Relevant bibliographies by topics / In vivo assay

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

Academic literature on the topic 'In vivo assay'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "In vivo assay"

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Hayashi, Makoto, James T. MacGregor, David G. Gatehouse, David H. Blakey, Stephen D. Dertinger, Lilianne Abramsson-Zetterberg, Gopala Krishna, et al. "In vivo erythrocyte micronucleus assay." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 627, no. 1 (February 2007): 10–30. http://dx.doi.org/10.1016/j.mrgentox.2006.08.010.

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Kim, So-Jung, Young-Jae Chung, and Taek-Kyun Lee. "In vivo Comet Assay on Flounder and Clam Exposed to BaP and TBT." Ocean and Polar Research 33, no. 2 (June 30, 2011): 127–33. http://dx.doi.org/10.4217/opr.2011.33.2.127.

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Matute, Alexis, Jessica Tabart, Jean-Paul Cheramy-Bien, Claire Kevers, Jacques Dommes, Jean-Olivier Defraigne, and Joël Pincemail. "Ex Vivo Antioxidant Capacities of Fruit and Vegetable Juices. Potential In Vivo Extrapolation." Antioxidants 10, no. 5 (May 12, 2021): 770. http://dx.doi.org/10.3390/antiox10050770.

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Background: In support of claims that their products have antioxidant properties, the food industry and dietary supplement manufacturers rely solely on the in vitro determination of the ORAC (oxygen radical antioxidant capacity) value, despite its acknowledged lack of any in vivo relevance. It thus appears necessary to use tests exploiting biological materials (blood, white blood cells) capable of producing physiological free radicals, in order to evaluate more adequately the antioxidant capacities of foods such as fruit and vegetable juices. Materials: Two approaches to assessing the antioxidant capacities of 21 commercial fruit and vegetable juices were compared: the ORAC assay and the “PMA–whole blood assay,” which uses whole blood stimulated by phorbol myristate acetate to produce the superoxide anion. We described in another paper the total polyphenol contents (TPCs) and individual phenolic compound contents of all the juices were investigated. Results: Ranking of the juices from highest to lowest antioxidant capacity differed considerably according to the test used, so there was no correlation (r = 0.33, p = 0.13) between the two assays when considering all juices. Although the results of the ORAC assay correlated positively with TPC (r = 0.50, p = 0.02), a much stronger correlation (r = 0.70, p = 0.004) emerged between TPC and % superoxide anion inhibition. In the PMA–whole blood assay, peonidin-3-O-glucoside, epigallocatechin gallate, catechin, and quercetin present in juices were found to inhibit superoxide anion production at concentrations below 1 µM, with a strong positive correlation. Conclusions: Associated with the determination of total and individual phenolic compounds contained in fruit and vegetable juices, the PMA–whole blood assay appears better than the ORAC assay for evaluating juice antioxidant capacity.
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Simpson, David M., Edward W. Stoller, and Loyd M. Wax. "An in vivo Acetolactate Synthase Assay." Weed Technology 9, no. 1 (March 1995): 17–22. http://dx.doi.org/10.1017/s0890037x00022879.

