Relevant bibliographies by topics / Β-Trefoil

Academic literature on the topic 'Β-Trefoil'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic "Β-Trefoil"

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Longo, Liam M., Rachel Kolodny, and Shawn E. McGlynn. "Evidence for the emergence of β-trefoils by ‘Peptide Budding’ from an IgG-like β-sandwich." PLOS Computational Biology 18, no. 2 (February 14, 2022): e1009833. http://dx.doi.org/10.1371/journal.pcbi.1009833.

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As sequence and structure comparison algorithms gain sensitivity, the intrinsic interconnectedness of the protein universe has become increasingly apparent. Despite this general trend, β-trefoils have emerged as an uncommon counterexample: They are an isolated protein lineage for which few, if any, sequence or structure associations to other lineages have been identified. If β-trefoils are, in fact, remote islands in sequence-structure space, it implies that the oligomerizing peptide that founded the β-trefoil lineage itself arose de novo. To better understand β-trefoil evolution, and to probe the limits of fragment sharing across the protein universe, we identified both ‘β-trefoil bridging themes’ (evolutionarily-related sequence segments) and ‘β-trefoil-like motifs’ (structure motifs with a hallmark feature of the β-trefoil architecture) in multiple, ostensibly unrelated, protein lineages. The success of the present approach stems, in part, from considering β-trefoil sequence segments or structure motifs rather than the β-trefoil architecture as a whole, as has been done previously. The newly uncovered inter-lineage connections presented here suggest a novel hypothesis about the origins of the β-trefoil fold itself–namely, that it is a derived fold formed by ‘budding’ from an Immunoglobulin-like β-sandwich protein. These results demonstrate how the evolution of a folded domain from a peptide need not be a signature of antiquity and underpin an emerging truth: few protein lineages escape nature’s sewing table.
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Murzin, Alexey G., Arthur M. Lesk, and Cyrus Chothia. "β-Trefoil fold." Journal of Molecular Biology 223, no. 2 (January 1992): 531–43. http://dx.doi.org/10.1016/0022-2836(92)90668-a.

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Valenti, Maria Teresa, Giulia Marchetto, Massimiliano Perduca, Natascia Tiso, Monica Mottes, and Luca Dalle Carbonare. "BEL β-Trefoil Reduces the Migration Ability of RUNX2 Expressing Melanoma Cells in Xenotransplanted Zebrafish." Molecules 25, no. 6 (March 11, 2020): 1270. http://dx.doi.org/10.3390/molecules25061270.

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RUNX2, a master osteogenic transcript ion factor, is overexpressed in several cancer cells; in melanoma it promotes cells migration and invasion as well as neoangiogenesis. The annual mortality rates related to metastatic melanoma are high and novel agents are needed to improve melanoma patients’ survival. It has been shown that lectins specifically target malignant cells since they present the Thomsen–Friedenreich antigen. This disaccharide is hidden in normal cells, while it allows selective lectins binding in transformed cells. Recently, an edible lectin named BEL β-trefoil has been obtained from the wild mushroom Boletus edulis. Our previous study showed BEL β-trefoil effects on transcription factor RUNX2 downregulation as well as on the migration ability in melanoma cells treated in vitro. Therefore, to better understand the role of this lectin, we investigated the BEL β-trefoil effects in a zebrafish in vivo model, transplanted with human melanoma cells expressing RUNX2. Our data showed that BEL β-trefoil is able to spread in the tissues and to reduce the formation of metastases in melanoma xenotransplanted zebrafish. In conclusion, BEL β-trefoil can be considered an effective biomolecule to counteract melanoma disease.
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Avanzo Caglič, Petra, Miha Renko, Dušan Turk, Janko Kos, and Jerica Sabotič. "Fungal β-trefoil trypsin inhibitors cnispin and cospin demonstrate the plasticity of the β-trefoil fold." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1844, no. 10 (October 2014): 1749–56. http://dx.doi.org/10.1016/j.bbapap.2014.07.004.

