Relevant bibliographies by topics / Protein S100

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

Academic literature on the topic 'Protein S100'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Protein S100"

1

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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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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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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Glenney, J. R., M. S. Kindy, and L. Zokas. "Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution." Journal of Cell Biology 108, no. 2 (1989): 569–78. http://dx.doi.org/10.1083/jcb.108.2.569.

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A low molecular mass protein which we term S100L was isolated from bovine lung. S100L possesses many of the properties of brain S100 such as self association, Ca++-binding (2 sites per subunit) with moderate affinity, and exposure of a hydrophobic site upon Ca++-saturation. Antibodies to brain S100 proteins, however, do not cross react with S100L. Tryptic peptides derived from S100L were sequenced revealing similarity to other members of the S100 family. Oligonucleotide probes based on these sequences were used to screen a cDNA library derived from a bovine kidney cell line (MDBK). A 562-nucle
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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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Smith, Steven P., and Gary S. Shaw. "A change-in-hand mechanism for S100 signalling." Biochemistry and Cell Biology 76, no. 2-3 (1998): 324–33. http://dx.doi.org/10.1139/o98-062.

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S100 proteins are a group of small dimeric calcium-binding proteins making up a large subclass of the EF-hand family of calcium-binding proteins. Members of this family of proteins have been proposed to act as intracellular calcium modulatory proteins in a fashion analogous to that of the EF-hand sensor proteins troponin-C and calmodulin. Recently, NMR spectroscopy has provided the three-dimensional structures of the S100 family members S100A6 and S100B in both the apo- and calcium-bound forms. These structures have allowed for the identification of a novel calcium-induced conformational chang
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Santamaria-Kisiel, Liliana, Anne C. Rintala-Dempsey, and Gary S. Shaw. "Calcium-dependent and -independent interactions of the S100 protein family." Biochemical Journal 396, no. 2 (2006): 201–14. http://dx.doi.org/10.1042/bj20060195.

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The S100 proteins comprise at least 25 members, forming the largest group of EF-hand signalling proteins in humans. Although the proteins are expressed in many tissues, each S100 protein has generally been shown to have a preference for expression in one particular tissue or cell type. Three-dimensional structures of several S100 family members have shown that the proteins assume a dimeric structure consisting of two EF-hand motifs per monomer. Calcium binding to these S100 proteins, with the exception of S100A10, results in an approx. 40° alteration in the position of helix III, exposing a br
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Emberley, Ethan D., Leigh C. Murphy, and Peter H. Watson. "S100 proteins and their influence on pro-survival pathways in cancer." Biochemistry and Cell Biology 82, no. 4 (2004): 508–15. http://dx.doi.org/10.1139/o04-052.

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The S100 gene family is composed of at least 20 members that share a common structure defined in part by the Ca2+ binding EF-hand motif. These genes which are expressed in a discriminate fashion in specific cells and tissues, have been described to have either an intracellular or extracellular function, or both. S100 proteins are implicated in the immune response, differentiation, cytoskeleton dynamics, enzyme activity, Ca2+ homeostasis and growth. A potential role for S100 proteins in neoplasia stems from these activities and from the observation that several S100 proteins have altered levels
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Liu, Ying, Jian Cui, Yun-Liang Tang, Liang Huang, Cong-Yang Zhou, and Ji-Xiong Xu. "Prognostic Roles of mRNA Expression of S100 in Non-Small-Cell Lung Cancer." BioMed Research International 2018 (2018): 1–11. http://dx.doi.org/10.1155/2018/9815806.

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The S100 protein family is involved in cancer cell invasion and metastasis, but its prognostic value in non-small-cell lung cancer (NSCLC) has not been elucidated. In the present study we investigated the prognostic role of mRNA expression of each individual S100 in NSCLC patients through the Kaplan–Meier plotter (KM plotter) database. Expression of 14 members of the S100 family correlated with overall survival (OS) for all NSCLC patients; 18 members were associated with OS in adenocarcinoma, but none were associated with OS in squamous cell carcinoma. In particular, high mRNA expression level
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Liang, Jie, Guanhong Luo, Xiaoxuan Ning, et al. "Differential expression of calcium-related genes in gastric cancer cells transfected with cellular prion protein." Biochemistry and Cell Biology 85, no. 3 (2007): 375–83. http://dx.doi.org/10.1139/o07-052.

