Relevant bibliographies by topics / Allosteric regulation

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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 'Allosteric regulation'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "Allosteric regulation"

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Leander, Megan, Yuchen Yuan, Anthony Meger, Qiang Cui, and Srivatsan Raman. "Functional plasticity and evolutionary adaptation of allosteric regulation." Proceedings of the National Academy of Sciences 117, no. 41 (September 30, 2020): 25445–54. http://dx.doi.org/10.1073/pnas.2002613117.

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Allostery is a fundamental regulatory mechanism of protein function. Despite notable advances, understanding the molecular determinants of allostery remains an elusive goal. Our current knowledge of allostery is principally shaped by a structure-centric view, which makes it difficult to understand the decentralized character of allostery. We present a function-centric approach using deep mutational scanning to elucidate the molecular basis and underlying functional landscape of allostery. We show that allosteric signaling exhibits a high degree of functional plasticity and redundancy through myriad mutational pathways. Residues critical for allosteric signaling are surprisingly poorly conserved while those required for structural integrity are highly conserved, suggesting evolutionary pressure to preserve fold over function. Our results suggest multiple solutions to the thermodynamic conditions of cooperativity, in contrast to the common view of a finely tuned allosteric residue network maintained under selection.
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Sengupta, Ushnish, and Birgit Strodel. "Markov models for the elucidation of allosteric regulation." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1749 (May 7, 2018): 20170178. http://dx.doi.org/10.1098/rstb.2017.0178.

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Allosteric regulation refers to the process where the effect of binding of a ligand at one site of a protein is transmitted to another, often distant, functional site. In recent years, it has been demonstrated that allosteric mechanisms can be understood by the conformational ensembles of a protein. Molecular dynamics (MD) simulations are often used for the study of protein allostery as they provide an atomistic view of the dynamics of a protein. However, given the wealth of detailed information hidden in MD data, one has to apply a method that allows extraction of the conformational ensembles underlying allosteric regulation from these data. Markov state models are one of the most promising methods for this purpose. We provide a short introduction to the theory of Markov state models and review their application to various examples of protein allostery studied by MD simulations. We also include a discussion of studies where Markov modelling has been employed to analyse experimental data on allosteric regulation. We conclude our review by advertising the wider application of Markov state models to elucidate allosteric mechanisms, especially since in recent years it has become straightforward to construct such models thanks to software programs like PyEMMA and MSMBuilder. This article is part of a discussion meeting issue ‘Allostery and molecular machines’.
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Motlagh, Hesam N., Jing Li, E. Brad Thompson, and Vincent J. Hilser. "Interplay between allostery and intrinsic disorder in an ensemble." Biochemical Society Transactions 40, no. 5 (September 19, 2012): 975–80. http://dx.doi.org/10.1042/bst20120163.

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Allostery is a biological phenomenon of critical importance in metabolic regulation and cell signalling. The fundamental premise of classical models that describe allostery is that structure mediates ‘action at a distance’. Recently, this paradigm has been challenged by the enrichment of IDPs (intrinsically disordered proteins) or ID (intrinsically disordered) segments in transcription factors and signalling pathways of higher organisms, where an allosteric response from external signals is requisite for regulated function. This observation strongly suggests that IDPs elicit the capacity for finely tunable allosteric regulation. Is there a set of transferable ground rules that reconcile these disparate allosteric phenomena? We focus on findings from the human GR (glucocorticoid receptor) which is a nuclear transcription factor in the SHR (steroid hormone receptor) family. GR contains an intrinsically disordered NTD (N-terminal domain) that is obligatory for transcription activity. Different GR translational isoforms have various lengths of NTD and by studying these isoforms we found that the full-length ID NTD consists of two thermodynamically distinct coupled regions. The data are interpreted in the context of an EAM (ensemble allosteric model) that considers only the intrinsic and measurable energetics of allosteric systems. Expansion of the EAM is able to reconcile the paradox that ligands for SHRs can be agonists and antagonists in a cell-context-dependent manner. These findings suggest a mechanism by which SHRs in particular, and IDPs in general, may have evolved to couple thermodynamically distinct ID segments. The ensemble view of allostery that is illuminated provides organizing principles to unify the description of all allosteric systems and insight into ‘how’ allostery works.
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Abrusán, György, David B. Ascher, and Michael Inouye. "Known allosteric proteins have central roles in genetic disease." PLOS Computational Biology 18, no. 2 (February 9, 2022): e1009806. http://dx.doi.org/10.1371/journal.pcbi.1009806.

