{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T02:25:26Z","timestamp":1791685526429,"version":"4.3.4"},"reference-count":216,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2024,2,17]],"date-time":"2024-02-17T00:00:00Z","timestamp":1708128000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Institutes of Health","award":["NS130702"],"award-info":[{"award-number":["NS130702"]}]},{"name":"National Institutes of Health","award":["NS101134"],"award-info":[{"award-number":["NS101134"]}]},{"name":"National Institutes of Health","award":["NS123770"],"award-info":[{"award-number":["NS123770"]}]},{"name":"National Institutes of Health","award":["NS116921"],"award-info":[{"award-number":["NS116921"]}]},{"name":"National Institutes of Health","award":["AG075656"],"award-info":[{"award-number":["AG075656"]}]},{"name":"National Institutes of Health","award":["MJFF-001006"],"award-info":[{"award-number":["MJFF-001006"]}]},{"name":"National Institutes of Health","award":["MJFF-022157"],"award-info":[{"award-number":["MJFF-022157"]}]},{"name":"Michael J. Fox foundation for Parkinson\u2019s Research","award":["NS130702"],"award-info":[{"award-number":["NS130702"]}]},{"name":"Michael J. Fox foundation for Parkinson\u2019s Research","award":["NS101134"],"award-info":[{"award-number":["NS101134"]}]},{"name":"Michael J. Fox foundation for Parkinson\u2019s Research","award":["NS123770"],"award-info":[{"award-number":["NS123770"]}]},{"name":"Michael J. Fox foundation for Parkinson\u2019s Research","award":["NS116921"],"award-info":[{"award-number":["NS116921"]}]},{"name":"Michael J. Fox foundation for Parkinson\u2019s Research","award":["AG075656"],"award-info":[{"award-number":["AG075656"]}]},{"name":"Michael J. Fox foundation for Parkinson\u2019s Research","award":["MJFF-001006"],"award-info":[{"award-number":["MJFF-001006"]}]},{"name":"Michael J. Fox foundation for Parkinson\u2019s Research","award":["MJFF-022157"],"award-info":[{"award-number":["MJFF-022157"]}]},{"name":"the American Parkinson Disease Association","award":["NS130702"],"award-info":[{"award-number":["NS130702"]}]},{"name":"the American Parkinson Disease Association","award":["NS101134"],"award-info":[{"award-number":["NS101134"]}]},{"name":"the American Parkinson Disease Association","award":["NS123770"],"award-info":[{"award-number":["NS123770"]}]},{"name":"the American Parkinson Disease Association","award":["NS116921"],"award-info":[{"award-number":["NS116921"]}]},{"name":"the American Parkinson Disease Association","award":["AG075656"],"award-info":[{"award-number":["AG075656"]}]},{"name":"the American Parkinson Disease Association","award":["MJFF-001006"],"award-info":[{"award-number":["MJFF-001006"]}]},{"name":"the American Parkinson Disease Association","award":["MJFF-022157"],"award-info":[{"award-number":["MJFF-022157"]}]},{"name":"the Puri Family philanthropy","award":["NS130702"],"award-info":[{"award-number":["NS130702"]}]},{"name":"the Puri Family philanthropy","award":["NS101134"],"award-info":[{"award-number":["NS101134"]}]},{"name":"the Puri Family philanthropy","award":["NS123770"],"award-info":[{"award-number":["NS123770"]}]},{"name":"the Puri Family philanthropy","award":["NS116921"],"award-info":[{"award-number":["NS116921"]}]},{"name":"the Puri Family philanthropy","award":["AG075656"],"award-info":[{"award-number":["AG075656"]}]},{"name":"the Puri Family philanthropy","award":["MJFF-001006"],"award-info":[{"award-number":["MJFF-001006"]}]},{"name":"the Puri Family philanthropy","award":["MJFF-022157"],"award-info":[{"award-number":["MJFF-022157"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Neurodegenerative diseases encompass a heterogeneous group of disorders that afflict millions of people worldwide. Characteristic protein aggregates are histopathological hallmark features of these disorders, including Amyloid \u03b2 (A\u03b2)-containing plaques and tau-containing neurofibrillary tangles in Alzheimer\u2019s disease, \u03b1-Synuclein (\u03b1-Syn)-containing Lewy bodies and Lewy neurites in Parkinson\u2019s disease and dementia with Lewy bodies, and mutant huntingtin (mHTT) in nuclear inclusions in Huntington\u2019s disease. These various aggregates are found in specific brain regions that are impacted by neurodegeneration and associated with clinical manifestations. Transglutaminase (TG2) (also known as tissue transglutaminase) is the most ubiquitously expressed member of the transglutaminase family with protein crosslinking activity. To date, A\u03b2, tau, \u03b1-Syn, and mHTT have been determined to be substrates of TG2, leading to their aggregation and implicating the involvement of TG2 in several pathophysiological events in neurodegenerative disorders. In this review, we summarize the biochemistry and physiologic functions of TG2 and describe recent advances in the pathogenetic role of TG2 in these diseases. We also review TG2 inhibitors tested in clinical trials and discuss recent TG2-targeting approaches, which offer new perspectives for the design of future highly potent and selective drugs with improved brain delivery as a disease-modifying treatment for neurodegenerative disorders.<\/jats:p>","DOI":"10.3390\/ijms25042364","type":"journal-article","created":{"date-parts":[[2024,2,19]],"date-time":"2024-02-19T05:39:56Z","timestamp":1708321196000},"page":"2364","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Pathogenetic Contributions and Therapeutic Implications of Transglutaminase 2 in Neurodegenerative Diseases"],"prefix":"10.3390","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8671-0040","authenticated-orcid":false,"given":"Jun","family":"Liu","sequence":"first","affiliation":[{"name":"RWJMS Institute for Neurological Therapeutics and Department of Neurology, Rutgers-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. Maral","family":"Mouradian","sequence":"additional","affiliation":[{"name":"RWJMS Institute for Neurological Therapeutics and Department of Neurology, Rutgers-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,2,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-3233(08)60217-X","article-title":"The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases","volume":"31","author":"Folk","year":"1977","journal-title":"Adv. Protein Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"12636","DOI":"10.1073\/pnas.1635052100","article-title":"Evolutionary specialization of a tryptophan indole group for transition-state stabilization by eukaryotic transglutaminases","volume":"100","author":"Iismaa","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Tatsukawa, H., and Hitomi, K. (2021). Role of Transglutaminase 2 in Cell Death, Survival, and Fibrosis. Cells, 10.","DOI":"10.3390\/cells10071842"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"34495","DOI":"10.18632\/oncotarget.26130","article-title":"Transglutaminase is a mesothelioma cancer stem cell survival protein that is required for tumor formation","volume":"9","author":"Adhikary","year":"2018","journal-title":"Oncotarget"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"5","DOI":"10.5483\/BMBRep.2018.51.1.227","article-title":"New insight into transglutaminase 2 and link to neurodegenerative diseases","volume":"51","author":"Min","year":"2018","journal-title":"BMB Rep."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1096\/fj.201902155R","article-title":"Glycolysis regulated transglutaminase 2 activation in cardiopulmonary fibrogenic remodeling","volume":"34","author":"Bhedi","year":"2020","journal-title":"FASEB J."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Moon, J.J., Choi, Y., Kim, K.H., Seo, A., Kwon, S., Kim, Y.C., Kim, D.K., Kim, Y.S., and Yang, S.H. (2022). Inhibiting Transglutaminase 2 Mediates Kidney Fibrosis via Anti-Apoptosis. Biomedicines, 10.","DOI":"10.3390\/biomedicines10061345"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Paolella, G., Sposito, S., Romanelli, A.M., and Caputo, I. (2022). Type 2 Transglutaminase in Coeliac Disease: A Key Player in Pathogenesis, Diagnosis and Therapy. