrices Drive Neuronal Cells to Differentiate

Russo, L., Sgambato, A., Lecchi, M., Pastori, V., Raspanti, M., Natalello, A., Doglia, S. M., Nicotra, F., & Cipolla, L. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn400222s · Cited by 47 · see citing works

O-GlcNAcylation Reduces Ischemia-Reperfusion–Induced Brain Injury

Gu, J., Shi, J., Dai, C., Ge, J., Yang, Z., Chen, Y., Yu, Q., Qin, Z., Iqbal, K., Liu, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10635-0 · Cited by 46 · see citing works

How do PrPSc Prions Spread between Host Species, and within Hosts?

Mabbott, N. A. (2017) · Pathogens · doi:10.3390/pathogens6040060 · Cited by 46 · see citing works

Glycans in Sera of Amyotrophic Lateral Sclerosis Patients and Their Role in Killing Neuronal Cells

Edri‐Brami, M., Rosental, B., Hayoun, D., Welt, M., Rosen, H., Wirguin, I., Nefussy, B., Drory, V. E., Porgador, A., & Lichtenstein, R. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035772 · Cited by 45 · see citing works

Lectin-Array Blotting: Profiling Protein Glycosylation in Complex Mixtures

Etxebarria, J., Calvo, J., Martín‐Lomas, M., & Reichardt, N. (2012) · ACS Chemical Biology · doi:10.1021/cb300262x · Cited by 43 · see citing works

Pharmacological inhibition of mannose-binding lectin ameliorates neurobehavioral dysfunction following experimental traumatic brain injury

Blasio, D. D., Fumagalli, S., Longhi, L. G., Orsini, F., Palmioli, A., Stravalaci, M., Vegliante, G., Zanier, E. R., Bernardi, A., Gobbi, M., et al. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16647397 · Cited by 43 · see citing works

Complete spatial characterisation of N-glycosylation upon striatal neuroinflammation in the rodent brain

Rebelo, A. L., Gubinelli, F., Roost, P., Jan, C., Brouillet, E., Camp, N. V., Drake, R. R., Saldova, R., & Pandit, A. S. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02163-6 · Cited by 43 · see citing works

Extracellular matrixes and neuroinflammation

Jang, D. G., Sim, H. J., Song, E. K., Kwon, T., & Park, T. J. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.10.156 · Cited by 42 · see citing works

Deficiency of α1,6-fucosyltransferase promotes neuroinflammation by increasing the sensitivity of glial cells to inflammatory mediators

Xu, L., Zhang, D., Shoji, H., Duan, C., Zhang, G., Isaji, T., Wang, Y., Fukuda, T., & Gu, J. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.12.008 · Cited by 41 · see citing works

Recognition of Bisecting N-Glycans on Intact Glycopeptides by Two Characteristic Ions in Tandem Mass Spectra

Dang, L., Shen, J., Zhao, T., Zhao, F., Li, J., Zhu, B., Ma, C., Chen, D., Zhao, Y., & Sun, S. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05639 · Cited by 41 · see citing works

Multiple sclerosis-associated single-nucleotide polymorphisms in CLEC16A correlate with reduced SOCS1 and DEXI expression in the thymus

Leikfoss, I. S., Mero, I.-L., Dahle, M. K., Lie, B. A., Harbo, H. F., Spurkland, A., & Berge, T. (2012) · Genes and Immunity · doi:10.1038/gene.2012.52 · Cited by 40 · see citing works

Surface chemistry and linker effects on lectin–carbohydrate recognition for glycan microarrays

Kilcoyne, M., Gerlach, J. Q., Kane, M., & Joshi, L. (2012) · Analytical Methods · doi:10.1039/c2ay25532d · Cited by 39 · see citing works

Neural cell type-specific responses to glycomimetic functionalized collagen

Masand, S. N., Perron, I. J., Schachner, M., & Shreiber, D. I. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.10.013 · Cited by 39 · see citing works

