Добірка наукової літератури з теми "Prone proteins"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся зі списками актуальних статей, книг, дисертацій, тез та інших наукових джерел на тему "Prone proteins".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Статті в журналах з теми "Prone proteins"
De Baets, Greet, Joost Schymkowitz, and Frederic Rousseau. "Predicting aggregation-prone sequences in proteins." Essays in Biochemistry 56 (August 18, 2014): 41–52. http://dx.doi.org/10.1042/bse0560041.
Повний текст джерелаLebendiker, Mario, and Tsafi Danieli. "Production of prone-to-aggregate proteins." FEBS Letters 588, no. 2 (November 6, 2013): 236–46. http://dx.doi.org/10.1016/j.febslet.2013.10.044.
Повний текст джерелаGalves, Margarita, Ritu Rathi, Gali Prag, and Avraham Ashkenazi. "Ubiquitin Signaling and Degradation of Aggregate-Prone Proteins." Trends in Biochemical Sciences 44, no. 10 (October 2019): 872–84. http://dx.doi.org/10.1016/j.tibs.2019.04.007.
Повний текст джерелаTartaglia, Gian Gaetano, Amol P. Pawar, Silvia Campioni, Christopher M. Dobson, Fabrizio Chiti, and Michele Vendruscolo. "Prediction of Aggregation-Prone Regions in Structured Proteins." Journal of Molecular Biology 380, no. 2 (July 2008): 425–36. http://dx.doi.org/10.1016/j.jmb.2008.05.013.
Повний текст джерелаBerger, Zdenek, Brinda Ravikumar, Fiona M. Menzies, Lourdes Garcia Oroz, Benjamin R. Underwood, Menelas N. Pangalos, Ina Schmitt, et al. "Rapamycin alleviates toxicity of different aggregate-prone proteins." Human Molecular Genetics 15, no. 3 (December 20, 2005): 433–42. http://dx.doi.org/10.1093/hmg/ddi458.
Повний текст джерелаChennamsetty, Naresh, Vladimir Voynov, Veysel Kayser, Bernhard Helk, and Bernhardt L. Trout. "Prediction of Aggregation Prone Regions of Therapeutic Proteins." Journal of Physical Chemistry B 114, no. 19 (May 20, 2010): 6614–24. http://dx.doi.org/10.1021/jp911706q.
Повний текст джерелаSalomons, Florian A., Victoria Menéndez-Benito, Claudia Böttcher, Brett A. McCray, J. Paul Taylor, and Nico P. Dantuma. "Selective Accumulation of Aggregation-Prone Proteasome Substrates in Response to Proteotoxic Stress." Molecular and Cellular Biology 29, no. 7 (January 21, 2009): 1774–85. http://dx.doi.org/10.1128/mcb.01485-08.
Повний текст джерелаRavikumar, Brinda, Abraham Acevedo-Arozena, Sara Imarisio, Zdenek Berger, Coralie Vacher, Cahir J. O'Kane, Steve D. M. Brown, and David C. Rubinsztein. "Dynein mutations impair autophagic clearance of aggregate-prone proteins." Nature Genetics 37, no. 7 (June 26, 2005): 771–76. http://dx.doi.org/10.1038/ng1591.
Повний текст джерелаKnaevelsrud, Helene, and Anne Simonsen. "Fighting disease by selective autophagy of aggregate-prone proteins." FEBS Letters 584, no. 12 (April 20, 2010): 2635–45. http://dx.doi.org/10.1016/j.febslet.2010.04.041.
Повний текст джерелаKällquist, Linda, Markus Hansson, Ann-Maj Persson, Hans Janssen, Jero Calafat, Hans Tapper, and Inge Olsson. "The tetraspanin CD63 is involved in granule targeting of neutrophil elastase." Blood 112, no. 8 (October 15, 2008): 3444–54. http://dx.doi.org/10.1182/blood-2007-10-116285.
Повний текст джерелаДисертації з теми "Prone proteins"
Malm, Linus. "Size determination of hyaluronan and multivariate analysis of amyloid prone proteins." Doctoral thesis, Umeå universitet, Institutionen för medicinsk kemi och biofysik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-46601.
Повний текст джерелаBerger, Z. "The biology of aggregate-prone proteins and possible therapeutic interventions against their toxicity." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596587.
Повний текст джерелаGallo, Annastassia Dawn. "Homeostasis and trafficking of hydrolysis-prone metals in cells, proteins, and small molecules." Diss., Temple University Libraries, 2019. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/568230.