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23147513"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1152\/physrev.00003.2023","article-title":"Tissue transglutaminase: A multifunctional and multisite regulator in health and disease","volume":"104","author":"Yao","year":"2024","journal-title":"Physiol. Rev."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"30715","DOI":"10.1074\/jbc.274.43.30715","article-title":"Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer\u2019s disease","volume":"274","author":"Kim","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1111\/j.1365-2796.2010.02275.x","article-title":"Type 2 transglutaminase in Huntington\u2019s disease: A double-edged sword with clinical potential","volume":"268","author":"Mastroberardino","year":"2010","journal-title":"J. Intern. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1016\/j.nbd.2011.10.012","article-title":"Increase in endoplasmic reticulum-associated tissue transglutaminase and enzymatic activation in a cellular model of Parkinson\u2019s disease","volume":"45","author":"Verhaar","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.nbd.2017.01.007","article-title":"Identification of brain substrates of transglutaminase by functional proteomics supports its role in neurodegenerative diseases","volume":"101","author":"Andre","year":"2017","journal-title":"Neurobiol. Dis."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1056\/NEJMoa2032441","article-title":"A Randomized Trial of a Transglutaminase 2 Inhibitor for Celiac Disease","volume":"385","author":"Schuppan","year":"2021","journal-title":"N. Engl. J. Med."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Buchold, C., Hils, M., Gerlach, U., Weber, J., Pelzer, C., Heil, A., Aeschlimann, D., and Pasternack, R. (2022). Features of ZED1227: The First-In-Class Tissue Transglutaminase Inhibitor Undergoing Clinical Evaluation for the Treatment of Celiac Disease. Cells, 11.","DOI":"10.3390\/cells11101667"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/s00726-011-1127-4","article-title":"Expression of transglutaminase-2 isoforms in normal human tissues and cancer cell lines: Dysregulation of alternative splicing in cancer","volume":"44","author":"Phatak","year":"2013","journal-title":"Amino Acids"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"12603","DOI":"10.1074\/jbc.M600146200","article-title":"Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity","volume":"281","author":"Begg","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/B978-0-12-394305-7.00001-X","article-title":"Cellular functions of tissue transglutaminase","volume":"294","author":"Nurminskaya","year":"2012","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Sestito, C., Breve, J.J.P., Killestein, J., Teunissen, C.E., Wilhelmus, M.M.M., Drukarch, B., and van Dam, A.M. (2018). Differential Expression of Tissue Transglutaminase Splice Variants in Peripheral Blood Mononuclear Cells of Primary Progressive Multiple Sclerosis Patients. Med. Sci., 6.","DOI":"10.3390\/medsci6040108"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Sima, L.E., Matei, D., and Condello, S. (2022). The Outside-In Journey of Tissue Transglutaminase in Cancer. Cells, 11.","DOI":"10.3390\/cells11111779"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"23675","DOI":"10.1074\/jbc.M503323200","article-title":"Identification of a novel recognition sequence for fibronectin within the NH2-terminal beta-sandwich domain of tissue transglutaminase","volume":"280","author":"Hang","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1007\/s00726-016-2296-y","article-title":"Dissecting the interaction between transglutaminase 2 and fibronectin","volume":"49","author":"Cardoso","year":"2017","journal-title":"Amino Acids"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"7083","DOI":"10.1111\/j.1742-4658.2009.07420.x","article-title":"Functional significance of five noncanonical Ca2+-binding sites of human transglutaminase 2 characterized by site-directed mutagenesis","volume":"276","author":"Kiraly","year":"2009","journal-title":"FEBS J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2743","DOI":"10.1073\/pnas.042454899","article-title":"Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity","volume":"99","author":"Liu","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"11815","DOI":"10.1073\/pnas.96.21.11815","article-title":"Interactions of G(h)\/transglutaminase with phospholipase Cdelta1 and with GTP","volume":"96","author":"Murthy","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0167-4838(93)90055-V","article-title":"Site-directed mutagenesis of human tissue transglutaminase: Cys-277 is essential for transglutaminase activity but not for GTPase activity","volume":"1202","author":"Lee","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"28273","DOI":"10.1021\/acsomega.0c04226","article-title":"Role of Tissue Transglutaminase Catalytic and Guanosine Triphosphate-Binding Domains in Renal Cell Carcinoma Progression","volume":"5","author":"Ulukan","year":"2020","journal-title":"ACS Omega"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"19683","DOI":"10.1073\/pnas.0609283103","article-title":"Mechanism of allosteric regulation of transglutaminase 2 by GTP","volume":"103","author":"Begg","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2738","DOI":"10.1073\/pnas.052715799","article-title":"Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity","volume":"99","author":"Murthy","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1560","DOI":"10.4103\/1673-5374.303027","article-title":"Targeting transglutaminase 2 as a potential disease modifying therapeutic strategy for synucleinopathies","volume":"16","author":"Zhang","year":"2021","journal-title":"Neural Regen. Res."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4717","DOI":"10.1111\/j.1742-4658.2011.08345.x","article-title":"Protein transamidation by transglutaminase 2 in cells: A disputed Ca2+-dependent action of a multifunctional protein","volume":"278","author":"Kiraly","year":"2011","journal-title":"FEBS J."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.bioorg.2014.06.003","article-title":"Acyl transfer mechanisms of tissue transglutaminase","volume":"57","author":"Keillor","year":"2014","journal-title":"Bioorg. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Maddock, R.M.A., Pollard, G.J., Moreau, N.G., Perry, J.J., and Race, P.R. (2020). Enzyme-catalysed polymer cross-linking: Biocatalytic tools for chemical biology, materials science and beyond. Biopolymers, 111.","DOI":"10.1002\/bip.23390"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Savoca, M.P., Tonoli, E., Atobatele, A.G., and Verderio, E.A.M. (2018). Biocatalysis by Transglutaminases: A Review of Biotechnological Applications. Micromachines, 9.","DOI":"10.3390\/mi9110562"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Tabolacci, C., De Martino, A., Mischiati, C., Feriotto, G., and Beninati, S. (2019). The Role of Tissue Transglutaminase in Cancer Cell Initiation, Survival and Progression. Med. Sci., 7.","DOI":"10.3390\/medsci7020019"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Occhigrossi, L., D\u2019Eletto, M., Barlev, N., and Rossin, F. (2021). The Multifaceted Role of HSF1 in Pathophysiology: Focus on Its Interplay with TG2. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22126366"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2420","DOI":"10.4049\/jimmunol.2001122","article-title":"Transglutaminase 2 Regulates Innate Immunity by Modulating the STING\/TBK1\/IRF3 Axis","volume":"206","author":"Occhigrossi","year":"2021","journal-title":"J. Immunol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1007\/s00018-023-04698-8","article-title":"Type 2 transglutaminase in the nucleus: The new epigenetic face of a cytoplasmic enzyme","volume":"80","author":"Rossin","year":"2023","journal-title":"Cell Mol. Life Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1038\/ncb3586","article-title":"Innate immune sensing of cytosolic chromatin fragments through cGAS promotes senescence","volume":"19","author":"Gluck","year":"2017","journal-title":"Nat. Cell Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1038\/s41586-023-06373-1","article-title":"cGAS-STING drives ageing-related inflammation and neurodegeneration","volume":"620","author":"Gulen","year":"2023","journal-title":"Nature"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/S1357-2725(99)00045-X","article-title":"Tissue transglutaminase: An enzyme with a split personality","volume":"31","author":"Chen","year":"1999","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.2741\/4536","article-title":"Tissue transglutaminase (TG2) and mitochondrial function and dysfunction","volume":"22","author":"Lai","year":"2017","journal-title":"Front. Biosci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"5166","DOI":"10.1016\/S0021-9258(18)89194-3","article-title":"Retinoic acid-induced expression of tissue transglutaminase in human promyelocytic leukemia (HL-60) cells","volume":"260","author":"Davies","year":"1985","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/S0301-0082(99)00052-0","article-title":"Tissue transglutaminase: A possible role in neurodegenerative diseases","volume":"61","author":"Lesort","year":"2000","journal-title":"Prog. Neurobiol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1007\/s00726-011-1018-8","article-title":"Monitoring of transglutaminase 2 under different oxidative stress conditions","volume":"42","author":"Caccamo","year":"2012","journal-title":"Amino Acids"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1038\/onc.2009.342","article-title":"Transglutaminase 2 suppresses apoptosis by modulating caspase 3 and NF-kappaB activity in hypoxic tumor cells","volume":"29","author":"Jang","year":"2010","journal-title":"Oncogene"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Su, T., Qin, X.Y., and Furutani, Y. (2021). Transglutaminase 2 as a Marker for Inflammation and Therapeutic Target in Sepsis. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22041897"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1165\/rcmb.2016-0379OC","article-title":"Extracellular Matrix Cross-Linking Enhances Fibroblast Growth and Protects against Matrix Proteolysis in Lung Fibrosis","volume":"58","author":"Philp","year":"2018","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"53725","DOI":"10.1074\/jbc.M407627200","article-title":"Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia","volume":"279","author":"Lee","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"7697","DOI":"10.4049\/jimmunol.180.11.7697","article-title":"Tissue transglutaminase activation modulates inflammation in cystic fibrosis via PPARgamma down-regulation","volume":"180","author":"Maiuri","year":"2008","journal-title":"J. Immunol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1016\/j.neuint.2010.08.019","article-title":"Transglutaminase 2 expression induced by lipopolysaccharide stimulation together with NO synthase induction in cultured astrocytes","volume":"57","author":"Takano","year":"2010","journal-title":"Neurochem. Int."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"12798","DOI":"10.1074\/jbc.273.21.12798","article-title":"Identification of a transforming growth factor-beta1\/bone morphogenetic protein 4 (TGF-beta1\/BMP4) response element within the mouse tissue transglutaminase gene promoter","volume":"273","author":"Ritter","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1007\/s00403-005-0582-8","article-title":"TGF-beta1 up-regulates transglutaminase two and fibronectin in dermal fibroblasts: A possible mechanism for the stabilization of tissue inflammation","volume":"297","author":"Quan","year":"2005","journal-title":"Arch. Dermatol. Res."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1006\/jaut.1999.0339","article-title":"The inhibitory effects of transforming growth factor-beta-1 (TGF-beta1) in autoimmune diseases","volume":"14","author":"Piccirillo","year":"2000","journal-title":"J. Autoimmun."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1093\/jb\/mvq043","article-title":"Cellular and molecular basis for the regulation of inflammation by TGF-beta","volume":"147","author":"Yoshimura","year":"2010","journal-title":"J. Biochem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/j.pharmthera.2011.12.003","article-title":"Transglutaminase 2: Biology, relevance to neurodegenerative diseases and therapeutic implications","volume":"133","author":"Grosso","year":"2012","journal-title":"Pharmacol. Ther."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Pinkas, D.M., Strop, P., Brunger, A.T., and Khosla, C. (2007). Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol., 5.","DOI":"10.1371\/journal.pbio.0050327"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1152\/physrev.00019.2013","article-title":"Transglutaminase regulation of cell function","volume":"94","author":"Eckert","year":"2014","journal-title":"Physiol. Rev."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3915","DOI":"10.1074\/jbc.275.6.3915","article-title":"Opposite effects of Ca(2+) and GTP binding on tissue transglutaminase tertiary structure","volume":"275","author":"Rossi","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1126\/science.7911253","article-title":"Gh: A GTP-binding protein with transglutaminase activity and receptor signaling function","volume":"264","author":"Nakaoka","year":"1994","journal-title":"Science"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1016\/S0021-9258(19)75724-X","article-title":"Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity","volume":"262","author":"Achyuthan","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1046\/j.1432-1327.1999.00437.x","article-title":"The structural basis for the regulation of tissue transglutaminase by calcium ions","volume":"262","author":"Casadio","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Tempest, R., Guarnerio, S., Maani, R., Cooper, J., and Peake, N. (2021). The Biological and Biomechanical Role of Transglutaminase-2 in the Tumour Microenvironment. Cancers, 13.","DOI":"10.3390\/cancers13112788"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Siegel, M., Strnad, P., Watts, R.E., Choi, K., Jabri, B., Omary, M.B., and Khosla, C. (2008). Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0001861"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"25402","DOI":"10.1074\/jbc.M109.097162","article-title":"Redox regulation of transglutaminase 2 activity","volume":"285","author":"Stamnaes","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"37866","DOI":"10.1074\/jbc.M111.287490","article-title":"Activation of extracellular transglutaminase 2 by thioredoxin","volume":"286","author":"Jin","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2775","DOI":"10.4049\/jimmunol.0900993","article-title":"SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation","volume":"183","author":"Luciani","year":"2009","journal-title":"J. Immunol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1016\/j.febslet.2009.01.032","article-title":"Degradation of transglutaminase 2 by calcium-mediated ubiquitination responding to high oxidative stress","volume":"583","author":"Jeong","year":"2009","journal-title":"FEBS Lett."