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Allostery is a form of protein regulation, where ligands that bind sites located apart from the active site can modify the activity of the protein. The molecular mechanisms of allostery have been extensively studied, because allosteric sites are less conserved than active sites, and drugs targeting them are more specific than drugs binding the active sites. Here we quantify the importance of allostery in genetic disease. We show that 1) known allosteric proteins are central in disease networks, contribute to genetic disease and comorbidities much more than non-allosteric proteins, and there is an association between being allosteric and involvement in disease; 2) they are enriched in many major disease types like hematopoietic diseases, cardiovascular diseases, cancers, diabetes, or diseases of the central nervous system; 3) variants from cancer genome-wide association studies are enriched near allosteric proteins, indicating their importance to polygenic traits; and 4) the importance of allosteric proteins in disease is due, at least partly, to their central positions in protein-protein interaction networks, and less due to their dynamical properties.
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Christopoulos, A., L. T. May, V. A. Avlani, and P. M. Sexton. "G-protein-coupled receptor allosterism: the promise and the problem(s)." Biochemical Society Transactions 32, no. 5 (October 26, 2004): 873–77. http://dx.doi.org/10.1042/bst0320873.

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Allosteric modulators of G-protein-coupled receptors interact with binding sites that are topographically distinct from the orthosteric site recognized by the receptor's endogenous agonist. Allosteric ligands offer a number of advantages over orthosteric drugs, including the potential for greater receptor subtype selectivity and a more ‘physiological’ regulation of receptor activity. However, the manifestations of allosterism at G-protein-coupled receptors are quite varied, and significant challenges remain for the optimization of screening methods to ensure the routine detection and validation of allosteric ligands.
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Hadzipasic, Adelajda, Christopher Wilson, Vy Nguyen, Nadja Kern, Chansik Kim, Warintra Pitsawong, Janice Villali, Yuejiao Zheng, and Dorothee Kern. "Ancient origins of allosteric activation in a Ser-Thr kinase." Science 367, no. 6480 (February 20, 2020): 912–17. http://dx.doi.org/10.1126/science.aay9959.

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A myriad of cellular events are regulated by allostery; therefore, evolution of this process is of fundamental interest. Here, we use ancestral sequence reconstruction to resurrect ancestors of two colocalizing proteins, Aurora A kinase and its allosteric activator TPX2 (targeting protein for Xklp2), to experimentally characterize the evolutionary path of allosteric activation. Autophosphorylation of the activation loop is the most ancient activation mechanism; it is fully developed in the oldest kinase ancestor and has remained stable over 1 billion years of evolution. As the microtubule-associated protein TPX2 appeared, efficient kinase binding to TPX2 evolved, likely owing to increased fitness by virtue of colocalization. Subsequently, TPX2-mediated allosteric kinase regulation gradually evolved. Surprisingly, evolution of this regulation is encoded in the kinase and did not arise by a dominating mechanism of coevolution.
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Vinkenborg, Jan L., Nora Karnowski, and Michael Famulok. "Aptamers for allosteric regulation." Nature Chemical Biology 7, no. 8 (July 18, 2011): 519–27. http://dx.doi.org/10.1038/nchembio.609.

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VanHook, Annalisa M. "Allosteric regulation of Warts." Science Signaling 9, no. 409 (January 5, 2016): ec2-ec2. http://dx.doi.org/10.1126/scisignal.aaf1721.

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Horovitz, Amnon, and Keith R. Willison. "Allosteric regulation of chaperonins." Current Opinion in Structural Biology 15, no. 6 (December 2005): 646–51. http://dx.doi.org/10.1016/j.sbi.2005.10.001.