Повний текст джерелаPh.D.
Nature uses inorganic elements for biological processes based on the useful chemistry, abundance, and availability of each metal. Transition metals are critical in the biogeochemical cycling of essential elements and the bioinorganic chemistry of organisms. Hydrolysis-prone metals such as iron and titanium are abundant on Earth but are mostly insoluble in oxic aqueous environments. Nearly every organism requires iron for survival, therefore Nature evolved to stabilize iron from hydrolysis and hydrolytic precipitation through protein and small molecule mechanisms. Like iron, titanium primarily exists as insoluble mineral oxides and is second only to iron as the most abundant transition metal in the Earth’s crust. Despite the reputation as an inert and insoluble metal, titanium can be solubilized and made bioavailable through by chemical and biological weathering. Currently there is no known native role for titanium, however it is quite bioactive. As a stronger Lewis acid, titanium can compete with iron in binding to biomolecules and proteins. It is of interest to investigate the interactions between hydrolysis-prone metals and biological systems, from whole cell organisms to proteins and small molecules. The non-pathogenic bacterium Rhodococcus ruber GIN-1 was isolated for its ability to strongly adhere to titanium dioxide (TiO2) over other metal oxides, providing an opportunity to study the interactions between whole bacterial cells and metal oxides. The GIN-1 strain incorporates Ti(IV) ions into its biomass after adherence to anatase, rutile, and a mixture of the two morphologies. Six metals were quantitated in TiO2-exposed and control (unexposed) cells by inductively coupled plasma optical emission spectroscopy. The exposure to TiO2 caused a significant uptake of titanium with concomitant loss of iron, zinc, and possibly manganese. A collaborative project with the Strongin laboratory at Temple University works to develop stable, biomaterial photocatalysts for environment remediation of toxic inorganic contaminants. Ferritins are a class of proteins that mineralizes and stores iron as a non- toxic ferrihydrite nanoparticle. These proteins can be photoactivated with ultraviolet light to release iron from its core to remediate environmental contaminants. Ferritin can be sensitized with plasmonic gold nanoparticles to extend the photoactivity of the catalyst to the visible spectrum. Work in this thesis highlights the contribution to this collaboration from the Valentine laboratory, included the expression and purification of proteins in E. coli (human H-chain ferritin, human L-chain ferritin, and bacterial DNA protection from starved cells protein), mutation of proteins to improve sensitization of catalyst, and biomineralization with iron and titanium. The trafficking of hydrolysis prone metals is vital for the survival of nearly every organism. Iron transport proteins such as transferrins are studied to understand how nature utilizes a difficult essential metal across the domains of life. Most transferrins have two homologous lobes and are believed to have evolved from a gene duplication of a monolobal transferrin. The ascidian Ciona intestinalis has genes for both a bilobal and monolobal transferrin. Nicatransferrin (nicaTf), the monolobal transferrin from C. intestinalis, is a primitive protein that may provide insight on the evolution of transferrins in higher organisms. It is advantageous to use E. coli expression systems to produce recombinant proteins, however protein misfolding and aggregation can be a concern. To improve expression of nicaTf in E. coli, codon optimization and disulfide bonded protein expression were used. Finally, siderophores are small, high affinity iron-chelating molecules secreted from lower organisms that scavenge iron in iron-limiting conditions. R. ruber GIN-1 and R. ruber DSM 43338 strains both secrete siderophores in artificial seawater media. There are several siderophores identified from Rhodococcus species, however none have been reported from any R. ruber strain. A new siderophore was isolated and preliminary work has been done to purify and characterize the molecule. Understanding the siderophore- metal ion interactions may help elucidate the mechanism of how R. ruber cells obtain titanium from the metal-oxide particles.
Temple University--Theses
Williams, Andrea. "Characterisation of novel autophagy pathways : implications in the clearance of disease-causing aggregate-prone proteins." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612132.
Повний текст джерелаVincenz-Donnelly, Lisa Verfasser], та Franz-Ulrich [Akademischer Betreuer] [Hartl. "How the mammalian endoplasmic reticulum handles aggregation-prone β-sheet proteins / Lisa Vincenz-Donnelly ; Betreuer: Franz-Ulrich Hartl". München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2016. http://d-nb.info/1122019467/34.