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The prion protein (PrPC) has a primary role in the pathogenesis of transmissible spongiform encephalopathies, which causes prion disorders partially due to Ca2+ dysregulation. In our previous work, we found that overexpressed PrPC in gastric cancer was involved in apoptosis, cell proliferation, and metastasis of gastric cancer. To better understand how PrPC acts in gastric cancer, a human microarray was performed to select differentially regulated genes that correlate with the biological function of PrPC. The microarray data were analyzed and revealed 3798 genes whose expression increased at l
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Dissertations / Theses on the topic "Protein S100"

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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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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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Ilschner, Maud. "Diagnostische Wertigkeit von Protein S100 und Neuronenspezifischer Enolase bei Patienten mit spontaner Subarachnoidalblutung." kostenfrei, 2008. http://www.opus-bayern.de/uni-regensburg/volltexte/2009/1209/.

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Stoll, Alexander. "Neurologische Komplikationen nach Herzoperationen unter der Berücksichtigung der Hypoxiemarker NSE und Protein S100 /." Hamburg : Akademos Wiss.-Verl, 2003. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=010456703&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Irvine, Andrew Francis. "Characterising the interaction between metastasis-associated protein S100A4 and non-muscle myosin IIA in vitro and in vivo." Thesis, University of Leicester, 2012. http://hdl.handle.net/2381/27622.

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S100A4 is a member of the S100 family of proteins and increases the motility of many cell types. This is also thought to explain its association with the epithelial-mesenchymal transition (EMT), a developmental program re-activated during tumourigenesis. Mechanistically, S100A4 interacts with a number of targets including Smad3 and liprin-β1; however, the best characterised is non-muscle myosin IIA (NMIIA) which regulates many aspects of the cytoskeleton. There is a large body of in vitro data indicating that S100A4 promotes the monomeric state of NMIIA; however, in vivo evidence for the inter
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Okada, Kouki. "CD68 on rat macrophages binds tightly to S100A8 and S100A9 and helps to regulate the cells’ immune functions." 京都大学 (Kyoto University), 2017. http://hdl.handle.net/2433/225517.

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Wilhelm, Kristina Rebecca. "Protein complexes assembly, structure and function /." Umeå : Umeå university, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-29792.

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Camara, Ramatoulie. "Design, synthesis and biological evaluation of potential inhibitors of S100P, a protein implicated in pancreatic cancer." Thesis, University of Hertfordshire, 2015. http://hdl.handle.net/2299/17117.

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Pancreatic cancer is relatively uncommon. Despite its relative scarcity, it is the fourth-ranked cancer killer in the Western world with less than a 5% 5-year survival rate. The high mortality rate is due to the asymptomatic nature of the disease and the advanced stage at which it is usually diagnosed. S100P is a calcium-binding protein that has been shown to be highly expressed in the early stages of pancreatic cancer and has been proposed as a potential therapeutic target via the blocking of its interaction with its receptor RAGE, the receptor for advanced glycation end-products. In this the
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Reinhardt, Katharina [Verfasser], and Ursula [Akademischer Betreuer] Holzer. "Role of monocyte-induced development of Th17 cells, the heat shock protein 90 and proinflammatory S100 proteins in the pathogenesis of graft-versus-host disease / Katharina Reinhardt ; Betreuer: Ursula Holzer." Tübingen : Universitätsbibliothek Tübingen, 2015. http://d-nb.info/1196982422/34.

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Dellagrammaticas, Demosthenes. "Cerebral haemodynamic control and carotid endarterectomy : comparison of general and locoregional anaesthesia." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/cerebral-haemodynamic-control-and-carotid-endarterectomy-comparison-of-general-and-locoregional-anaesthesia(a7b50cfa-d56d-40ff-b8d8-dbc1a2ff105e).html.

