Relevant bibliographies by topics / S100 proteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'S100 proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 July 2025

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Journal articles on the topic "S100 proteins"

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Zimmer, Danna B., and David J. Weber. "The Calcium-Dependent Interaction of S100B with Its Protein Targets." Cardiovascular Psychiatry and Neurology 2010 (August 17, 2010): 1–17. http://dx.doi.org/10.1155/2010/728052.

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S100B is a calcium signaling protein that is a member of the S100 protein family. An important feature of S100B and most other S100 proteins (S100s) is that they often bind Ca2+ ions relatively weakly in the absence of a protein target; upon binding their target proteins, Ca2+-binding then increases by as much as from 200- to 400-fold. This manuscript reviews the structural basis and physiological significance of increased Ca2+-binding affinity in the presence of protein targets. New information regarding redundancy among family members and the structural domains that mediate the interaction o
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Kazakov, Alexey S., Alexander D. Sofin, Nadezhda V. Avkhacheva, et al. "Interferon Beta Activity Is Modulated via Binding of Specific S100 Proteins." International Journal of Molecular Sciences 21, no. 24 (2020): 9473. http://dx.doi.org/10.3390/ijms21249473.

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Interferon-β (IFN-β) is a pleiotropic cytokine used for therapy of multiple sclerosis, which is also effective in suppression of viral and bacterial infections and cancer. Recently, we reported a highly specific interaction between IFN-β and S100P lowering IFN-β cytotoxicity to cancer cells (Int J Biol Macromol. 2020; 143: 633–639). S100P is a member of large family of multifunctional Ca2+-binding proteins with cytokine-like activities. To probe selectivity of IFN-β—S100 interaction with respect to S100 proteins, we used surface plasmon resonance spectroscopy, chemical crosslinking, and crysta
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Zeng, Meng-Lu, Xian-Jin Zhu, Jin Liu, et al. "An Integrated Bioinformatic Analysis of the S100 Gene Family for the Prognosis of Colorectal Cancer." BioMed Research International 2020 (November 26, 2020): 1–15. http://dx.doi.org/10.1155/2020/4746929.

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Background. S100 family genes exclusively encode at least 20 calcium-binding proteins, which possess a wide spectrum of intracellular and extracellular functions in vertebrates. Multiple lines of evidences suggest that dysregulated S100 proteins are associated with human malignancies including colorectal cancer (CRC). However, the diverse expression patterns and prognostic roles of distinct S100 genes in CRC have not been fully elucidated. Methods. In the current study, we analyzed the mRNA expression levels of S100 family genes and proteins and their associations with the survival of CRC pati
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Verma, Rachna, Priyanka Verma, Snehil Budhwar, and Kiran Singh. "S100 proteins." Indian Journal of Medical Research 148, Suppl 1 (2018): S100—S106. https://doi.org/10.4103/ijmr.ijmr_494_18.

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S100 proteins are calcium (Ca2+)-binding proteins and these have an important function in progression, manifestation and therapeutic aspects of various inflammatory, metabolic and neurodegenerative disorders. Based on their involvement in intracellular or extracellular regulatory effects, S100 proteins are classified into three subgroups: one subgroup is specialized in exerting only intracellular effects, other performs both intracellular and extracellular functions and the third subgroup members only display extracellular regulatory effects. S100 proteins are expressed particularly in vertebr
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Kazakov, Alexey S., Evgenia I. Deryusheva, Maria E. Permyakova, et al. "Calcium-Bound S100P Protein Is a Promiscuous Binding Partner of the Four-Helical Cytokines." International Journal of Molecular Sciences 23, no. 19 (2022): 12000. http://dx.doi.org/10.3390/ijms231912000.