Повний текст джерелаBorn, Ariane. "Etablierung und Optimierung der Error-Prone-PCR und eines Aktivitätsscreenings für Styrol-Monooxygenasen." Master's thesis, Technische Universitaet Bergakademie Freiberg Universitaetsbibliothek "Georgius Agricola", 2011. http://nbn-resolving.de/urn:nbn:de:bsz:105-qucosa-77143.
Повний текст джерелаStyrene monooxygenases (SMOs) play an important role in the bacterial degradation of styrene. They epoxidize the hydrocarbon highly enantioselective to (S)-styrene oxide. Most of the styrene monooxygenases known so far were identified in Gram-negative microorganisms like pseudomonads. Rhodococcus opacus 1CP, a Gram-positive nocardioform actinobacterium, which uses styrene as energy and carbon source was recently found to possess a novel type of SMO, StyA2B. This protein represents a natural fusion between an FAD:NADH oxidoreductase (StyB) and a single monooxygenase subunit (StyA2) and might act in combination with another single oxygenase StyA1 in strain 1CP. Two artificial analogs to StyA2B, designated StyAL1B and StyAL2B, were recently prepared by a fusion of styA and styB of Pseudomonas fluorescens ST and both showed oxygenating activity. For StyA1/StyA2B as well as the artificial fusion proteins StyAL1B and StyAL2B, it was tried to enhance the specific oxygenation activity in order to support their biotechnological applicability. The method of error prone PCR was used for that purpose. In order to identify favorable modifications with increased catalytic activity from a high number of mutants, an easy and simple screening test is necessary. Therefore, it is reasonable to use the ability of SMOs to oxidize indole to the blue dye indigo. However, the expression of SMOs as soluble proteins is an important requirement for any activity screening. Attempts to modify the genes styA2B and styA1/styA2B by means of a commercial error prone PCR kit yielded 300 to 1,200 potential mutants. Unfortunately, none of the obtained colonies showed any indole-oxidizing activity and the formation of insoluble inclusion bodies was assumed to be a likely explanation. In contrast to StyA2B and StyA1, recombinant expression of the artificial fused SMOs StyAL1B und StyAL2B should yield detectable amounts of active proteins. In fact, cultivation of clones expressing both types of proteins showed a blue coloration. Since the coloration of clones from one single solid medium evolved in a non-uniform manner, cultivation conditions were varied in order to identify factors which promote a more uniform tendency for indole oxidation. Although a high NaCl concentration in the medium was shown to favor indole oxidation, the latter one seems to be influenced by additional physiological factors, hardly to control. For the artificially fused proteins an error prone PCR was carried out, too. Although the initial step of mutagenic PCR was found to be successful, completing the vector system by a second ll-up PCR reaction failed. Alternative strategies like the usage of alternative DNA polymerases as well as a conventional cloning approach of various genes into a digested expression vector did not lead to detectable clones. The cultivation of identical clones on petri dishes provided no uniform tendency for indole oxidation and thus did not allow the reliable comparison of mutants in respect of their specific SMO activities. Cultivation of mutants in liquid medium should lead to more reproducible conditions and for that purpose a method was successfully established to quantify indigo formation and cell density
Liu, Xueyun, and Xueyun Liu. "Probe Ca2+/Camodulin reguation of membrane proteins engineering." Digital Archive @ GSU, 2013. http://digitalarchive.gsu.edu/chemistry_theses/59.
Повний текст джерелаMossuto, Maria Francesca. "Protein amyloidogenesis: characterization of aggregation prone conformations and fibrils structure." Doctoral thesis, Università degli studi di Padova, 2008. http://hdl.handle.net/11577/3425566.
Повний текст джерелаSOUZA, Renata Silva Cabral de. "Avalia??o do potencial antioxidante e antimicrobiano de prote?nas do soro de leite concentradas por membranas e hidrolisadas por diferentes enzimas comerciais." Universidade Federal Rural do Rio de Janeiro, 2013. https://tede.ufrrj.br/jspui/handle/jspui/2534.