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2498","DOI":"10.1096\/fj.07-095455","article-title":"TGFbeta mediates activation of transglutaminase 2 in response to oxidative stress that leads to protein aggregation","volume":"22","author":"Shin","year":"2008","journal-title":"FASEB J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.redox.2015.08.010","article-title":"Calcium and ROS: A mutual interplay","volume":"6","author":"Gorlach","year":"2015","journal-title":"Redox Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"C817","DOI":"10.1152\/ajpcell.00139.2004","article-title":"Calcium, ATP, and ROS: A mitochondrial love-hate triangle","volume":"287","author":"Brookes","year":"2004","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Baev, A.Y., Vinokurov, A.Y., Novikova, I.N., Dremin, V.V., Potapova, E.V., and Abramov, A.Y. (2022). Interaction of Mitochondrial Calcium and ROS in Neurodegeneration. Cells, 11.","DOI":"10.3390\/cells11040706"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/S0006-291X(03)00835-0","article-title":"Activation of in situ tissue transglutaminase by intracellular reactive oxygen species","volume":"305","author":"Lee","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Wongmekiat, O., Leelarungrayub, D., and Thamprasert, K. (2013). Alpha-lipoic acid attenuates renal injury in rats with obstructive nephropathy. Biomed. Res. Int., 2013.","DOI":"10.1155\/2013\/138719"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"fcad356","DOI":"10.1093\/braincomms\/fcad356","article-title":"Role of oxidative stress in neurodegenerative disorders: A review of reactive oxygen species and prevention by antioxidants","volume":"6","author":"Houldsworth","year":"2024","journal-title":"Brain Commun."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"3099","DOI":"10.1021\/acs.molpharmaceut.1c00322","article-title":"Co-Silencing of Tissue Transglutaminase-2 and Interleukin-15 Genes in a Celiac Disease Mimetic Mouse Model Using a Nanoparticle-in-Microsphere Oral System","volume":"18","author":"Attarwala","year":"2021","journal-title":"Mol. Pharm."},{"key":"ref_77","first-page":"567","article-title":"CRISPR\/Cas9 genome editing for neurodegenerative diseases","volume":"22","author":"Erguder","year":"2023","journal-title":"EXCLI J."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/s41392-023-01309-7","article-title":"CRISPR\/Cas9 therapeutics: Progress and prospects","volume":"8","author":"Li","year":"2023","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"4740","DOI":"10.1111\/j.1742-4658.2011.08347.x","article-title":"Novel roles for biogenic monoamines: From monoamines in transglutaminase-mediated post-translational protein modification to monoaminylation deregulation diseases","volume":"278","author":"Walther","year":"2011","journal-title":"FEBS J."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"14819","DOI":"10.1021\/bi701422h","article-title":"GTP-binding-defective forms of tissue transglutaminase trigger cell death","volume":"46","author":"Datta","year":"2007","journal-title":"Biochemistry"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1046\/j.1471-4159.2002.00898.x","article-title":"Transglutaminase overexpression sensitizes neuronal cell lines to apoptosis by increasing mitochondrial membrane potential and cellular oxidative stress","volume":"81","author":"Piacentini","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1007\/s00726-010-0500-z","article-title":"Transglutaminase 2: A multi-functional protein in multiple subcellular compartments","volume":"39","author":"Park","year":"2010","journal-title":"Amino Acids"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"3573","DOI":"10.1016\/j.celrep.2018.11.094","article-title":"Transglutaminase Type 2 Regulates ER-Mitochondria Contact Sites by Interacting with GRP75","volume":"25","author":"Rossin","year":"2018","journal-title":"Cell Rep."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"14377","DOI":"10.1074\/jbc.M111.326074","article-title":"Transglutaminase 2 promotes both caspase-dependent and caspase-independent apoptotic cell death via the calpain\/Bax protein signaling pathway","volume":"287","author":"Yoo","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/S0014-5793(99)00018-6","article-title":"Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3","volume":"446","author":"Peng","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"e2002","DOI":"10.1038\/cddis.2015.339","article-title":"Molecular mechanism by which acyclic retinoid induces nuclear localization of transglutaminase 2 in human hepatocellular carcinoma cells","volume":"6","author":"Shrestha","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"2973","DOI":"10.1016\/j.yexcr.2006.05.019","article-title":"Complex formation between tissue transglutaminase II (tTG) and vascular endothelial growth factor receptor 2 (VEGFR-2): Proposed mechanism for modulation of endothelial cell response to VEGF","volume":"312","author":"Dardik","year":"2006","journal-title":"Exp. Cell Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"2662","DOI":"10.1096\/fj.07-097709","article-title":"Transglutaminase 2 protects against ischemic insult, interacts with HIF1beta, and attenuates HIF1 signaling","volume":"22","author":"Filiano","year":"2008","journal-title":"FASEB J."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1097\/WNR.0000000000000895","article-title":"Subcellular localization patterns of transglutaminase 2 in astrocytes and neurons are differentially altered by hypoxia","volume":"28","author":"Feola","year":"2017","journal-title":"Neuroreport"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1053\/j.gastro.2009.01.007","article-title":"Role of transglutaminase 2 in liver injury via cross-linking and silencing of transcription factor Sp1","volume":"136","author":"Tatsukawa","year":"2009","journal-title":"Gastroenterology"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/s41586-019-1024-7","article-title":"Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3","volume":"567","author":"Farrelly","year":"2019","journal-title":"Nature"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"18817","DOI":"10.1074\/jbc.271.31.18817","article-title":"Core histones are glutaminyl substrates for tissue transglutaminase","volume":"271","author":"Ballestar","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1922","DOI":"10.1021\/bi001575b","article-title":"Conformational changes in the nucleosome followed by the selective accessibility of histone glutamines in the transglutaminase reaction: Effects of ionic strength","volume":"40","author":"Ballestar","year":"2001","journal-title":"Biochemistry"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1007\/s00441-014-1990-x","article-title":"Characterization of distinct sub-cellular location of transglutaminase type II: Changes in intracellular distribution in physiological and pathological states","volume":"358","author":"Piacentini","year":"2014","journal-title":"Cell Tissue Res."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"e2208672119","DOI":"10.1073\/pnas.2208672119","article-title":"TGM2-mediated histone transglutamination is dictated by steric accessibility","volume":"119","author":"Lukasak","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1002\/emmm.201000092","article-title":"Deja vu with a twist: Transglutaminases in bioenergetics and transcriptional dysfunction in Huntington\u2019s disease","volume":"2","year":"2010","journal-title":"EMBO Mol. Med."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1002\/emmm.201000084","article-title":"Inhibition of transglutaminase 2 mitigates transcriptional dysregulation in models of Huntington disease","volume":"2","author":"McConoughey","year":"2010","journal-title":"EMBO Mol. Med."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/s10930-008-9128-1","article-title":"Size distribution and molecular associations of plasma fibronectin and fibronectin crosslinked by transglutaminase 2","volume":"27","author":"Nelea","year":"2008","journal-title":"Protein J."