{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n FSD1 is a multifaceted protein entity that has been assigned distinct functions in different biological contexts. In the realm of growth‐factor regulation, studies on follistatin variants have shown that a specific FSD1 region contributes preferentially to myostatin binding, such that its manipulation can yield antagonists with reduced activin and GDF11 inhibition."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In a completely separate context, FSD1 has been identified as a centrosome‐associated protein that physically anchors microtubule asters to interphase centrosomes. This anchorage is critical for proper transition zone assembly during ciliogenesis and, hence, for normal embryonic development."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In plants, the designation “FSD1” is also used for an iron superoxide dismutase isoform that is part of the antioxidant defense machinery. Differential regulation of this FSD1 (along with related FSD2 proteins) has been associated with rapid stress-adaptive responses against conditions that induce oxidative damage."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " In human tissues, an unrelated FSD1 gene – encoding a protein that contains BBC, FN3, and SPRY domains and is predominantly expressed in the brain – has been characterized, suggesting roles in neural function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In addition, FSD1 has served as a valuable model in the field of protein design. A series of studies have computationally engineered a 28–residue mini-protein, commonly referred to as FSD‐1, which adopts a ββα (beta–beta–alpha) motif based on the zinc finger scaffold of Zif268 yet folds independently of metal coordination. Such work has provided significant insights into protein folding, stability, and the relationship between sequence variation and structural integrity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Finally, emerging evidence in oncological settings has linked aberrant epigenetic modifications of the FSD1 promoter to gastric carcinoma, which points to its potential use as a diagnostic biomarker and hints at roles in tumor biology."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": " Moreover, peptides derived from FSD1 have been detected with distinct spatial distributions in brain tissues, further suggesting that fragments of this protein may serve as useful markers of disease states."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In summary, FSD1 refers to a set of proteins with diverse, context-dependent functions – from modulating growth factor signaling and ensuring proper microtubule organization during ciliogenesis, to participating in antioxidative responses, neural functions, and even serving as a benchmark in de novo protein design – thereby underscoring its importance across several fields of biomedical research.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Alan L Schneyer, Yisrael Sidis, Anisha Gulati, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Endocrinology (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/en.2008-0259"}], "href": "https://doi.org/10.1210/en.2008-0259"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18535106"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18535106"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Hai-Qing Tu, Xuan-He Qin, Zhi-Bin Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Microtubule asters anchored by FSD1 control axoneme assembly and ciliogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-018-07664-2"}], "href": "https://doi.org/10.1038/s41467-018-07664-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30538248"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30538248"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Wojciech Pokora, Zbigniew Tukaj "}, {"type": "b", "children": [{"type": "t", "text": "Induction time of Fe-SOD synthesis and activity determine different tolerance of two Desmodesmus (green algae) strains to chloridazon: a study with synchronized cultures."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pestic Biochem Physiol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.pestbp.2013.05.007"}], "href": "https://doi.org/10.1016/j.pestbp.2013.05.007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25149238"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25149238"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "L Carim-Todd, M Escarceller, X Estivill, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Characterization of human FSD1, a novel brain specific gene on chromosome 19 with paralogy to 9q31."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2001)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0167-4781(01)00178-6"}], "href": "https://doi.org/10.1016/s0167-4781(01"}, {"type": "t", "text": "00178-6) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11267680"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11267680"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "B I Dahiyat, S L Mayo "}, {"type": "b", "children": [{"type": "t", "text": "De novo protein design: fully automated sequence selection."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (1997)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.278.5335.82"}], "href": "https://doi.org/10.1126/science.278.5335.82"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "9311930"}], "href": "https://pubmed.ncbi.nlm.nih.gov/9311930"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Katarzyna Koscielska-Kasprzak, Tomasz Cierpicki, Jacek Otlewski "}, {"type": "b", "children": [{"type": "t", "text": "Importance of alpha-helix N-capping motif in stabilization of betabetaalpha fold."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Protein Sci (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1110/ps.0301703"}], "href": "https://doi.org/10.1110/ps.0301703"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12761399"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12761399"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Chih-Chi Kuo, Ching-Yu Lin, Yu-Lueng Shih, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Frequent methylation of HOXA9 gene in tumor tissues and plasma samples from human hepatocellular carcinomas."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Chem Lab Med (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1515/cclm-2013-0780"}], "href": "https://doi.org/10.1515/cclm-2013-0780"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24681432"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24681432"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Bijon Chatterji, Clarissa Dickhut, Svenja Mielke, et al. "}, {"type": "b", "children": [{"type": "t", "text": "MALDI imaging mass spectrometry to investigate endogenous peptides in an animal model of Usher's disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proteomics (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/pmic.201300558"}], "href": "https://doi.org/10.1002/pmic.201300558"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24841751"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24841751"}]}]}]}