Relevant bibliographies by topics / Ligards (Biochemistry)

Academic literature on the topic 'Ligards (Biochemistry)'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Ligards (Biochemistry)"

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Mitchell, Peter D. "Foundations of Vectorial Metabolism and Osmochemistry." Bioscience Reports 24, no. 4-5 (August 10, 2004): 386–435. http://dx.doi.org/10.1007/s10540-005-2739-2.

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Chemical transformations, like osmotic translocations, are transport processes when looked at in detail. In chemiosmotic systems, the pathways of specific ligand conduction are spatially orientated through osmoenzymes and porters in which the actions of chemical group, electron and solute transfer occur as vectorial (or higher tensorial order) diffusion processes down gradients of total potential energy that represent real spatially directed fields of force. Thus, it has been possible to describe classical bag-of-enzymes biochemistry as well as membrane biochemistry in terms of transport. But it would not have been possible to explain biological transport in terms of classical transformational biochemistry or chemistry. The recognition of this conceptual asymmetry in favour of transport has seemed to be upsetting to some biochemists and chemists; and they have resisted the shift towards thinking primarily in terms of the vectorial forces and co-linear displacements of ligands in place of their much less informative scalar products that correspond to the conventional scalar energies. Nevertheless, considerable progress has been made in establishing vectorial metabolism and osmochemistry as acceptable biochemical disciplines embracing transport and metabolism, and bioenergetics has been fundamentally transformed as a result.
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Mitchell, Peter. "Foundations of vectorial metabolism and osmochemistry." Bioscience Reports 11, no. 6 (December 1, 1991): 297–346. http://dx.doi.org/10.1007/bf01130212.

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Chemical transformations, like osmotic translocations, are transport processes when looked at in detail. In chemiosmotic systems, the pathways of specific ligand conduction are spatially orientated through osmoenzymes and porters in which the actions of chemical group, electron and solute transfer occur as vectorial (or higher tensorial order) diffusion processes down gradients of total potential energy that represent real spatially-directed fields of force. Thus, it has been possible to describe classical bag-of-enzymes biochemistry as well as membrane biochemistry in terms of transport. But it would not have been possible to explain biological transport in terms of classical transformational biochemistry or chemistry. The recognition of this conceptual asymmetry in favour of transport has seemed to be upsetting to some biochemists and chemists; and they have resisted the shift towards thinking primarily in terms of the vectorial forces and co-linear displacements of ligands in place of their much less informative scalar products that correspond to the conventional scalar energies. Nevertheless, considerable progress has been made in establishing vectorial metabolism and osmochemistry as acceptable biochemical disciplines embracing transport and metabolism, and bioenergetics has been fundamentally transformed as a result.
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Chin, G. J. "BIOCHEMISTRY: Making Metal Ligands." Science 298, no. 5597 (November 15, 2002): 1303b—1303. http://dx.doi.org/10.1126/science.298.5597.1303b.

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Velesinović, Aleksandar, and Goran Nikolić. "Protein-protein interaction networks and protein-ligand docking: Contemporary insights and future perspectives." Acta Facultatis Medicae Naissensis 38, no. 1 (2021): 5–17. http://dx.doi.org/10.5937/afmnai38-28322.

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Traditional research means, such as in vitro and in vivo models, have consistently been used by scientists to test hypotheses in biochemistry. Computational (in silico) methods have been increasingly devised and applied to testing and hypothesis development in biochemistry over the last decade. The aim of in silico methods is to analyze the quantitative aspects of scientific (big) data, whether these are stored in databases for large data or generated with the use of sophisticated modeling and simulation tools; to gain a fundamental understanding of numerous biochemical processes related, in particular, to large biological macromolecules by applying computational means to big biological data sets, and by computing biological system behavior. Computational methods used in biochemistry studies include proteomics-based bioinformatics, genome-wide mapping of protein-DNA interaction, as well as high-throughput mapping of the protein-protein interaction networks. Some of the vastly used molecular modeling and simulation techniques are Monte Carlo and Langevin (stochastic, Brownian) dynamics, statistical thermodynamics, molecular dynamics, continuum electrostatics, protein-ligand docking, protein-ligand affinity calculations, protein modeling techniques, and the protein folding process and enzyme action computer simulation. This paper presents a short review of two important methods used in the studies of biochemistry - protein-ligand docking and the prediction of protein-protein interaction networks.
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Di Marzo, Vincenzo, and Dale G. Deutsch. "Biochemistry of the Endogenous Ligands of Cannabinoid Receptors." Neurobiology of Disease 5, no. 6 (December 1998): 386–404. http://dx.doi.org/10.1006/nbdi.1998.0214.