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S100 proteins are multifunctional calcium-binding proteins of vertebrates that act intracellularly, extracellularly, or both, and are engaged in the progression of many socially significant diseases. Their extracellular action is typically mediated by the recognition of specific receptor proteins. Recent studies indicate the ability of some S100 proteins to affect cytokine signaling through direct interaction with cytokines. S100P was shown to be the S100 protein most actively involved in interactions with some four-helical cytokines. To assess the selectivity of the S100P protein binding to f
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Kazakov, Alexey S., Evgenia I. Deryusheva, Andrey S. Sokolov, et al. "Erythropoietin Interacts with Specific S100 Proteins." Biomolecules 12, no. 1 (2022): 120. http://dx.doi.org/10.3390/biom12010120.

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Erythropoietin (EPO) is a clinically significant four-helical cytokine, exhibiting erythropoietic, cytoprotective, immunomodulatory, and cancer-promoting activities. Despite vast knowledge on its signaling pathways and physiological effects, extracellular factors regulating EPO activity remain underexplored. Here we show by surface plasmon resonance spectroscopy, that among eighteen members of Ca2+-binding proteins of the S100 protein family studied, only S100A2, S100A6 and S100P proteins specifically recognize EPO with equilibrium dissociation constants ranging from 81 nM to 0.5 µM. The inter
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Kazakov, Alexey S., Evgenia I. Deryusheva, Victoria A. Rastrygina, et al. "Interaction of S100A6 Protein with the Four-Helical Cytokines." Biomolecules 13, no. 9 (2023): 1345. http://dx.doi.org/10.3390/biom13091345.

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S100 is a family of over 20 structurally homologous, but functionally diverse regulatory (calcium/zinc)-binding proteins of vertebrates. The involvement of S100 proteins in numerous vital (patho)physiological processes is mediated by their interaction with various (intra/extra)cellular protein partners, including cell surface receptors. Furthermore, recent studies have revealed the ability of specific S100 proteins to modulate cell signaling via direct interaction with cytokines. Previously, we revealed the binding of ca. 71% of the four-helical cytokines via the S100P protein, due to the pres
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Melville, Zephan, Ehson Aligholizadeh, Laura E. McKnight, Dylan J. Weber, Edwin Pozharski, and David J. Weber. "X-ray crystal structure of human calcium-bound S100A1." Acta Crystallographica Section F Structural Biology Communications 73, no. 4 (2017): 215–21. http://dx.doi.org/10.1107/s2053230x17003983.

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S100A1 is a member of the S100 family of Ca2+-binding proteins and regulates several cellular processes, including those involved in Ca2+signaling and cardiac and skeletal muscle function. In Alzheimer's disease, brain S100A1 is overexpressed and gives rise to disease pathologies, making it a potential therapeutic target. The 2.25 Å resolution crystal structure of Ca2+-S100A1 is solved here and is compared with the structures of other S100 proteins, most notably S100B, which is a highly homologous S100-family member that is implicated in the progression of malignant melanoma. The observed stru
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Koltzscher, Max, Claudia Neumann, Simone König, and Volker Gerke. "Ca2+-dependent Binding and Activation of Dormant Ezrin by Dimeric S100P." Molecular Biology of the Cell 14, no. 6 (2003): 2372–84. http://dx.doi.org/10.1091/mbc.e02-09-0553.

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S100 proteins are EF hand type Ca2+ binding proteins thought to function in stimulus-response coupling by binding to and thereby regulating cellular targets in a Ca2+-dependent manner. To isolate such target(s) of the S100P protein we devised an affinity chromatography approach that selects for S100 protein ligands requiring the biologically active S100 dimer for interaction. Hereby we identify ezrin, a membrane/F-actin cross-linking protein, as a dimer-specific S100P ligand. S100P-ezrin complex formation is Ca2+ dependent and most likely occurs within cells because both proteins colocalize at
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Mandarino, Angelo, Swetha Thiyagarajan, Allana C. F. Martins, Roberto da Silva Gomes, Stefan W. Vetter, and Estelle Leclerc. "S100s and HMGB1 Crosstalk in Pancreatic Cancer Tumors." Biomolecules 13, no. 8 (2023): 1175. http://dx.doi.org/10.3390/biom13081175.