Повний текст джерелаMade available in DSpace on 2018-11-29T17:12:51Z (GMT). No. of bitstreams: 1 2013 - Renata Silva Cabral de Souza.pdf: 1753830 bytes, checksum: 2dff8752eb3f7974e34f8809d059f126 (MD5) Previous issue date: 2013-05-23
CAPES
The aim of this study was to evaluate the process of protein concentration in bovine whey proteins by ultrafiltration process and subsequently the protein hydrolysate obtained by enzymatic hydrolysis to produce bioactive peptides with potential antimicrobial and antioxidant activities. For concentration process was used a ceramic ultrafiltration membrane with a molecular range cut-off of 10-20 kDa, transmembrane pressure of 5 bar and, temperature of 30 ?C, 40 ?C and 50 ?C . The optimum temperature condition was at 40 ?C. The Volume Concentrate Factor (VCF) parameter was used as a end-point of the ultrafiltration process and fixed at 2, corresponding on concentrating the initial volume twice, in volume. At the temperature of 40 ?C, VCF had a correspondence on final protein concentration on the concentrated fraction by ultrafiltration and confirmed by Bradford method. Two commercial enzymes were tested Alcalase, Flavourzyme and an equivalent mixture of both 50:50 (w/w) in the hydrolysis reaction. The hydrolysis conditions were determined according to manufacturer instructions and confirmed by other studies: 60 ?C and pH 8 for Alcalase; 50 ?C and pH 7 for Flavourzyme; 50 ?C and pH 8 for enzyme mixture with enzyme / substrate ratio (w / w) 5/100 for all enzymes. The reaction was monitored by pH Stat method. The final Degree of Hydrolysis (DH) achieved was 15%, 52% and 63% for Flavourzyme, Alcalase and enzyme mixture, respectively. Five aliquots were collected along the hydrolysis for each enzyme reaction corresponding to differents DH in order to evaluatethe antioxidant activity by ORAC and ABTS assays with final values between 597- 1092 m? TE (ABTS) and from 1615 to 2920 ?M TE (ORAC) for Flavourzyme; 998-6290 ?M TE (ABTS) and 3092-7567 ?M TE ( ORAC) for Alcalase and finally 913-2678 ?M TE (ABTS) and 2547-5903 ?M TE (ORAC) for the enzyme mixture. The samples from all hydrolysates showed no antimicrobial activity against strains of Salmonella choleraesuis subsp. Enteritidis (ATCC 13076) and Listeria monocytogenes (ATCC 9117).
A proposta do presente trabalho foi avaliar a concentra??o das prote?nas do soro de leite bovino por ultrafiltra??o e posterior obten??o de hidrolisados proteicos deste concentrado via hidr?lise enzim?tica visando obter pept?deos bioativos com potencial atividade antimicrobiana e antioxidante. Para concentra??o das prote?nas do soro foi utilizada membrana cer?mica de ultrafiltra??o com massa molar de corte de 10-20 kDa, press?o aplicada ? membrana de 5 bar, temperaturas testadas (30 ?C, 40 ?C e 50 ?C) . A temperatura ?tima selecionada foi de 40 ?C. O Fator de Concentra??o Volum?trica foi o par?metro utilizado para indicar o final do processo de ultrafiltra??o sendo fixado em duas vezes o volume inicial da alimenta??o. Na temperatura de 40 ?C foi obtida correspond?ncia entre a concentra??o volum?trica e a concentra??o proteica final na fra??o retida pela UF, que tamb?m foi o dobro da encontrada na fra??o alimenta??o, avaliada pelo m?todo de Bradford. Foram testadas duas enzimas comerciais: Alcalase, Flavourzyme e uma mistura equivalente de ambas, na propor??o 50:50 (m/m) na rea??o de hidr?lise. As condi??es de rea??o enzim?tica foram determinadas de acordo com instru??es do fabricante e corroboradas por outros estudos em: 60 ?C, pH 8 para Alcalase; 50 ?C, pH 7 para Flavourzyme; 50 ?C, pH 8 para mistura enzim?tica e rela??o enzima/substrato (g/g) foi de 5/100 para todas as enzimas. A rea??o de hidr?lise foi monitorada pelo m?todo pH Stat. Os Graus de Hidr?lise (GH) finais alcan?ados foram de 15 %, 52 % e 63 % para Flavourzyme, mistura enzim?tica e Alcalase, respectivamente. Foram coletadas cinco al?quotas correspondentes a diferentes GH ao longo da rea??o para cada condi??o enzim?tica utilizada e avaliadas quanto a atividade antioxidante pelos m?todos ABTS e ORAC tendo valores entre 597 a 1092 ?M TE (ABTS) e 1615 a 2920 ?M TE (ORAC) para Flavourzyme, 998 a 6290 ?M TE (ABTS) e 3092 a 7567 ?M TE (ORAC) para Alcalase e por fim, 913 a 2678 ?M TE (ABTS) e 2547 a 5903 ?M TE (ORAC) para a mistura enzim?tica. Nenhuma das amostras de hidrolisado com diferentes GH apresentou atividade antimicrobiana contra cepas de Salmonella choleraesuis subsp. Enteritidis (ATCC 13076) e Listeria monocytogenes (ATCC 9117).
