Thematische Bibliographien / Affinity labeling

Inhaltsverzeichnis

  1. Zeitschriftenartikel
  2. Dissertationen
  3. Bücher
  4. Buchteile
  5. Konferenzberichte
  6. Berichte der Organisationen

Auswahl der wissenschaftlichen Literatur zum Thema „Affinity labeling“

Autor: Grafiati
Veröffentlicht am 4. Juni 2021
Zuletzt aktualisiert am 25. Februar 2023

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Zeitschriftenartikel zum Thema "Affinity labeling"

1

Ji, Tae H., and Inhae Ji. "Macromolecular affinity labeling." In Vitro Cellular & Developmental Biology 25, no. 8 (August 1989): 676–78. http://dx.doi.org/10.1007/bf02623719.

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Martini, C., and A. Lucacchini. "Affinity Labeling of Adenosine A1Binding Sites." Journal of Neurochemistry 49, no. 3 (September 1987): 681–84. http://dx.doi.org/10.1111/j.1471-4159.1987.tb00947.x.

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SWEET, FREDERICK, and GARY L. MURDOCK. "Affinity Labeling of Hormone-Specific Proteins*." Endocrine Reviews 8, no. 2 (May 1987): 154–84. http://dx.doi.org/10.1210/edrv-8-2-154.

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Shi, Yi Qun, Setsuo Furuyoshi, Ivo Hubacek, and Robert R. Rando. "Affinity labeling of lecithin retinol acyltransferase." Biochemistry 32, no. 12 (March 1993): 3077–80. http://dx.doi.org/10.1021/bi00063a019.

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Li, Hong-yu, Ying Liu, Kan Fang, and Koji Nakanishi. "A simple photo-affinity labeling protocol." Chemical Communications, no. 4 (1999): 365–66. http://dx.doi.org/10.1039/a809507h.

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SYVERTSEN, Christian, and John S. McKINLEY-McKEE. "Affinity Labeling of Liver Alcohol Dehydrogenase." European Journal of Biochemistry 117, no. 1 (March 3, 2005): 165–70. http://dx.doi.org/10.1111/j.1432-1033.1981.tb06316.x.

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Vinkenborg, Jan L., Günter Mayer, and Michael Famulok. "Aptamer-Based Affinity Labeling of Proteins." Angewandte Chemie International Edition 51, no. 36 (August 2, 2012): 9176–80. http://dx.doi.org/10.1002/anie.201204174.

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Takaoka, Yousuke, Yuuki Nukadzuka, and Minoru Ueda. "Reactive group-embedded affinity labeling reagent for efficient intracellular protein labeling." Bioorganic & Medicinal Chemistry 25, no. 11 (June 2017): 2888–94. http://dx.doi.org/10.1016/j.bmc.2017.02.059.

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Nakanishi, Shuichi, Hiroyuki Tanaka, Kazuhito Hioki, Kohei Yamada, and Munetaka Kunishima. "Labeling study of avidin by modular method for affinity labeling (MoAL)." Bioorganic & Medicinal Chemistry Letters 20, no. 23 (December 2010): 7050–53. http://dx.doi.org/10.1016/j.bmcl.2010.09.109.

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Rivera-Monroy, Zuly, Guenther K. Bonn, and András Guttman. "Fluorescent isotope-coded affinity tag 2: Peptide labeling and affinity capture." ELECTROPHORESIS 30, no. 7 (April 2009): 1111–18. http://dx.doi.org/10.1002/elps.200800830.

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Dissertationen zum Thema "Affinity labeling"

1

Kuzmich, Oleksandra. "Metal Labeling for Low Affinity Binding Biomolecules." Doctoral thesis, Humboldt-Universität zu Berlin, 2018. http://dx.doi.org/10.18452/18862.