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Pancreatic cancer remains a disease that is very difficult to treat. S100 proteins are small calcium binding proteins with diverse intra- and extracellular functions that modulate different aspects of tumorigenesis, including tumor growth and metastasis. High mobility group box 1 (HMGB1) protein is a multifaceted protein that also actively influences the development and progression of tumors. In this study, we investigate the possible correlations, at the transcript level, between S100s and HMGB1 in pancreatic cancer. For this purpose, we calculated Pearson’s correlations between the transcrip
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Dissertations / Theses on the topic "S100 proteins"

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Alwash, Ban Hussein Kadhim. "S100 proteins control cytoskeletal dynamics in cancer." Thesis, University of Leicester, 2018. http://hdl.handle.net/2381/42867.

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The S100 family of calcium binding proteins exhibits a unique pattern of cell type specific expression. These proteins are found in the cytoplasm and/or nucleus of a variety of cells, and involved in the control of a wide range of cellular processes such as cell cycle progression and differentiation. S100A4 and S100A6 are members of the S100 protein family that interact with several molecular targets including the heavy chain of non-muscle myosin IIA (NM IIA) and annexin II, respectively. NM IIA is a major actin-associated motor protein, which is involved in cell motility and cytokinesis. Asse
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Robinson, Matthew James. "An investigation into the function of two S100 proteins, S100 A12 and MRP-14." Thesis, University College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.394031.

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Newton, Rebecca Anne. "A role for S100 proteins in leukocyte adhesion." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298801.

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Al, Ismaeel Qais Ibraheem. "Regulation and function of S100 proteins in pancreatic carcinoma." Thesis, University of Leicester, 2017. http://hdl.handle.net/2381/40889.

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Pancreatic cancer (PC) is one of the leading causes of cancer-related death worldwide with the survival rate less than 5% because of late diagnosis. Development of PC is complex, it is promoted by the tumour microenvironment and often accompanied by inflammation. Epithelial mesenchymal transition (EMT) is an embryonic genetic program reactivated in cancer. EMT is implicated in the escape from senescence, tumour cell invasiveness, cancer metastasis, and drug resistance. EMT encompasses global reorganisation of the gene expression profiles, loss of epithelial markers and activation of mesenchyma
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Wheeler, Lucas. "The Evolution of Metal and Peptide Binding in the S100 Protein Family." Thesis, University of Oregon, 2018. http://hdl.handle.net/1794/23178.

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Proteins perform an incredible array of functions facilitated by a diverse set of biochemical properties. Changing these properties is an essential molecular mechanism of evolutionary change, with major questions in protein evolution surrounding this topic. How do new functional biochemical features evolve? How do proteins change following gene duplication events? I used the S100 protein family as a model to probe these aspects of protein evolution. The S100s are signaling proteins that play a diverse range of biological roles binding Calcium ions, transition metal ions, and other prote
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Brant, Stephen. "Distribution of renal S100 proteins in physiological and pathological models." Thesis, University of East London, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342101.

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Turnier, Jessica L. M. D. "Urine S100 Proteins as Potential Biomarkers of Lupus Nephritis Activity." University of Cincinnati / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1491308278173071.

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Goyette, Jesse Davis Medical Sciences Faculty of Medicine UNSW. "The extracellular functions of S100A12." Publisher:University of New South Wales. Medical Sciences, 2008. http://handle.unsw.edu.au/1959.4/41302.

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The S100s comprise a group of Ca2+-binding proteins of the EF-hand superfamily with varied functions. Within this family, three inflammatory-related proteins - S100A8, S100A9 and S100A12 - form a subcluster known as the 'calgranulins'. S100A12 levels are elevated in sera from patients with inflammatory diseases, such as rheumatoid arthritis and inflammatory bowel disease. S100A12 is constitutively expressed in neutrophils and induced in monocytes by LPS and TNFα, and in macrophages by IL-6. S100A12 is a potent monocyte and mast cell chemoattractant and its potentiation of mast cell activation
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Rahimi, Ahmed Farid Medical Sciences Faculty of Medicine UNSW. "Regulation of inflammation-associated S100 proteins in fibroblasts and their expression in atherosclerosis." Awarded by:University of New South Wales. School of Medical Sciences, 2004. http://handle.unsw.edu.au/1959.4/20503.