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A method was developed and tested for in vivo assay of acetolactate synthase (ALS). The method used foliar application of 1,1-cyclopropanedicarboxylic acid (CPCA) to inhibit ketol-acid reductoisomerase, the enzyme immediately following ALS in biosynthesis of branched-chain amino acids, thereby causing accumulation of acetolactate. Since the amount of acetolactate accumulation is a function of carbon flux through ALS, quantification of acetolactate accumulation determined ALS activity. Accumulation of acetolactate in soybean leaves resulted from CPCA rates as low as 15 g/ha and occurred within 1.5 h. Accumulation rates in soybean leaflets declined with leaf age from 84 μg/h/g tissue at 3 d to 17 μg/h/g tissue at 7 d. Foliar application of CPCA also caused acetolactate accumulation in corn, grain sorghum, velvetleaf, common cocklebur, and smooth pigweed. The ability of the in vivo assay to quantify the reduction in ALS activity following applications of ALS-inhibiting herbicides was validated by comparing ALS activity following thifensulfuron application to ‘Williams 82’ soybean, which has a sulfonylurea-sensitive ALS, and ‘Asgrow 3200’ soybean, which has a sulfonylurea-insensitive ALS. Thifensulfuron reduced ALS activity in Williams 82 soybean to 0, 0.8, 3.3, and 15.6% of the CPCA control at 6, 12, 24, and 48 HAT, but ALS activity in Asgrow 3200 soybean was reduced only to 34, 40, 57, and 88% of the CPCA control.
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Hayashi, Makoto, Raymond R. Tice, James T. MacGregor, Diana Anderson, David H. Blakey, M. Kirsh-Volders, Frederick B. Oleson, et al. "In vivo rodent erythrocyte micronucleus assay." Mutation Research/Environmental Mutagenesis and Related Subjects 312, no. 3 (June 1994): 293–304. http://dx.doi.org/10.1016/0165-1161(94)90039-6.

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Spach, Colette, and Roland Motta. "In vivo eight-day ‘MLR’ assay." Journal of Immunological Methods 97, no. 2 (March 1987): 259–62. http://dx.doi.org/10.1016/0022-1759(87)90468-6.

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Uccellini, Melissa B., Sadaf Aslam, Sean T. H. Liu, Fahmida Alam, and Adolfo García-Sastre. "Development of a Macrophage-Based ADCC Assay." Vaccines 9, no. 6 (June 17, 2021): 660. http://dx.doi.org/10.3390/vaccines9060660.

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Fc-dependent effector functions are an important determinant of the in vivo potency of therapeutic antibodies. Effector function is determined by the combination of FcRs bound by the antibody and the cell expressing the relevant FcRs, leading to antibody-dependent cellular cytotoxicity (ADCC). A number of ADCC assays have been developed; however, they suffer from limitations in terms of throughput, reproducibility, and in vivo relevance. Existing assays measure NK cell-mediated ADCC activity; however, studies suggest that macrophages mediate the effector function of many antibodies in vivo. Here, we report the development of a macrophage-based ADCC assay that relies on luciferase expression in target cells as a measure of live cell number. In the presence of primary mouse macrophages and specific antibodies, loss of luciferase signal serves as a surrogate for ADCC-dependent killing. We show that the assay functions for a variety of mouse and human isotypes with a model antigen/antibody complex in agreement with the known effector function of the isotypes. We also use this assay to measure the activity of a number of influenza-specific antibodies and show that the assay correlates well with the known in vivo effector functions of these antibodies.
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Hosking, Laine, Christine Czakjo, and Sharon Choo. "Implementation of an ex vivo TH17 assay." Pathology 49 (February 2017): S43. http://dx.doi.org/10.1016/j.pathol.2016.12.102.

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Bertaccini, Alessandro, Catia Giovannini, Domenico Viola, Francesco Comerci, Luca Ronci, Michela Lacchini, Roberto Rusconi, Pasquale Chieco, and Giuseppe Martorana. "Telomerase assay from ex vivo prostate biopsies." European Urology Supplements 1, no. 1 (January 2002): 119. http://dx.doi.org/10.1016/s1569-9056(02)80461-4.

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Tang, De-chu, Adi F. Gazdar, and David P. Carbone. "In vivo cytotoxicity assay for assessing immunity." Journal of Immunological Methods 189, no. 2 (January 1996): 173–82. http://dx.doi.org/10.1016/0022-1759(95)00234-0.

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Dissertations / Theses on the topic "In vivo assay"

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Kreps, Amina. "Development of an «In Vivo» eIF4E-RNA immunoprecipitation assay." Thesis, McGill University, 2014. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=123304.