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"5486","DOI":"10.1016\/j.biomaterials.2009.07.014","article-title":"The treatment of collagen fibrils by tissue transglutaminase to promote vascular smooth muscle cell contractile signaling","volume":"30","author":"Spurlin","year":"2009","journal-title":"Biomaterials"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"6518","DOI":"10.1016\/j.biomaterials.2005.04.017","article-title":"The cellular response to transglutaminase-cross-linked collagen","volume":"26","author":"Chau","year":"2005","journal-title":"Biomaterials"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1007\/s00726-008-0125-7","article-title":"Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin","volume":"36","author":"Forsprecher","year":"2009","journal-title":"Amino Acids"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/nrm1014","article-title":"Transglutaminases: Crosslinking enzymes with pleiotropic functions","volume":"4","author":"Lorand","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"4704","DOI":"10.1111\/j.1742-4658.2011.08346.x","article-title":"Extracellular TG2: Emerging functions and regulation","volume":"278","author":"Belkin","year":"2011","journal-title":"FEBS J."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"18005","DOI":"10.1074\/jbc.M111.337089","article-title":"Transglutaminase-2 interaction with heparin: Identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix","volume":"287","author":"Burhan","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"40995","DOI":"10.1038\/srep40995","article-title":"Astrocyte-derived tissue Transglutaminase affects fibronectin deposition, but not aggregation, during cuprizone-induced demyelination","volume":"7","author":"Breve","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Condello, S., Prasad, M., Atwani, R., and Matei, D. (2022). Tissue transglutaminase activates integrin-linked kinase and beta-catenin in ovarian cancer. J. Biol. Chem., 298.","DOI":"10.1016\/j.jbc.2022.102242"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"45049","DOI":"10.1038\/srep45049","article-title":"Global identification and analysis of isozyme-specific possible substrates crosslinked by transglutaminases using substrate peptides in mouse liver fibrosis","volume":"7","author":"Tatsukawa","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1093\/cvr\/cvx053","article-title":"Tissue transglutaminase induction in the pressure-overloaded myocardium regulates matrix remodelling","volume":"113","author":"Shinde","year":"2017","journal-title":"Cardiovasc. Res."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1038\/s41419-018-0573-2","article-title":"Cardiac fibrosis can be attenuated by blocking the activity of transglutaminase 2 using a selective small-molecule inhibitor","volume":"9","author":"Wang","year":"2018","journal-title":"Cell Death Dis."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Rudlong, J., Cheng, A., and Johnson, G.V.W. (2020). The role of transglutaminase 2 in mediating glial cell function and pathophysiology in the central nervous system. Anal. Biochem., 591.","DOI":"10.1016\/j.ab.2019.113556"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Elahi, A., Emerson, J., Rudlong, J., Keillor, J.W., Salois, G., Visca, A., Girardi, P., Johnson, G.V.W., and Proschel, C. (2021). Deletion or Inhibition of Astrocytic Transglutaminase 2 Promotes Functional Recovery after Spinal Cord Injury. Cells, 10.","DOI":"10.1101\/2021.09.15.460455"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"e33385","DOI":"10.7554\/eLife.33385","article-title":"Microglial transglutaminase-2 drives myelination and myelin repair via GPR56\/ADGRG1 in oligodendrocyte precursor cells","volume":"7","author":"Giera","year":"2018","journal-title":"Elife"},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Szondy, Z., Korponay-Szabo, I., Kiraly, R., Sarang, Z., and Tsay, G.J. (2017). Transglutaminase 2 in human diseases. Biomedicine, 7.","DOI":"10.1051\/bmdcn\/2017070315"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1038\/s41593-020-0687-6","article-title":"Synergy between amyloid-beta and tau in Alzheimer\u2019s disease","volume":"23","author":"Busche","year":"2020","journal-title":"Nat. Neurosci."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/s41572-021-00269-y","article-title":"Alzheimer disease","volume":"7","author":"Knopman","year":"2021","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1016\/j.bbamcr.2018.07.018","article-title":"Calcium signaling in Alzheimer\u2019s disease & therapies","volume":"1865","author":"Tong","year":"2018","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.ceca.2009.12.014","article-title":"The dysregulation of intracellular calcium in Alzheimer disease","volume":"47","author":"Supnet","year":"2010","journal-title":"Cell Calcium"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"449","DOI":"10.2217\/fnl.09.17","article-title":"Transglutaminase activation in neurodegenerative diseases","volume":"4","author":"Jeitner","year":"2009","journal-title":"Future Neurol."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Schrank, S., Barrington, N., and Stutzmann, G.E. (2020). Calcium-Handling Defects and Neurodegenerative Disease. Cold Spring Harb. Perspect. Biol., 12.","DOI":"10.1101\/cshperspect.a035212"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"709","DOI":"10.3389\/fphar.2020.00709","article-title":"Changes in PGC-1alpha\/SIRT1 Signaling Impact on Mitochondrial Homeostasis in Amyloid-Beta Peptide Toxicity Model","volume":"11","author":"Panes","year":"2020","journal-title":"Front. Pharmacol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.tins.2020.10.004","article-title":"Mitochondria and Calcium in Alzheimer\u2019s Disease: From Cell Signaling to Neuronal Cell Death","volume":"44","author":"Bacskai","year":"2021","journal-title":"Trends Neurosci."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1042\/CS20200844","article-title":"Mitochondria-associated membranes (MAMs): A potential therapeutic target for treating Alzheimer\u2019s disease","volume":"135","author":"Yu","year":"2021","journal-title":"Clin. Sci."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/nn.3028","article-title":"The toxic Abeta oligomer and Alzheimer\u2019s disease: An emperor in need of clothes","volume":"15","author":"Benilova","year":"2012","journal-title":"Nat. Neurosci."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Panes-Fernandez, J., Godoy, P.A., Gavilan, J., Ramirez-Molina, O., Burgos, C.F., Marileo, A., Flores-Nunez, O., Castro, P.A., Moraga-Cid, G., and Yevenes, G.E. (2023). TG2 promotes amyloid beta aggregates: Impact on ER-mitochondria crosstalk, calcium homeostasis and synaptic function in Alzheimer\u2019s disease. Biomed. Pharmacother., 162.","DOI":"10.1016\/j.biopha.2023.114596"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"20569","DOI":"10.1038\/srep20569","article-title":"Catalytically active tissue transglutaminase colocalises with Abeta pathology in Alzheimer\u2019s disease mouse models","volume":"6","author":"Wilhelmus","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Wilhelmus, M.M.M., Chouchane, O., Loos, M., Jongenelen, C.A.M., Breve, J.J.P., Jonker, A., Bol, J., Smit, A.B., and Drukarch, B. (2022). Absence of tissue transglutaminase reduces amyloid-beta pathology in APP23 mice. Neuropathol. Appl. Neurobiol., 48.","DOI":"10.1111\/nan.12796"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Wilhelmus, M.M.M., Tonoli, E., Coveney, C., Boocock, D.J., Jongenelen, C.A.M., Breve, J.J.P., Verderio, E.A.M., and Drukarch, B. (2022). The Transglutaminase-2 Interactome in the APP23 Mouse Model of Alzheimer\u2019s Disease. Cells, 11.","DOI":"10.3390\/cells11030389"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0006-8993(96)01431-X","article-title":"Transglutaminase activity is increased in Alzheimer\u2019s disease brain","volume":"751","author":"Johnson","year":"1997","journal-title":"Brain Res."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1006\/nbdi.2002.0535","article-title":"Cerebrospinal fluid tissue transglutaminase as a biochemical marker for Alzheimer\u2019s disease","volume":"11","author":"Bonelli","year":"2002","journal-title":"Neurobiol. Dis."