Auswahl der wissenschaftlichen Literatur zum Thema „Small Heat Schok Protein“
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Zeitschriftenartikel zum Thema "Small Heat Schok Protein"
Friedrich, Kenneth L., Kim C. Giese, Nicole R. Buan und Elizabeth Vierling. „Interactions between Small Heat Shock Protein Subunits and Substrate in Small Heat Shock Protein-Substrate Complexes“. Journal of Biological Chemistry 279, Nr. 2 (22.10.2003): 1080–89. http://dx.doi.org/10.1074/jbc.m311104200.
Der volle Inhalt der QuelleLee, Garrett J., und Elizabeth Vierling. „A Small Heat Shock Protein Cooperates with Heat Shock Protein 70 Systems to Reactivate a Heat-Denatured Protein“. Plant Physiology 122, Nr. 1 (01.01.2000): 189–98. http://dx.doi.org/10.1104/pp.122.1.189.
Der volle Inhalt der QuelleLindner, Robyn A., John A. Carver, Monika Ehrnsperger, Johannes Buchner, Gennaro Esposito, Joachim Behlke, Gudrun Lutsch, Alexey Kotlyarov und Matthias Gaestel. „Mouse Hsp25, a small heat shock protein“. European Journal of Biochemistry 267, Nr. 7 (April 2000): 1923–32. http://dx.doi.org/10.1046/j.1432-1327.2000.01188.x.
Der volle Inhalt der QuelleVos, Michel J., Marianne P. Zijlstra, Serena Carra, Ody C. M. Sibon und Harm H. Kampinga. „Small heat shock proteins, protein degradation and protein aggregation diseases“. Autophagy 7, Nr. 1 (Januar 2011): 101–3. http://dx.doi.org/10.4161/auto.7.1.13935.
Der volle Inhalt der QuelleLaskowska, Ewa, Ewelina Matuszewska und Dorota Kuczynska-Wisnik. „Small Heat Shock Proteins and Protein-Misfolding Diseases“. Current Pharmaceutical Biotechnology 11, Nr. 2 (01.02.2010): 146–57. http://dx.doi.org/10.2174/138920110790909669.
Der volle Inhalt der QuelleFujita, Eri. „Protein Homeostasis-Small Heat Shock Proteins and Cytoskeleton“. Biological Sciences in Space 22, Nr. 4 (2008): 148–57. http://dx.doi.org/10.2187/bss.22.148.
Der volle Inhalt der QuelleKim, Kyeong Kyu, Rosalind Kim und Sung-Hou Kim. „Crystal structure of a small heat-shock protein“. Nature 394, Nr. 6693 (August 1998): 595–99. http://dx.doi.org/10.1038/29106.
Der volle Inhalt der QuelleShi, Xiaodong, Zhao Wang, Linxuan Yan, Anastasia N. Ezemaduka, Guizhen Fan, Rui Wang, Xinmiao Fu, Changcheng Yin und Zengyi Chang. „Small heat shock protein AgsA forms dynamic fibrils“. FEBS Letters 585, Nr. 21 (12.10.2011): 3396–402. http://dx.doi.org/10.1016/j.febslet.2011.09.042.
Der volle Inhalt der QuelleLelj-Garolla, Barbara, und A. Grant Mauk. „Self-association of a Small Heat Shock Protein“. Journal of Molecular Biology 345, Nr. 3 (Januar 2005): 631–42. http://dx.doi.org/10.1016/j.jmb.2004.10.056.
Der volle Inhalt der QuelleXi, Jing-hua, Fang Bai, Julia Gross, R. Reid Townsend, A. Sue Menko und Usha P. Andley. „Mechanism of Small Heat Shock Protein Functionin Vivo“. Journal of Biological Chemistry 283, Nr. 9 (05.12.2007): 5801–14. http://dx.doi.org/10.1074/jbc.m708704200.
Der volle Inhalt der QuelleDissertationen zum Thema "Small Heat Schok Protein"
Bellanger, Tiffany. „Mécanismes de résistance au stress chez les bactéries lactiques impliquant des sHSPs : investigation du mécanisme mis en jeu dans l’activité lipochaperon de la protéine Lo18 chez O. oeni“. Electronic Thesis or Diss., Bourgogne Franche-Comté, 2024. http://www.theses.fr/2024UBFCK004.