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Cheloha, Ross W., Thibault J. Harmand, Charlotte Wijne, Thomas U. Schwartz, and Hidde L. Ploegh. "Exploring cellular biochemistry with nanobodies." Journal of Biological Chemistry 295, no. 45 (August 31, 2020): 15307–27. http://dx.doi.org/10.1074/jbc.rev120.012960.

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Reagents that bind tightly and specifically to biomolecules of interest remain essential in the exploration of biology and in their ultimate application to medicine. Besides ligands for receptors of known specificity, agents commonly used for this purpose are monoclonal antibodies derived from mice, rabbits, and other animals. However, such antibodies can be expensive to produce, challenging to engineer, and are not necessarily stable in the context of the cellular cytoplasm, a reducing environment. Heavy chain–only antibodies, discovered in camelids, have been truncated to yield single-domain antibody fragments (VHHs or nanobodies) that overcome many of these shortcomings. Whereas they are known as crystallization chaperones for membrane proteins or as simple alternatives to conventional antibodies, nanobodies have been applied in settings where the use of standard antibodies or their derivatives would be impractical or impossible. We review recent examples in which the unique properties of nanobodies have been combined with complementary methods, such as chemical functionalization, to provide tools with unique and useful properties.
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Hutchens, T. W., and J. O. Porath. "Protein recognition of immobilized ligands: promotion of selective adsorption." Clinical Chemistry 33, no. 9 (September 1, 1987): 1502–8. http://dx.doi.org/10.1093/clinchem/33.9.1502.

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Abstract We are using simple immobilized ligands to evaluate the biochemistry and mechanisms of selective, high-affinity, protein adsorption events. Several specific means have recently been developed to more selectively utilize the favorable entropy changes associated with the displacement of protein-bound water during the formation and stabilization of protein-ligand recognition events. For protein and peptide immobilization these include, besides hydrophobic interaction, for example, metal ion, pi-electron-mediated, and thiophilic interactions. This latter type of protein-ligand recognition process represents a previously unrecognized interaction mechanism of considerable selectivity, affinity, and utility. Specific examples of the above-mentioned principles and protein fractionations include (a) thiophilic adsorption of immunoglobulins to achieve immunoglobulin-free serum for in vitro production and purification of monoclonal antibodies and (b) urea-induced binding of estrogen-receptor proteins to immobilized DNA. The interaction mechanisms are discussed in terms of the molecular architecture of protein surfaces. We present possibilities for the further utilization of these immobilized ligands and their associated proteins in the areas of clinical biochemistry and immunology.
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Seasholtz, AF, RA Valverde, and RJ Denver. "Corticotropin-releasing hormone-binding protein: biochemistry and function from fishes to mammals." Journal of Endocrinology 175, no. 1 (October 1, 2002): 89–97. http://dx.doi.org/10.1677/joe.0.1750089.

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Corticotropin-releasing hormone (CRH) plays multiple roles in vertebrate species. In mammals, it is the major hypothalamic releasing factor for pituitary adrenocorticotropin secretion, and is a neurotransmitter or neuromodulator at other sites in the central nervous system. In non-mammalian vertebrates, CRH not only acts as a neurotransmitter and hypophysiotropin, it also acts as a potent thyrotropin-releasing factor, allowing CRH to regulate both the adrenal and thyroid axes, especially in development. The recent discovery of a family of CRH-like peptides suggests that multiple CRH-like ligands may play important roles in these functions. The biological effects of CRH and the other CRH-like ligands are mediated and modulated not only by CRH receptors, but also via a highly conserved CRH-binding protein (CRH-BP). The CRH-BP has been identified not only in mammals, but also in non-mammalian vertebrates including fishes, amphibians, and birds, suggesting that it is a phylogenetically ancient protein with extensive structural and functional conservation. In this review, we discuss the biochemical properties of the characterized CRH-BPs and the functional roles of the CRH-BP. While much of the in vitro and in vivo data to date support an 'inhibitory' role for the CRH-BP in which it binds CRH and other CRH-like ligands and prevents the activation of CRH receptors, the possibility that the CRH-BP may also exhibit diverse extra- and intracellular roles in a cell-specific fashion and at specific times in development is also discussed.
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Caflisch, Amedeo, Rudolf Wälchli, and Claus Ehrhardt. "Computer-Aided Design of Thrombin Inhibitors." Physiology 13, no. 4 (August 1998): 182–89. http://dx.doi.org/10.1152/physiologyonline.1998.13.4.182.