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1111\/j.1750-3639.2008.00197.x","article-title":"Transglutaminases and transglutaminase-catalyzed cross-links colocalize with the pathological lesions in Alzheimer\u2019s disease brain","volume":"19","author":"Wilhelmus","year":"2009","journal-title":"Brain Pathol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1016\/j.neurobiolaging.2012.10.005","article-title":"Tissue transglutaminase colocalizes with extracellular matrix proteins in cerebral amyloid angiopathy","volume":"34","author":"Schul","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Wilhelmus, M.M.M., Jongenelen, C.A., Bol, J., and Drukarch, B. (2020). Interaction between tissue transglutaminase and amyloid-beta: Protein-protein binding versus enzymatic crosslinking. Anal. Biochem., 592.","DOI":"10.1016\/j.ab.2020.113578"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2607","DOI":"10.1046\/j.1471-4159.1998.71062607.x","article-title":"Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase","volume":"71","author":"Murthy","year":"1998","journal-title":"J. Neurochem."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1871","DOI":"10.1046\/j.1471-4159.1999.01871.x","article-title":"Tau is modified by tissue transglutaminase in situ: Possible functional and metabolic effects of polyamination","volume":"73","author":"Tucholski","year":"1999","journal-title":"J. Neurochem."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/s13024-023-00601-y","article-title":"Common mouse models of tauopathy reflect early but not late human disease","volume":"18","author":"Wenger","year":"2023","journal-title":"Mol. Neurodegener."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1226","DOI":"10.1523\/JNEUROSCI.3263-04.2005","article-title":"Tau protein is cross-linked by transglutaminase in P301L tau transgenic mice","volume":"25","author":"Halverson","year":"2005","journal-title":"J. Neurosci."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1186\/s40478-023-01546-5","article-title":"Human tau-overexpressing mice recapitulate brainstem involvement and neuropsychiatric features of early Alzheimer\u2019s disease","volume":"11","author":"Khan","year":"2023","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"3295","DOI":"10.1074\/jbc.M004776200","article-title":"Intron-exon swapping of transglutaminase mRNA and neuronal Tau aggregation in Alzheimer\u2019s disease","volume":"276","author":"Citron","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0197-0186(01)00061-4","article-title":"Transglutaminase bonds in neurofibrillary tangles and paired helical filament tau early in Alzheimer\u2019s disease","volume":"40","author":"Singer","year":"2002","journal-title":"Neurochem. Int."},{"key":"ref_140","first-page":"427","article-title":"Parkinson\u2019s Disease Drug Therapies in the Clinical Trial Pipeline: 2023 Update","volume":"13","author":"McFarthing","year":"2023","journal-title":"J. Park. Dis."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1038\/s41419-023-05672-9","article-title":"Alpha-synuclein in Parkinson\u2019s disease and other synucleinopathies: From overt neurodegeneration back to early synaptic dysfunction","volume":"14","author":"Calabresi","year":"2023","journal-title":"Cell Death Dis."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrn.2016.178","article-title":"Selective neuronal vulnerability in Parkinson disease","volume":"18","author":"Surmeier","year":"2017","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.1073\/pnas.0438021100","article-title":"Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson\u2019s disease and dementia with Lewy bodies","volume":"100","author":"Junn","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1096\/fj.03-0829fje","article-title":"Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson\u2019s disease","volume":"18","author":"Andringa","year":"2004","journal-title":"FASEB J."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"4280","DOI":"10.1096\/fj.14-251413","article-title":"Transglutaminase 2 exacerbates alpha-synuclein toxicity in mice and yeast","volume":"28","author":"Grosso","year":"2014","journal-title":"FASEB J."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.neuroscience.2020.05.047","article-title":"Transglutaminase 2 Depletion Attenuates alpha-Synuclein Mediated Toxicity in Mice","volume":"441","author":"Zhang","year":"2020","journal-title":"Neuroscience"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.neuint.2011.03.004","article-title":"Blockade of enzyme activity inhibits tissue transglutaminase-mediated transamidation of alpha-synuclein in a cellular model of Parkinson\u2019s disease","volume":"58","author":"Verhaar","year":"2011","journal-title":"Neurochem. Int."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0197-0186(01)00062-6","article-title":"Protein crosslinking, tissue transglutaminase, alternative splicing and neurodegeneration","volume":"40","author":"Citron","year":"2002","journal-title":"Neurochem. Int."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"13128","DOI":"10.1074\/jbc.M809067200","article-title":"Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: Implications for the pathogenesis of Parkinson disease","volume":"284","author":"Schmid","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1002\/jnr.23535","article-title":"PINK1 phosphorylates transglutaminase 2 and blocks its proteasomal degradation","volume":"93","author":"Min","year":"2015","journal-title":"J. Neurosci. Res."},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Leitao, A.D.G., Rudolffi-Soto, P., Chappard, A., Bhumkar, A., Lau, D., Hunter, D.J.B., Gambin, Y., and Sierecki, E. (2021). Selectivity of Lewy body protein interactions along the aggregation pathway of alpha-synuclein. Commun. Biol., 4.","DOI":"10.1038\/s42003-021-02624-x"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1038\/s41582-020-0389-4","article-title":"Huntington disease: New insights into molecular pathogenesis and therapeutic opportunities","volume":"16","author":"Tabrizi","year":"2020","journal-title":"Nat. Rev. Neurol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"3517","DOI":"10.1016\/j.neuron.2023.09.036","article-title":"HD and SCA1: Tales from two 30-year journeys since gene discovery","volume":"111","author":"Thompson","year":"2023","journal-title":"Neuron"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.expneurol.2011.12.013","article-title":"Protein aggregates in Huntington\u2019s disease","volume":"238","author":"Arrasate","year":"2012","journal-title":"Exp. Neurol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","article-title":"Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain","volume":"277","author":"DiFiglia","year":"1997","journal-title":"Science"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"6579","DOI":"10.1038\/s41467-021-26684-z","article-title":"Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties","volume":"12","author":"Riguet","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"42","DOI":"10.3389\/fnmol.2013.00042","article-title":"Expression of genes encoding the calcium signalosome in cellular and transgenic models of Huntington\u2019s disease","volume":"6","author":"Czeredys","year":"2013","journal-title":"Front. Mol. Neurosci."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/S0896-6273(03)00366-0","article-title":"Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1","volume":"39","author":"Tang","year":"2003","journal-title":"Neuron"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"76","DOI":"10.4161\/pri.23581","article-title":"Neuronal Ca(2+) dyshomeostasis in Huntington disease","volume":"7","author":"Giacomello","year":"2013","journal-title":"Prion"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1093\/jnen\/62.1.14","article-title":"Transglutaminase cross-links in intranuclear inclusions in Huntington disease","volume":"62","author":"Zainelli","year":"2003","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1954","DOI":"10.1523\/JNEUROSCI.4424-03.2004","article-title":"Calmodulin regulates transglutaminase 2 cross-linking of huntingtin","volume":"24","author":"Zainelli","year":"2004","journal-title":"J. Neurosci."