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Khan, Farha, Devanshu Kurre, and K. Suguna. "Crystal structures of a β-trefoil lectin from Entamoeba histolytica in monomeric and a novel disulfide bond-mediated dimeric forms." Glycobiology 30, no. 7 (January 21, 2020): 474–88. http://dx.doi.org/10.1093/glycob/cwaa001.

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Abstract β-Trefoil lectins are galactose/N-acetyl galactosamine specific lectins, which are widely distributed across all kingdoms of life and are known to perform several important functions. However, there is no report available on the characterization of these lectins from protozoans. We have performed structural and biophysical studies on a β-trefoil lectin from Entamoeba histolytica (EntTref), which exists as a mixture of monomers and dimers in solution. Further, we have determined the affinities of EntTref for rhamnose, galactose and different galactose-linked sugars. We obtained the crystal structure of EntTref in a sugar-free form (EntTref_apo) and a rhamnose-bound form (EntTref_rham). A novel Cys residue-mediated dimerization was revealed in the crystal structure of EntTref_apo while the structure of EntTref_rham provided the structural basis for the recognition of rhamnose by a β-trefoil lectin for the first time. To the best of our knowledge, this is the only report of the structural, functional and biophysical characterization of a β-trefoil lectin from a protozoan source and the first report of Cys-mediated dimerization in this class of lectins.
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Renko, Miha, Tanja Zupan, David F. Plaza, Stefanie S. Schmieder, Milica Perišić Nanut, Janko Kos, Dušan Turk, Markus Künzler, and Jerica Sabotič. "Cocaprins, β-trefoil Fold Inhibitors of Cysteine and Aspartic Proteases from Coprinopsis cinerea." International Journal of Molecular Sciences 23, no. 9 (April 28, 2022): 4916. http://dx.doi.org/10.3390/ijms23094916.

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We introduce a new family of fungal protease inhibitors with β-trefoil fold from the mushroom Coprinopsis cinerea, named cocaprins, which inhibit both cysteine and aspartic proteases. Two cocaprin-encoding genes are differentially expressed in fungal tissues. One is highly transcribed in vegetative mycelium and the other in the stipes of mature fruiting bodies. Cocaprins are small proteins (15 kDa) with acidic isoelectric points that form dimers. The three-dimensional structure of cocaprin 1 showed similarity to fungal β-trefoil lectins. Cocaprins inhibit plant C1 family cysteine proteases with Ki in the micromolar range, but do not inhibit the C13 family protease legumain, which distinguishes them from mycocypins. Cocaprins also inhibit the aspartic protease pepsin with Ki in the low micromolar range. Mutagenesis revealed that the β2-β3 loop is involved in the inhibition of cysteine proteases and that the inhibitory reactive sites for aspartic and cysteine proteases are located at different positions on the protein. Their biological function is thought to be the regulation of endogenous proteolytic activities or in defense against fungal antagonists. Cocaprins are the first characterized aspartic protease inhibitors with β-trefoil fold from fungi, and demonstrate the incredible plasticity of loop functionalization in fungal proteins with β-trefoil fold.
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Renko, Miha, Jerica Sabotič, and Dušan Turk. "β-Trefoil inhibitors – from the work of Kunitz onward." Biological Chemistry 393, no. 10 (October 1, 2012): 1043–54. http://dx.doi.org/10.1515/hsz-2012-0159.

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Abstract Protein protease inhibitors are the tools of nature in controlling proteolytic enzymes. They come in different shapes and sizes. The β-trefoil protease inhibitors that come from plants, first discovered by Kunitz, were later complemented with representatives from higher fungi. They inhibit serine (families S1 and S8) and cysteine proteases (families C1 and C13) as well as other hydrolases. Their versatility is the result of the plasticity of the loops coming out of the stable β-trefoil scaffold. For this reason, they display several different mechanisms of inhibition involving different positions of the loops and their combinations. Natural diversity, as well as the initial successes in de novo protein engineering, makes the β-trefoil proteins a promising starting point for the generation of strong, specific, multitarget inhibitors capable of inhibiting multiple types of hydrolytic enzymes and simultaneously interacting with different protein, carbohydrate, or DNA molecules. This pool of knowledge opens up new possibilities for the exploration of their naturally occurring as well as modified properties for applications in many fields of medicine, biotechnology, and agriculture.
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Blaber, Michael. "Cooperative hydrophobic core interactions in the β‐trefoil architecture." Protein Science 30, no. 5 (March 16, 2021): 956–65. http://dx.doi.org/10.1002/pro.4059.

