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The calmodulin binding domains are present in proteins that serve as\nrisk factors and biomarkers associated with Alzheimer\u2019s disease, Parkinson\u2019s disease, Huntington\u2019s\ndisease, Amyotrophic Lateral Sclerosis, and other neurodegenerative diseases, suggesting calmodulin\nligands as emerging therapeutic targets for treatment. Inhibiting CaM to develop new therapies\nhas drawbacks, as CaM is a ubiquitous molecule involved in many regulatory pathways. Recently,\nnew strategies for disrupting CaM interactions with its targets have shown promising approaches to\ntreatment.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>:<\/jats:title>\n                    <jats:p>The structures of human CaM, its binding proteins, and inhibitors are well studied, with particular\nemphasis on the conservation of CaM amino acid sequences and the ability to bind protein fragments\nof high sequence variability, which exhibit common characteristics of amphipathic helices\ncarrying basic amino acids.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>:<\/jats:title>\n                    <jats:p>In this review, we discuss structural characteristics of CaM and its ligands in the context of transcriptional\nregulation. Specific binding of CaM to (1) basic region\/helix-loop-helix\/leucine zipper\nand (2) helix-turn-helix high mobility group box containing Sox families of transcription factors\nhighlights common features of CaM binding sequences, which suggest their regulatory functions.\nWe describe key proteins involved in neurodegeneration and transcription factors subject to calmodulin\nregulation that are candidates for the development of new approaches to treating neuronal\ndiseases.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.2174\/0113895575403663250812115441","type":"journal-article","created":{"date-parts":[[2025,8,24]],"date-time":"2025-08-24T11:05:16Z","timestamp":1756033516000},"page":"965-974","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Role of Calmodulin in Neurodegeneration and Neuroprotection"],"prefix":"10.2174","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5989-9944","authenticated-orcid":true,"given":"Natalya","family":"Kurochkina","sequence":"first","affiliation":[{"name":"Department of Biophysics, The School of Theoretical Modeling, Washington, DC, 20006, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7537-3130","authenticated-orcid":true,"given":"Parvathi","family":"Rudrabhatla","sequence":"additional","affiliation":[{"name":"Department of Biophysics, The School of Theoretical Modeling, Washington, DC, 20006, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"965","reference":[{"key":"ref=1","doi-asserted-by":"publisher","first-page":"183","DOI":"10.3390\/biom14020183","volume":"14","author":"Lisek M.","year":"2024","unstructured":"Lisek M.; Tomczak J.; Boczek T.; Zylinska L.; Calcium-associated proteins in neuroregeneration. 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