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Computer-aided ligand design is an active, challenging, and multidisciplinary research field that blends knowledge of biochemistry, physics, and computer sciences. Whenever it is possible to experimentally determine or to model the three-dimensional structure of a pharmacologically relevant enzyme or receptor, computational approaches can be used to design specific high-affinity ligands. This article describes methods, applications, and perspectives of computer-assisted ligand design.
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Sharon, Nathan. "Protein–carbohydrate interactions: At the heart of biochemistry." Biochemist 28, no. 3 (June 1, 2006): 13–17. http://dx.doi.org/10.1042/bio02803013.

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Proteins that possess the ability to bind carbohydrates specifically and reversibly abound in nature, being present in all living organisms, from viruses to humans. Their interactions with their ligands are the basis of a myriad of biological processes, both normal and pathological1–3 (Table 1). The high selectivity required for these interactions is provided by a specific stereochemical fit between complementary molecules, the protein on the one hand and the carbohydrate on the other. This concept has its origins in the lock-and-key hypothesis, introduced by Emil Fischer at the end of the 19th Century to explain the specificity of interactions between enzymes (he studied glycosidases) and their substrates (carbohydrates), i.e. between molecules in solution. In time it was extended to describe the interactions of cells with soluble molecules and with other cells.
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Dissertations / Theses on the topic "Ligards (Biochemistry)"

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Wade, R. C. "Ligand-macromolecule interactions." Thesis, University of Oxford, 1988. http://ora.ox.ac.uk/objects/uuid:576ce119-6a93-4eb0-a7e4-1f2513736dbd.

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The optimisation of ligand-macromolecule interactions is fundamental to the design of therapeutic agents. The GRID method is a procedure for determining energetically favourable ligand binding sites on molecules of known structure using an empirical energy potential. In this thesis, it has been extended, tested, and then applied to the design of anti-influenza agents. In the GRID method, the energy of a hydrogen-bond is determined by a function which is dependent on the length of the hydrogen-bond, its orientation at the hydrogen-bond donor and acceptor atoms, and the chemical nature of these atoms. This function has been formulated in order to reproduce experimental observations of hydrogen-bond geometries. The reorientation of hydrogen atoms and lone-pair orbitals on the formation of hydrogen-bonds is calculated analytically. The experimentally observed water structures of crystals of four biological molecules have been used as model systems for testing the GRID method. It has been shown that the location of well-ordered waters can be predicted accurately. The ability of the GRID method to assist in the assignment of water sites during crystallographic refinement has been demonstrated. It has also been shown that waters in the active site of an enzyme may be both stabilized and displaced by a bound substrate. Ligands have been designed to block the highly conserved host cell receptor site of the influenza virus haemagglutinin in order to prevent the attachment of the virus to the host cells. The protein was mapped energetically by program GRID and specific ligand binding sites were identified. Ligands, which exploited these binding sites, were then designed using computer graphics and energy minimization techniques. Some of the designed ligands were peptides and these were synthesised and assayed. Preliminary results indicate that they may possess anti-influenza activity.
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Kandala, Srikanth. "Diphosphine Ligand Substitution in H4Ru4(CO)12: X-ray Diffraction Structures and Reactivity Studies of the Diphosphine Substituted Cluster Products." Thesis, University of North Texas, 2006. https://digital.library.unt.edu/ark:/67531/metadc5410/.