Polysialylation at Early Stages of Oligodendrocyte Differentiation Promotes Myelin Repair

Werneburg, S., Fuchs, H. L. S., Albers, I., Burkhardt, H., Gudi, V., Skripuletz, T., Stangel, M., Gerardy‐Schahn, R., & Hildebrandt, H. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1147-17.2017 · Cited by 38 · see citing works

Mgat5 Deficiency in T Cells and Experimental Autoimmune Encephalomyelitis

Grigorian, A., & Demetriou, M. (2011) · ISRN Neurology · doi:10.5402/2011/374314 · Cited by 37 · see citing works

Glycans in Nanomedicine, Impact and Perspectives

Sampaolesi, S., Nicotra, F., & Russo, L. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0368 · Cited by 36 · see citing works

Differential expression of selectins by mouse brain capillary endothelial cells in vitro in response to distinct inflammatory stimuli

Coisne, C., Faveeuw, C., Delplace, Y., Dehouck, L., Miller, F., Cecchelli, R., & Dehouck, B. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.09.028 · Cited by 35 · see citing works

Deciphering glycomics and neuroproteomic alterations in experimental traumatic brain injury: Comparative analysis of aspirin and clopidogrel treatment

Abou‐Abbass, H., Bahmad, H. F., Abou‐El‐Hassan, H., Zhu, R., Zhou, S., Dong, X., Hamade, E., Mallah, K., Zebian, A., Ramadan, N., et al. (2016) · Electrophoresis · doi:10.1002/elps.201500583 · Cited by 32 · see citing works

New Insights Into the Biology of Protein O-GlcNAcylation: Approaches and Observations

Mueller, T., Ouyang, X., Johnson, M. S., Qian, W., Chatham, J. C., Darley-Usmar, V. M., & Zhang, J. (2021) · Frontiers in Aging · doi:10.3389/fragi.2020.620382 · Cited by 30 · see citing works

Glycoproteomics

Singh, A. K. (2021) · Nature Methods · doi:10.1038/s41592-020-01028-9 · Cited by 27 · see citing works

Integration of lectin–glycan recognition systems and immune cell networks in CNS inflammation

Méndez‐Huergo, S. P., Maller, S. M., Farez, M., Mariño, K. V., Correale, J. D., & Rabinovich, G. A. (2014) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.02.003 · Cited by 26 · see citing works

Array-Based Functional Screening of Heparin Glycans

Puvirajesinghe, T. M., Ahmed, Y., Powell, A. K., Fernig, D. G., Guimond, S. E., & Turnbull, J. E. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.03.011 · Cited by 24 · see citing works

Ligand-mediated Galectin-1 endocytosis prevents intraneural H2O2 production promoting F-actin dynamics reactivation and axonal re-growth

Quintá, H. R., Wilson, C., Blidner, A. G., González-Billault, C. E., Pasquini, L. A., Rabinovich, G. A., & Pasquini, J. M. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.06.009 · Cited by 24 · see citing works

Bioinformatics for glycobiology and glycomics : an introduction

von der Lieth, C., Lütteke, T., & Frank, M. (2009) · Wiley-Blackwell eBooks · Cited by 23 · see citing works

Dietary mannose supplementation in phosphomannomutase 2 deficiency (PMM2-CDG)

Taday, R., Grüneberg, M., Chesne, I. D., Reunert, J., & Marquardt, T. (2020) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-020-01528-z · Cited by 22 · see citing works

O-GlcNAc glycosylation of p27kip1 promotes astrocyte migration and functional recovery after spinal cord contusion

Mao, X., Zhang, D., Tao, T., Liu, X., Sun, X., Wang, Y., & Shen, A. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.11.007 · Cited by 21 · see citing works

Glycan-Functionalized Collagen Hydrogels Modulate the Glycoenvironment of a Neuronal Primary Culture

