Bibliografías temáticas / Protein binding

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Literatura académica sobre el tema "Protein binding"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 25 de julio de 2025

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Artículos de revistas sobre el tema "Protein binding"

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Sawicka, Kirsty, Martin Bushell, Keith A. Spriggs, and Anne E. Willis. "Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein." Biochemical Society Transactions 36, no. 4 (2008): 641–47. http://dx.doi.org/10.1042/bst0360641.

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PTB (polypyrimidine-tract-binding protein) is a ubiquitous RNA-binding protein. It was originally identified as a protein with a role in splicing but it is now known to function in a large number of diverse cellular processes including polyadenylation, mRNA stability and translation initiation. Specificity of PTB function is achieved by a combination of changes in the cellular localization of this protein (its ability to shuttle from the nucleus to the cytoplasm is tightly controlled) and its interaction with additional proteins. These differences in location and trans-acting factor requiremen
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Anil, Kumar Tomar, Saraswat Mayank, Singh Sooch Balwinder, Singh Sarman, P. Singh Tej, and Yadav Savita. "Prediction of Heparin binding sites on Human Serum Albumin, Matrix Metalloproteinase-2 and DNA Topoisomerase1." International Journal of BioSciences and Technology (IJBST) ISSN: 0974-3987 3, no. 1 (2010): 21–26. https://doi.org/10.5281/zenodo.1438292.

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<strong>ABSTRACT:</strong> Heparin binds a wide range of proteins of different structure as well as functions and play crucial roles in a number of biological processes. Human seminal plasma consists of many heparin binding proteins (HBPs). HBPs play crucial role in modulation of capacitation through heparin and have been correlated with fertility in many species. Very little scientific information is available about the binding modes of heparin and HBPs. There is not any well defined binding space, characterized by some consensus sequence over protein except that binding region always do cons
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Viswanathan, Raji, Eduardo Fajardo, Gabriel Steinberg, Matthew Haller, and Andras Fiser. "Protein—protein binding supersites." PLOS Computational Biology 15, no. 1 (2019): e1006704. http://dx.doi.org/10.1371/journal.pcbi.1006704.

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Wilkins, Anna L., Yiming Ye, Wei Yang, Hsiau-Wei Lee, Zhi-ren Liu, and Jenny J. Yang. "Metal-binding studies for a de novo designed calcium-binding protein." Protein Engineering, Design and Selection 15, no. 7 (2002): 571–74. http://dx.doi.org/10.1093/protein/15.7.571.

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NAKANO, Akihiko. "Protein Secretion and GTP-binding Proteins." Seibutsu Butsuri 31, no. 2 (1991): 53–57. http://dx.doi.org/10.2142/biophys.31.53.

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Rodilla-Sala, E., G. C. Lunazzi, W. Stremmel, and C. Tiribelli. "BSP-bilirubin binding protein, fatty acid binding protein and bilitranslocase are immunological distinct proteins." Journal of Hepatology 11 (January 1990): S53. http://dx.doi.org/10.1016/0168-8278(90)91545-8.

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Guo, Ting, Yanxin Shi, and Zhirong Sun. "A novel statistical ligand-binding site predictor: application to ATP-binding sites." Protein Engineering, Design and Selection 18, no. 2 (2005): 65–70. http://dx.doi.org/10.1093/protein/gzi006.

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ESPEJO, Alexsandra, Jocelyn CÔTÉ, Andrzej BEDNAREK, Stephane RICHARD, and Mark T. BEDFORD. "A protein-domain microarray identifies novel protein–protein interactions." Biochemical Journal 367, no. 3 (2002): 697–702. http://dx.doi.org/10.1042/bj20020860.

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Protein domains mediate protein—protein interactions through binding to short peptide motifs in their corresponding ligands. These peptide recognition modules are critical for the assembly of multiprotein complexes. We have arrayed glutathione S-transferase (GST) fusion proteins, with a focus on protein interaction domains, on to nitrocellulose-coated glass slides to generate a protein-domain chip. Arrayed protein-interacting modules included WW (a domain with two conserved tryptophans), SH3 (Src homology 3), SH2, 14.3.3, FHA (forkhead-associated), PDZ (a domain originally identified in PSD-95
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Lipovsek, D. "Adnectins: engineered target-binding protein therapeutics." Protein Engineering Design and Selection 24, no. 1-2 (2010): 3–9. http://dx.doi.org/10.1093/protein/gzq097.

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Siggers, Trevor, and Raluca Gordân. "Protein–DNA binding: complexities and multi-protein codes." Nucleic Acids Research 42, no. 4 (2013): 2099–111. http://dx.doi.org/10.1093/nar/gkt1112.

