Relevant bibliographies by topics / Binding kinetics

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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 'Binding kinetics'

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

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Journal articles on the topic "Binding kinetics"

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Bernetti, Mattia, Matteo Masetti, Walter Rocchia, and Andrea Cavalli. "Kinetics of Drug Binding and Residence Time." Annual Review of Physical Chemistry 70, no. 1 (June 14, 2019): 143–71. http://dx.doi.org/10.1146/annurev-physchem-042018-052340.

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The kinetics of drug binding and unbinding is assuming an increasingly crucial role in the long, costly process of bringing a new medicine to patients. For example, the time a drug spends in contact with its biological target is known as residence time (the inverse of the kinetic constant of the drug-target unbinding, 1/ koff). Recent reports suggest that residence time could predict drug efficacy in vivo, perhaps even more effectively than conventional thermodynamic parameters (free energy, enthalpy, entropy). There are many experimental and computational methods for predicting drug-target residence time at an early stage of drug discovery programs. Here, we review and discuss the methodological approaches to estimating drug binding kinetics and residence time. We first introduce the theoretical background of drug binding kinetics from a physicochemical standpoint. We then analyze the recent literature in the field, starting from the experimental methodologies and applications thereof and moving to theoretical and computational approaches to the kinetics of drug binding and unbinding. We acknowledge the central role of molecular dynamics and related methods, which comprise a great number of the computational methods and applications reviewed here. However, we also consider kinetic Monte Carlo. We conclude with the outlook that drug (un)binding kinetics may soon become a go/no go step in the discovery and development of new medicines.
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Borisov, D. V., and A. V. Veselovsky. "Ligand-receptor binding kinetics in drug design." Biomeditsinskaya Khimiya 66, no. 1 (January 2020): 42–53. http://dx.doi.org/10.18097/pbmc20206601042.

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Traditionally, the thermodynamic values of affinity are considered as the main criterion for the development of new drugs. Usually, these values for drugs are measured in vitro at steady concentrations of the receptor and ligand, which are differed from in vivo environment. Recent studies have shown that the kinetics of the process of drug binding to its receptor make significant contribution in the drug effectiveness. This has increased attention in characterizing and predicting the rate constants of association and dissociation of the receptor ligand at the stage of preclinical studies of drug candidates. A drug with a long residence time can determine ligand-receptor selectivity (kinetic selectivity), maintain pharmacological activity of the drug at its low concentration in vivo. The paper discusses the theoretical basis of protein-ligand binding, molecular determinants that control the kinetics of the drug-receptor binding. Understanding the molecular features underlying the kinetics of receptor-ligand binding will contribute to the rational design of drugs with desired properties.
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Kiger, Laurent, Julien Uzan, Sylvia Dewilde, Thorsten Burmester, Thomas Hankeln, Luc Moens, Djemel Hamdane, Veronique Baudin-Creuza, and Michael Marden. "Neuroglobin Ligand Binding Kinetics." IUBMB Life 56, no. 11 (November 2004): 709–19. http://dx.doi.org/10.1080/15216540500037711.

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Singh, Arunima. "RNA-binding protein kinetics." Nature Methods 18, no. 4 (April 2021): 335. http://dx.doi.org/10.1038/s41592-021-01122-6.

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Ferruz, Noelia, and Gianni De Fabritiis. "Binding Kinetics in Drug Discovery." Molecular Informatics 35, no. 6-7 (May 27, 2016): 216–26. http://dx.doi.org/10.1002/minf.201501018.

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Hall, Denver G. "Relaxation kinetics of ion binding." Journal of the Chemical Society, Faraday Transactions 86, no. 4 (1990): 639. http://dx.doi.org/10.1039/ft9908600639.

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Gushimana, Y., B. Doepner, E. Martinez-Hackert, and G. Ilgenfritz. "Kinetics of quinine-deuterohemin binding." Biophysical Chemistry 47, no. 2 (August 1993): 153–62. http://dx.doi.org/10.1016/0301-4622(93)85033-e.