Rebelo, A. L., Bizeau, J., Russo, L., & Pandit, A. S. (2020) · Biomacromolecules · doi:10.1021/acs.biomac.0c00387 · Cited by 19 · see citing works

Neuroprotective role of galectin-1 in central nervous system pathophysiology

Mahajan, S. D., & Aalinkeel, R. (2016) · Neural Regeneration Research · doi:10.4103/1673-5374.184455 · Cited by 18 · see citing works

Structure and Function of Mammalian Carbohydrate-Lectin Interactions

Anderson, K. E., Evers, D. L., & Rice, K. G. (2008) · Springer eBooks · doi:10.1007/978-3-540-30429-6_63 · Cited by 16 · see citing works

Analysis of N- and O-Linked Glycosylation: Differential Glycosylation after Rat Spinal Cord Injury

Osimanjiang, W., Roballo, K. C. S., Houck, B. D., Ito, M., Antonopoulos, A., Dell, A., Haslam, S. M., & Bushman, J. S. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2019.6974 · Cited by 15 · see citing works

Reactivity of anti-HNK-1 antibodies to branched O-mannose glycans associated with demyelination

Sakuda, K., Kizuka, Y., Yamaguchi, Y., Tanaka, K., Ogiwara, K., Segawa, T., Hagiwara, Y., Matsuo, I., Ogawa, H. K., Taniguchi, N., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.04.085 · Cited by 14 · see citing works

Differential Glycosylation Expression in Injured Rat Spinal Cord Treated with Immunosuppressive Drug Cyclosporin-A

Kilcoyne, M., Patil, V., O’Grady, C., Bradley, C., & McMahon, S. S. (2019) · ACS Omega · doi:10.1021/acsomega.8b02524 · Cited by 14 · see citing works

Sweet tailoring of glyco-modulatory extracellular matrix-inspired biomaterials to target neuroinflammation

Rebelo, A. L., Chevalier, M. T., Russo, L., & Pandit, A. S. (2021) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2021.100321 · Cited by 13 · see citing works

β4GalT1 Mediates PPARγ N-Glycosylation to Attenuate Microglia Inflammatory Activation

Liu, X., Li, A., Ju, Y., Liu, W., Shi, H., Hu, R., Zhou, Z., & Sun, X. (2018) · Inflammation · doi:10.1007/s10753-018-0789-4 · Cited by 9 · see citing works

The Impact of β-1,4-Galactosyltransferase V on Microglial Function

Wang, X., Shi, N., Hui, M., Jin, H., Gao, S., Zhou, Q., Zhang, L., Yan, M., & Shen, H. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.723308 · Cited by 9 · see citing works

Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation

Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516 · see citing works

Glycosylation and behavioral symptoms in neurological disorders

Pradeep, P., Kang, H., & Lee, B. (2023) · Translational Psychiatry · doi:10.1038/s41398-023-02446-x · Cited by 119 · see citing works

Understanding glycosylation: Regulation through the metabolic flux of precursor pathways

Scheper, A. F., Schofield, J., Bohara, R. A., Ritter, T., & Pandit, A. S. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108184 · Cited by 68 · see citing works

The dynamic brain N-glycome

Klarić, T., & Lauc, G. (2022) · Glycoconjugate Journal · doi:10.1007/s10719-022-10055-x · Cited by 294 · see citing works

Functions and mechanisms of protein lysine butyrylation (Kbu): Therapeutic implications in human diseases

Xue, Q., Yang, Y., Li, H., Li, X., Zou, L., Li, T., Ma, H., Qi, H., Wang, J., & Yu, T. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.10.025 · Cited by 30 · see citing works

Glycomics in Human Diseases and Its Emerging Role in Biomarker Discovery

Onigbinde, S. B., Adeniyi, M., Daramola, O. E., Chukwubueze, F. M., Bhuiyan, M. M. A. A., Nwaiwu, J. I., Bhattacharjee, T., & Mechref, Y. S. (2025) · Biomedicines · doi:10.3390/biomedicines13082034 · Cited by 28 · see citing works