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The tetraruthenium cluster H4Ru4(CO)12 has been studied for its reactivity with the unsaturated diphosphine ligands (Z)-Ph2PCH=CHPPh2, 4,5-bis (diphenylphosphino)-4-cyclopenten-1,3-dione, bis(diphenyphosphino)benzene and 1,8- bis(diphenyl phosphino)naphthalene under thermal, near-UV photolysis, and Me3NO-assisted activation. All three cluster activation methods promote loss of CO and furnish the anticipated substitution products that possess a chelating diphosphine ligand. Clusters 1, 2, 3 and 4 have been characterized in solution by IR and NMR spectroscopies, and these data are discussed with respect to the crystallographically determined structures for all new cluster compounds. The 31P NMR spectral data and the solid-state structures confirm the presence of a chelating diphosphine ligand in all four new clusters. Sealed NMR tubes containing clusters 1, 2, 3 and 4 were found to be exceeding stable towards near-UV light and temperatures up to ca. 100°C. The surprisingly robust behavior of the new clusters is contrasted with the related cluster Ru3(CO)10(bpcd) that undergoes fragmentation to the donor-acceptor compound Ru2(CO)6(bpcd) and the phosphido-bridged compound Ru2(CO)6 (µ-PPh2)[µ-C=C(PPh2)C(O)CH2C(O)] under mild conditions. The electrochemical properties have been investigated in the case of clusters 1 and 2 by cyclic voltammetry, and the findings are discussed with respect to the reported electrochemical data on the parent cluster H4Ru4(CO)12.
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Duraj-Thatte, Anna. "Fluorescent GFP chromophores as potential ligands for various nuclear receptors." Diss., Georgia Institute of Technology, 2012. http://hdl.handle.net/1853/44764.

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Nuclear receptors are ligand activated transcription factors, where upon binding with small molecule ligands, these proteins are involved in the regulation of gene expression. To date there are approximately 48 human nuclear receptors known, involved in multiple biological and cellular processes, ranging from differentiation to maintenance of homeostasis. Due to their critical role in transcriptional regulation, these receptors are implicated in several diseases. Currently, 13% of prescribed drugs in the market are NR ligands for diseases such as cancer, diabetes and osteoporosis. In addition to drug discovery, the mechanism of function, mobility and trafficking of these receptors is poorly understood. Gaining insight into the relationship between the function and /or dysfunction of these receptors and their mobility will aid in a better understanding of the role of these receptors. The green fluorescent protein (GFP) has revolutionized molecular biology by providing the ability to monitor protein function and structure via fluorescence. The fluorescence contribution from this biological marker is the chromophore, formed from the polypeptide backbone of three amino acid residues, buried inside 11-stranded â-barrel protein. Synthesis of GFP derivatives of is based on the structure of the arylmethyleneimidazolidinone (AMI), creating a molecule that is only weakly fluorescent. Characterizing these AMI derivatives for other proteins can provide a powerful visualization tool for analysis of protein function and structure. This development could provide a very powerful method for protein analysis in vitro and in vivo. Development of such fluorescent ligands will prove beneficial for the nuclear receptors. In this work, libraries of AMIs derviatives were synthesized by manipulating various R groups around the core structure, and tested for their ability to serve as nuclear receptor ligands with the ability to fluoresce upon binding. The fluorogens are developed for steroidal and non-steroidal receptors, two general classes of nuclear receptors. Specific AMIs were designed and developed for steroid receptor estrogen receptor á (ERá). These ligands are showed to activate the receptor with an EC50 of value 3 ìM and the 10-fold activation with AMI 1 and AMI 2 in comparison to the 21-fold activation observed with natural ERá ligand, 17â-estradiol. These novel ligands were not able to display the fluorescence upon binding the receptor. However, fluorescence localized in nucleus was observed in case of another AMI derivative, AMI 10, which does not activate the receptor. Such ligands open new avenues for developing fluorescent probes for ERá that do not involve fluorescent conjugates attached to a known ERá ligand core. AMIs were also characterized for non-steroidal receptors,specifically the pregnane x receptor (PXR) and retinoic acid receptor á (RARá). To date, fluorogens which turn fluorescence upon binding and activate the receptor have not been developed for these receptors. With respect to PXR, several AMI derivatives were discovered to bind and activate this receptor with a fold-activation better than the known agonist, rifampicin. The best characterized AMI derivative, AMI 4, activates the receptor with an EC50 of value 6.3 ìM and the 154-fold activation in comparison to the 90-fold activation and an EC50 value of 1.3 ìM seen with rifamipicin. This ligand is not only able to activate PXR but also displays fluorescence upon binding to the receptor. The fluroscence pattern was observed around the nucleus. Besides AMI 4, 16 other AMI derivatives are identified that activate PXR with different activation profiles. Thus, a novel class of PXR ligands with fluorescence ability has been developed. The AMI derivatives able to bind and activate RAR, also displayed activation profiles that were comparable to the wild-type ligand, all trans retinoic acid. These ligands activated the receptor with an EC50 value of 220 nM with AMI 109 in comparison to an EC50 value of 0.8 nM with the natural ligand for RARá. When these ligands were tested for fluorescence in yeast, the yeast were able to fluoresce only in the presence of the receptor and the AMI derivative, indicating that these agonists also have the ability to fluoresce.
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Carlsson, Jens. "Challenges in Computational Biochemistry: Solvation and Ligand Binding." Doctoral thesis, Uppsala University, Department of Cell and Molecular Biology, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-8738.