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Barril, Xavier, and Helena Danielsson. "Binding kinetics in drug discovery." Drug Discovery Today: Technologies 17 (October 2015): 35–36. http://dx.doi.org/10.1016/j.ddtec.2015.10.011.

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McNeely, Patrick M., Andrea N. Naranjo, Kimberly Forsten-Williams, and Anne Skaja Robinson. "A2AR Binding Kinetics in the Ligand Depletion Regime." SLAS DISCOVERY: Advancing the Science of Drug Discovery 22, no. 2 (September 27, 2016): 166–75. http://dx.doi.org/10.1177/1087057116667256.

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Ligand binding plays a fundamental role in stimulating the downstream signaling of membrane receptors. Here, ligand-binding kinetics of the full-length human adenosine A2A receptor (A2AR) reconstituted in detergent micelles were measured using a fluorescently labeled ligand via fluorescence anisotropy. Importantly, to optimize the signal-to-noise ratio, these experiments were conducted in the ligand depletion regime. In the ligand depletion regime, the assumptions used to determine analytical solutions for one-site binding models for either one or two ligands in competition are no longer valid. We therefore implemented a numerical solution approach to analyze kinetic binding data as experimental conditions approach the ligand depletion regime. By comparing the results from the numerical and the analytical solutions, we highlight the ligand-receptor ratios at which the analytical solution begins to lose predictive accuracy. Using the numerical solution approach, we determined the kinetic rate constants of the fluorescent ligand, FITC-APEC, and those for three unlabeled ligands using competitive association experiments. The association and dissociation rate constants of the unlabeled ligands determined from the competitive association experiments were then independently validated using competitive dissociation data. Based on this study, a numerical solution is recommended to determine kinetic ligand-binding parameters for experiments conducted in the ligand-depletion regime.
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Rundell, K. W., P. C. Tullson, and R. L. Terjung. "Altered kinetics of AMP deaminase by myosin binding." American Journal of Physiology-Cell Physiology 263, no. 2 (August 1, 1992): C294—C299. http://dx.doi.org/10.1152/ajpcell.1992.263.2.c294.

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AMP deaminase catalyzes the deamination of AMP to inosine 5'-monophosphate (IMP) and ammonia. Factors controlling the enzyme in muscle can rapidly promote high rates of IMP formation when ATP utilization exceeds supply. We evaluated whether binding of AMP deaminase to myosin, which occurs during intense contraction conditions, alters the kinetic behavior of the enzyme. Reaction kinetics of myosin-bound and free AMP deaminase were evaluated. Reaction kinetics of the free enzyme yielded a near-linear double-reciprocal plot with an expected Km of approximately 1 mM AMP concentration (AMP). In contrast, reaction kinetics of AMP deaminase became bimodal when bound to myosin. At [AMP] less than 0.15 mM, a high-affinity Km (0.05-0.10 mM) with maximal velocity approximately 20% that of free enzyme was evident. At [AMP] greater than 0.15 mM, the Km and maximal velocity values were similar to that of the free enzyme. The 10- to 20-fold higher affinity Km would allow for a higher rate of AMP deamination at the low [AMP] found physiologically. AMP deaminase binding to myosin also induced a marked resistance to orthophosphate inhibition (10 mM) in the presence of 50 microM ADP. Results were similar for purified preparations of AMP deaminase bound to myosin subfragment 2 and crude extracts obtained from contracting muscle. Our results add further support to the hypothesis that AMP deaminase binding to myosin serves an important role in control of enzyme activity in contracting muscle.
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Dissertations / Theses on the topic "Binding kinetics"

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Talbert, Ann Marie. "Drug protein binding kinetics from chromatographic profiles." Thesis, Imperial College London, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.406921.

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Fisher, Joshua. "In Vitro Binding Kinetics of ChemoFilter with Cisplatin." Thesis, University of California, San Francisco, 2016. http://pqdtopen.proquest.com/#viewpdf?dispub=10165379.