Therapeutic potential of targeting galectins – A biomaterials-focused perspective

Martín‐Saldaña, S., Chevalier, M. T., & Pandit, A. S. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121585 · Cited by 29 · see citing works

Glycosylation in neuroinflammation: mechanisms, implications, and therapeutic strategies for neurodegenerative diseases

Cheng, S., Xiao, B., & Luo, Z. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00506-4 · Cited by 29 · see citing works

The multifaceted roles of activating transcription factor 3 (ATF3) in inflammatory responses – Potential target to regulate neuroinflammation in acute brain injury

Li, Y., Fan, Q., Li, F., Pang, R., Chen, C., Li, P., Wang, X., Xuan, W., & Yu, W. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231171999 · Cited by 26 · see citing works

Protein glycosylation and glycoinformatics for novel biomarker discovery in neurodegenerative diseases

Costa, J., Hayes, C. A., & Lisacek, F. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101991 · Cited by 26 · see citing works

Exploring the properties and potential of the neural extracellular matrix for next‐generation regenerative therapies

Ortega, J. A., de Aguiar, G. P. S., Chandravanshi, P., Levy, N., Engel, E., & Álvarez, Z. (2024) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1962 · Cited by 26 · see citing works

Changes in tissue protein N-glycosylation and associated molecular signature occur in the human Parkinsonian brain in a region-specific manner

Rebelo, A. L., Drake, R. R., Marchetti‐Deschmann, M., Saldova, R., & Pandit, A. S. (2023) · PNAS Nexus · doi:10.1093/pnasnexus/pgad439 · Cited by 19 · see citing works

The emerging role of GlycoRNAs in immune regulation and recognition

Montag, N., Gousis, P., & Wittmann, J. (2025) · Immunology Letters · doi:10.1016/j.imlet.2025.107048 · Cited by 17 · see citing works

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2021–2022

Harvey, D. J. (2024) · Mass Spectrometry Reviews · doi:10.1002/mas.21873 · Cited by 15 · see citing works

Immunomodulatory role of glycoRNAs in the brain

Chokkalla, A. K., Jeong, S., Subramanian, S., & Vemuganti, R. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231151995 · Cited by 14 · see citing works

Genetic effects of sequence-conserved enhancer-like elements on human complex traits

Zhu, X., Ma, S., & Wong, W. H. (2024) · Genome biology · doi:10.1186/s13059-023-03142-1 · Cited by 13 · see citing works

Profiling of long non-coding RNAs in hippocampal–entorhinal system subfields: impact of RN7SL1 on neuroimmune response modulation in Alzheimer’s disease

Liu, H., Li, J., Wang, X., Luo, S., Luo, D., Ge, W., & Ma, C. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03083-x · Cited by 9 · see citing works

Moringa oleifera Lam. seed lectin (WSMoL) reduces chronic stress-induced anxiety and depression in mice by lessening inflammation and balancing brain chemicals

Patriota, L. L. D. S., de Lima, B. R. F., Marinho, A. D. O., da Costa, J. A., de Lucena, A. L. A., Paiva, P. M. G., Napoleão, D. C., Cavalcanti, J. V. F. L., Pereira, M. C., Napoleão, T. H., et al. (2024) · Behavioural Brain Research · doi:10.1016/j.bbr.2024.115318 · Cited by 10 · see citing works

Dessert or Poison? The Roles of Glycosylation in Alzheimer's, Parkinson's, Huntington's Disease, and Amyotrophic Lateral Sclerosis

Yang, J., Li, H., & Zhao, Y. (2023) · ChemBioChem · doi:10.1002/cbic.202300017 · Cited by 9 · see citing works

Decoding Glycosylation in Neurodegenerative Diseases: Mechanistic Insights and Therapeutic Opportunities

Yu, H., Chen, X., Yang, Y., Gu, M., Ren, K., & Wei, Z. (2025) · The FASEB Journal · doi:10.1096/fj.202502809r · Cited by 9 · see citing works

Glycosylation: A new signaling paradigm for the neurovascular diseases.