Wikström, Malin. "Synthesis and protein curing abilities of membrane glycolipids." Doctoral thesis, Stockholm University, Department of Biochemistry and Biophysics, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1361.
Повний текст джерелаThere are many types of membrane lipids throughout Nature. Still little is known about synthesizing pathways and how different lipids affect the embedded membrane proteins. The most common lipids are glycolipids since they dominate plant green tissue. Glycolipids also exist in mammal cells as well as in most Gram-positive bacteria. Glycosyltransferases (GTs) catalyze the final enzymatic steps for these glycolipids. In the bacteria Acholeplasma laidlawii and Streptococcus pneumonie and in the plant Arabidopsis thaliana, GTs for mono-/di-glycosyl-diacylglycerol (-DAG) are suggested to be regulated to keep a certain membrane curvature close to a bilayer/nonbilayer phase transition. The monoglycosylDAGs are nonbilayer-prone with small headgroups, hence by themselves they will not form bilayer structures.
Here we have determined the genes encoding the main glycolipids of A. laidlawii and S. pneumonie. We have also shown that these GTs belong to a large enzyme group widely spread in Nature, and that all four enzymes are differently regulated by membrane lipids. The importance of different lipid properties were traced in a lipid mutant of Escherichia coli lacking the major (75 %), nonbilayer-prone/zwitterionic, lipid phosphatidylethanolamine. Introducing the genes for the GTs of A. laidlawii and two analogous genes from A. thaliana yielded new strains containing 50 percent of glyco-DAG lipids. The monoglyco-DAG strains contain significant amounts of nonbilayer-prone lipids while the diglyco-DAG strains contain no such lipids. Comparing these new strains for viability and the state of membrane-associated functions made it possible to connect different functions to certain lipid properties. In summary, a low surface charge density of anionic lipids is important in E.coli membranes, but this fails to be supportive if the diluting species have a too large headgroup. This indicates that a certain magnitude of the curvature stress is crucial for the membrane bilayer in vivo.
Книги з теми "Prone proteins"
R, Ansari Rafat, and United States. National Aeronautics and Space Administration., eds. A fiber optic probe for monitoring protein aggregation, nucleation, and crystallization. Washington, DC: National Aeronautics and Space Administration, 1997.
Знайти повний текст джерелаKeromnes, Anne. Synthesis of a novel chemically modified tetrasaccharide to probe carbohydrate-protein interactions. Birmingham: University of Birmingham, 1996.
Знайти повний текст джерелаProf, Miller Lawrence W., ed. Probes and tags to study biomolecular function: For proteins, RNA, and membranes. Weinheim: Wiley-VCH Verlag, 2008.
Знайти повний текст джерелаPieribone, Vincent. Aglow in the dark: The revolutionary science of biofluorescence. Cambridge, Mass: Belknap Press of Harvard University Press, 2005.
Знайти повний текст джерелаMin, Zhang, Yin Bin-Cheng, and SpringerLink (Online service), eds. Nano-Bio Probe Design and Its Application for Biochemical Analysis. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012.
Знайти повний текст джерелаLes recettes Dukan: Mon re gime en 350 recettes. Paris: J'ai lu, 2008.
Знайти повний текст джерелаLes recettes Dukan: Mon régime en 350 recettes. [Paris]: Flammarion, 2011.
Знайти повний текст джерелаNanomedicine. Austin, Tex: Landes Bioscience, 1999.
Знайти повний текст джерелаAnna, Brajter-Toth, and Chambers James Q, eds. Electroanalytical methods for biological materials. New York: Marcel Dekker, 2002.
Знайти повний текст джерелаTinker-Mill, Claire Louisa. Nanoscale Imaging and Characterisation of Amyloid-β. Springer International Publishing AG, 2016.
Знайти повний текст джерелаЧастини книг з теми "Prone proteins"
Kumar, Sandeep, Xiaoling Wang, and Satish K. Singh. "Identification and Impact of Aggregation-Prone Regions in Proteins and Therapeutic Monoclonal Antibodies." In Aggregation of Therapeutic Proteins, 103–18. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470769829.ch3.