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Unter den Techniken der chemischen Proteomik hat Capture Compound – Massenspektrometrie (CCMS) den Vorteil, Interaktionen von Molekülen mit geringer Affinität zueinander effektiv untersuchen zu können. CCMS beruht auf kleinen molekularen Sonden (Capture Compounds, CCs), die aus drei funktionalen Bestandteilen bestehen: die Selektivitätsfunktion, ist ein kleines Molekül, das mit einem Zielprotein eine schwache Wechselwirkung eingeht. Die zweite Funktionalität erlaubt kovalente Anhaftung der molekularen Sonde an Proteine. Der dritte Anteil erlaubt Detektion mit sehr guten Sensitivität; allerding
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Attiya, Said. "Antibody labeling methods for automated affinity electrophoresis on microchips." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0010/NQ59926.pdf.

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Seebregts, Christopher J. "Photoaffinity labeling the nucleotide sites of the sarcoplasmic reticulum Ca²⁺-ATPase." Doctoral thesis, University of Cape Town, 1989. http://hdl.handle.net/11427/27167.

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We have synthesized a new class of photoaffinity analogs, 2',3'-O-(2,4,6-trinitrophenyl)-8-azido-ATP, -ADP and -AMP (TNP- 8N₃ATP, -ADP and -AMP), and their radiolabeled derivatives, and characterized their interaction with the sarcoplasmic reticulum Ca²⁺-ATPase. The TNP-8N₃-nucleotides were synthesized from ATP in three steps involving bromination in the 8-position of the adenine ring followed by displacement with an azido group and then trinitrophenylation of the resulting 8N₃-nucleotide with TNBS. Inclusion of the oxidizing agent, DTNB, in the final reaction was found to be necessary to prev
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Perols, Anna. "Site-specific labeling of affinity molecules for in vitro and in vivo studies." Doctoral thesis, KTH, Proteinteknologi, 2014. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-152349.

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The thesis is focused on site-specific labeling of affinity molecules for different applications where two types of binding proteins, Affibody molecules and antibodies, have been used. For the purpose of improving the properties of Affibody molecules for in vivo imaging, novel bi-functional chelators for radiolabeling using the radionuclide 111In were evaluated. In a first study, two chelators denoted NOTA and DOTA, respectively, were separately conjugated via maleimide chemistry to a C-terminal cysteine residue in a HER2-binding Affibody molecule (ZHER2:2395). In vivo evaluation using mice wi
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Lui, James Kwok Ching. "A fluorescent labelling technique to detect changes in the thiol redox state of proteins following mild oxidative stress." University of Western Australia. School of Biomedical, Biomolecular and Chemical Sciences, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0056.

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There is increasing evidence that hydrogen peroxide (H2O2) can act as a signalling molecule capable of modulating a variety of biochemical and genetic systems. Using Jurkat T-lymphocytes, this study initially investigated the involvement of H2O2 in the activation of a specific signalling protein extracellular signal-regulated protein kinase (ERK). It was found that as a result of H2O2 treatment, mitochondrial complex activities decreased which led to subsequent increase of mitochondrial reactive oxygen species (ROS) production. The increase of ROS resulted in higher cellular H2O2 as well as i
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Tran, Hang T. "Photocleavable Linker for Protein Affinity Labeling to Identify the Binding Target of KCN-1." Digital Archive @ GSU, 2010. http://digitalarchive.gsu.edu/chemistry_theses/35.

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KCN-1 is known to reduce tumor growth 6-fold in mice implanted with LN229 glioma cells. Although this inhibitor is effective, the mechanism of action for KCN-1 is not well understood. Based on preliminary studies, KCN-1 reduces tumor growth by disrupting the HIF 1 (hypoxia-induced factor-1) pathway. The binding target of KCN-1 needs to be investigated in order to develop KCN-1 or its analogs for therapeutic applications. In this research, a molecule was designed and synthesized for the identification of the binding target of KCN-1. Specifically, this molecule contains the inhibitor (KCN-1
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Song, Zhi-Ning. "Development of novel affinity-guided catalysts for specific labeling of endogenous proteins in living systems." Kyoto University, 2017. http://hdl.handle.net/2433/228238.