Kaur, D., Khan, H., Grewal, A., & Singh, T. (2023) · Life Science · doi:10.1016/j.lfs.2023.122303 · Cited by 10 · see citing works

Implications of Mucin-Type O-Glycosylation in Alzheimer’s Disease

Navarro, N. V., Mundim, G. D. N., & Čudić, M. (2025) · Molecules · doi:10.3390/molecules30091895 · Cited by 5 · see citing works

Further evidence supporting the role of GTDC1 in glycine metabolism and neurodevelopmental disorders

Errichiello, E., Lecca, M., Vantaggiato, C., Motta, Z., Zanotta, N., Zucca, C., Bertuzzo, S., Piubelli, L., Pollegioni, L., & Bonaglia, M. C. (2024) · European Journal of Human Genetics · doi:10.1038/s41431-024-01603-0 · Cited by 5 · see citing works

N -Glycan profile of the cell membrane as a probe for lipopolysaccharide-induced microglial neuroinflammation uncovers the effects of common fatty acid supplementation

Grijaldo-Alvarez, S. J. B., Alvarez, M. R., Schindler, R. L., Oloumi, A., Hernandez, N., Seales, T., Angeles, J. G. C., Nacario, R. C., Completo, G. C. J., Zivkovic, A. M., et al. (2024) · Food & Function · doi:10.1039/d4fo01598c · Cited by 5 · see citing works

Rescue of mitochondrial dysfunction through alteration of extracellular matrix composition in barth syndrome cardiac fibroblasts

Piñeiro-Llanes, J., Suzuki‐Hatano, S., Jain, A., Venigalla, S., Kamat, M. N., Basso, K. B. G., Cade, W. T., Simmons, C. S., & Pacak, C. A. (2024) · Biomaterials · doi:10.1016/j.biomaterials.2024.122922 · Cited by 4 · see citing works

Unique N-glycosylation signatures in human iPSC derived microglia activated by Aβ oligomer and lipopolysaccharide

Tang, X., Schindler, R. L., Lucente, J. D., Oloumi, A., Tena, J., Harvey, D. J., Lebrilla, C. B., Zivkovic, A. M., Jin, L., & Maezawa, I. (2025) · Scientific Reports · doi:10.1038/s41598-025-96596-1 · Cited by 6 · see citing works

Exploration of biomarkers for inhibitor development in persons with hemophilia A

Fan, M., Shen, T., Konkle, B. A., Cai, X., Chao, T.-Y., Manco‐Johnson, M. J., Faino, A., Zhang, J., Bao, S., Xiao, W., et al. (2025) · Research and Practice in Thrombosis and Haemostasis · doi:10.1016/j.rpth.2025.102877 · Cited by 3 · see citing works

Mass Spectrometry-Based Comparative Analysis of N -Glycosylation Alterations in Three Human Body Fluids in Parkinson’s Disease

Zhao, L., Hou, C., Gao, Y., Jin, H., Liu, C., Li, S., Ma, J., & Yang, S. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00654 · Cited by 3 · see citing works

PIGK defects induce apoptosis in Purkinje cells and acceleration of neuroectodermal differentiation

Chen, S., You, J., Zhou, X., Li, Y., Liu, F., Teng, Y., Teng, H., Li, Y., Liang, D., Li, Z., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07201-8 · Cited by 3 · see citing works

Glioblastoma - Current Evidence

Agrawal, A., & Kunwar, D. S. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.100846 · Cited by 3 · see citing works

Exome-wide analysis reveals role of LRP1 and additional novel loci in cognition

Chakraborty, S., & Kahali, B. (2023) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2023.100208 · Cited by 3 · see citing works