Повний текст джерелаRavikumar, Brinda, Sovan Sarkar, and David C. Rubinsztein. "Clearance of Mutant Aggregate-Prone Proteins by Autophagy." In Autophagosome and Phagosome, 195–211. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-157-4_13.
Повний текст джерелаNeedle, Danielle, and David S. Waugh. "Rescuing Aggregation-Prone Proteins in Escherichia coli with a Dual His6-MBP Tag." In Protein Affinity Tags, 81–94. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1034-2_7.
Повний текст джерелаSinnige, Tessa, Anan Yu, and Richard I. Morimoto. "Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Human Disease." In Advances in Experimental Medicine and Biology, 53–68. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-40204-4_4.
Повний текст джерелаKronqvist, Nina, Anna Rising, and Jan Johansson. "A Novel Approach for the Production of Aggregation-Prone Proteins Using the Spidroin-Derived NT* Tag." In Methods in Molecular Biology, 113–30. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1859-2_6.
Повний текст джерелаRanganathan, Umarani, and Steven P. C. Groot. "Seed Longevity and Deterioration." In Seed Science and Technology, 91–108. Singapore: Springer Nature Singapore, 2023. http://dx.doi.org/10.1007/978-981-19-5888-5_5.
Повний текст джерелаSljoka, Adnan. "Structural and Functional Analysis of Proteins Using Rigidity Theory." In Sublinear Computation Paradigm, 337–67. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-4095-7_14.
Повний текст джерелаGrubmüller, Helmut. "Force Probe Molecular Dynamics Simulations." In Protein-Ligand Interactions, 493–515. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-912-5_493.
Повний текст джерелаPeterson, Cynthia B., and Michael N. Blackburn. "Localization and Interaction of Functional Sites on Antithrombin III. Use of an Anti-Hapten Antibody as a Structural Probe." In Proteins, 665–72. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1787-6_67.
Повний текст джерелаFrauenfelder, Hans. "The Nucleus as a Probe (C. E. Schulz1)." In The Physics of Proteins, 393–414. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-1044-8_28.
Повний текст джерелаТези доповідей конференцій з теми "Prone proteins"
Abakumets, V. Y., and K. Ya Bulanava. "THE INFLUENCE OF INSULIN FIBRILLATION." In SAKHAROV READINGS 2021: ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. International Sakharov Environmental Institute of Belarusian State University, 2021. http://dx.doi.org/10.46646/sakh-2021-2-7-10.
Повний текст джерелаGolmohamadi, Farzin Ghane, Amna Mehmood, Franz-Josef Schmitt, and Jan Laufer. "Pump-probe photoacoustic spectroscopy of red fluorescent proteins." In European Conference on Biomedical Optics. Washington, D.C.: Optica Publishing Group, 2021. http://dx.doi.org/10.1364/ecbo.2021.em2d.2.
Повний текст джерелаReed, Scott M., Min S. Wang, and Erica L. Curello. "Electrophoretic Mobility of Lipid Coated Nanoparticles: Understanding the Influence of Size and Charge on a Lipoprotein Particle Mimic." In ASME 2011 International Mechanical Engineering Congress and Exposition. ASMEDC, 2011. http://dx.doi.org/10.1115/imece2011-64158.
Повний текст джерелаChurch, W., T. Messier, P. Howard, J. Amiral, D. Meyer, and K. Mam. "A SHARED EPITOPE ON HUMAN PROTEIN C, FACTOR X, FACTOR VII, AND PROTTOBIN DEFINED BY A MONOCLONAL ANTIBODY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643937.
Повний текст джерелаAleixo, Frederico, Matthias Knorr, and João Leite. "Revising Boolean Logical Models of Biological Regulatory Networks." In 20th International Conference on Principles of Knowledge Representation and Reasoning {KR-2023}. California: International Joint Conferences on Artificial Intelligence Organization, 2023. http://dx.doi.org/10.24963/kr.2023/2.
Повний текст джерелаVilleneuve, Pierre, Jeanne Duplessis-Kergomard, Melina Robert, Gilles Paboeuf, Nathalie Barouh, Olivier Schafer, Tim Wooster, Claire Bourlieu-Lacanal, and Veronique Vie. "Effect of Processing and Fat Content on the Oxidative Stability and Interfacial Behavior of Tree Nut Oil-bodies." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/djlm1220.
