Relevant bibliographies by topics / Calcium sensor proteins

Academic literature on the topic 'Calcium sensor proteins'

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Published: 11 March 2023

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Journal articles on the topic "Calcium sensor proteins"

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D. Burgoyne, Robert. "The neuronal calcium-sensor proteins." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1742, no. 1-3 (December 2004): 59–68. http://dx.doi.org/10.1016/j.bbamcr.2004.08.008.

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Hams, Nicole, Murugesh Padmanarayana, Weihong Qiu, and Colin P. Johnson. "Otoferlin is a multivalent calcium-sensitive scaffold linking SNAREs and calcium channels." Proceedings of the National Academy of Sciences 114, no. 30 (July 10, 2017): 8023–28. http://dx.doi.org/10.1073/pnas.1703240114.

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Sensory hair cells rely on otoferlin as the calcium sensor for exocytosis and encoding of sound preferentially over the neuronal calcium sensor synaptotagmin. Although it is established that synaptotagmin cannot rescue the otoferlin KO phenotype, the large size and low solubility of otoferlin have prohibited direct biochemical comparisons that could establish functional differences between these two proteins. To address this challenge, we have developed a single-molecule colocalization binding titration assay (smCoBRA) that can quantitatively characterize full-length otoferlin from mammalian cell lysate. Using smCoBRA, we found that, although both otoferlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type calcium channel Cav1.3, showing a significant difference between the synaptic proteins. Furthermore, otoferlin was found capable of interacting with multiple SNARE and Cav1.3 proteins simultaneously, forming a heterooligomer complex. We also found that a deafness-causing missense mutation in otoferlin attenuates binding between otoferlin and Cav1.3, suggesting that deficiencies in this interaction may form the basis for otoferlin-related hearing loss. Based on our results, we propose a model in which otoferlin acts as a calcium-sensitive scaffolding protein, localizing SNARE proteins proximal to the calcium channel so as to synchronize calcium influx with membrane fusion. Our findings also provide a molecular-level explanation for the observation that synaptotagmin and otoferlin are not functionally redundant. This study also validates a generally applicable methodology for quantitatively characterizing large, multivalent membrane proteins.
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Badura, Aleksandra, Xiaonan Richard Sun, Andrea Giovannucci, Laura A. Lynch, and Samuel S. H. Wang. "Fast calcium sensor proteins for monitoring neural activity." Neurophotonics 1, no. 2 (October 17, 2014): 025008. http://dx.doi.org/10.1117/1.nph.1.2.025008.

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O'Callaghan, D. W., and R. D. Burgoyne. "Role of myristoylation in the intracellular targeting of neuronal calcium sensor (NCS) proteins." Biochemical Society Transactions 31, no. 5 (October 1, 2003): 963–65. http://dx.doi.org/10.1042/bst0310963.

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The control of the intracellular localization of NCS (neuronal calcium sensor) proteins is of importance for their ability to respond appropriately to differing calcium signals. We examine the localization of three NCS proteins: NCS-1, KChIP-1 (potassium-channel-interacting protein 1) and hippocalcin. Additionally, the [Ca2+] dependency of the calcium-induced translocation of hippocalcin is investigated. The implications of the differential targeting of these proteins on calcium signal interpretation are considered.
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BURGOYNE, Robert D., and Jamie L. WEISS. "The neuronal calcium sensor family of Ca2+-binding proteins." Biochemical Journal 353, no. 1 (January 1, 2000): 1. http://dx.doi.org/10.1042/0264-6021:3530001.

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BURGOYNE, R. D., and J. L. WEISS. "The neuronal calcium sensor family of Ca2+-binding proteins." Biochemical Journal 354, no. 3 (March 15, 2001): 727. http://dx.doi.org/10.1042/0264-6021:3540727v.

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BURGOYNE, Robert D., and Jamie L. WEISS. "The neuronal calcium sensor family of Ca2+-binding proteins." Biochemical Journal 353, no. 1 (December 18, 2000): 1–12. http://dx.doi.org/10.1042/bj3530001.