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Accurate calculations of free energies for molecular association and solvation are important for the understanding of biochemical processes, and are useful in many pharmaceutical applications. In this thesis, molecular dynamics (MD) simulations are used to calculate thermodynamic properties for solvation and ligand binding.

The thermodynamic integration technique is used to calculate pKa values for three aspartic acid residues in two different proteins. MD simulations are carried out in explicit and Generalized-Born continuum solvent. The calculated pKa values are in qualitative agreement with experiment in both cases. A combination of MD simulations and a continuum electrostatics method is applied to examine pKa shifts in wild-type and mutant epoxide hydrolase. The calculated pKa values support a model that can explain some of the pH dependent properties of this enzyme.

Development of the linear interaction energy (LIE) method for calculating solvation and binding free energies is presented. A new model for estimating the electrostatic term in the LIE method is derived and is shown to reproduce experimental free energies of hydration. An LIE method based on a continuum solvent representation is also developed and it is shown to reproduce binding free energies for inhibitors of a malaria enzyme. The possibility of using a combination of docking, MD and the LIE method to predict binding affinities for large datasets of ligands is also investigated. Good agreement with experiment is found for a set of non-nucleoside inhibitors of HIV-1 reverse transcriptase.

Approaches for decomposing solvation and binding free energies into enthalpic and entropic components are also examined. Methods for calculating the translational and rotational binding entropies for a ligand are presented. The possibility to calculate ion hydration free energies and entropies for alkali metal ions by using rigorous free energy techniques is also investigated and the results agree well with experimental data.

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Mallov, Ian. "Coordination Chemistry of Diindole Ligands: Synthesis and Reactivity of a Di(indolyl)bicyclononylborate Ligand and Explorations in Main Group Diindolylmethane Chemistry." Thesis, University of Ottawa (Canada), 2010. http://hdl.handle.net/10393/28584.