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"7388","DOI":"10.1073\/pnas.96.13.7388","article-title":"Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington\u2019s disease brain nuclei","volume":"96","author":"Karpuj","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1111\/j.1471-4159.2008.05350.x","article-title":"Increased levels of gamma-glutamylamines in Huntington disease CSF","volume":"106","author":"Jeitner","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.1093\/hmg\/ddr075","article-title":"Mutant huntingtin causes defective actin remodeling during stress: Defining a new role for transglutaminase 2 in neurodegenerative disease","volume":"20","author":"Munsie","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"982074","DOI":"10.3389\/fncel.2022.982074","article-title":"Cytoskeletal dysregulation and neurodegenerative disease: Formation, monitoring, and inhibition of cofilin-actin rods","volume":"16","author":"Wurz","year":"2022","journal-title":"Front. Cell Neurosci."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"72","DOI":"10.4161\/nucl.14508","article-title":"The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation","volume":"2","author":"Obrdlik","year":"2011","journal-title":"Nucleus"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1999","DOI":"10.1002\/ar.23959","article-title":"Nuclear Actin: From Discovery to Function","volume":"301","author":"Kelpsch","year":"2018","journal-title":"Anat. Rec."},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Schulze-Krebs, A., Canneva, F., Stemick, J., Plank, A.C., Harrer, J., Bates, G.P., Aeschlimann, D., Steffan, J.S., and von Horsten, S. (2021). Transglutaminase 6 Is Colocalized and Interacts with Mutant Huntingtin in Huntington Disease Rodent Animal Models. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22168914"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Azam, S., Haque, M.E., Balakrishnan, R., Kim, I.S., and Choi, D.K. (2021). The Ageing Brain: Molecular and Cellular Basis of Neurodegeneration. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.683459"},{"key":"ref_170","doi-asserted-by":"crossref","unstructured":"Jankovska, N., and Matej, R. (2021). Molecular Pathology of ALS: What We Currently Know and What Important Information Is Still Missing. Diagnostics, 11.","DOI":"10.3390\/diagnostics11081365"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1111763","DOI":"10.3389\/fnins.2022.1111763","article-title":"Comparing therapeutic modulators of the SOD1 G93A Amyotrophic Lateral Sclerosis mouse pathophysiology","volume":"16","author":"Lee","year":"2022","journal-title":"Front. Neurosci."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/S0022-510X(98)00088-4","article-title":"Transglutaminase activity in serum and cerebrospinal fluid in sporadic amyotrophic lateral sclerosis: A possible use as an indicator of extent of the motor neuron loss","volume":"158","author":"Fujita","year":"1998","journal-title":"J. Neurol. Sci."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1111\/jnc.12441","article-title":"Transglutaminase 2 accelerates neuroinflammation in amyotrophic lateral sclerosis through interaction with misfolded superoxide dismutase 1","volume":"128","author":"Oono","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"1622","DOI":"10.1002\/glia.21204","article-title":"Tissue transglutaminase activity is involved in the differentiation of oligodendrocyte precursor cells into myelin-forming oligodendrocytes during CNS remyelination","volume":"59","author":"Baron","year":"2011","journal-title":"Glia"},{"key":"ref_175","doi-asserted-by":"crossref","unstructured":"Chrobok, N.L., Bol, J., Jongenelen, C.A., Breve, J.J.P., El Alaoui, S., Wilhelmus, M.M.M., Drukarch, B., and van Dam, A.M. (2018). Characterization of Transglutaminase 2 activity inhibitors in monocytes in vitro and their effect in a mouse model for multiple sclerosis. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0196433"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1093\/jnen\/nlz030","article-title":"Tissue Transglutaminase Appears in Monocytes and Macrophages but Not in Lymphocytes in White Matter Multiple Sclerosis Lesions","volume":"78","author":"Chrobok","year":"2019","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"e998","DOI":"10.1212\/NXI.0000000000000998","article-title":"Tissue Transglutaminase Expression Associates With Progression of Multiple Sclerosis","volume":"8","author":"Sestito","year":"2021","journal-title":"Neurol. Neuroimmunol. Neuroinflamm."},{"key":"ref_178","doi-asserted-by":"crossref","unstructured":"Pearse, D.D., Hefley, A.B., Morales, A.A., and Ghosh, M. (2022). Comparative Profiling of TG2 and Its Effectors in Human Relapsing Remitting and Progressive Multiple Sclerosis. Biomedicines, 10.","DOI":"10.3390\/biomedicines10061241"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/j.clim.2012.08.009","article-title":"Transglutaminase 2 exacerbates experimental autoimmune encephalomyelitis through positive regulation of encephalitogenic T cell differentiation and inflammation","volume":"145","author":"Oh","year":"2012","journal-title":"Clin. Immunol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.bbi.2015.06.023","article-title":"Tissue Transglutaminase contributes to experimental multiple sclerosis pathogenesis and clinical outcome by promoting macrophage migration","volume":"50","author":"Chrobok","year":"2015","journal-title":"Brain Behav. Immun."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1080\/14728222.2021.1989410","article-title":"Transglutaminase 2 as a therapeutic target for neurological conditions","volume":"25","author":"Keillor","year":"2021","journal-title":"Expert. Opin. Ther. Targets"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.tips.2014.10.014","article-title":"Inhibitors of tissue transglutaminase","volume":"36","author":"Keillor","year":"2015","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1021\/acsmedchemlett.3c00443","article-title":"Development and Utilization of Novel Transglutaminase 2 Inhibitors for Potential Treatment of Autoimmune Disease and Gastrointestinal Disorder","volume":"14","author":"Kargbo","year":"2023","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/j.pharmthera.2007.05.003","article-title":"Transglutaminase 2 inhibitors and their therapeutic role in disease states","volume":"115","author":"Siegel","year":"2007","journal-title":"Pharmacol. Ther."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"3454","DOI":"10.1016\/S0021-9258(19)69630-4","article-title":"Binding and internalization of 125I-alpha 2-macroglobulin by cultured fibroblasts","volume":"256","author":"Dickson","year":"1981","journal-title":"J. Biol. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1038\/ng0298-111","article-title":"Suppression of aggregate formation and apoptosis by transglutaminase inhibitors in cells expressing truncated DRPLA protein with an expanded polyglutamine stretch","volume":"18","author":"Igarashi","year":"1998","journal-title":"Nat. Genet."},{"key":"ref_187","doi-asserted-by":"crossref","unstructured":"Jeitner, T.M., Pinto, J.T., and Cooper, A.J.L. (2018). Cystamine and cysteamine as inhibitors of transglutaminase activity in vivo. Biosci. Rep., 38.","DOI":"10.1042\/BSR20180691"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"3359","DOI":"10.1021\/acs.biochem.8b00204","article-title":"Cystamine and Disulfiram Inhibit Human Transglutaminase 2 via an Oxidative Mechanism","volume":"57","author":"Palanski","year":"2018","journal-title":"Biochemistry"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.3389\/fneur.2019.01315","article-title":"Therapeutic Applications of Cysteamine and Cystamine in Neurodegenerative and Neuropsychiatric Diseases","volume":"10","author":"Paul","year":"2019","journal-title":"Front. Neurol."