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Kuzmich, Oleksandra [Verfasser], Michael [Gutachter] Linscheid, Hubert [Gutachter] Köster, and Michael [Gutachter] Weller. "Metal Labeling for Low Affinity Binding Biomolecules / Oleksandra Kuzmich ; Gutachter: Michael Linscheid, Hubert Köster, Michael Weller." Berlin : Humboldt-Universität zu Berlin, 2018. http://d-nb.info/1185579265/34.

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Bagchi, Pritha. "Expanding the metallomics toolbox: Development of chemical and biological methods in understanding copper biochemistry." Diss., Georgia Institute of Technology, 2013. http://hdl.handle.net/1853/52160.

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Copper is an essential trace element and required for various biological processes, but free copper is toxic. Therefore, copper is tightly regulated in living cells and disruptions in this homeostatic machinery are implicated in numerous diseases. The current understanding of copper homeostasis is substantial but incomplete, particularly in regard to storage and exchange at the subcellular level. Intracellular copper is primarily present in the monovalent oxidation state. Therefore, copper(I) selective fluorescent probes can be utilized for imaging exchangeable copper ions in live cells, but t
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Barnett, Derek W. "PART 1. SYNTHESIS OF STABLE-ISOTOPE LABELED AMINO ACIDS PART 2. SYNTHESIS OF MECHANISTIC PROBES OF RETINOID ACTION." The Ohio State University, 2002. http://rave.ohiolink.edu/etdc/view?acc_num=osu1038951598.

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Bücher zum Thema "Affinity labeling"

1

Viktorovich, Vlasov Valentin, ed. Affinity modification of biopolymers. Boca Raton, Fla: CRC Press, 1989.

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H, Gronemeyer, ed. Affinity labelling and cloning of steroid and thyroid hormone receptors. Weinheim, Federal Republic of Germany: VCH, 1988.

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Protein affinity tags: Methods and protocols. New York: Humana Press, 2014.

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1940-, Creighton Thomas E., ed. Protein function: A practical approach. Oxford: IRL Press, 1989.

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Lajambe, Roxanne. Affinity labelling of functionally active caspases in Sp2/0-Ag14 cells during l-glutamine deprivation. Sudbury, Ont: Laurentian University, 2004.

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1949-, Müller S. C., ed. Synthetic peptides as antigens. Amsterdam: Elsevier, 1999.

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1962-, Meier T., and Fahrenholz F, eds. A laboratory guide to biotin-labeling in biomolecule analysis. Basel: Birkhäuser Verlag, 1996.

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Maeda, Dean Yoshimasa. Synthesis and evaluation of affinity labels based on peptide antagonists for delta opioid receptors. 1997.

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Leelasvatanakij, Leena. Synthetic strategies for the preparation of affinity label dynorphin A(1-11)NH₂ analogues. 1996.

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Warth, Rainer K. Large subunit of vaccinia cirus ribonucleotide reductase: Affinity chromatography-based purification and photoaffinity labeling. 1993.

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Buchteile zum Thema "Affinity labeling"

1

Patchornik, A., K. Jacobson, and M. P. Strub. "Photo Reversible Affinity Labeling." In Design and Synthesis of Organic Molecules Based on Molecular Recognition, 235–41. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70926-5_20.

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Tamura, Tomonori, and Itaru Hamachi. "Labeling Proteins by Affinity-Guided DMAP Chemistry." In Site-Specific Protein Labeling, 229–42. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2272-7_16.

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Landgraf, Peter, Elmer R. Antileo, Erin M. Schuman, and Daniela C. Dieterich. "BONCAT: Metabolic Labeling, Click Chemistry, and Affinity Purification of Newly Synthesized Proteomes." In Site-Specific Protein Labeling, 199–215. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2272-7_14.