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The multigene family of Ca2+-binding S100 proteins comprises 22 members that have various important intra- and extracellular roles. The three inflammation-associated members of this family???S100A8, S100A9 and S100A12 (collectively termed &quotcalgranulins&quot)???are constitutive neutrophil and monocyte proteins also expressed by macrophages within acute and chronic inflammatory lesions, but not in tissue macrophages. They are expressed in human/murine wounds and by appropriately activated macrophages, microvascular endothelial cells and keratinocytes in vitro. The &quot calgranulins&quot are
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Cunden, Lisa Stephanie. "A molecular investigation of the antimicrobial functions of the human S100 host-defense proteins." Thesis, Massachusetts Institute of Technology, 2019. https://hdl.handle.net/1721.1/121779.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 2019<br>Cataloged from PDF version of thesis. Vita.<br>Includes bibliographical references.<br>The human host is continually exposed to potentially harmful organisms and the innate immune response is the first line of defense against microbial invasion. One strategy employed by the human innate immune system includes the release of antimicrobial host-defense proteins (HDPs). The goal of this thesis is to understand the antimicrobial functions of four host-defense proteins of the S100 family of proteins: calprotecti
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Books on the topic "S100 proteins"

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Brant, Stephen. Distribution of renal S100 proteins in psysiological and pathological models. University of East London, 2000.

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Ilg, Evelyn Claudia. The S100 calcium-binding proteins: Purification, characterization and expression pattern in human tumors. 1997.

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Neilson, Karen Mary *. Studies of the human S100 protein -subunit gene. 1988.

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Ruiz, Rafael. S100b: Serum Detection, Functions and Clinical Significance. Nova Science Publishers, Incorporated, 2015.

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Pedrocchi, Michele. Die S100-Proteine CAPL und CACY: Herstellung und Charakterisierung von rekombinanten Proteinen ; funktionelle Untersuchungen im Herzen und im Mammakarzinom. 1993.

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Landry, Charles Francis. Expression from the gene encoding the gbs-subunit of the S100 protein during development of the rodent brain. 1992.

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Willumeit, Regine. Lokalisierung der Proteine L1, S6 und S10 des E. coli Ribosoms mit spinabhängiger Neutronenkleinwinkelstreuung. 1996.

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Book chapters on the topic "S100 proteins"

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Dempsey, Brian R., Anne C. Rintala-Dempsey, and Gary S. Shaw. "S100 Proteins." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_426.

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Dempsey, Brian R., Anne C. Rintala-Dempsey, and Gary S. Shaw. "S100 Proteins." In Encyclopedia of Signaling Molecules. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_426-1.

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Dempsey, Brian R., Anne C. Rintala-Dempsey, Gary S. Shaw, et al. "S100 Proteins." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_426.

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Donato, Rosario, Carolyn L. Geczy, and David J. Weber. "S100 Proteins." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_48.

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Heizmann, Claus W. "S100 Proteins." In Encyclopedia of Molecular Pharmacology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-21573-6_225-1.

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Heizmann, Claus W. "S100 Proteins." In Encyclopedia of Molecular Pharmacology. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-21573-6_225-2.

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Heizmann, Claus W. "S100 Proteins." In Encyclopedia of Molecular Pharmacology. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_225.

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Holzinger, Dirk, Christoph Kessel, and Dirk Foell. "S100 Proteins in Autoinflammation." In Textbook of Autoinflammation. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-98605-0_9.

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Martínez-Aguilar, Juan, and Mark P. Molloy. "Targeted Mass Spectrometry of S100 Proteins." In Methods in Molecular Biology. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9030-6_41.

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Donato, Rosario. "Interaction of Annexins with S100 Proteins." In Annexins. Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9214-7_7.

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Conference papers on the topic "S100 proteins"

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Rastrygina, V. A., A. S. Kazakov, E. I. Deryusheva, et al. "INTERACTION OF S100P AND S100A6 PROTEINS WITH THE FOUR-HELICAL CYTOKINES." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-208.