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Biswas, Kabir H. "Allosteric regulation of proteins." Resonance 22, no. 1 (January 2017): 37–50. http://dx.doi.org/10.1007/s12045-017-0431-z.

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Dissertations / Theses on the topic "Allosteric regulation"

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Wawrzynów, Bartosz. "Allosteric regulation of MDM2 protein." Thesis, University of Edinburgh, 2010. http://hdl.handle.net/1842/4507.

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The diverse functions of the MDM2 oncoprotein in growth control and tumourigenesis are managed through coordinated regulation of its discrete domains induced by both extrinsic and intrinsic stimuli. A picture of MDM2 is immerging where structurally discrete but interdependent functional domains are linked through changes in conformation. However compelling insights into how this process is carried out have been hindered by inadequate information on the structure and conformation of the full-length protein. The data presented indicates that the C-terminal RING domain of MDM2, primarily responsible of the E3 ubiquitin ligase activity of the protein, has other intriguing functions. The binding of ATP within the RING domain, triggers conformational changes of MDM2 and its main interaction partner – p53. This in effect promotes efficient binding of the p53 tumour suppressor to specific DNA promoter sequences. Moreover, results presented in this thesis demonstrate a novel role for the RING domain of MDM2 in determining the conformation and activity of its N-terminal hydrophobic cleft, the key target of anticancer drugs designed to activate the function of p53 tumour suppressor protein. Specific modulations within the RING domain, affecting Zinc coordination are synonymous with increased binding affinity of the hydrophobic pocket to the transactivation domain of p53 resulting in a gain of MDM2 transrepressor function thus leading to a decrease in p53-dependant gene expression. ThermoFluor measurements and size exclusion chromatography show that changes in the RING motif lack an effect on the overall integrity of the MDM2 protein. The intrinsic fluorescence measurements manifest that these changes generate long range conformational transitions that are transmitted through the core/central acidic domain of MDM2 resulting in allosteric regulation of the N-terminal hydrophobic pocket. Such RING generated conformational changes result in the relaxation of the hydrophobic pocket. Additionally, it is shown that the cooperation between the RING and the hydrophobic cleft in MDM2 has implications in the efficiency of binding of anticancer drugs such as Nutlin by MDM2. Cooperation between the RING and hydrophobic domain of MDM2 to regulate function demonstrates an allosteric relationship and highlights the need to study MDM2 in a native conformation. In essence the presented data demonstrates that the complex relationship between different domains of MDM2 can impact on the efficacy of anticancer drugs directed towards its hydrophobic pocket.
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Livingstone, Emma Kathrine. "Allosteric Regulation of the First Enzyme in Histidine Biosynthesis." Thesis, University of Canterbury. Chemistry, 2015. http://hdl.handle.net/10092/10470.

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The ATP-PRTase enzyme catalyses the first committed step of histidine biosynthesis in archaea, bacteria, fungi and plants.1 As the catalyst of an energetically expensive pathway, ATP-PRTase is subject to a sophisticated, multilevel regulatory system.2 There are two families of this enzyme, the long form (HisGL) and the short form (HisGS) that differ in their molecular architecture. A single HisGL chain comprises three domains. Domains I and II house the active site of HisGL while domain III, a regulatory domain, forms the binding site for histidine as an allosteric inhibitor. The long form ATP-PRTase adopts a homo-hexameric quaternary structure.3,4 HisGS comprises a similar catalytic core to HisGL but is devoid of the regulatory domain and associates with a second protein, HisZ, to form a hetero-octameric assembly.5 This thesis explores the allosteric regulation of the short form ATP-PRTase, as well as the functional and evolutionary relationship between the two families. New insight into the mode allosteric inhibition of the short form ATP-PRTase from Lactococcus lactis is reported in chapter two. A conformational change upon histidine binding was revealed by small angle X-ray scattering, illuminating a potential mechanism for the allosteric inhibition of the enzyme. Additionally, characterisation of histidine binding to HisZ by isothermal titration calorimetry, in the presence and absence of HisGS, provided evidence toward the location of the functional allosteric binding site within the HisZ subunit. Chapter three details the extensive effort towards the purification of the short form ATP-PRTase from Neisseria menigitidis, the causative agent of bacterial meningitis. This enzyme is of particular interest as a potential target for novel, potent inhibitors to combat this disease. The attempts to purify the long form ATP-PRTase from E. coli, in order to clarify earlier research on the functional multimeric state of the enzyme, are also discussed. Chapter four reports the investigation of a third ATP-PRTase sequence architecture, in which hisZ and hisGS comprise a single open reading frame, forming a putative fusion enzyme. The engineering of two covalent linkers between HisZ and HisGS from L. lactis and the transfer of the regulatory domain from HisGL to HisGS, is also discussed, in an attempt to delineate the evolutionary pathway of the ATP-PRTase enzymes. Finally, the in vivo activity of each functional and putative ATP-PRTase was assessed by E. coli BW25113∆hisG complementation assays.
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Cohen, Fiona Rachel. "The allosteric regulation of adenosine receptors." Thesis, University College London (University of London), 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.309286.