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Although eIF4E plays an important role in the development and progression of cancer, the mechanism through which it acts has not been directly characterised. In order to aid in the progression of this knowledge, an in vivo eIF4E-mRNA immunoprecipitation assay was developed and validated in NIH 3T3 cells. This assay demonstrates its ability to specifically pull down capped mRNAs bound to ectopically expressed 3X-FLAG tagged eIF4E. Mutations in eIF4E that affected cap binding and/or interaction with eIF4G or 4E-BP were also evaluated for their RNA binding potential. Elution of mRNAs from eIF4E with m7GTP competition was not observed following cell lysis, indicating that post-lysis association did not affect the immunoprecipitated mRNA pool. Our assay was able to document small molecule inhibition of eIF4E activity in cells ex vivo. The assay demonstrated a significant, reproducible decrease in mRNA binding following treatment with mTOR kinase inhibitor PP242, and will be useful in the evaluation of the eIF4E-interactome as well as assessing small molecule inhibitors of eIF4E-cap interaction.
Bien que le facteur de traduction eIF4E joue un rôle important dans le développement et la progression des cellules cancéreuses, le mécanisme avec lequel il y participe reste encore très méconnu. Afin d'aider à élucider ce rôle, nous avons développé une méthode d'immunoprécipitation vérifiant l'interaction entre eIF4E et les ARNm in vivo à partir de cellules NIH 3T3. Cette méthode permet l'isolement spécifique des ARNm qui sont liés à la protéine eIF4E exprimée de manière ectopique et qui contient une séquence 3X-FLAG. Le mutant eIF4E-W56A, qui empêche la liaison de la protéine au cap, le mutant G139D, qui bloque son interaction à eIF4G ou 4E-BP, ainsi qu'un double mutant ont été utilisés afin de valider la méthode. Notre méthode à permis de démontrer que l'ajout de composés bloquant l'interaction entre eIF4E et les ARNm induit une perte significative d'ARNm recouvré suite à la purification. Par contre, nous n'avons pas observé de pertes d'ARNm lorsque nous avons ajouté le compétiteur de la liaison au cap, le m7GTP, suite à la lyse cellulaire, indiquant que l'interaction potentielle entre eIF4E et les ARNm qui pourrait avoir lieu suite à la lyse est négligeable. De plus, nous avons démontré en utilisant notre méthode qu'une diminution reproductible dans la liaison d'eIF4E aux ARNm est détectée en utilisant l'inhibiteur de la kinase mTOR PP242. Cet inhibiteur, ainsi que les composés qui bloquent l'interaction entre eIF4E et les ARNm seront maintenant utilisés afin d'évaluer la totalité de l'interactome entre eIF4E et les ARNm cellulaires.
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Schmid, Oliver. "Untersuchungen zur Genotoxizität von Formaldehyd in vitro und in vivo." [S.l. : s.n.], 2009. http://nbn-resolving.de/urn:nbn:de:bsz:289-vts-66943.

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Herron, R. "The in vivo significance of erythrocyte autoantibodies assessed by in vitro methods." Thesis, University of Portsmouth, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.372840.

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Schuster, Sascha. "Ein GFP-basierter in vivo Assay für das Hochdurchsatz-Screening nach Hydrolaseaktivität." [S.l. : s.n.], 2005. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-24718.

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Broström, Oscar. "Development of a single-molecule tracking assay for the lac repressor in Escherichia coli." Thesis, Uppsala universitet, Institutionen för cell- och molekylärbiologi, 2019. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-388075.