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Ca2+ plays a central role in the function of neurons as the trigger for neurotransmitter release, and many aspects of neuronal activity, from rapid modulation to changes in gene expression, are controlled by Ca2+. These actions of Ca2+ must be mediated by Ca2+-binding proteins, including calmodulin, which is involved in Ca2+ regulation, not only in neurons, but in most other cell types. A large number of other EF-hand-containing Ca2+-binding proteins are known. One family of these, the neuronal calcium sensor (NCS) proteins, has a restricted expression in retinal photoreceptors or neurons and neuroendocrine cells, suggesting that they have specialized roles in these cell types. Two members of the family (recoverin and guanylate cyclase-activating protein) have established roles in the regulation of phototransduction. Despite close sequence similarities, the NCS proteins have distinct neuronal distributions, suggesting that they have different functions. Recent work has begun to demonstrate the physiological roles of members of this protein family. These include roles in the modulation of neurotransmitter release, control of cyclic nucleotide metabolism, biosynthesis of polyphosphoinositides, regulation of gene expression and in the direct regulation of ion channels. In the present review we describe the known sequences and structures of the NCS proteins, information on their interactions with target proteins and current knowledge about their cellular and physiological functions.
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BURGOYNE, R. D., and J. L. WEISS. "The neuronal calcium sensor family of Ca2+-binding proteins." Biochemical Journal 354, no. 3 (March 8, 2001): 727. http://dx.doi.org/10.1042/bj3540727v.

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Sorkin, Raya, Margherita Marchetti, Emma Logtenberg, Emma Kerklingh, Guy Brand, Rashmi Voleti, Josep Rizo, Wouter H. Roos, Alexander J. Groffen, and Gijs J. L. Wuite. "Membrane Binding, Bending and Remodeling by Calcium Sensor Proteins." Biophysical Journal 116, no. 3 (February 2019): 368a. http://dx.doi.org/10.1016/j.bpj.2018.11.2002.

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Zimmer, Danna B., Jeannine O. Eubanks, Dhivya Ramakrishnan, and Michael F. Criscitiello. "Evolution of the S100 family of calcium sensor proteins." Cell Calcium 53, no. 3 (March 2013): 170–79. http://dx.doi.org/10.1016/j.ceca.2012.11.006.

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Dissertations / Theses on the topic "Calcium sensor proteins"

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Fitzgerald, Daniel John. "The identification and characterisation of neuronal calcium sensor interacting proteins." Thesis, University of Liverpool, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.433412.

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Robin, Jörg [Verfasser], Christoph [Akademischer Betreuer] Lienau, and Walter [Akademischer Betreuer] Pfeiffer. "Time-resolved spectroscopy of Rydberg electrons at a gold nanotip and calcium sensor proteins / Jörg Robin ; Christoph Lienau, Walter Pfeiffer." Oldenburg : BIS der Universität Oldenburg, 2016. http://d-nb.info/1124981772/34.

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Noack, Cornelia [Verfasser]. "Immunzytochemische Untersuchungen zur Ko-Lokalisation des neuronalen Calcium-Sensor- (NCS-) Proteins VILIP-1 mit dem nikotinischen Acetylcholinrezeptor (alpha4beta2) / Cornelia Noack." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2010. http://d-nb.info/1023959461/34.

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Delgado, Malcom Arturo. "Biochemical Study of Engineered Fluorescent Proteins as Calcium Sensors and the Effect of Calcium and PH in Cell Reproduction and Protein Expression." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/chemistry_theses/23.

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Calcium plays important roles in both eukaryotic and prokaryotic cells. Its actions help to stabilize cell synthesis, growth and development. In this thesis, studies have been completed to determine effects of calcium and pH on bacterial cell growth and protein expression using the bacterial cell strain E.coli BL21(DE3). Our studies demonstrated the addition of calcium addition in the media does not affect growth but increases protein expression, while reducing the pH from 7 to 4 through the addition of 10mM EGTA in LB media inhibits both. Additionally, we report studies on the design, expression, and purification of fluorescent mCherry variants and their differences in their optical properties, including: extinction coefficients , quantum yields and pKa values. Also, we report progress in the crystallization of two GFP calcium sensors: G1 and D1, using 13 and15% PEG 4000 and 3350 respectively in 50mM HEPES buffer (pH 6.8-7.0) in an effort to optimize crystallization.
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Okorocha, Albert Egwu. "Fluorescent protein calcium sensor for monitoring synaptic transmission." Thesis, University of Leicester, 2016. http://hdl.handle.net/2381/37615.