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Marshall, Kristin Ann. "Group I aptazymes as genetic regulatory switches." Access restricted to users with UT Austin EID Full text (PDF) from UMI/Dissertation Abstracts International, 2001. http://wwwlib.umi.com/cr/utexas/fullcit?p3034980.

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Cockrell, Gregory Mercer. "New Insights into Catalysis and Regulation of the Allosteric Enzyme Aspartate Transcarbamoylase." Thesis, Boston College, 2013. http://hdl.handle.net/2345/3156.

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Thesis advisor: Evan R. Kantrowitz
The enzyme aspartate transcarbamoylase (ATCase) is an enzyme in the pyrimidine nucleotide biosynthetic pathway. It was once an attractive target for anti-proliferation drugs but has since become a teaching model due to kinetic properties such as cooperativity and allostery exhibited by the Escherichia coli form of the enzyme. ATCase from E. coli has been extensively studied over that last 60 years and is the textbook example of allosteric enzymes. Through this past research it is understood that ATCase is allosterically inhibited by CTP, the end product of pyrimidine biosynthesis, and allosterically activated by ATP, the end product of the parallel purine biosynthetic pathway. Part of the work discussed in this dissertation involves further understanding the catalytic properties of ATCase by examining an unregulated trimeric form from Bacillus subtilis, a bacterial ATCase that more closely resembles the mammalian form than E. coli ATCase. Through X-ray crystallography and molecular modeling, the complete catalytic cycle of B. subtilis ATCase was visualized, which provided new insights into the manifestation of properties such as cooperativity and allostery in forms of ATCase that are regulated. Most of the work described in the following chapters involves understanding allostery in E. coli ATCase. The work here progressively builds a new model of allostery through new X-ray structures of ATCase*NTP complexes. Throughout these studies it has been determined that the allosteric site is bigger than previously thought and that metal ions play a significant role in the kinetic response of the enzyme to nucleotide effectors. This work proves that what is known about ATCase regulation is inaccurate and that currently accepted, and taught, models of allostery are wrong. This new model of allostery for E. coli ATCase unifies all old and current data for ATCase regulation, and has clarified many previously unexplainable results
Thesis (PhD) — Boston College, 2013
Submitted to: Boston College. Graduate School of Arts and Sciences
Discipline: Chemistry
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Brear, Paul. "The search for allosteric inhibitors." Thesis, University of St Andrews, 2013. http://hdl.handle.net/10023/3451.