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The role of CEA for stroke prevention in the presence of symptomatic carotid artery stenosis is well established. In order to maximize the benefit of surgery, several perioperative processes of care have been under scrutiny, of which one is the choice of anaesthetic method. The differing effects of GA vs. LA on the cerebral circulation after CEA may be of significance, since changes in the cerebral circulation post-CEA may give rise to cerebral hyperperfusion and intracerebral haemorrhage. This work assessed the effect of GA vs. LA on cerebral haemodynamic control after CEA using transcranial
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Books on the topic "Protein S100"

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

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

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Book chapters on the topic "Protein S100"

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Holdenrieder, S., and P. Stieber. "S100-Protein." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_2727.

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Holdenrieder, S., and P. Stieber. "S100-Protein." In Lexikon der Medizinischen Laboratoriumsdiagnostik. Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_2727-1.

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Dempsey, Brian R., Anne C. Rintala-Dempsey, Gary S. Shaw, et al. "S100 Calcium-Binding Protein." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101220.

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Kiss, Bence, Péter Ecsédi, Márton Simon, and László Nyitray. "Isolation and Characterization of S100 Protein-Protein Complexes." In Methods in Molecular Biology. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9030-6_21.

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Weber, David J., Richard R. Rustandi, France Carrier, and Danna B. Zimmer. "Interaction of Dimeric S100B(ββ) with the Tumor Suppressor Protein p53: A Model for Ca2+-Dependent S100-Target Protein Interactions." In Calcium: The Molecular Basis of Calcium Action in Biology and Medicine. Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-010-0688-0_31.

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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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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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Conference papers on the topic "Protein S100"

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Akiyama, N., H. Hozumi, H. Yasui, et al. "Clinical Utility of Serum S100 Calcium Binding Protein A4 in Idiopathic Pulmonary Fibrosis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a7131.

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Ren, Hui, Ting Wang, and Mingwei Chen. "Expression and clinical significance of S100 calcium binding protein A2 in lung cancer." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa2868.

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Kawczyk-Krupka, Aleksandra, Zenon Czuba, Wojciech Latos, Anna Mertas, Grzegorz Cieslar, and Aleksander Sieroń. "The influence of ALA-mediated photodynamic therapy on secretion of selected growth factors, interleukins and s100 protein (S100) by colon cancer cells in vitro." In 17th International Photodynamic Association World Congress, edited by Tayyaba Hasan. SPIE, 2019. http://dx.doi.org/10.1117/12.2525526.

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Terao, Mineko. "Abstract 3620: RARalpha interactome in breast cancer, the S100 calcium binding protein A3 binds tothe retinoid receptor." 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.am2017-3620.

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Park, J. S., J. U. Lee, C. S. Park, H. S. Chang, J. S. Park, and E. S. Go. "Upregulation of S100 Calcium Binding Protein A9 Levels in the Lungs of Patients with Idiopathic Pulmonary Fibrosis." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a3083.

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Zhou, Taimei, Xueying Zheng, Deqing Yi, and Qingying Zhang. "Molecular Modeling and Structure Analysis of S100 Calcium Binding Protein A14: Molecular Modeling and Structure Analysis of S100A14." In 2009 2nd International Conference on Biomedical Engineering and Informatics. IEEE, 2009. http://dx.doi.org/10.1109/bmei.2009.5301740.

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Railwah, C. N., J. Poon, G. Gupta, et al. "Chemical Inhibition of S100 Calcium-Binding Protein A9 Signaling Reduces Cigarette Smoke-Induced Loss of Lung Function in Mice." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a3770.

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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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Marcovina, S., R. Coppola, M. P. Protti, C. Gelfi, and P. M. Mannucci. "EDTA-DEPENDENT MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644294.

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Splenocytes from a Balb/c mouse immunized with purified human protein S (PS) were fused with murine hybridoma cell line SP2/0-Agl4 and cultured in Iscove's medium without addition of fetal bovine serum. Hybrid supernatants were screened for the presence of specific antibodies by solid-phase ELISA and cloned by the limiting dilution technique. Pour clones, named S2, S3, S8, and S10, were selected, recloned several times, and injected intraperitoneally into Balb/c mice for the production of antibody-rich ascitic fluid. The monoclonal antibodies (Mabs), all of IgGl subclass with k light chain, we
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