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Monitoring Ca²⁺ in intracellular compartments remains an uphill task. Fluorescent, organic calcium dyes and genetically encoded calcium indicators (GECIs) have been widely used to increase our understanding of neural activity. Notable among the GECIs is the GCaMP family. The first versions of this family showed potential but were relatively dim and had poor signal to noise ratios. To overcome these weaknesses, our laboratory developed three new ratiometric versions of the SyGCaMP2 family called SyGCaMP2-mCherry, SyGCaMP2-mCherry⁺ and GCaMP2-mCherry. The purpose of the work presented here was to establish whether these sensors were functional and to then use them to examine calcium signalling within the presynaptic terminals of cultured hippocampal and cerebral cortical neurones. The sensors were expressed in HEK 293T cells and their sensitivities to changes in intracellular free Ca²⁺concentration ascertained. The dissociation constants calculated for SyGCaMP2-mCherry⁺ and SyGCaMP2-mCherry were 140 ± 3.1 nM and 149 ± 3.3 nM respectively, but GCaMP2-mCherry was not accurately measured. Sensors were expressed in cortical and hippocampal neurones using lipofection based transfection methods and the expression patterns of each recorded. Both SyGCaMP2-mCherry and SyGCaMP2-mCherry⁺ were expressed in puncta that co-localised with presynaptic markers bassoon and VGlut1. Neurones were activated using field stimulation and the responses to different intensities and patterns of stimulation evaluated. Using the Thy1.2 promotor for neuronal expression, two transgenic mice (SyG 14 and SyG 37) were engineered in our lab that expressed SyGCaMP2-mCherry and responses to electrical stimulation were characterised in hippocampal brain slices. The roles of intracellular Ca²⁺stores in shaping the presynaptic Ca²⁺dynamics were examined and results demonstrated that inhibiting the sarcoendoplasmic reticulum calcium transport ATPase (SERCA pump) with Cyclopiazonic acid (CPA) and thapsigargin led to an enhancement in synaptic strength. In addition, activating ryanodine receptors (RYRs) with caffeine and low concentrations of ryanodine altered presynaptic Ca²⁺ dynamics.
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Ayar, Ahmet. "An investigation of calcium-induced calcium-release (CICR) in cultured rat sensory neurones." Thesis, University of Aberdeen, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285521.

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In this study the mechanisms of Ca2+-induced-Ca2+-release, effects of membrane depolarizations and the actions of pharmacological intracellular Ca2+-modulators were examined in cultured rat dorsal root ganglion (DRG) neurones. The whole cell configuration of the patch clamp technique was used to record action potentials, action potential after-potentials and voltage-activated calcium currents, (ICa), calcium-activated chloride currents, (ICI(Ca)), and non-selective cation currents, (ICAN), under current and voltage clamp recording conditions, respectively. A sub population of DRG neurones expressed action potential after-depolarizations and ICI(Ca) tail currents which were due to activation of Ca2+-activated Cl- channels as a result of Ca2+ entry. ICAN was dominantly activated due to Ca2+ release from intracellular stores evoked by pharmacological Ca2+-releasing agents such as caffeine, ryanodine and dihydrosphingosine. Calcium-activated conductances were identified by estimating reversal potentials of the activated currents, using selective pharmacological blockers and extracellular ionic replacement studies. Calcium-dependence of activated currents was also examined by using high concentration of intracellular Ca2+ buffer, EGTA, to prevent elevation of intracellular Ca2+-levels and by rapidly buffering raised intracellular Ca2+ using intracellular 'caged Ca2+ chelator', diazo-2. The involvement of intracellular Ca2+- stores was examined by performing experiments in Ca2+-free extracellular recording medium and pharmacologically inhibiting release of Ca2+ from intracellular stores, using dantrolene. Ryanodine had complex actions on DRG neurones, which reflected its ability to mobilize Ca2+, deplete Ca2+ stores, and inhibit Ca2+ release channels. Ryanodine inhibited action potential after-depolarizations and ICI(Ca) tail currents by interacting with intracellular stores and preventing amplification of Ca2+ signalling by CICR. It was found that CICR observed under physiological conditions in rat DRG neurones involves intracellular Ca2+ stores which were sensitive to ryanodine. In addition to ryanodine sensitivity these intracellular Ca2+ stores could be mobilized by caffeine and dihydrosphingosine.
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Ivings, Lenka. "Investigation of the neuronal calcium sensor protein neurocalcin #delta#." Thesis, University of Liverpool, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.250351.