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This thesis describes the development of chemical tools that inhibit the sialidases NanA and NanB from Streptococcus pneumonia. The primary focus was on the discovery of allosteric inhibitors of NanA and NanB, however, promising inhibitors that act by binding at the active site of these enzymes were also investigated. Chapter 1 gives an overview of the use of chemical tools in the field of chemical biology. It focuses in particular on chemical tools that function by the allosteric regulation of their target proteins. The uses, advantages and methods of discovery of allosteric tools are discussed. Finally this chapter introduces the use of serendipitous binders for the discovery of allosteric sites. In particular, the use of CHES to identify novel allosteric sites on the sialidase NanB is proposed. Chapter 2 describes how the ‘hits' from a series of high throughput screens were reanalysed using a wide range of secondary assays to eliminate any false positives that were contaminating the results. This process removed eight of the eleven ‘hits'. Two of the remaining three compounds were then analysed further in an attempt to characterise their binding mode to NanA and/or NanB using modelling and X-ray crystallographic studies. Whilst, it was not possible to confirm the binding mode by X-ray crystallography modelling studies using the modelling software GOLD generated possible binding modes for these inhibitors. A structure activity relationship study was conducted for both compounds in an attempt to generate more potent inhibitors. Chapter 3 moves from the use of high throughput screens to identify hits against NanA and NanB to the use of the serendipitous binding of N-cyclohexyl-2-aminoethanesulfonic acid in the active site of NanB for the development of selective NanB inhibitors. First taurine was identified as the minimum unit of N-cyclohexyl-2-aminoethanesulfonic acid required to bind to the active site of NanB. Taurine was then used as the basis of an optimisation study. This chapter concludes with the identification of 2-(benzylammonio)ethanesulfonate as the next key intermediate in the development of N-cyclohexyl-2-aminoethanesulfonic acid based active site inhibitors of NanB. Chapter 4 follows on from Chapter 3 with the optimisation of 2-(benzylammonio)ethanesulfonate describing the design and synthesis of a wide range of analogues. From these compounds 2-[(3-chlorobenzyl)ammonio]ethanesulfonate was identified as the most potent and selective inhibitor. Detailed analysis of the binding of 2-[(3-chlorobenzyl)ammonio]ethanesulfonate to NanB gave a rationale for its improved inhibitory activity. The increase in inhibition occurred because on binding of 2-[(3-chlorobenzyl)ammonio]ethanesulfonate to the active site of NanB a well coordinated water molecule was displaced. The displacement of this water caused an increase in the flexibility of the enzyme's 352 loop. A detailed study of the flexibility of this loop in response to various N-cyclohexyl-2-aminoethanesulfonic acid based chemical tools was then conducted. The research in chapters 2 and 3 has recently been published. In Chapter 5 a molecule of N-cyclohexyl-2-aminoethanesulfonic acid that binds serendipitously in a previously unmentioned secondary site is elaborated into a ligand, known as Optactin, that binds strongly and selectively at this secondary site. It was then shown that Optactin inhibited NanB by binding at this secondary site. It was therefore concluded that this secondary site was in fact an allosteric site that could be used for the regulation of NanB. Chapter 6 describes the development of a rationalisation for the inhibition of NanB by Optactin. This study included the X-ray crystallographic analysis of the apo-NanB structure and the NanB-Optactin complex under a range of conditions. This was followed by mechanistic studies that identified the point in the catalytic cycle at which Optactin was inhibiting NanB. This chapter concludes with a hypothesis for the mechanism of inhibition of NanB by Optactin.
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Larsson, Karl-Magnus. "Allosteric regulation and radical transfer in ribonucleotide reductase /." Stockholm : Institutionen för biokemi och biofysik, Univ, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-251.

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Rofougaran, Reza. "DNA precursor biosynthesis-allosteric regulation and medical applications." Doctoral thesis, Umeå : Univ, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1678.

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Ali, Mahesheema na. "Allosteric Regulation of Prothrombin Activation by factor Va." Cleveland State University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=csu1462805026.

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Schwebach, Christopher L. "Allosteric and Calcium-Dependent Regulation of Human Plastins." The Ohio State University, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1563329156932864.

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Books on the topic "Allosteric regulation"

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Allostery: Methods and protocols. New York: Humana Press, 2011.

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Centro linceo interdisciplinare "Beniamino Segre.", Università degli studi di Roma "La Sapienza." Dipartimento di scienze biochimiche., and Instituto di biologia e patologia molecolari (Italy), eds. Allosteric proteins: 40 years with Monod-Wyman-Changeux : convegno internazionale : Roma, 24 maggio 2005. Roma: Accademia nazionale dei Lincei, 2006.