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Gene regulation by transcription factors are one of the key processes that are important to sustain all kinds of life. In the prokaryote Escherichia coli this has shown to especially crucial. The operator sequence to which these transcription factors bind to are very small in comparison to the whole genome of E. coli, thus the question becomes how these proteins can find these sequences quickly. One particularly well-studied transcription factor in this regard is the lac repressor. It has been shown that this transcription factors finds its operators faster than the limit of three dimensional diffusion. The leading model for how the repressor does that is facilitated diffusion and this model has gained more experimental evidence, particularly using single-molecule fluorescence microscopy. This study aimed at measuring the unspecific binding time between the lac repressor and DNA in vivo, but in the end the project evolved to trying to establish a single-molecule tracking assay of the repressor in vivo. In this study a mutant of the repressor was expressed and purified, labelled with a synthetic fluorophore, electroporated into E. coli and tracking was performed under a microscope. One of the three types of experiments were partially analysed with an image analysis software. Unfortunately, analysis was not completed for all experiments which made it difficult to compare the results. In the end the data was compared by eye while also using the results from image analysis. With slight optimism it can be concluded that the assay worked, but it needs more development.
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Tashiro, Takahiro. "In vivo and ex vivo cetuximab sensitivity assay using three-dimensional primary culture system to stratify KRAS mutant colorectal cancer." Kyoto University, 2018. http://hdl.handle.net/2433/232473.

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Bourns, Brenda. "Development and characterization of a new assay to examine telomere-protein interactions in vivo /." Thesis, Connect to this title online; UW restricted, 1997. http://hdl.handle.net/1773/6336.

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Kim, Paula. "A novel TAFIa assay and its use to measure TAFI activation in vivo in primate models and the determination of the kinetics of TAFIa-catalyzed release of bound plasminogen from soluble fibrin degradation products." Thesis, Kingston, Ont. : [s.n.], 2007. http://hdl.handle.net/1974/863.

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Tsuda, Masataka. "In vivo evidence for translesion synthesis by the replicative DNA polymerase δ." Kyoto University, 2017. http://hdl.handle.net/2433/225985.

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Sklenak, Stefanie. "Pathomorphologic analysis and therapeutic in vivo assay on two murine models of uromodulin-associated kidney disease." Diss., Ludwig-Maximilians-Universität München, 2013. http://nbn-resolving.de/urn:nbn:de:bvb:19-165316.

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Books on the topic "In vivo assay"

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Grawe, Jan. Automating the in vivo micronucleus assay in the mouse: Flow-cytometric assessment of genetic damage induced by lowlevels of ionizing radiation and by chemicals with different induction mechanisms. Uppsala: Sveriges Lantbruksuniversitet, 1993.

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Test No. 489: In Vivo Mammalian Alkaline Comet Assay. OECD Publishing, 2014. http://dx.doi.org/10.1787/9789264224179-en.

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Test No. 489: In Vivo Mammalian Alkaline Comet Assay. OECD, 2016. http://dx.doi.org/10.1787/9789264264885-en.

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International Program on Chemical Safety., United Nations Environment Programme, International Labour Organisation, and World Health Organization, eds. Summary report on the evaluation of short-term tests for carcinogens: (collaborative study on in vivo tests). Geneva: World Health Organization, 1990.

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New Scoping Document on in vitro and ex vivo Assays for the Identification of Modulators of Thyroid Hormone Signalling. OECD, 2017. http://dx.doi.org/10.1787/9789264274716-en.

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John, Ashby, and International Program on Chemical Safety., eds. Evaluation of short-term tests for carcinogens: Report of the International Programme on Chemical Safety's collaborative study on in vivo assays. Cambridge [England]: Published by Cambridge University Press on behalf of the World Health Organization, 1988.

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John, Ashby, and International Programme on Chemical Safety., eds. Evaluation of short-term tests for carcinogens: Report of the International Programme on Chemical Safety's collaborative study on in vivo assays. Elsevier Science, 1985.

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Book chapters on the topic "In vivo assay"

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Liu, Lijing, Qingzhen Zhao, and Qi Xie. "In Vivo Ubiquitination Assay by Agroinfiltration." In Methods in Molecular Biology, 153–62. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-809-2_12.