Reduced Expression of CLEC4G in Neurons Is Associated with Alzheimer’s Disease

Feng, X., Qi, F., Huang, Y., Zhang, G., & Deng, W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094621 · Cited by 2 · see citing works

Regulation of N‐Glycosylation of CDNF on Its Protein Stability and Function in Hypoxia/Reoxygenation Model of H9C2 Cells

Huang, Q., Dong, H., Jia, W., Ren, Y., Li, W., Zhong, L., Gong, L., & Yang, J. (2025) · Cell Biology International · doi:10.1002/cbin.70000 · Cited by 2 · see citing works

Changes in Protein N -Glycosylation Regulation Occur in the Human Parkinsonian Brain in a Region-Specific MannerPreprint

Rebelo, A. L., Drake, R. R., Marchetti‐Deschmann, M., Saldova, R., & Pandit, A. S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.19.492623 · Cited by 2 · see citing works

APOE E4 Alzheimer’s Risk Converges on an Oligodendrocyte Subtype in the Human Entorhinal CortexPreprint

Huuki-Myers, L. A., Divecha, H. R., Bach, S. V., Valentine, M. R., Eagles, N. J., Mulvey, B., Bharadwaj, R. A., Zhang, R., Evans, J. R., Grant‐Peters, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.20.689483 · Cited by 3 · see citing works

Differential Glycosylation Patterns in Parkinson’s Disease: Emphasis on Male-Specific Changes Identified via HILIC-LC-MS

Demeter, B., Kutás, A., Viskolcz, B., Oláh, C., Petercsák, E., Garami, A., & Váradi, C. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27010552 · Cited by 1 · see citing works

New Approaches in the Treatment of Glioblastoma Multiforme

Morgan, L. R., Jursic, B. S., Ware, M. L., & Weiner, R. S. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.105886

Exome sequencing reveals aggregates of rare variants in glycosyltransferase and other genes influencing immunoglobulin G and transferrin glycosylationPreprint

Landini, A., Timmers, P. R. H. J., Frkatović-Hodžić, A., Trbojević‐Akmačić, I., Vučković, F., Pribić, T., Tzoneva, G., Shuldiner, A. R., Polašek, O., Hayward, C., et al. (2022) · medRxiv · doi:10.1101/2022.12.26.22283911

Additional file 1 of Genetic effects of sequence-conserved enhancer-like elements on human complex traits

Zhu, X., Ma, S., & Wong, W. H. (2024) · Figshare · doi:10.6084/m9.figshare.24934202

Additional file 1 of Profiling of long non-coding RNAs in hippocampal–entorhinal system subfields: impact of RN7SL1 on neuroimmune response modulation in Alzheimer’s disease

Liu, H., Li, J., Wang, X., Luo, S., Luo, D., Ge, W., & Ma, C. (2024) · Figshare · doi:10.6084/m9.figshare.26703235

Additional file 3 of Genetic effects of sequence-conserved enhancer-like elements on human complex traits

Zhu, X., Ma, S., & Wong, W. H. (2024) · Figshare · doi:10.6084/m9.figshare.26658229

Additional file 2 of Profiling of long non-coding RNAs in hippocampal–entorhinal system subfields: impact of RN7SL1 on neuroimmune response modulation in Alzheimer’s disease

Liu, H., Li, J., Wang, X., Luo, S., Luo, D., Ge, W., & Ma, C. (2024) · Figshare · doi:10.6084/m9.figshare.26703238

Additional file 2 of Genetic effects of sequence-conserved enhancer-like elements on human complex traits

Zhu, X., Ma, S., & Wong, W. H. (2024) · Figshare · doi:10.6084/m9.figshare.24934550

Discovering Glycosylation-Dependent Protein Function by Thermal Proteome ProfilingPreprint

Hevler, J. F., Sojitra, M., Čaval, T., Schoof, M., Mateus, A., & Bertozzi, C. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.06.692499