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Fujii, Yuki. "Cell Function Research of β-Trefoil Lectins from Mytilidae." YAKUGAKU ZASSHI 141, no. 4 (April 1, 2021): 481–88. http://dx.doi.org/10.1248/yakushi.20-00215.

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Liu, Chengsong, Dwayne Chu, Rhonda D. Wideman, R. Scott Houliston, Hannah J. Wong, and Elizabeth M. Meiering. "Thermodynamics of Denaturation of Hisactophilin, a β-Trefoil Protein†." Biochemistry 40, no. 13 (April 2001): 3817–27. http://dx.doi.org/10.1021/bi002609i.

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Dissertations / Theses on the topic "Β-Trefoil"

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GONZALEZ, Maria Cecilia. "Engineering Two Human Proteins with β-Trefoil Fold for Therapeutic Applications." Doctoral thesis, 2017. http://hdl.handle.net/11562/960618.

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The expression of glycoproteins containing immature truncated O-glycans such as the Thomsen-Friedenreich antigen (Ser/Thr-O-Galβ1–3GalNAc; T-antigen) and the Lewis antigen (sialyl-T-antigen) is a characteristic feature observed on almost all malignant epithelial cells. Those antigens can be recognized by lectins, a group of highly specific carbohydrate-binding proteins whose three-dimensional structure has been studied in our laboratory by X-ray crystallography. BEL β-trefoil is a lectin found in mushrooms that contains three binding sites for the T-antigen, its antiproliferative activity was demonstrated in various human tumor cell lines and it has also been employed for the targeting of antitumor drugs. Unlike other lectins with these properties, BEL β-trefoil presents a structural fold that is also found in human proteins, unlocking the opportunity to use protein engineering tools to design new anticancer therapeutics. This thesis explores the possibility of modifying existing human proteins to recognize the carbohydrate antigens present on the surface of cancer cells, in order to reduce the potential immunogenicity risk that foreign lectins could have and allowing their future application in drug-delivery targeting. To reach this purpose, two human proteins structurally similar to BEL β-trefoil were modified following different strategies. Human acidic fibroblast growth factor (FGF1) was modified in an attempt to create a new carbohydrate binding site, while a truncated form of human N-acetylgalactosaminyltranferase-6 (GalNAc-T6) was produced to exploit its affinity to N-acetylgalactosamine for this new purpose. Biophysical methods such as spectrofluorimetry and isothermal titration calorimetry were used to analyze the ability of the engineered proteins to bind the T-antigen monosaccharides. The binding dissociation constant (Kd) of the protein-carbohydrate interaction was determined. The stability of each protein was also studied through their thermodynamic parameters of unfolding using differential scanning calorimetry. Crystallization screenings were set up using a broad variety of precipitants in order to produce crystals to be used to study the three-dimensional structure of the engineered proteins using X-ray diffraction. The crystals that were grown were taken to the European Synchrotron Radiation Facility (ESRF) in Grenoble (France) to carry out the diffraction experiments. In conclusion, this work provides a new and interesting insight for the production of optimized protein therapeutics applied in drug-delivery methods for cancer treatment. The present biophysical data are the prerequisite for future studies regarding the biological properties of the engineered proteins and clinical parameters for their potential use in medicine.
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Book chapters on the topic "Β-Trefoil"

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Fujii, Yuki, S. M. Abe Kawsar, Imtiaj Hasan, Hideaki Fujita, Marco Gerdol, and Yasuhiro Ozeki. "Purification and Functional Characterization of the Effects on Cell Signaling of Mytilectin: A Novel β-Trefoil Lectin from Marine Mussels." In Methods in Molecular Biology, 201–13. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0430-4_21.

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