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Abstract Binding of proteins to particular DNA sites across the genome is a primary determinant of specificity in genome maintenance and gene regulation. DNA-binding specificity is encoded at multiple levels, from the detailed biophysical interactions between proteins and DNA, to the assembly of multi-protein complexes. At each level, variation in the mechanisms used to achieve specificity has led to difficulties in constructing and applying simple models of DNA binding. We review the complexities in protein–DNA binding found at multiple levels and discuss how they confound the idea of simple
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Tesis sobre el tema "Protein binding"

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Jones, Marc. "Folate binding protein : partial characterisation of bovine milk folate binding protein, includings its ligand binding /." [St. Lucia, Qld], 2004. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe18263.pdf.

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Zeng, Bin. "Functional characterization of acyl-CoA binding protein (ACBP) and oxysterol binding protein-related proteins (ORPS) from Cryptosporidium parvum." Thesis, [College Station, Tex. : Texas A&M University, 2006. http://hdl.handle.net/1969.1/ETD-TAMU-1211.

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Tse, Muk-hei. "Investigations on recombinant Arabidopsis acyl-coenzyme A binding protein 1." View the Table of Contents & Abstract, 2005. http://sunzi.lib.hku.hk/hkuto/record/B36427664.

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Crombie, Catriona Ann. "Histone hairpin binding protein, an RNA binding protein, essential for development." Thesis, University of Aberdeen, 2003. http://digitool.abdn.ac.uk/R?func=search-advanced-go&find_code1=WSN&request1=AAIU602058.

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Histones are proteins found in the nuclei of eukaryotic cells where they are complexed to DNA in chromatin. Rephcation-dependent histones are expressed only during S-phase. Regulation of expression of replication-dependent histone genes requires a highly conserved hairpin RNA element in the 3' untranslated region of histone mRNAs. Replication-dependent histone mRNAs are not polyadenylated; their 3' end is formed by an endonucleolytic cleavage event, 3' of a hairpin element, which is recognised by the Hairpin Binding Protein, HBP (also known as Stem-Loop Binding Protein, SLBP). This protein-RNA
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Prigge, Justin Robert. "Identification and characterization of novel protein-protein interactions with the basal transcription factor, TATA-binding protein." Diss., Montana State University, 2006. http://etd.lib.montana.edu/etd/2006/prigge/PriggeJ0506.pdf.

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Wei, Heng. "Split PH domain identification & redundancy analyses in the classification of PDZ domains /." View abstract or full-text, 2006. http://library.ust.hk/cgi/db/thesis.pl?BICH%202006%20WEI.

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Fang, Lin. "Mechanism of client protein binding by heat shock protein 90 /." view abstract or download file of text, 2006. http://proquest.umi.com/pqdweb?did=1251819301&sid=2&Fmt=2&clientId=11238&RQT=309&VName=PQD.

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Thesis (Ph. D.)--University of Oregon, 2006.<br>Typescript. Includes vita and abstract. Includes bibliographical references (leaves 115-121). Also available for download via the World Wide Web; free to University of Oregon users.
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Ranganathan, Anirudh. "Protein – Ligand Binding: Estimation of Binding Free Energies." Thesis, KTH, Skolan för kemivetenskap (CHE), 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-147527.

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Accurate prediction of binding free energies of protein-ligand system has long been a focus area for theoretical and computational studies; with important implications in fields like pharmaceuticals, enzyme-redesign, etc. The aim of this project was to develop such a predictive model for calculating binding free energies of protein-ligand systems based on the LIE-SASA methods. Many models have been successfully fit to experimental data, but a general predictive model, not reliant on experimental values, would make LIE-SASA a more powerful and widely applicable method. The model was developed s
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Gao, Wei, and 高威. "Characterization of protein interactors of Arabidopsis acyl-coenzymea-binding protein 2." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B43223837.

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Chung, Jo-Lan. "Identifying protein-protein binding sites and binding partners using sequence and structure information /." Diss., Connect to a 24 p. preview or request complete full text in PDF formate. Access restricted to UC campuses, 2007. http://wwwlib.umi.com/cr/ucsd/fullcit?p3244170.

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Libros sobre el tema "Protein binding"

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Symposium, Fundación Dr Antonio Esteve. Drug-protein binding. Praeger, 1986.

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Symposium, Esteve Foundation. Drug-protein binding. Praeger, 1985.

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1934-, Reidenberg M. M., and Erill Sergio, eds. Drug-protein binding. Praeger, 1985.

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Colin, Kleanthous, ed. Protein-protein recognition. Oxford University Press, 2000.

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Pauls, Thomas Lawrence. Metal-binding properties and cation-dependent conformational changes in rat parvalbumin wild-type and mutant proteins. Hartung-Gorre, 1995.