Der volle Inhalt der QuelleLactic acid bacteria (LAB), such as O. oeni, involved in the malolactic fermentation of wine, are subjected to major environmental stresses. Most of these stresses adversely affect the survival of the micro-organisms. Among the various response strategies employed by LAB are biofilm formation and the production of small heat shock proteins (sHSPs). sHSPs are described for their molecular chaperone activity. As such, they are capable of folding native proteins that have been partially denatured by environmental stresses. A small number have been described to have a second molecular lipochaperon activity, enabling them to maintain optimal membrane fluidity during environmental stresses. At present, little is known about the mechanisms involved in the interaction between membranes and sHSPs. It would appear that when the oligomers of these sHSPs dissociate into dimers at the membrane surface, electrostatic and hydrophobic forces deform the protein, allowing it to penetrate the membrane and help maintain its fluidity.The Lo18 protein, the only sHSP in O. oeni, is one of the sHSPs described for these two activities. In this context, we undertook an exploration of the fundamental mechanisms involved in the interaction between the Lo18 protein and membranes using in silico, in vitro and in vivo techniques, including anisotropy measurements, circular synchrotron radiation as well as immunolabelling and modelling techniques. Our research revealed that, under the influence of both the nature of the membrane lipids and certain residues of the protein, the protein structure of Lo18 is modified. This structural modification, particularly at the level of the secondary structure, proves to be essential for its lipochaperon activity. Finally, our work has also demonstrated the involvement of Lo18 in the resistance of O. oeni biofilms to acid stress, a stress found mainly in wine. Taken together, this work has led to a better understanding of the fundamental mechanisms in the response to stress involving sHSPs
Collier, Miranda. „Small heat shock protein interactions with in vivo partners“. Thesis, University of Oxford, 2018. http://ora.ox.ac.uk/objects/uuid:24cf8041-c82d-4bc4-87a7-0ae7e38f1879.
Der volle Inhalt der QuelleFranzmann, Titus Marcellus. „Chaperone mechanism of the small heat shock protein Hsp26“. kostenfrei, 2008. http://mediatum2.ub.tum.de/doc/652224/652224.pdf.
Der volle Inhalt der QuelleSund, Derrick T. „Replica Exchange Molecular Dynamics of a Small Heat Shock Protein“. Thesis, The University of Arizona, 2011. http://hdl.handle.net/10150/144990.
Der volle Inhalt der QuelleMorris, Amie Michelle. „Structure and function of the mammalian small heat shock protein Hsp25“. Access electronically Access electronically, 2007. http://www.library.uow.edu.au/adt-NWU/public/adt-NWU20080605.104334/index.html.
Der volle Inhalt der QuelleCarson, Kenneth Harris. „Study and characterization of a novel small heat shock protein from Babesia“. [College Station, Tex. : Texas A&M University, 2006. http://hdl.handle.net/1969.1/ETD-TAMU-1813.
Der volle Inhalt der Quelledi, Bard Barbara Lelj Garolla. „Self-association and chaperon activity of the small heat shock protein 27“. Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31382.
Der volle Inhalt der QuelleMedicine, Faculty of
Biochemistry and Molecular Biology, Department of
Graduate
Dabbaghizadeh, Afrooz. „Structure and function of mitochondrial small heat shock protein 22 in Drosophila melanogaster“. Doctoral thesis, Université Laval, 2018. http://hdl.handle.net/20.500.11794/34491.
Der volle Inhalt der QuelleThe small heat shock proteins (sHsps) were first discovered in Drosophila. Members of this family are molecular chaperones and are present in most eukaryotic and prokaryotic. Although, they are induced in response to most of the stressors including heat shock, they are also expressed in absence of stress. SHsps for mdynamic structures that assemble into oligomers which are essential during stress conditions by preventing aggregation of denatured proteins and promoting their folding by ATP dependent molecular chaperones. Drosophila melanogaster genome encodes 12 sHsps, that have developmental expression patterns, diverse intracellular localizations and distinct substrate specificities. DmHsp22 is up to now the only sHsp localized in mitochondria before and after heat shock. It is preferentially regulated during ageing and in response to heat and oxidative stresses. Over-expression of DmHsp22 increases lifespan and resistance to stress and its down-regulation is detrimental. It is an efficient chaperone and could be involved in the mitochondrial unfolding protein response (UPRMT). However, the exact mechanism of its action is poorly understood. Structurally, DmHsp22 forms one population of oligomers similar to the many metazoan sHsps but DmHsp27. Sequence alignment of DmHsp22 with sHsps in Drosophilaand other organisms at the alpha crystalline domain (ACD) region demonstrated the presence of three highly conserved arginine residues in this domain. Strong conservation of these residues suggest their possible involvement in structure and function of DmHsp22. Substitution of highly conserved arginine residues in mammalian sHsps is associated with some pathogenesis and triggers protein conformational changes as well as intracellular protein aggregation. Mutation of arginine to glycine at three highly conserved residues of ACD in DmHsp22 (R105, R109, R110) results in one oligomeric population as well which in the case of R110G disrupts the structure and causes formation of smaller oligomers. Although DmHsp22 as well as mutants have been characterized as effective in vitro chaperones, the exact mechanism(s) of action in mitochondria and information about protective behavior requires defining of in vivoprotein interacting network. We have used immunoaffinity conjugation (IAC) technique to recover 60 proteins that specifically interact with DmHsp22 in vivo during normal and heat treatment using cell extract of mammalian cells expressing DmHsp22. The IAC performed on mitochondrial fraction identified 39 proteins that specifically interact with DmHsp22. Combination of IAC with mass spectroscopy analysis of mitochondria of HeLa cells transfected with DmHsp22 resulted in identification of DmHsp22-binding partners under normal andunder heat shock conditions. Interaction between DmHsp22 and two other mitochondrial chaperones was validated by immunoblotting. Our approach showed that HeLa cells expressing DmHsp22 increase maximal mitochondrial oxygen consumption and ATP contents which provides a new mechanistic role for DmHsp22 in mitochondria. Further more, exogenous luciferase activity slightly increased in HeLa cells expressing DmHsp22 after the enzyme activity reduced as a result of exposure to heat. In summary, this project has characterized the oligomeric structure of DmHsp22 and a number of mutants inthe alpha crystalline domain while providing a potential mechanistic role in mitochondrial homeostasis. Determining mitochondrial network of DmHsp22 suggest its importance in this organelle not only as a molecular chaperone but also as a protein involved in several significant cellular functions.