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Perutz, Max F. Mechanisms of cooperativity and allosteric regulation in proteins. Cambridge [England]: Cambridge University Press, 1990.

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1947-, Johnson Michael L., and Ackers Gary K, eds. Energetics of biological macromolecules. San Diego, CA: Academic Press, 2000.

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Fenton, Aron W. Allostery: Methods and Protocols. Humana Press, 2016.

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Allosteric Receptor Modulation in Drug Targeting. Informa Healthcare, 2006.

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Levitzki, Alexander. Quantitative Aspects of Allosteric Mechanisms. Springer, 2011.

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Bowery, Norman G. Allosteric Receptor Modulation in Drug Targeting. Taylor & Francis Group, 2016.

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Bowery, Norman G. Allosteric Receptor Modulation in Drug Targeting. Taylor & Francis Group, 2016.

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Direct and allosteric control of glutamate receptors. Boca Raton: CRC Press, 1994.

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Book chapters on the topic "Allosteric regulation"

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Nahler, Gerhard. "allosteric regulation." In Dictionary of Pharmaceutical Medicine, 7. Vienna: Springer Vienna, 2009. http://dx.doi.org/10.1007/978-3-211-89836-9_52.

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Stadtman, E. R. "Allosteric Regulation of Enzyme Activity." In Advances in Enzymology - and Related Areas of Molecular Biology, 41–154. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122730.ch2.

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Eriksson, S., and L. Thelander. "Allosteric Regulation of Calf Thymusribonucleotide Reductase." In Ciba Foundation Symposium 68 - Enzyme Defects and Immune Dysfunction, 165–75. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720516.ch10.

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Nussinov, Ruth, Chung-Jung Tsai, and Hyunbum Jang. "Dynamic Protein Allosteric Regulation and Disease." In Advances in Experimental Medicine and Biology, 25–43. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-8719-7_2.

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Hervé, Guy. "Molecular Mechanisms of Allosteric Regulation in Aspartate Transcarbamylase." In Enzyme Dynamics and Regulation, 155–61. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3744-0_19.

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Lucius, Aaron L., P. Keith Veronese, and Ryan P. Stafford. "Dynamic Light Scattering to Study Allosteric Regulation." In Methods in Molecular Biology, 175–86. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-334-9_9.

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Giladi, Moshe, and Daniel Khananshvili. "Molecular Determinants of Allosteric Regulation in NCX Proteins." In Advances in Experimental Medicine and Biology, 35–48. Boston, MA: Springer US, 2012. http://dx.doi.org/10.1007/978-1-4614-4756-6_4.

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Jamil, Haris, and Neil B. Madsen. "Acetyl-CoA Carboxylase: Correlation of Phosphorylation State with Allosteric Properties and Physiological State." In Enzyme Dynamics and Regulation, 121–27. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3744-0_15.

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Canagarajah, Bertram, William J. Smith, and James H. Hurley. "Structural Mechanisms of Allosteric Regulation by Membrane-binding Domains." In Protein-Lipid Interactions, 423–36. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527606769.ch17.

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White, Jordan T., Hesam N. Motlagh, Jing Li, E. Brad Thompson, and Vincent J. Hilser. "Allosteric Regulation and Intrinsic Disorder in Nuclear Hormone Receptors." In Nuclear Receptors: From Structure to the Clinic, 73–91. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-18729-7_5.

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Conference papers on the topic "Allosteric regulation"

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Dolzhikova, O. A., O. A. Semikolenova, M. I. Meschaninova, and D. S. Novopashina. "ALLOSTERIC REGULATION OF CRISPR/CAS9 SYSTEM ON THE RNA LEVEL." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-71.

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CRISPR/Cas9 systems are commonly used for the introduction of double-strand break at the targeted point of DNA. A possible way to improve its specificity is allosteric regulation. Here, we designed guide RNA containing theophylline-binding or Mango aptamer and investigated their functional activity by the example of the model DNA cleavage either in absence or in presence of theophylline or thiazole orange respectively.
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"Inter-subunit crosstalk synergistically regulates allosteric activation of proapoptotic serine protease HtrA2." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-598.