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"129","DOI":"10.3233\/JHD-180312","article-title":"Cysteamine Protects Neurons from Mutant Huntingtin Toxicity","volume":"8","author":"Arbez","year":"2019","journal-title":"J. Huntingt. Dis."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1038\/jcbfm.2013.53","article-title":"Transglutaminase is a therapeutic target for oxidative stress, excitotoxicity and stroke: A new epigenetic kid on the CNS block","volume":"33","author":"Basso","year":"2013","journal-title":"J. Cereb. Blood Flow. Metab."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1002\/mds.20756","article-title":"CYTE-I-HD: Phase I dose finding and tolerability study of cysteamine (Cystagon) in Huntington\u2019s disease","volume":"21","author":"Dubinsky","year":"2006","journal-title":"Mov. Disord."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1002\/mds.26101","article-title":"A phase II, open-label evaluation of cysteamine tolerability in patients with Huntington\u2019s disease","volume":"30","author":"Prundean","year":"2015","journal-title":"Mov. Disord."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1111\/j.1747-0285.2008.00696.x","article-title":"Reversible and competitive cinnamoyl triazole inhibitors of tissue transglutaminase","volume":"72","author":"Pardin","year":"2008","journal-title":"Chem. Biol. Drug Des."},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Caron, N.S., Munsie, L.N., Keillor, J.W., and Truant, R. (2012). Using FLIM-FRET to measure conformational changes of transglutaminase type 2 in live cells. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0044159"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"2981","DOI":"10.1038\/onc.2016.452","article-title":"Transamidase site-targeted agents alter the conformation of the transglutaminase cancer stem cell survival protein to reduce GTP binding activity and cancer stem cell survival","volume":"36","author":"Kerr","year":"2017","journal-title":"Oncogene"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1002\/mc.22375","article-title":"Transglutaminase is a tumor cell and cancer stem cell survival factor","volume":"54","author":"Eckert","year":"2015","journal-title":"Mol. Carcinog."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1021\/bi061787u","article-title":"Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor","volume":"46","author":"Case","year":"2007","journal-title":"Biochemistry"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1161\/HYPERTENSIONAHA.120.15352","article-title":"Transglutaminase 2 Inhibitor LDN 27219 Age-Dependently Lowers Blood Pressure and Improves Endothelium-Dependent Vasodilation in Resistance Arteries","volume":"77","author":"Pinilla","year":"2021","journal-title":"Hypertension"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1038\/s41417-023-00641-y","article-title":"Transglutaminase 2 is associated with adverse colorectal cancer survival and represents a therapeutic target","volume":"30","author":"Malkomes","year":"2023","journal-title":"Cancer Gene Ther."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"34379","DOI":"10.18632\/oncotarget.26193","article-title":"A small molecule regulator of tissue transglutaminase conformation inhibits the malignant phenotype of cancer cells","volume":"9","author":"Katt","year":"2018","journal-title":"Oncotarget"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1039\/D2MD00417H","article-title":"Novel irreversible peptidic inhibitors of transglutaminase 2","volume":"14","author":"Cundy","year":"2023","journal-title":"RSC Med. Chem."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1039\/D2MD00378C","article-title":"The war on hTG2: Warhead optimization in small molecule human tissue transglutaminase inhibitors","volume":"14","author":"Mader","year":"2023","journal-title":"RSC Med. Chem."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"3861","DOI":"10.1007\/s00204-020-02852-w","article-title":"Neurite outgrowth inhibitory levels of organophosphates induce tissue transglutaminase activity in differentiating N2a cells: Evidence for covalent adduct formation","volume":"94","author":"Almami","year":"2020","journal-title":"Arch. Toxicol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/j.chembiol.2005.02.007","article-title":"Chemistry and biology of dihydroisoxazole derivatives: Selective inhibitors of human transglutaminase 2","volume":"12","author":"Choi","year":"2005","journal-title":"Chem. Biol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"2563","DOI":"10.1038\/sj.onc.1210048","article-title":"Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy","volume":"26","author":"Yuan","year":"2007","journal-title":"Oncogene"},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Dafik, L., Albertelli, M., Stamnaes, J., Sollid, L.M., and Khosla, C. (2012). Activation and inhibition of transglutaminase 2 in mice. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0030642"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"7493","DOI":"10.1021\/jm060839a","article-title":"Structure-activity relationship analysis of the selective inhibition of transglutaminase 2 by dihydroisoxazoles","volume":"49","author":"Watts","year":"2006","journal-title":"J. Med. Chem."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"20525","DOI":"10.18632\/oncotarget.3890","article-title":"Type II transglutaminase stimulates epidermal cancer stem cell epithelial-mesenchymal transition","volume":"6","author":"Fisher","year":"2015","journal-title":"Oncotarget"},{"key":"ref_210","first-page":"208","article-title":"The complex role of transglutaminase 2 in glioblastoma proliferation","volume":"19","author":"Gundemir","year":"2017","journal-title":"Neuro Oncol."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1517\/13543776.2016.1115836","article-title":"Transglutaminase inhibitors: A patent review","volume":"26","author":"Keillor","year":"2016","journal-title":"Expert. Opin. Ther. Pat."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"7910","DOI":"10.1021\/acs.jmedchem.7b01070","article-title":"Structure-Activity Relationships of Potent, Targeted Covalent Inhibitors That Abolish Both the Transamidation and GTP Binding Activities of Human Tissue Transglutaminase","volume":"60","author":"Akbar","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"114172","DOI":"10.1016\/j.ejmech.2022.114172","article-title":"Structure-activity relationships of N-terminal variants of peptidomimetic tissue transglutaminase inhibitors","volume":"232","author":"McNeil","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.2217\/nnm-2019-0443","article-title":"Current advances in the development of novel polymeric nanoparticles for the treatment of neurodegenerative diseases","volume":"15","author":"Cano","year":"2020","journal-title":"Nanomedicine"},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Lamptey, R.N.L., Chaulagain, B., Trivedi, R., Gothwal, A., Layek, B., and Singh, J. (2022). A Review of the Common Neurodegenerative Disorders: Current Therapeutic Approaches and the Potential Role of Nanotherapeutics. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23031851"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"2227","DOI":"10.1093\/brain\/awad014","article-title":"Multifaceted nanoparticles: Emerging mechanisms and therapies in neurodegenerative diseases","volume":"146","author":"Mistretta","year":"2023","journal-title":"Brain"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/4\/2364\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T14:01:10Z","timestamp":1760104870000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/4\/2364"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,2,17]]},"references-count":216,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2024,2]]}},"alternative-id":["ijms25042364"],"URL":"https:\/\/doi.org\/10.3390\/ijms25042364","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,2,17]]}}}