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Bahi-Buisson, Nadia. "Etude des mécanismes pathogéniques du retard mental lié aux mutations dans IL-1 Receptor Accessory Protein Like IL1RAPL." Paris 6, 2005. http://www.theses.fr/2005PA066079.

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Tam, Aleeza Hoi Ting. "Characterization of hippocalcin-like protein 1 (HPCAL1), a neuronal calcium sensor protein in the retina." Thesis, University of British Columbia, 2015. http://hdl.handle.net/2429/54575.

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Hippocalcin-like protein 1 (HPCAL1) is a neuronal calcium sensor (NCS) protein found in the brain and in the retina. NCS proteins have important roles in signaling pathways including phototransduction; however, the role of HPCAL1 in the retina remains unresolved. The objective of this thesis is to characterize HPCAL1 and identify its potential interacting partners in the retina. The first part of the thesis examines the localization and characteristics of HPCAL1 using a variety of biochemical assays. The presence of HPCAL1 in the retina was confirmed with RT-PCR, Western blotting analysis, and immunofluorescence microscopy. Since NCS proteins respond to intracellular calcium level changes, HPCAL1 was expressed and isolated from both mammalian cells and E. coli to study its calcium binding properties and other characteristics. Results from a gel mobility shift assay and a fluorescence assay clearly indicated that HPCAL1 undergoes conformational changes upon calcium binding. Furthermore, membrane association assays confirmed that retinal HPCAL1 possesses the calcium-myristoyl switch mechanism which responds to the presence or absence of calcium. NCS proteins often interact with other proteins to perform their functions; therefore, the second part of the study involves the use of mass spectrometry in an attempt to identify calcium-dependent interacting partners of HPCAL1. Over 300 potential interacting partners were identified, and selected proteins were subjected to co-immunoprecipitation and Western blotting analysis or co-localization studies using immunofluorescence microscopy in order to confirm their interactions with HPCAL1. TorsinA has been identified as a calcium-dependent interacting partner to HPCAL1; however, further studies will have to be conducted to determine the significance of this interaction and to confirm other potential interacting partners that were identified in the mass spectrometry analysis. The results of this study provide important technical information on the biochemical characterization of HPCAL1 and the properties of HPCAL1 in the retina. Not only has the identification of potential interacting partners of HPCAL1 provided first insights at its possible role or function in the retina, it has also pointed out the potential for identifying interacting partners of other NCS proteins using mass spectrometry.
Medicine, Faculty of
Biochemistry and Molecular Biology, Department of
Graduate
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Chen, Ning. "Design Genetic Fluorescent Probes to Detect Protease Activity and Calcium-Dependent Protein-Protein Interactions in Living Cells." Digital Archive @ GSU, 2008. http://digitalarchive.gsu.edu/chemistry_diss/43.