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Recent studies have revealed the ability of S100 proteins to affect cell signaling via direct interaction with cytokines. This work considers interaction of promiscuous representatives of S100 protein family with numerous four-helical cytokines. The binding of ca 71/73 % of the studied cytokines to S100P/S100A6 proteins respectively was established.
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Valenzuela, Stella M., Mark Berkahn, Donald K. Martin, Thuan Huynh, Zheng Yang, and Carolyn L. Geczy. "Elucidating the structure and function of S100 proteins in membranes." In Microelectronics, MEMS, and Nanotechnology, edited by Dan V. Nicolau. SPIE, 2005. http://dx.doi.org/10.1117/12.638873.

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Morozova-Roche, Ludmilla A. "AMYLOID-NEUROINFLAMMATORY CASCADE IN NEURODEGENERATIVE DISEASES – ROLE OF PRO-INFLAMMATORY S100 PROTEINS." In MODERN PROBLEMS IN SYSTEMIC REGULATION OF PHYSIOLOGICAL FUNCTIONS. NPG Publishing, 2019. http://dx.doi.org/10.24108/5-2019-confnf-6.

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Wakiya, Risa, Kiyo Ueeda, Shusaku Nakashima, et al. "AB0487 HCQ COULD ACT ON SLE PATIENTS THROUGH THE MODULATING EXPRESSION OF IL-8 ALONG WITH S100 PROTEINS." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.6457.

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Ogama, Naoko, Ryuuichi Nagashima, and Nobuyuki Tanaka. "Abstract 1891: Annexin A2-binding S100 proteins promote proliferation and cell cycle progression of EGFR positive cancer cells." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1891.

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Lines, Kate E., Namaa Audi, Claude Chelala, et al. "Abstract 5288: S100PBP is ubiquitously expressed and modulates the function of S100 calcium-binding proteins in pancreatic cancer." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5288.

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Wakiya, R., K. Ueeda, T. Kameda, et al. "AB0527 S100 proteins are novel biomarkers for the efficacy of hcq treatment to skin lesion in systemic lupus erythematosus." In Annual European Congress of Rheumatology, EULAR 2018, Amsterdam, 13–16 June 2018. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-eular.2109.

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Tronconi, Elena, Najla Aljaberi, Angela Merritt, et al. "AB1065 THE UTILISATION OF S100 PROTEINS TESTING IN PEDIATRIC RHEUMATOLOGY PATIENTS IN A TERTIARY CARE INSTITUTION AND IMPLICATIONS FOR CARE." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.3645.

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Šumová, B., J. Závada, LA Cerezo, et al. "P058 S100 proteins effectively discriminate systemic lupus erythematosus patients from healthy controls, but are not associated with measures of disease activity." In 38th European Workshop for Rheumatology Research, 22–24 February 2018, Geneva, Switzerland. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-ewrr2018.77.

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Bobrova, L. A., and M. Y. Zemskova. "STUDY OF THE INTERACTION BETWEEN GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR AND S100P PROTEIN ON THE MONOCYTIC LEUKEMIA CELL LINE THP-1." In XI МЕЖДУНАРОДНАЯ КОНФЕРЕНЦИЯ МОЛОДЫХ УЧЕНЫХ: БИОИНФОРМАТИКОВ, БИОТЕХНОЛОГОВ, БИОФИЗИКОВ, ВИРУСОЛОГОВ, МОЛЕКУЛЯРНЫХ БИОЛОГОВ И СПЕЦИАЛИСТОВ ФУНДАМЕНТАЛЬНОЙ МЕДИЦИНЫ. IPC NSU, 2024. https://doi.org/10.25205/978-5-4437-1691-6-221.

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Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a proinflammatory cytokine that regulates the differentiation of monocytes into macrophages; it can also participate in carcinogenesis. S100P is a calcium-binding protein that interacts with the RAGE receptor and assists in the processes of inflammation, proliferation, and differentiation of cells. We have found that GM-CSF binds to S100P. The biological activity of the GM-CSF/S100P complex was investigated in our research.
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