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Introduction: Endovascular chemotherapy treatment allows localized delivery adjacent to the target tumor; allowing an increased dosage and decreased leakage to other areas. It also allows for the opportunity to filter chemotherapy escaping the target tumor and entering the bloodstream. The ChemoFilter - a temporarily deployable, endovascular device will do just that; reducing systemic toxicity thus reducing adverse side effects from chemotherapy treatment. This will allow further increased dosage, increased tumor suppression, and increased tolerance to treatment. ChemoFilter has successfully filtered the chemotherapeutic Doxorubicin, but had yet to be tested in other chemotherapeutics. This study evaluates binding with new chemotherapeutics: Cisplatin, Carboplatin, and a cocktail comprised of Cisplatin and Doxorubicin.

Materials and Methods: ChemoFilter prototypes based on: 1.) Genomic DNA and 2.) Dowex (ion-exchange) resin, were evaluated for their ability to bind chemotherapy in vitro in phosphate-buffered saline (PBS). ChemoFilter was tested free in solution and encapsulated in nylon or polyester mesh packets of various dimensions. Concentrations were quantified using inductively coupled plasma mass spectrometry (IPC-MS), ultraviolet-visible spectrophotometry (UV-Vis), or fluorospectrometry. 11C, 13C, and/or 14C radiolabeling Carboplatin began for in vitro and in vivo ChemoFilter quantification. In vitro quantification can include scintillation and/or gamma counting. In vivo may include Positron Emission Tomography (PET) imaging, Hyperpolarized 13C Magnetic Resonance Imaging (MRI), and/or Magnetic Resonance Spectroscopy (MRS) for real-time visualization. Reactions were verified using High Performance Liquid Chromatography (HPLC) for chemical species identification.

Results and Discussion: Results indicate significant and nearly complete, ~99% (p<0.01) clearance of Cisplatin using the DNA ChemoFilter sequestered in Nylon mesh, quantified with gold standard ICP-MS (evidenced at 214 and 265 nm). The Ion-exchange ChemoFilter has significant clearance, within seconds, of both Doxorubicin and Cisplatin mixed in a cocktail solution. However, it appears some Cisplatin is binding to the Nylon Mesh itself. Size, shape, and material of the mesh have been optimized. A potential mechanism for 11C, 13C, or 14C radiolabeling of Carboplatin has been developed and early results have been successful. ChemoFilter works much more efficiently when sequestered in nylon packets of specific geometries. Significant improvements have been made to ChemoFilter, moving the device closer to clinical trials.

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Goold, Richard David. "The glutathione S-transferases : kinetics, binding and inhibition." Doctoral thesis, University of Cape Town, 1989. http://hdl.handle.net/11427/27175.

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The glutathione S-transferases are a group of enzymes which catalyse the conjugation of reduced glutathione with a variety of electrophilic molecules, and they are therefore thought to play a major role in drug biotransformation and the detoxification of xenobiotics. The cytosolic GSH S-transferase isoenzymes of rat, man and mouse have been assigned to three groups, Alpha, Mu and Pi, based on N-terrninal amino acid sequences, substrate specificities, immunological cross-reactivity and sensitivities to inhibitors. The kinetic mechanism of the GSH S-transferases is controversial, due to the observation of non-Michaelian (non-hyperbolic) substrate-rate saturation curves. The most detailed investigations of the steady-state kinetics of glutathione S-transferase have been performed with isoenzyme 3-3 (class Mu) and the substrate 1,2-dichloro-4-nitrobenzene (DCNB). Explanations for the apparently anomalous non-hyperbolic kinetics have included subunit cooperativity, steady-state mechanisms of differing degrees of complexity and the superimposition of either product inhibition or enzyme memory on these mechanisms. This study has confirmed the biphasic kinetics for isoenzyme 3-3 with DCNB and shown non-hyperbolic kinetics for this isoenzyme with 1-chloro-2,4-dinitrobenzene (CDNB) and for isoenzyme 3-4 with DCNB and CDNB. It is proposed that the basic steady-state random sequential Bi Bi mechanism is the simplest mechanism sufficient to explain the non-hyperbolic kinetics of GSH S-transferases 3-3 and 3-4 under initial rate conditions. Neither more complex steady-state mechanisms nor the superimposition of product inhibition or enzyme memory on the simplest steady-state mechanism are necessary.
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Thumser, Alfred Ernst Adolf. "The glutathione S-transferases : inhibition, activation, binding and kinetics." Thesis, University of Cape Town, 1990. http://hdl.handle.net/11427/28958.