Friedrich, Kenneth Lane. „Dynamic behavior of small heat shock protein subunits and their interactions with substrates“. Diss., The University of Arizona, 2003. http://hdl.handle.net/10150/280410.
Der volle Inhalt der QuelleBentley, Nicola Jane. „Structural and biochemical analysis of a small heat shock protein, Hsp26, from Saccharomyces cerevisiae“. Thesis, University of Kent, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.304620.
Der volle Inhalt der QuelleBücher zum Thema "Small Heat Schok Protein"
Kegel, Kimberly Beth. Small heat shock protein αB-crystallin: Functional analysis during hypertonic stress. 1997.
Den vollen Inhalt der Quelle findenClarke, Andrew. Metabolism. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780199551668.003.0008.
Der volle Inhalt der QuelleBuchteile zum Thema "Small Heat Schok Protein"
Boelens, Wilbert C. „Role of Small Heat Shock Protein HspB5 in Cancer“. In Heat Shock Proteins, 301–14. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16077-1_12.
Der volle Inhalt der QuelleVoellmy, R., Y. Luo, R. Mestril, J. Amin und J. Ananthan. „Mechanisms of Regulation of Small Heat Shock Protein Genes in Drosophila“. In Heat Shock, 35–42. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76679-4_4.
Der volle Inhalt der QuelleTörök, Zsolt, Ana-Maria Pilbat, Imre Gombos, Enikö Hocsák, Balázs Sümegi, Ibolya Horváth und László Vígh. „Evidence on Cholesterol-Controlled Lipid Raft Interaction of the Small Heat Shock Protein HSPB11“. In Heat Shock Proteins, 75–85. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4740-1_5.
Der volle Inhalt der QuelleNorris, Carol E., und Lawrence E. Hightower. „Discovery of Two Distinct Small Heat Shock Protein (HSP) Families in the Desert Fish Poeciliopsis“. In Small Stress Proteins, 19–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56348-5_2.
Der volle Inhalt der QuelleHärndahl, Ulrika, Niklas Gustavsson, Roberta Buffoni, Janet F. Bornman, Carin Jarl-Sunesson und Cecilia Sundby. „The Chloroplast Small Heat Shock Protein in Transgenic Arabidopsis Thaliana“. In Photosynthesis: Mechanisms and Effects, 2461–64. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_576.
Der volle Inhalt der QuelleOsteryoung, Katherine W., Brian Pipes, Nadja Wehmeyer und Elizabeth Vierling. „Studies of a Chloroplast-Localized Small Heat Shock Protein in Arabidopsis“. In Biochemical and Cellular Mechanisms of Stress Tolerance in Plants, 97–113. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-79133-8_5.
Der volle Inhalt der Quellevan Noort, Johannes M. „Microbial infection generates pro-inflammatory autoimmunity against the small heat shock protein alpha B-crystallin and provides the fuel for the development of multiple sclerosis“. In Heat Shock Proteins and Inflammation, 245–56. Basel: Birkhäuser Basel, 2003. http://dx.doi.org/10.1007/978-3-0348-8028-2_16.
Der volle Inhalt der QuelleArce, D. P., F. J. Krsticevic, M. R. Bertolaccini, J. Ezpeleta, S. D. Ponce und E. Tapia. „Analysis of Small Heat Shock Protein Gene Family Expression (RNA-Seq) during the Tomato Fruit Maturation“. In VI Latin American Congress on Biomedical Engineering CLAIB 2014, Paraná, Argentina 29, 30 & 31 October 2014, 679–82. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-13117-7_173.