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Vogel, Hans J. Calcium-Binding Protein Protocols. Humana Press, 2002. http://dx.doi.org/10.1385/1592591833.

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Vogel, Hans J. Calcium-Binding Protein Protocols. Humana Press, 2002. http://dx.doi.org/10.1385/1592591841.

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J, Vogel Hans, ed. Calcium-binding protein protocols. Humana Press, 2002.

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M, Thornton Janet, ed. Atlas of protein side-chain interactions. IRL Press at Oxford University Press, 1992.

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Singh, Juswinder. Atlas of protein side-chain interactions. IRL Press at Oxford University Press, 1992.

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Capítulos de libros sobre el tema "Protein binding"

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Kangueane, Pandjassarame, and Christina Nilofer. "Protein-Protein Binding." In Protein-Protein and Domain-Domain Interactions. Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-7347-2_2.

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Nahler, Gerhard. "protein binding." In Dictionary of Pharmaceutical Medicine. Springer Vienna, 2009. http://dx.doi.org/10.1007/978-3-211-89836-9_1151.

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Sparreboom, Alex, and Walter J. Loos. "Protein Binding." In Cancer Drug Discovery and Development. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9135-4_13.

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Mohler, Marjorie A., Jennifer E. Cook, and Gerhard Baumann. "Binding Proteins of Protein Therapeutics." In Pharmaceutical Biotechnology. Springer US, 1992. http://dx.doi.org/10.1007/978-1-4899-2329-5_2.

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Evtushenko, Vladimir I. "Protein Binding Matrices." In Manufacturing of Gene Therapeutics. Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-1353-7_6.

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McAllister-Williams, R. Hamish, Daniel Bertrand, Hans Rollema, et al. "Protein-Binding Microarray." In Encyclopedia of Psychopharmacology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_4483.

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Shoff, William H., Catherine T. Shoff, Suzanne M. Shepherd, et al. "Retinol-Binding Protein." In Encyclopedia of Intensive Care Medicine. Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-00418-6_2154.

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Ward, Tony Milford. "Retinol Binding Protein." In Proteins and Tumour Markers May 1995. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_74.

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Penalva, Luiz O. F. "RNA-binding Protein." In Encyclopedia of Systems Biology. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_313.

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Di Paola, Luisa. "Computational Protein Binding." In Fundamentals of Molecular Bioengineering. Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-42022-1_11.

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Actas de conferencias sobre el tema "Protein binding"

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Lazzari-Dean, Julia R., Alfred Millett-Sikking, Austin E. Y. T. Lefebvre, Maria Ingaramo, and Andrew G. York. "Revealing Protein Binding in Live Cells via Rotational Diffusion of Fluorescent Protein Triplets." In Novel Techniques in Microscopy. Optica Publishing Group, 2025. https://doi.org/10.1364/ntm.2025.nw1c.3.

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Protein-protein interactions underlie most proteins’ functions, but they are difficult to measure. We developed a new form of optical contrast based on triggerable fluorescence from triplet states, revealing interactions in situ with a single tag.
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Wu, Siwen, Jinbo Xu, and Jun-tao Guo. "Prediction of single-stranded DNA binding proteins with protein language model." In 2024 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2024. https://doi.org/10.1109/bibm62325.2024.10821845.

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Zhang, Li, Heng Chang, Zehua Sun, Wenjie Li, Li Zhu, and Han Wang. "PocketLG: Protein Binding Pocket Identification Using Protein Language Model and Graph Transformer." In 2024 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2024. https://doi.org/10.1109/bibm62325.2024.10821813.

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Kang, Keumseok, Sanghun Sel, Jeongmu Kim, and Giltae Song. "Predicting Protein-Ligand binding Residue with Token classification." In 2025 IEEE International Conference on Big Data and Smart Computing (BigComp). IEEE, 2025. https://doi.org/10.1109/bigcomp64353.2025.00032.

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Brabec, Matyáš, and David Hoksza. "Integrating Structural Features with Protein Language Models to Predict Protein-Ligand Binding Sites." In 2024 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2024. https://doi.org/10.1109/bibm62325.2024.10973773.

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A, Akhil P., Sooraj N, and Ani R. "Predicting Protein-Ligand Binding Affinities: A Machine Learning Approach." In 2024 Second International Conference on Inventive Computing and Informatics (ICICI). IEEE, 2024. http://dx.doi.org/10.1109/icici62254.2024.00029.

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Huang, Ruiyan, Xian Chen, Wangren Qiu, and Weizhong Lin. "Prediction of Protein-DNA Binding Sites Based on GraphSAGE." In 2024 5th International Conference on Computer, Big Data and Artificial Intelligence (ICCBD+AI). IEEE, 2024. https://doi.org/10.1109/iccbd-ai65562.2024.00009.