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Zhuravlev, A. M., V. V. Aksenov, V. N. Gavrilyuk, A. B. Golovanov, and I. V. Ivanov. "ALLOSTERIC INHIBITORS OF ALOX15 BASED ON LIGANDS PROVIDING MULTIDIRECTIONAL REGULATION OF LINOLEIC AND ARACHIDONIC ACIDS." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-76.

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Mammalian 15-lipoxygenases (ALOX15) are enzymes of lipid peroxidation. The pathophysiological role of ALOX15 metabolites, linoleic acid and arachidonic acid derivatives, has made this enzyme a target for pharmacological studies. Several indole and benzimidazole derivatives inhibit the activity of ALOX15 in a substrate-specific manner, but the molecular basis of this allosteric inhibition remains unclear.
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Shpakov, Alexander O. "Allosteric regulation of G-protein-coupled receptors: mechanisms, targets and pharmacological agents." In II Международная конференция, посвящеенная 100- летию И.А. Држевецкой. СКФУ, 2022. http://dx.doi.org/10.38006/9612-62-6.2022.344.347.

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Meslem, Nacim, and Vincent Fromion. "Lyapunov function for irreversible linear metabolic pathways with allosteric and genetic regulation." In 2011 50th IEEE Conference on Decision and Control and European Control Conference (CDC-ECC 2011). IEEE, 2011. http://dx.doi.org/10.1109/cdc.2011.6160805.

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"Allosteric ligand subpocket of S1P5 as a determinant of inverse agonism and ligand specificity." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-170.

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Stalnecker, Clint, Scott Ulrich, Jon Erickson, Sekar Ramachandran, Ralph DeBerardinis, and Rick Cerione. "Abstract 1155: Regulation of glutamine metabolism: Allosteric activation and inhibition of mitochondrial glutaminase." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1155.

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Panjarian, Shoghag B., Shugui Chen, Roxana Iacob, Thomas Wales, John R. Engen, and Thomas E. Smithgall. "Abstract 5599: Allosteric regulation of Abl and Bcr-Abl kinases by enhanced SH3:linker interaction." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-5599.

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Panjarian, Shoghag B., Shugui Chen, Roxana Iacob, Thomas E. Wales, John R. Engen, and Thomas E. Smithgall. "Abstract B75: Allosteric regulation of Abl and Bcr-Abl kinases by enhanced SH3:linker interaction." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-b75.

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Pereira, Marco, John Deak, Lynn Richard, Hui-Ling Chiu, Lynn Schilling, and R. J. Dwayne Miller. "Energetics and Dynamics of Global Protein Motion." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.thb4.

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Abstract:
Functionally important motions in biological systems requires the correlated displacement of thousands of atoms. The exact mechanism for the protein response to a stimulus for the functionally relevant motions is poorly understood. The classic models for deterministic protein motion rely on potential energy gradients that are created through the interaction with a stimulus to provide the forces that orchestrate the molecular motion. The question is over what length scale are these forces distributed and what are the magnitudes of the driving force, i.e., the energetics for the structural changes. In this regard, heme proteins provide ideal systems for addressing these issues. Photodissociation of the axial ligand at the heme site selectively triggers the functionally important structural changes involved in oxygen binding and allosteric regulation of oxygen transport in heme proteins.
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Reports on the topic "Allosteric regulation"

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Valdes, James J., Vicki L. Wolff, and David H. Ross. Dihydropyridine Receotprs: Possible Allosteric Regulation by Tremorgenic Toxins. Fort Belvoir, VA: Defense Technical Information Center, November 1986. http://dx.doi.org/10.21236/ada175458.

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Ye, Libin, Christopher Andrew Neale, Adnan Sljoka, Brent Lyda, Dmitry Pichugin, Nobuyuki Tsuchimura, Sacha T. Larda, et al. Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations. Office of Scientific and Technical Information (OSTI), April 2018. http://dx.doi.org/10.2172/1434450.

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