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Chapter One gives a brief overview of established coordination chemistry of pyrrole and indole-based ligands, and of the ansa-metallocene chemistry of ligands featuring a heteroatom in the bridging position. Proposals for syntheses of coordination compounds of two different ansa-indolyl ligand systems are outlined. Chapter Two describes the synthesis and characterization of an anionic diindolylborate ligand and outlines attempted reactivity with transition metal and main group halides. Spectroscopic results from these reactions as well as reactions to synthesize variants of this ligand are presented. The final section details syntheses of variants of a known diindolylmethane ligand. Chapter Three presents the first well-characterized Group 13 coordination compounds of the di(3-methylindol-2-yl)-4-bromophenylmethane ligand. Hydrogen-elimination reactions producing borane and alane complexes in high yield were employed. Spectroscopic characterization is presented, as well as solid-state structural characterization of the borane. Further reactivity with trimethylaluminum is explored but results are not as definitive. Chapter Four details the first explored reactivity of the diindolylmethane ligand with metals from the s-block. Dinuclear compounds of lithium, sodium, and potassium were obtained by reaction of di(3-methylindolyl)-4-bromophenylmethane with common amides of the metals. All three compounds proved reactive with metal halides and their utility as precursors to further coordination complexes was demonstrated by reaction with calcium iodide. The potassium salt yielded a calcium complex of di(3-methylindolyl)-4-bromophenylmethane, the first known Group 2 complex of diindolylmethane. Chapter Five explores reactivity with Group 15 phosphine and stibine reagents. Phosphine halides of both di(3-methylindolyl)-4-bromophenylmethane and di(3-methylindolyl)- 4-fluorophenylmethane were synthesized and characterized spectroscopically. A solid-state structure of di-(3-methylindol-2-yl)chlorophosphine-4-bromophenylmethane was obtained. The purposes of targeting these compounds was to establish diindolylmethane as a viable supporting framework for Group 15 compounds, to examine relative Lewis basic properties of the diindolylmethane ligand system, and to determine if they were a suitable route to phosphenium cations. A diindolylmethane complex of an amidostibine was also obtained and characterized by spectroscopic and elemental analysis. Attempts toward both phosphenium and stibenium cations through halide abstraction and substituent protonation, respectively, did not yield the expected cations.
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McGregor, Lynn Marie. "Methods for the Identification of Ligand-Target Pairs from Combined Libraries of Targes and Ligands." Thesis, Harvard University, 2014. http://dissertations.umi.com/gsas.harvard:11370.

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Advances in genome and proteome research have led to a dramatic increase in the number of macromolecular targets of interest to the life sciences. A solution-phase method to simultaneously reveal all ligand-target binding pairs from a single solution containing libraries of ligands and targets could significantly increase the efficiency and effectiveness of target-oriented screening efforts. Here, we describe interaction-dependent PCR (IDPCR), a solution-phase method to identify binding partners from combined libraries of small-molecule ligands and targets in a single experiment. Binding between DNA-linked targets and DNA-linked ligands induces formation of an extendable duplex. Extension links codes identifying the ligand and target into one selectively amplifiable DNA molecule. In a model selection, IDPCR resulted in the enrichment of DNA encoding all five known protein-ligand pairs out of 67,599 possible sequences.
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Fernández, Lola. "Studies on the biochemistry and cell biology of the glycosyl-phosphatidylinositol (GPI)-anchored NKG2D-ligands." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609534.

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Burton, Nicolas Paul. "Novel ligands for affinity chromatography." Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.359769.

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Proctor, Lavinia M. "Pharmacological activity of C3a and C3a receptor ligands /." [St. Lucia, Qld.], 2004. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe18423.pdf.

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Richmond, Meaghan L. "The design, synthesis, and application of new amino acid-based modular N-ethylenediamine ligands /." View online version; access limited to Brown University users, 2005. http://wwwlib.umi.com/dissertations/fullcit/3174664.

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Books on the topic "Ligards (Biochemistry)"

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Ligand-binder assays: Labels and analytical strategies. New York: M. Dekker, 1985.

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Krishna, Mallia A., and Smith Paul K, eds. Immobilized affinity ligand techniques. San Diego: Academic Press, 1992.

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Daëron, M. Techniques d'études des interactions ligands-récepteurs. Paris: Société française d'immunologie, 1989.

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H, Sawyer William, ed. Quantitative characterization of ligand binding. New York: Wiley-Liss, 1995.

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BLyS ligands and receptors. New York: Humana Press, 2010.

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Pellissier, Hélène. Chiral sulfur ligands: Asymmetric catalysis. Cambridge: Royal Society of Chemistry, 2009.

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Shartava, Tsisana. Ligands, polymers, and amino acids. New York: Nova Science Publishers, Inc., 2011.

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Woodbury, Charles P. Introduction to macromolecular binding equilibria. Boca Raton: CRC Press, 2008.

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G, Hughes Jason, and Robinson Alton J, eds. Inorganic biochemistry: Research progress. New York: Nova Science, 2008.

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

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Book chapters on the topic "Ligards (Biochemistry)"

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Nguyen, Henry C., Wei Wang, and Yong Xiong. "Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction." In Subcellular Biochemistry, 323–47. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-46503-6_12.