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Walker, F. J. "REGULATION OF THE ANTICOAGULANT ACTIVITY OF ACTIVATED PROTEIN C BY PROTEIN S AND PROTEIN S BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642964.

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Protein S is a vitamin K-dependent protein that acts as a cofactor for the anticoagulant activity of activated protein C both in the proteolytic inactivation of factor V and VIII. Protein S is a single chain protein with a molecular weight of approximately 62 kDa. When the molecular weight of protein S in plasma was determined it was found to be much larger than the single chain protein. The molecular weight of functional protein S when measured by sedimentation equilibrium with the air-driven ultracentrifuge was observed to be between 115 and 130 kDa. In high salt or in the presence of copper
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Suzuki, K., J. Nishioka, H. Kusumoto, and Y. Deyashiki. "BINDING SITE OF VITAMIN K-DEPENDENT PROTEIN S ON C4b-BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644637.

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Protein S, a cofactor for activated protein C, reversibly complexes with a regulatory complement component C4b-binding protein (C4bp) in plasma. In plasma of patients with congenital protein S deficiency, most protein S exists as a complex with C4bp, which has no cofactor activity. C4bp (Mw 550,000) is composed of approximately seven subunits with Mw 75,000 which are linked by disulfide bonds near the carboxy1-terminus. We report here about the complex formation between protein S and C4bp particularly on the binding site of protein S on C4bp molecule. Protein S and C4bp were purified from huma
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Malm, J., R. Bennhagen, L. Holmberg, and B. Dahlbäck. "LOW PLASMA CONCENTRATIONS OF C4b-BINDING PROTEIN AND VITAMIN K-DEPENDENT PROTEIN S IN PRETERM INFANTS WITH DECREASED FORMATION OF PROTEIN S-C4b-BINDING PROTEIN COMPLEXES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644265.

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Protein S is a vitamin K-dependent plasmaprotein functioning as a non-enzymatic cofactor to the activated form of protein C in the degradation of coagulationfactors Va and VIIa. In the circulation approximately 60% of protein S is complexed to the complement protein C4b-binding protein (C4BP). Only the remaining, free fraction exhibits protein Ca cofactor activity.The plasma concentrations of protein S and C4BP were determined in 25 term and 26 preterm infants. Both proteins werequantified with radioimmunoassays. The free, functionally active form of proteinS and the total protein S concentrat
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Informes sobre el tema "Protein binding"

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Hanke, Andreas. DNA Conforming Dynamics and Protein Binding. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada461014.

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Chamovitz, Daniel A., and Zhenbiao Yang. Chemical Genetics of the COP9 Signalosome: Identification of Novel Regulators of Plant Development. United States Department of Agriculture, 2011. http://dx.doi.org/10.32747/2011.7699844.bard.

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This was an exploratory one-year study to identify chemical regulators of the COP9 signalosome. Chemical Genetics uses small molecules to modify or disrupt the function of specific genes/proteins. This is in contrast to classical genetics, in which mutations disrupt the function of genes. The underlying concept is that the functions of most proteins can be altered by the binding of a chemical, which can be found by screening large libraries for compounds that specifically affect a biological, molecular or biochemical process. In addition to screens for chemicals which inhibit specific biologic
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Willmert, Leslie J. Cellular Retinoic Acid Binding Protein and Breast Cancer. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada437738.

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Clarke, Robert. X-Box Binding Protein-1 in Breast Cancer. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada446755.

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Donato, Leslie J. Cellular Retinoic Acid Binding Protein and Breast Cancer. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada455778.

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Clarke, Robert R. X-Box Binding Protein-1 in Breast Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada433869.

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Clarke, Robert R. X-Box Binding Protein-1 in Breast Cancer. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada421992.

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Willmert, Leslie J. Cellular Retinoic Acid Binding Protein and Breast Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada425991.

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Clarke, Robert. X-Box Binding Protein-1 in Breast Cancer. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada460787.

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Scavuzzo, Sebastian, Jonathan Cedeño, and Jaroslava Miksovska. In Silico Calculation of Interhelical Angles in NCS1. Florida International University, 2025. https://doi.org/10.25148/fiuurj.3.1.16.

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Proteins are important macromolecules responsible for a variety of processes in living organisms. One of the most important features of proteins is their ability to respond to environmental stimuli, such as changes in intracellular metal concentration by binding metal ions, which in turns triggers structural changes within the protein that can modify its function or allow the protein to participate in a signaling pathway. One such signaling protein is the so-called neuronal calcium sensor 1 protein or NCS1, which binds Ca2+ along with other abiogenic metals such as Li+, and the metal binding r
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