Der volle Inhalt der QuelleGustavsson, N., A. Emanuelsson, U. Härndahl und C. Sundby. „The Chloroplast Small Heat Shock Protein Studied by Peptide Mapping and Mass Spectrometry Using Purified Recombinant Protein From Arabidopsis Thaliana and Pea“. In Photosynthesis: Mechanisms and Effects, 2457–60. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_575.
Der volle Inhalt der QuelleKlosterhalfen, B., C. Töns, H. M. Klein, L. Tietze, C. Mittermayer, M. Anurov, B. S. Titkova und A. Öttinger. „Zinc Induces Heat Shock Protein-70 and Metallothionein Expression in the Small Bowel and Protects Against Ischemia“. In Peritoneal Adhesions, 64–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60433-1_7.
Der volle Inhalt der QuelleKonferenzberichte zum Thema "Small Heat Schok Protein"
Doseff, AI, OH Voss und ME Gonzalez-Mejia. „The Small Heat Shock Protein 27 Regulates Monocyte/Macrophage Survival and Differentiation.“ In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1354.
Der volle Inhalt der QuelleCai, Wenhao, und Lingyun Chen. „Fabrication of strong heat-induced protein gels by combing soluble pea protein aggregates and κ-carrageenan“. In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/iryd5248.
Der volle Inhalt der QuelleKwon, Jin-Sun, An-Na Moon, Joon-Tae Park, Soo-Jung Hong, Jin-Ah Jeong, Sung-Wook Kwon, Myong-Jae Lee et al. „Abstract 2768: IDH1057, A novel, synthetic, small molecule inhibitor of heat shock protein 90(Hsp90)“. In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2768.
Der volle Inhalt der QuelleBalaburski, Gregor M., Julie Leu, Seth A. Hayik, Mark Andrake, Roland Dunbrack, Donna George und Maureen E. Murphy. „Abstract 3771: Identification of novel small molecule inhibitors of the inducible heat shock protein Hsp70“. In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3771.
Der volle Inhalt der QuelleHendrix, A., D. Maynard, P. Pauwels, G. Braems, H. Denys, R. Van den Broecke, S. Van Belle et al. „The Secretory Small GTPase Rab27B Regulates Invasive Tumor Growth and Metastasis through Extracellular Heat Shock Protein 90α.“ In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-6144.
Der volle Inhalt der QuelleKomiya, Atsuki, Shigenao Maruyama und Shuichi Moriya. „Development of Precise Visualization System for Small Transient Diffusion Field of Protein Using Phase Shifting Interferometer“. In ASME/JSME 2007 Thermal Engineering Heat Transfer Summer Conference collocated with the ASME 2007 InterPACK Conference. ASMEDC, 2007. http://dx.doi.org/10.1115/ht2007-32617.
Der volle Inhalt der QuelleChen, Hongpeng, Xiaofeng Tan und Fangming Hu. „Cloning, Bioinformatics Analysis and Functional Identification of a Novel Small Heat Shock Protein Gene from Camellia oleifera Seed“. In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5162514.
Der volle Inhalt der QuelleTaldone, Tony, Pallav D. Patel, Yanlong Kang, Anna Rodina, Tanaji T. Talele und Gabriela Chiosis. „Abstract 3895: Rational design of small molecule inhibitors that bind to an allosteric pocket on human heat shock protein 70 (Hsp70)“. In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3895.
Der volle Inhalt der QuelleDong, H., X. Wan, J. Zhang, C. Ye, W. Zhong und S. Cai. „Targeting Extracellular Heat Shock Protein 90α to Overcome Resistance to Gefitinib in Non Small Cell Lung Cancer via Epithelial to Mesenchymal Transition“. 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.a3963.
Der volle Inhalt der QuelleDu, Jiangzhou, und Hangming Dong. „1G6-D7 regulates the extracellular heat shock protein 90 involved in DNA damage repair affecting tumor immunity in non-small cell lung cancer“. In ERS International Congress 2023 abstracts. European Respiratory Society, 2023. http://dx.doi.org/10.1183/13993003.congress-2023.oa1446.
Der volle Inhalt der QuelleBerichte der Organisationen zum Thema "Small Heat Schok Protein"
Hiremath, Shiv, Kirsten Lehtoma und Gopi K. Podila. Identification of a small heat-shock protein associated with a ras-mediated signaling pathway in ectomycorrhizal symbiosis. Newtown Square, PA: U.S. Department of Agriculture, Forest Service, Northern Research Station, 2009. http://dx.doi.org/10.2737/nrs-rp-7.
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