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Akwii, Racheal G., Md S. Sajib, Fatema T. Zahra, Hanumantha R. Madala, Kalkunte S. Srivenugopal, and Constantinos M. Mikelis. "In Vivo Ear Sponge Lymphangiogenesis Assay." In Methods in Molecular Biology, 85–96. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0845-6_9.

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Kim, Hwan D., Ruei-Zeng Lin, and Juan M. Melero-Martin. "In Vivo Vascular Network Forming Assay." In Methods in Molecular Biology, 193–203. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0916-3_14.

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Okunishi, Hideki, Jocelyn Spragg, and James Burton. "In Vivo Assay of Specific Kallikrein Inhibitors." In Vasodepressor Hormones in Hypertension: Prostaglandins and Kallikrein-Kinins, 381–90. Basel: Birkhäuser Basel, 1987. http://dx.doi.org/10.1007/978-3-0348-9299-5_40.

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Hernandez, Lorena, Tatiana Smirnova, Jeffrey Wyckoff, John Condeelis, and Jeffrey E. Segall. "In Vivo Assay for Tumor Cell Invasion." In Methods in Molecular Biology, 227–38. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-198-1_15.

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Malinda, Katherine M. "In Vivo Matrigel Migration and Angiogenesis Assay." In Methods in Molecular Biology, 287–94. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-241-0_17.

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Costa, Carla, and João Paulo Teixeira. "The Comet Assay In Vivo in Humans." In Genotoxicity and DNA Repair, 219–39. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1068-7_13.

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Zhong, Sheng, Zhijuan Wang, and Li-Jia Qu. "Semi-In Vivo Assay for Pollen Tube Attraction." In Pollen and Pollen Tube Biology, 83–92. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0672-8_6.

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Basketter, David A. "Identification of Skin Allergens by In Vivo Assay." In Kanerva’s Occupational Dermatology, 1579–88. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-68617-2_105.

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Jain, Abhishek Kumar, and Alok Kumar Pandey. "In Vivo Micronucleus Assay in Mouse Bone Marrow." In Methods in Molecular Biology, 135–46. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9646-9_7.

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Conference papers on the topic "In vivo assay"

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ten Cate, H., Ch P. HENNY, A. Sturk, A. Prins, and J. W. ten Cate. "COMPARATIVE INVESTIGATION OF CLOTTING AND CHROMOGENIC ASSAYS FOR HEPARIN AND LOW MOLECULAR WEIGHT HEPARIN-(OID) IN PLASMA OF VOLUNTEERS AND PATIENTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644166.

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Two recently developed and simplified anti-Xa methods, a chromogenic assay and a clot-based assay (Heptest) were investigated on their accuracy and ex-vivo characteristics. The coefficients of variation (c.v.) for heparin, a heparin fragment (K 2165) and a LMW hepa-rinoid (Org 10172) were respectively: Heptest, within assay c.v.: 5.4; 4.5; 5.0 % between-assay c.v.: 7.8; 5.8; 9.5 %. Chromogenic Anti-Xa assay, within assay c.v.: 3.7; 5.6; 4.6 %, between assay c.v.: 6.6; 8.2; 12.1 %. In plasma samples obtained from volunteers and patients who participated in clinical studies using heparin, K 2165 and Org 10172, the ex-vivo correlation between both assays were determined. Generally, heparin and K 2165 induced anti-Xa activities correlated very well (0.83 < r< 0.99) and the slopes of the regression lines approached the value of 1. K 2165 in haemodial-ysis patients produced much higher Heptest values compared to the chromogenic anti-Xa assay, for which no explanation is provided. For Org 10172 the anti-Xa assay was more sensitive than the Heptest, although both tests detected anti-Xa activities at very low levels (± 0.02 U/ml). After s.c. injection of Org 10172 a poor correlation was found (r=0.49), which may be due to inter-individual differences in bio-availability. In conclusion, the chromogenic anti-Xa assay and the Heptest are accurate and sensitive assays. However, the tests give substantial differences in results depending upon the heparin preparation and patient category treated.
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Nair, Praveen, Dileep Nair, Kaede Hinata, Cyrus Mirsaidi, Junjie Wu, Yong Hu, and Brett M. Hall. "Abstract 5767: Ex vivo three-dimensional tumor growth assay: 3DX-TGA." 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.am2017-5767.