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Shiffler, Stacy Marla. "Binding Kinetics of FlAsH and AsCy3 to Tetra-Cysteine Peptides." Thesis, The University of Arizona, 2011. http://hdl.handle.net/10150/144943.

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Willumsen, Bodil. "Kinetics of biological binding studied by flow injection fluorescence microscopy /." Thesis, Connect to this title online; UW restricted, 1997. http://hdl.handle.net/1773/8519.

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Zhang, Fang. "The regulation of conformation and binding kinetics of integrin alphaLbeta2." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2007. http://hdl.handle.net/1853/24678.

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Thesis (M. S.)--Biomedical Engineering, Georgia Institute of Technology, 2008.
Committee Chair: Zhu, Cheng; Committee Member: Babensee , Julia; Committee Member: Garcia, Andres; Committee Member: McIntire, Larry; Committee Member: Selvaraj, Periasamy; Committee Member: Springer, Timothy
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Kasturi, Rama. "Kinetics of calmodulin binding to its smooth muscle target proteins /." The Ohio State University, 1991. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487694702782747.

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Chernoff, Daniel Michael. "Kinetics of local anesthetic binding to sodium channels : role of pKa̳." Thesis, Massachusetts Institute of Technology, 1988. http://hdl.handle.net/1721.1/29203.

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Thesis (Ph. D.)--Harvard University--Massachusetts Institute of Technology Division of Health Sciences and Technology, Program in Medical Engineering and Medical Physics, 1989.
On t.p. "a" is subscript.
Includes bibliographical references (leaves 165-175).
by Daniel Michael Chernoff.
Ph.D.
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Lee, Isaish Chi Kin. "Measuring the binding kinetics of estrogen receptor alpha and dietary estrogens." HKBU Institutional Repository, 2014. https://repository.hkbu.edu.hk/etd_oa/28.

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Anti-estrogen drugs such as Tamoxifen and Raloxifene are widely prescribed for breast cancer patients. While they are effective, they also have serious side effects. Alternative drugs are therefore being developed. In the drug discovery process, the in vitro binding of estrogen receptors and lead compounds were studied. The binding strength was conventionally quantified in terms of equilibrium dissociation constants (K0 ). However, the binding kinetic rates and especially off-rates (k0 ff) were recently shown to be better indicators of drug potency. In this thesis, we identified a few dietary estrogens as candidate lead compounds. We studied the binding of full-length human recombinant ERa with these dietary estrogens. In particular, we measured for the first time their binding kinetics rate constants. We also measured the change in the receptor-ligand binding kinetics upon its recruitment of co-activators, as a means to gauge agonist/antagonist propensity ofthe ligand. Our results showed that the following dietary estrogens, a-Zearalenol, Zearalenone, and Coumestrol bind favorably to the estrogen receptor alpha.
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Books on the topic "Binding kinetics"

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Kuby, Stephen Allen. Enzyme catalysis, kinetics, and substrate binding. Boca Raton: CRC Press, 1991.

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Keserü, György M., and David C. Swinney, eds. Thermodynamics and Kinetics of Drug Binding. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.

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Engineering biosensors: Kinetics and design applications. San Diego, Calif: Academic, 2002.

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Fundamentals of receptor, enzyme, and transport kinetics. Boca Raton: CRC Press, 1993.

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(Firm), Knovel, ed. Engineering biosensors: Kinetics and design applications. San Diego: Academic Press, 2002.

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Numerical methods for the life scientist: Binding and enzyme kinetics calculated with GNU Octave and MATLAB. Heidelberg: Springer, 2011.

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Binding and Kinetics for Molecular Biologists. Cold Spring Harbor Laboratory Press, 2006.

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Goodrich, James A., and Jennifer F. Kugel. Binding and Kinetics for Molecular Biologists. Cold Spring Harbor Laboratory Press, 2006.