Повний текст джерелаKanchanawong, Pakorn (Tony). "Interference-Based Techniques in Superresolution Microscopy." In JSAP-OSA Joint Symposia. Washington, D.C.: Optica Publishing Group, 2017. http://dx.doi.org/10.1364/jsap.2017.6p_a409_1.
Повний текст джерелаHansen, John E., Sandra J. Rosenthal, and Graham R. Fleming. "Subpicosecond Fluorescence Anisotropy Measurements of Tryptophanyl Residues in Proteins." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1990. http://dx.doi.org/10.1364/up.1990.pdp2.
Повний текст джерелаde Vries, C. J. M., N. K. Veerman, and H. Pannekoek. "ARTIFICIAL EXON SHUFFLING: CONSTRUCTION OF HYBRID cDNAS CONTAINING DOMAINS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) AND UROKINASE (u-PA)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643940.
Повний текст джерелаNomura, Wataru, Nami Ohashi, Tetsuo Narumi, and Hirokazu Tamamura. "Tag-Probe System for Imaging of Intracellular Proteins." In The Twenty-Third American and the Sixth International Peptide Symposium. Prompt Scientific Publishing, 2013. http://dx.doi.org/10.17952/23aps.2013.174.
Повний текст джерелаЗвіти організацій з теми "Prone proteins"
Asenath-Smith, Emily, Emily Jeng, Emma Ambrogi, Garrett Hoch, and Jason Olivier. Investigations into the ice crystallization and freezing properties of the antifreeze protein ApAFP752. Engineer Research and Development Center (U.S.), September 2022. http://dx.doi.org/10.21079/11681/45620.
Повний текст джерелаEpel, Bernard L., Roger N. Beachy, A. Katz, G. Kotlinzky, M. Erlanger, A. Yahalom, M. Erlanger, and J. Szecsi. Isolation and Characterization of Plasmodesmata Components by Association with Tobacco Mosaic Virus Movement Proteins Fused with the Green Fluorescent Protein from Aequorea victoria. United States Department of Agriculture, September 1999. http://dx.doi.org/10.32747/1999.7573996.bard.
Повний текст джерелаGhanim, Murad, Joe Cicero, Judith K. Brown, and Henryk Czosnek. Dissection of Whitefly-geminivirus Interactions at the Transcriptomic, Proteomic and Cellular Levels. United States Department of Agriculture, February 2010. http://dx.doi.org/10.32747/2010.7592654.bard.
Повний текст джерелаBuck, D. R. Theoretical Simulations and Ultrafast Pump-probe Spectroscopy Experiments in Pigment-protein Photosynthetic Complexes. Office of Scientific and Technical Information (OSTI), September 2000. http://dx.doi.org/10.2172/764683.
Повний текст джерелаPorat, Ron, Gregory T. McCollum, Amnon Lers, and Charles L. Guy. Identification and characterization of genes involved in the acquisition of chilling tolerance in citrus fruit. United States Department of Agriculture, December 2007. http://dx.doi.org/10.32747/2007.7587727.bard.
Повний текст джерелаEpel, Bernard, and Roger Beachy. Mechanisms of intra- and intercellular targeting and movement of tobacco mosaic virus. United States Department of Agriculture, November 2005. http://dx.doi.org/10.32747/2005.7695874.bard.
Повний текст джерелаTerzyan, Aram. Belarus in the Wake of a Revolution: Domestic and International Factors. Eurasia Institutes, December 2020. http://dx.doi.org/10.47669/eea-3-2020.
Повний текст джерелаBraun, Alexander. The Interaction between a Thiol Specific Probe (OPA) and the Single Channel Characteristics of the Reconstituted Ca++ Release Protein from Skeletal Muscle Sarcoplasmic Reticulum. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.6745.
Повний текст джерелаRafaeli, Ada, Russell Jurenka, and Daniel Segal. Isolation, Purification and Sequence Determination of Pheromonotropic-Receptors. United States Department of Agriculture, July 2003. http://dx.doi.org/10.32747/2003.7695850.bard.
Повний текст джерелаShapira, Roni, Judith Grizzle, Nachman Paster, Mark Pines, and Chamindrani Mendis-Handagama. Novel Approach to Mycotoxin Detoxification in Farm Animals Using Probiotics Added to Feed Stuffs. United States Department of Agriculture, May 2010. http://dx.doi.org/10.32747/2010.7592115.bard.
Повний текст джерела