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Cosman, David. "The Tumor-Necrosis-Factor-Related Superfamily of Ligands and Receptors." In Blood Cell Biochemistry, 51–77. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-0-585-31728-1_3.

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Lasseter, Benjamin F. "Fluorescence Studies of Ligand Binding." In Biochemistry in the Lab, 159–68. Names: Lasseter, Benjamin F., author. Title: Biochemistry in the lab : a manual for undergraduates / by Benjamin F. Lasseter. Description: Boca Raton, Florida : CRC Press, [2020]: CRC Press, 2019. http://dx.doi.org/10.1201/9780429491269-16.

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Montenay-Garestier, T., J. S. Sun, J. Chomilier, J. L. Mergny, M. Takasugi, U. Asseline, N. T. Thuong, M. Rougee, and C. Helene. "Design of Bifunctional Nucleic Acid Ligands." In The Jerusalem Symposia on Quantum Chemistry and Biochemistry, 275–90. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-011-3728-7_19.

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Mao, Youdong. "Structure, Dynamics and Function of the 26S Proteasome." In Subcellular Biochemistry, 1–151. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-58971-4_1.

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AbstractThe 26S proteasome is the most complex ATP-dependent protease machinery, of ~2.5 MDa mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated proteins and plays fundamentally indispensable roles in regulating almost all major aspects of cellular activities. To serve as the sole terminal “processor” for myriad ubiquitylation pathways, the proteasome evolved exceptional adaptability in dynamically organizing a large network of proteins, including ubiquitin receptors, shuttle factors, deubiquitinases, AAA-ATPase unfoldases, and ubiquitin ligases, to enable substrate selectivity and processing efficiency and to achieve regulation precision of a vast diversity of substrates. The inner working of the 26S proteasome is among the most sophisticated, enigmatic mechanisms of enzyme machinery in eukaryotic cells. Recent breakthroughs in three-dimensional atomic-level visualization of the 26S proteasome dynamics during polyubiquitylated substrate degradation elucidated an extensively detailed picture of its functional mechanisms, owing to progressive methodological advances associated with cryogenic electron microscopy (cryo-EM). Multiple sites of ubiquitin binding in the proteasome revealed a canonical mode of ubiquitin-dependent substrate engagement. The proteasome conformation in the act of substrate deubiquitylation provided insights into how the deubiquitylating activity of RPN11 is enhanced in the holoenzyme and is coupled to substrate translocation. Intriguingly, three principal modes of coordinated ATP hydrolysis in the heterohexameric AAA-ATPase motor were discovered to regulate intermediate functional steps of the proteasome, including ubiquitin-substrate engagement, deubiquitylation, initiation of substrate translocation and processive substrate degradation. The atomic dissection of the innermost working of the 26S proteasome opens up a new era in our understanding of the ubiquitin-proteasome system and has far-reaching implications in health and disease.
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Wiesinger, Heiner, and Hans Jürgen Hinz. "Thermodynamic Data for Protein-Ligand Interaction." In Thermodynamic Data for Biochemistry and Biotechnology, 211–26. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71114-5_7.

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Heidrich, Corina G., and Christian Berens. "Probing RNA Structure and Ligand Binding Sites on RNA by Fenton Cleavage." In Handbook of RNA Biochemistry, 301–18. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527647064.ch15.

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Heims, Florian, and Kallol Ray. "Multiple Spin Scenarios in Transition-Metal Complexes Involving Redox Non-Innocent Ligands." In Spin States in Biochemistry and Inorganic Chemistry, 229–62. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch11.

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Papish, Elizabeth T., Natalie A. Dixon, and Mukesh Kumar. "Biomimetic Chemistry with Tris(triazolyl)borate Ligands: Unique Structures and Reactivity via Interactions with the Remote Nitrogens." In Molecular Design in Inorganic Biochemistry, 115–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/430_2012_86.

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Mi, Yan-Ni, Na-Na Ping, and Yong-Xiao Cao. "Ligands and Signaling of Mas-Related G Protein-Coupled Receptor-X2 in Mast Cell Activation." In Reviews of Physiology, Biochemistry and Pharmacology, 139–88. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/112_2020_53.

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