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Miziorko, Henry M., and Christine A. Brodt. "Affinity Labeling of Phosphoribulokinase by Adenosine Polyphosphopyridoxals." In Current Research in Photosynthesis, 2881–84. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_651.

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Hughes, David A. "Applications of Affinity Labeling in Biomedical Sciences." In Immunocytochemistry and In Situ Hybridization in the Biomedical Sciences, 223–53. Boston, MA: Birkhäuser Boston, 2001. http://dx.doi.org/10.1007/978-1-4612-0139-7_11.

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Fabry, M., and D. Brandenburg. "Photoreactive Biotinylated Peptide Ligands for Affinity Labeling." In A Laboratory Guide to Biotin-Labeling in Biomolecule Analysis, 65–81. Basel: Birkhäuser Basel, 1996. http://dx.doi.org/10.1007/978-3-0348-7349-9_4.

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Kodama, Hiroaki, Teruo Yasunaga, Michio Kondo, Rei Matsueda, and Yasuyuki Shimohigashi. "Discriminative affinity labeling of δ- and μ-opioid receptors." In Peptides 1990, 635–36. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_263.

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Thiele, Christoph, and Falk Fahrenholz. "Synthesis of Photocleavable Biotinylated Ligands and Application for Affinity Chromatography." In A Laboratory Guide to Biotin-Labeling in Biomolecule Analysis, 31–44. Basel: Birkhäuser Basel, 1996. http://dx.doi.org/10.1007/978-3-0348-7349-9_2.

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Colman, Roberta F. "Affinity Labeling of Nucleotide Binding Sites of Enzymes and Platelets." In Advances in Experimental Medicine and Biology, 257–63. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3806-6_26.

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Donner, David B., Kazuyo Yamada, Kenneth E. Lipson, and Andrea Dorato. "Structural Studies of the Growth Hormone Receptor by Affinity Labeling." In Human Growth Hormone, 463–73. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7201-5_37.

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Konferenzberichte zum Thema "Affinity labeling"

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Das, Nilaksh, Sanya Chaba, Renzhi Wu, Sakshi Gandhi, Duen Horng Chau, and Xu Chu. "GOGGLES: Automatic Image Labeling with Affinity Coding." In SIGMOD/PODS '20: International Conference on Management of Data. New York, NY, USA: ACM, 2020. http://dx.doi.org/10.1145/3318464.3380592.

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Surber, Bruce, Shomir Ghosh, Anne-Laure Grillot, Jyoti Patel, Charlotte Woodall, Yuanwei Chen, Lin Yi, Irini Zanze, and Ye Yao. "Uniform Tritium Labeling of Combinatorial Libraries for Affinity Selection Screening." In Proceedings of the 3rd International Conference on Isotopes. WORLD SCIENTIFIC, 2000. http://dx.doi.org/10.1142/9789812793867_0109.

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Jefferson, J. R., J. T. Harmon, and G. A. Jamieson. "ADP-BINDING SITES IN PLATELETS: CHARACTERIZATION BY PHOTOAFFINITY LABELING AND BINDING STUDIES WITH FIXED PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644463.

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Attempts to photoaffinity label platelet ADP receptors with 2-azidoADP have not been successful possibly due to the absence of a spacer arm between the nucleotide and the photolabile group. We have synthesized a probe having a long spacer arm by coupling 2-(3-aminopropylthio)-ADP to succinimidyl 4-3H-azidobenzoate. Labeling competable by ADP could not demonstrated with intact platelets. With isolated platelet membranes, three bands (Mr 140,000, 110,000 and 46,000) were labeled that were not competed by ADP while three other bands (Mr 188,000, 92,000 and 51,000) were competable by 100 uM ADP.An
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Bandi, Adithya, Karuna Joshi, and Varish Mulwad. "Affinity Propagation Initialisation Based Proximity Clustering For Labeling in Natural Language Based Big Data Systems." In 2020 IEEE 6th Intl Conference on Big Data Security on Cloud (BigDataSecurity), IEEE Intl Conference on High Performance and Smart Computing, (HPSC) and IEEE Intl Conference on Intelligent Data and Security (IDS). IEEE, 2020. http://dx.doi.org/10.1109/bigdatasecurity-hpsc-ids49724.2020.00012.