Injury-transduced SerpinOLs modulate neuroinflammation and glial activation in the diseased and non-diseased CNSPreprint

Wang, Y., Zhu, M., Park, J., Kim, H. K., Ge, X., Chen, X., Chen, B., Ding, S., Lin, W., & Guo, F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.29.702669

Glycosylation modulation as a therapeutic strategy for neuroinflammatory disorders: The potential of Tanshinone IIA

Li, Y., Duan, K., Liu, G., Yan, J., Wang, Q., Zhang, Y., Wang, Y., Guo, B., Zhang, P. F., Zhang, W., et al. (2026) · iScience · doi:10.1016/j.isci.2026.116012

Mass Spectrometry-Based N-Glycomics of Total Serum and IgG Provides Complementary Insights into Multiple Sclerosis

Dojcsák, D., Bladergroen, M. R., Wang, W. Y., Mayboroda, O. A., Váradi, C., Pongrácz, T., & Wuhrer, M. (2026) · ACS Omega · doi:10.1021/acsomega.6c01969

A robust HPLC-HILIC enrichment system for O-glycoproteomics profiling of plasma and cerebrospinal fluid across Alzheimer's disease progression

Deng, Z., Wang, Y., Liu, L., Guo, X., Zhu, H., Dong, M., Ge, Y., Yu, Y., & Ye, M. (2026) · Analytica Chimica Acta · doi:10.1016/j.aca.2026.345899

Mendelian Randomization and Transcriptome Analysis Identify Ischemic Stroke Biomarkers With Putative Relevance to Cerebrospinal Fluid

Xiong, J., Zhang, J., Cheng, X., Zhou, Z. Z., Zhang, L. D., & Chen, C. E. (2026) · BioMed Research International · doi:10.1155/bmri/2880611

Spatiotemporal crosstalk of post-translational modifications: A therapeutic avenue in spinal cord injury

Liang, W., Wang, C., Xu, Y., Sun, D., Zhang, X., Yin, P., Han, B., Qu, X., & Hai, Y. (2026) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2026.08.032

Glycosylation as a design component of biomaterials in implant design

Pandit, A. (2026) · Military Medical Research · doi:10.1016/j.mmr.2026.100070

Glycosylation in neuroinflammation: mechanisms, implications, and therapeutic strategies for neurodegenerative diseases

Cheng, S., Xiao, B., & Luo, Z. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00506-4 · Cited by 29 · see citing works

Glycosylation modulation as a therapeutic strategy for neuroinflammatory disorders: The potential of Tanshinone IIA

Li, Y., Duan, K., Liu, G., Yan, J., Wang, Q., Zhang, Y., Wang, Y., Guo, B., Zhang, P. F., Zhang, W., et al. (2026) · iScience · doi:10.1016/j.isci.2026.116012

Decoding Glycosylation in Neurodegenerative Diseases: Mechanistic Insights and Therapeutic Opportunities

Yu, H., Chen, X., Yang, Y., Gu, M., Ren, K., & Wei, Z. (2025) · The FASEB Journal · doi:10.1096/fj.202502809r · Cited by 9 · see citing works

Glycosylation in neurological disorders: Mechanisms, crosstalk, and therapeutic implications

Wu, W., Wang, W., Xu, L., Yao, Y., Zhao, X., Zhong, J., Hu, J., Wang, L., Zhu, Y., & Wang, J. (2026) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2026.112144

Glycomic and Glycoproteomic Techniques in Neurodegenerative Disorders and Neurotrauma: Towards Personalized Markers

Kobeissy, F. H., Kobaisi, A., Peng, W., Barsa, C., Goli, M., Sibahi, A., Hayek, S. E., Abdelhady, S., Haidar, M. A., Sabra, M., et al. (2022) · Cells · doi:10.3390/cells11030581 · Cited by 28 · see citing works