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Principles of Biomolecular Kinetics and Binding. CRC, 1994.

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Folkers, Gerd, Raimund Mannhold, Hugo Kubinyi, David C. Swinney, and Gy�rgy Keser�. Thermodynamics and Kinetics of Drug Binding. Wiley & Sons, Incorporated, John, 2015.

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Book chapters on the topic "Binding kinetics"

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Prinz, Heino. "Binding Kinetics." In Numerical Methods for the Life Scientist, 71–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-20820-1_6.

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Woerlee, Gerald M. "Plasma Protein Binding." In Kinetics and Dynamics of Intravenous Anesthetics, 180–87. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-0-585-28009-7_8.

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Vauquelin, Georges, Walter Huber, and David C. Swinney. "Experimental Methods to Determine Binding Kinetics." In Thermodynamics and Kinetics of Drug Binding, 169–89. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch9.

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Ferenczy, György G. "Computation of Drug-Binding Thermodynamics." In Thermodynamics and Kinetics of Drug Binding, 37–61. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch3.

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Freire, Ernesto. "The Binding Thermodynamics of Drug Candidates." In Thermodynamics and Kinetics of Drug Binding, 1–13. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch1.

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Romanowska, Julia, Daria B. Kokh, Jonathan C. Fuller, and Rebecca C. Wade. "Computational Approaches for Studying Drug Binding Kinetics." In Thermodynamics and Kinetics of Drug Binding, 211–35. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch11.

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Keserü, György M., and David C. Swinney. "Thermodynamics and Binding Kinetics in Drug Discovery." In Thermodynamics and Kinetics of Drug Binding, 313–29. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch16.

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Chang, Andrew, Kanishk Kapilashrami, Eleanor K. H. Allen, and Peter J. Tonge. "The Kinetics and Thermodynamics ofStaphylococcus aureusFabI Inhibition." In Thermodynamics and Kinetics of Drug Binding, 295–311. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch15.

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Waring, Michael J., Andrew G. Leach, and Duncan C. Miller. "Challenges in the Medicinal Chemical Optimization of Binding Kinetics." In Thermodynamics and Kinetics of Drug Binding, 191–210. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch10.

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Schiele, Felix, Pelin Ayaz, and Anke Müller-Fahrnow. "The Use of Structural Information to Understand Binding Kinetics." In Thermodynamics and Kinetics of Drug Binding, 237–56. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527673025.ch12.

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Conference papers on the topic "Binding kinetics"

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Jones, S. A., and B. C. Hollins. "Determining Binding Kinetics for Microfluidic Carbonylated Protein Enrichment." In 2013 29th Southern Biomedical Engineering Conference (SBEC 2013). IEEE, 2013. http://dx.doi.org/10.1109/sbec.2013.70.

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Yu, Chih-Jen, Chien Chou, Hsien-Yeh Hsu, Tsu-Shin Chan, Zheng-Yuan Lee, and Hsieh-Ting Wu. "Fiber optic biosensor for monitoring protein binding kinetics." In Biomedical Optics 2005, edited by Israel Gannot. SPIE, 2005. http://dx.doi.org/10.1117/12.589616.

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Gross, David, and Johnson Chung. "Time-dynamic imaging of individual cell ligand binding kinetics." In BiOS '97, Part of Photonics West, edited by Daniel L. Farkas and Bruce J. Tromberg. SPIE, 1997. http://dx.doi.org/10.1117/12.274332.

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Sato, Susumu, Elizabeth B. Suki, Samir D. Amin, Arnab Majumdar, and Bela Suki. "Binding Kinetics Of Elastase In The Normal And Digested Lung Tissue." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5792.

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Christensen, Ulla. "Kinetics of piasminogen-activation. Effects of ligands binding to the AH-site of plasminogen." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644420.