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Chir, Jiunly, Steven Withers, Chin-Feng Wan, and Yaw-Kuen Li. "IDENTIFICATION OF THE ESSENTIAL GROUPS OF A FAMILY 3 BETA-GLUCOSIDASE BY AFFINITY LABELING AND TANDEM MASS SPECTROMETRIC ANALYSIS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.746.

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Hannan, Tanveer, Rajat Koner, Jonathan Kobold, and Matthias Schubert. "Box Supervised Video Segmentation Proposal Network." In 24th Irish Machine Vision and Image Processing Conference. Irish Pattern Recognition and Classification Society, 2022. http://dx.doi.org/10.56541/azwk8552.

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Bounding box supervision provides a balanced compromise between labeling effort and result quality for image segmentation. However, there exists no such work explicitly tailored for videos. Applying the image segmentation methods directly to videos produces sub-optimal solutions because they do not exploit the temporal information. In this work, we propose a box-supervised video segmentation proposal network. We take advantage of intrinsic video properties by introducing a novel box-guided motion calculation pipeline and a motion-aware affinity loss. As the motion is utilized only during train
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Kirby, Edward P., Mary Ann Mascelli, Carol Silverman, and Daniel W. Karl. "LOCALIZATION OF THE PLATELET-BINDING AND HEPARIN-BINDING DOMAINS OF BOVINE VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644097.

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Bovine von Willebrand Factor (vWF) binds directly to human platelets and also to heparin-agarose. Cleavage of vWF with Protease I, a metalloenzyme isolated from the venom of the western diamondback rattlesnake, produces two major fragments with apparent Mr of 250 kD and 200 kD. The 200 kD fragment competes with native vWF for binding to the GPIb-associated vWF receptor on formalin-fixed human platelets and has weak platelet-agglutinating activity. It is composed of three polypeptide chains of apparent Mr of 97 kD, 61 kD, and 35 kD. Monoclonal antibodies #2 and H-9, which inhibit binding of vWF
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Apap-Bologna, Angela, Ailsa Webster, Fiona Raitt, and Graham Kemp. "THE DYNAMIC STRUCTURE OF FIBRINOGEN PROBED BY SURFACE LABELLING AND CHEMICAL CROSS-LINKING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642886.

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There is much controversy regarding the conformation of fibrinogen. Several models have been proposed ranging from an almost linear trinodular arrangement to a globular conformation. Consequently, it has been suggested that fibrinogen has a flexible structure where the actual conformation is influenced by its environment - one major factor being calcium concentration. Although the importance of tightly bound calcium ions (Kd ∼ luM) to fibrinogen structure is well established, the role of the larger number of low affinity sites (Kd∼lmM) is still a matter of debate.We have utilised the technique
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Kruithof, E. KO, W. D. Schleuning, and F. Bachman. "PLASMINOGEN ACTIVATOR INHIBITOR BIOCHEMICAL AND CLINICAL ASPECTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644764.

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Plasminogen activator (PAs) are enzymes that convert the zymogen plasminogen into the trypsin-like protease plasmin, which degrades extracellular matrix proteins and fibrin in the course of fibrinolysis, embryogenesis, tissue remodeling and in tumor metastasis. Plasminogen activator inhibitors (PAIs) are important modulators of PA activity. Several proteins have been identified which inhibit at fast rates urokinase (u-PA) and tissue-type PA (t-PA). In the order of inhibition rate constants these are: a) PAI-1, present in human plasma and platelet extracts and purified from human endothelial ce
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Taki, M., K. Sato, Y. Ikeda, M. Yamamoto, and K. Watanabe. "THE FUNCTIONAL DOMAIN OF PLATELET MEMBRANE GLYCOPROTEIN lb FOR VON WILLEBRAND FACTOR AND THROMBIN-BINDING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643512.