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Buhr, CR, N. Wiesmann, A. Watermann, M. Klünker, W. Tremel, and J. Brieger. "The Chorioallantoic Membrane Assay (CAM-Assay) as an in vivo model analysing the remaining of therapeutically applied nanoparticles." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1685971.

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Buhr, CR, N. Wiesmann, A. Watermann, M. Klünker, W. Tremel, and J. Brieger. "Der Chorion-Allantois-Membran-Assay (CAM-Assay) als in vivo-Modell zur Analyse des Verbleibs applizierter therapeutisch nutzbarer Nanopartikel." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1685831.

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DSouza, Alisha V., Brendan P. Flynn, Jason R. Gunn, Kimberley S. Samkoe, Sanjay Anand, Edward V. Maytin, Tayyaba Hasan, and Brian W. Pogue. "ALA-PpIX variability quantitatively imaged in A431 epidermoid tumors using in vivo ultrasound fluorescence tomography and ex vivo assay." In SPIE BiOS, edited by David H. Kessel and Tayyaba Hasan. SPIE, 2014. http://dx.doi.org/10.1117/12.2037800.

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Giddings, J. C. "AN IMMUNORADIOMETRIC ASSAY (IRMA) FOR HUMANTHROMBOMODULIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643963.

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Thrombomodulin was separated from detergent-soluble fractions of human placenta using a combination of DEAE-Sepharose and thrombin-Sepharose chromatography. The final product demonstrated one major band (Mr approximately 100000) and three minor bands (Mr 40000 - 80000) on SDS-polyacrylamide gel electrophoresis. The purified protein markedly enhanced the rate of activation of human protein C by thrombin in the presence of calcium ions. Polyclonal antibodies to the isolated thrombomodulin were raised in rabbits and were shown to inhibit thrombin co-factor activity. Immunofluorescence of fibroblasts and of human umbilical vein endothelial cells in culture demonstrated that thrombomodulin antigen was specifically located in endothelial cell membranes. Affinity purified antibody was labelled with 125I and was used to establish an immunoradiometric assay (IRMA). The method was sensitive to approximately 10.0μg purified thrombomodulin per litre. The concentration of thrombomodulin in detergent-solubilised endothelial cells obtained at intervals during primary culture was proportional to the number of cells harvested for assay and appeared to reflect cell growth. Confluent cells from four experiments (approximately 2 × 106 cells per culture dish) contained on average 8.4ng thrombomodulin. Incubation of confluent endothelial cells with medium containing 1 unit per ml human α-thrombin for 10 mins at 37°C reduced the amount of cellular thrombomodulin detected in this assay by up to 30%. Assays of human plasma confirmed that low levels of thrombomodulin are present in normal circulating blood. A mean level of 160μg per litre was detected in 20 normal donors. The levels of thrombomodulin antigen in 10 normal serum were not significantly different from those in the corresponding normal plasma. Preliminary results illustrated that increased levels of thrombomodulin might be found in the plasma of some patients with a variety of clinical disorders. The data suggest that quantitative assays of thrombomodulin might provide a useful index of endothelial disturbances in vivo.
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Smith, Mark E., and Yan Chen. "Thrombogenicity Testing Results for Control Legally Marketed Comparator Devices (LMCD): Comparison Between Traditional Non-Anticoagulated Venous Implant (NAVI) Assay and an In Vitro Ovine Blood Loop Test." In 2020 Design of Medical Devices Conference. American Society of Mechanical Engineers, 2020. http://dx.doi.org/10.1115/dmd2020-9073.