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Detailed kinetic studies of the urokinase catalysed conversion of Lys-77- and Val-440-plasminogens in the presence and absence of ligands binding to the AH-site of the plasminogens shows that the effects of such ligand-binding correspond with a model of the activation reaction in which the effective Km and kc decreases, but kc/Km increases when the ligands bind. Apparently plasminogen with a free AH-site is a less specific substrate for urokinase, than is plasminogen with an AH-site-bound ligand.The AH-site is a weak lysine binding site of plasminogen located in the mini plasminogen part (Val-440-Asn-790) of plasminogen and is suggested to participate in the binding of the plasminogens to undegraded fibrin.
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Jen, Chun-Ping, Ching-Te Huang, and Yun-Hung Lu. "Numerical investigation of biochemical binding kinetics on the microfluidic chip with FO-LPR." In 2009 4th IEEE International Conference on Nano/Micro Engineered and Molecular Systems. IEEE, 2009. http://dx.doi.org/10.1109/nems.2009.5068687.

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Lee, Dongheon, Akshi Singla, Hung-Jen Wu, and Joseph Sang-Il Kwon. "Dynamic Modeling of Binding Kinetics Between GD1b Ganglioside and Cholera Toxin Subunit B." In 2018 Annual American Control Conference (ACC). IEEE, 2018. http://dx.doi.org/10.23919/acc.2018.8431824.

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Lu, Hua, Jianmin Ma, Yujie Zhao, and Zu-Hong Lu. "Optical fiber immunosensor for the real-time analysis of ligand-receptor binding kinetics." In International Symposium on Biomedical Optics, edited by Qingming Luo, Britton Chance, Lihong V. Wang, and Steven L. Jacques. SPIE, 1999. http://dx.doi.org/10.1117/12.364378.

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Patel, Nisha S., and Alisa Morss Clyne. "A Computational Model of Fibroblast Growth Factor-2 Binding to Isolated and Intact Cell Surface Receptors: Effects of Fibroblast Growth Factor-2 Concentration, Flow and Delivery Mode." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80798.

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Fibroblast growth factor-2 (FGF2) plays an important role in both healthy vascular cell functions and pathogenesis in cancer, atherosclerosis and reduced perfusion in diabetes (1–4). FGF2 therapy and targeted drug delivery have great potential in the treatment of such diseases, but have had little clinical success. FGF2 binding kinetics to heparan sulfate proteoglycan (HSPG) and fibroblast growth factor receptors (FGFR) have been largely studied under static conditions (5), however FGF2 binding to endothelial cells occurs physiologically under fluid flow conditions. Understanding complex FGF2 binding kinetics would enable the development of new anti- and pro-angiogenic therapeutics. We developed a computational model of FGF2 binding to FGFR and HSPG with flow to investigate the effect of fluid flow and FGF2 delivery mode on FGF2 binding to isolated or combined binding sites.
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Al Balushi, Ahmed A., and Reuven Gordon. "Label-Free Free Solution Single Protein-Small Molecule Binding Kinetics: An Optical Tweezer Approach." In Optical Trapping Applications. Washington, D.C.: OSA, 2015. http://dx.doi.org/10.1364/ota.2015.ott2e.3.

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Reports on the topic "Binding kinetics"

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Martin, Leigh R., Aaron T. Johnson, and Stephen P. Mezyk. Neptunium Binding Kinetics with Arsenazo(III). Office of Scientific and Technical Information (OSTI), August 2014. http://dx.doi.org/10.2172/1173085.

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Butt, D. P., K. S. Lackner, C. H. Wendt, R. Vaidya, D. L. Pile, Y. Park, T. Holesinger, D. M. Harradine, and Koji Nomura. The kinetics of binding carbon dioxide in magnesium carbonate. Office of Scientific and Technical Information (OSTI), August 1998. http://dx.doi.org/10.2172/661545.

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Zauche, Timothy. Kinetics and mechanisms of the oxidation of alcohols and hydroxylamines by hydrogen peroxide, catalyzed by methyltrioxorhenium, MTO, and the oxygen binding properties of cobalt Schiff base complexes. Office of Scientific and Technical Information (OSTI), February 1999. http://dx.doi.org/10.2172/770652.

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K4DD drug target binding kinetics data. EMBL-EBI, May 2018. http://dx.doi.org/10.6019/chembl3885741.

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