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In this paper, we have examined the functional domain of platelet membrane glycoprotein lb (GPIb) by using elastase and a monoclonal antibody against GPIb which specific inhibits both von Willebrand factor (vWF) and thrombin interaction with platelets. Elastase was purified from human granulocytes by using affinity column chromatography according to the method of Okada et al.. A monoclonal antibody against platelet membrane GPIb (56-2) which inhibits both vWF and thrombin-binding to platelets was used for this study. Platelet surface glycoproteins were labelled with 3H by the method of Nurden
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Berichte der Organisationen zum Thema "Affinity labeling"

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Yang, KyoungLang, and Gunda I. Georg. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Fort Belvoir, VA: Defense Technical Information Center, May 2005. http://dx.doi.org/10.21236/ada443679.

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Yang, Kyounglang, and AGunda I. Georg. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada432471.

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Ramadas, Vidya. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Fort Belvoir, VA: Defense Technical Information Center, May 2003. http://dx.doi.org/10.21236/ada416994.

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Yang, KyoungLang, and Gunda I. Georg. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Fort Belvoir, VA: Defense Technical Information Center, May 2006. http://dx.doi.org/10.21236/ada474734.

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Pines, Mark, Arieh Bar, David A. Carrino, Arnold I. Caplan, and James A. Dennis. Extracellular Matrix Molecules of the Eggshell as Related to Eggshell Quality. United States Department of Agriculture, 1997. http://dx.doi.org/10.32747/1997.7575270.bard.

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The extracellular matrix of the mineralizing eggshell contains molecules hypothesized to be regulators biomineralization. To study eggshell matrix molecules, a bank of monoclonal antibodies was generated that bound demineralized eggshell matrix or localized to oviduct epithelium. Immunofluorescence staining revealed several staining patterns for antibodies that recognized secretory cells: staining for a majority of columnar lining cells, staining for a minor sub-set of columnar lining cells, intensified staining within epithelial crypts, and staining of the entire tubular gland. Western blotti
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Wisniewski, Michael, Samir Droby, John Norelli, Dov Prusky, and Vera Hershkovitz. Genetic and transcriptomic analysis of postharvest decay resistance in Malus sieversii and the identification of pathogenicity effectors in Penicillium expansum. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7597928.bard.

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Use of Lqh2 mutants (produced at TAU) and rNav1.2a mutants (produced at the US side) for identifying receptor site-3: Based on the fact that binding of scorpion alpha-toxins is voltage-dependent, which suggests toxin binding at the mobile voltage-sensing region, we analyzed which of the toxin bioactive domains (Core-domain or NC-domain) interacts with the DIV Gating-module of rNav1.2a. This analysis was based on the assumption that the dissociation of toxin mutants upon depolarization would vary from that of the unmodified toxin should the substitutions affect a site of interaction with the ch
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Shomer, Ilan, Louise Wicker, Uzi Merin, and William L. Kerr. Interactions of Cloud Proteins, Pectins and Pectinesterases in Flocculation of Citrus Cloud. United States Department of Agriculture, February 2002. http://dx.doi.org/10.32747/2002.7580669.bard.

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The overall objective was to understand the cloud flocculation of citrus juice by characterization of the interactions between proteins and pectins, and to determine the role of PE isozymes in catalyzing this phenomenon. Specific objectives were to: 1. identify/characterize cloud-proteins in relation to their coagulable properties and affinity to pectins; 2. to determine structural changes of PME and other proteins induced by cation/pectin interactions; 3. localize cloud proteins, PME and bound protein/pectates in unheated and pasteurized juices; 4. to create "sensitized" pectins and determine
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