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Abstract Legally marketed comparator devices (LMCD) are required by many regulatory bodies in as a control for thrombogenicity testing when evaluating new devices. It is assumed by both the medical device manufacturing industry and regulatory bodies that these LMCD’s have good clinical history and should perform with no to minimal thrombus accumulation and thereby serve as valid negative controls for the assay. APS regularly performs these assays for many medical device manufacturers, all of whom select a predicate comparator device (required by FDA to be an LMCD), for both the in vivo Non-Anticoagulated Venous Implant (NAVI) assay as well as a custom in vitro blood loop AVI. In this retrospective analysis, we have compiled thrombogenicity scores of control/predicate devices (limited to assays which used LMCD’s), both the discrete score from the classification standard scoring scheme and the continuous values obtained from the percent surface area associated with thrombus. We have compared results from 37 NAVI studies and 22 in vitro blood loop studies. These compiled results show ∼25% of LMCDs score ≥ 3 (&gt; 50% of the surface covered in thrombus) in the NAVI model while &lt; 5% of LMCDs score ≥ 3 (&gt; 50% thrombus) in the Blood-Loop assay. In addition, the median score and mean % thrombus for LMCD in the blood loop assay is substantially lower than the median and mean scores for LMCD in the NAVI assay. This retrospective assessment highlights a high proportion of false-positive scores for LMCD in a large number of NAVI assays.
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Pogue, Brian W., Jonathan D. Pitts, Mary-Ann Mycek, Roger D. Sloboda, Carmen M. Wilmot, John F. Brandsema, and Julia A. O'Hara. "Endogenous Fluorescence Monitoring In Vivo as an Assay for Cellular Damage in Photodynamic Therapy." In Biomedical Topical Meeting. Washington, D.C.: OSA, 2002. http://dx.doi.org/10.1364/bio.2002.wd6.

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Millard, Melissa, Kathryn M. Appleton, Ashley Elrod, Nicholas W. Bateman, Tamara Abulez, Kelly Conrads, Brian Hood, Thomas P. Conrads, Lillia M. Holmes, and Teresa M. DesRochers. "Abstract 6018: The perfused 3DKUBE™ rare tumor assay models in vivo drug response." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-6018.

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Topman, Gil, Orna Sharabani-Yosef, and Amit Gefen. "A Method for Quantitative Analysis of the Kinematics of Fibroblast Migration in a Monolayer Wound Model." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53070.

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A wound healing assay is simple but effective method to study cell migration in vitro. Cell migration in vitro was found to mimic migration in vivo to some extent [1,2]. In wound healing assays, a “wound” is created by either scraping or mechanically crushing cells in a monolayer, thereby forming a denuded area. Cells migrate into the denuded area to complete coverage, and thereby “heal” the wound. Micrographs at regular time intervals are captured during such experiments for analysis of the process of migration.
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Reports on the topic "In vivo assay"

1

Carlson, George A., and Leroy E. Hood. Early Host Responses to Prion Infection: Development of In Vivo and In Vitro Assays. Fort Belvoir, VA: Defense Technical Information Center, May 2005. http://dx.doi.org/10.21236/ada446923.

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Carlson, George A., and Leroy E. Hood. Early Host Responses to Prion Infection: Development of In Vivo and In Vitro Assays. Fort Belvoir, VA: Defense Technical Information Center, May 2006. http://dx.doi.org/10.21236/ada456572.

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3

Prochownik, Edward V. Development of Rapid In Vitro and In Vivo Assays to Detect and Quantify MYC Network Protein Associations. Fort Belvoir, VA: Defense Technical Information Center, January 2002. http://dx.doi.org/10.21236/ada405251.

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4

Prochownick, Edward V. Development of Rapid in Vitro and In Vivo Assays to Detect and Quantify MYC Network Protein Associations. Fort Belvoir, VA: Defense Technical Information Center, January 2001. http://dx.doi.org/10.21236/ada393274.

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