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Proteases are essential for regulating a wide range of physiological and pathological processes. The imbalance of protease activation and inhibition will result in a number of major diseases including cancers, atherosclerosis, and neurodegenerative diseases. Although fluorescence resonance energy transfer (FRET)-based protease probes, a small molecular dye and other methods are powerful, they still have drawbacks or limitations for providing significant information about the dynamics and pattern of endogenous protease activation and inhibition in a single living cell or in vivo. Currently protease sensors capable of quantitatively measuring specific protease activity in real time and monitoring activation and inhibition of enzymatic activity in various cellular compartments are highly desired. In this dissertation, we report a novel strategy to create protease sensors by grafting an enzymatic cleavage linker into a sensitive location for changing chromophore properties of enhanced green fluorescent protein (EGFP) following protease cleavage, which can be used to determine protease activity and track protease activation and inhibition with a ratiometric measurement mode in living cells. Our designed protease sensors exhibit large relative ratiometric optical signal change in both absorbance and fluorescence, and fast response to proteases. Meanwhile, these protease sensors exhibiting high enzymatic selectivity and kinetic responses are comparable or better than current small peptide probes and FRET-based protease probes. Additionally, our protease sensors can be utilized for real-time monitoring of cellular enzymogen activation and effects of inhibitors in living cells. This novel strategy opens a new avenue for developing specific protease sensors to investigate enzymatic activity in real time, to probe disease mechanisms corresponding to proteases in vitro and in vivo, and to screen protease inhibitors with therapeutic effects. Strong fluorescence was still retained in the cleaved EGFP-based protease sensors, which stimulated us to identify the EGFP fragment with fluorescence properties for further understanding chromophore formation mechanisms and investigating protein-protein interactions through fluorescence complementation of split EGFP fragments. Through fusing EF-hand motifs from calbindin D9k to split EGFP fragments, a novel molecular probe was developed to simultaneously track the calcium change or calcium signaling pathways and calcium-dependent protein-protein interaction in living cells in real time.
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Books on the topic "Calcium sensor proteins"

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(Editor), Pavel P. Philippov, and Karl-wilhelm Koch (Editor), eds. Neuronal Calcium Sensor Proteins. Nova Science Publishers, 2006.

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Gombos, Zoltan. Calexcitin B: a new calcium-sensor protein in the nervous system of the squid. 2004.

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Book chapters on the topic "Calcium sensor proteins"

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Ames, James B. "Calcium, Neuronal Sensor Proteins." In Encyclopedia of Metalloproteins, 499–510. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_45.

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Gibhardt, Christine S., Adina Vultur, and Ivan Bogeski. "Measuring Calcium and ROS by Genetically Encoded Protein Sensors and Fluorescent Dyes." In Calcium Signalling, 183–96. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9018-4_17.

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Dolphin, Annette C., Anatole Menon-Johansson, Veronica Campbell, Nick Berrow, and Marva I. Sweeney. "Modulation of Voltage Dependent Calcium Channels by GABAb Receptors and G Proteins in Cultured Rat Dorsal Root Ganglion Neurons: Relevance to Transmitter Release and Its Modulation." In Cellular Mechanisms of Sensory Processing, 47–61. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78762-1_4.

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Fain, Gordon L. "Metabotropic signal transduction." In Sensory Transduction, 57–75. Oxford University Press, 2019. http://dx.doi.org/10.1093/oso/9780198835028.003.0004.

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“Metabotropic signal transduction” is the fourth chapter of the book Sensory Transduction and reviews the structure and function of G-protein cascades, which are essential components of transduction in many sensory receptors. G-protein cascades are found throughout the body and are responsible for mediating the effects of many hormones and synaptic transmitters in the CNS. The chapter describes the components of these cascades, including G-protein-coupled receptors, heterotrimeric G proteins, effector molecules, and second messengers including calcium. It then describes the special properties of channels gated by second messengers, including cyclic-nucleotide-gated channels, which were first discovered in sensory receptors. It concludes with a description of transduction in the lizard parietal eye, where a single cell type can respond to light in two different ways.
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Murugesan, Janaranjani, Ajithkumar Balakrishnan, Premkumar Kumpati, and Hemamalini Vedagiri. "Cellular Functions of ER Chaperones in Regulating Protein Misfolding and Aggregation: An Emerging Therapeutic Approach for Preeclampsia." In Preeclampsia. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.101271.

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Proteinuria is one of the hallmarks of preeclampsia (PE) that differentiates other hypertensive disorders of pregnancy. Protein misfolding and aggregation is an emerging pathological condition underlying many chronic metabolic diseases and neurodegenerative diseases. Recent studies indicate protein aggregation as an emerging biomarker of preeclampsia, wherein several proteins are aggregated and dysregulated in the body fluids of preeclamptic women, provoking the multi-systemic clinical manifestations of the disease. At the cellular level, these misfolded and aggregated proteins are potentially toxic interfering with the normal physiological process, eliciting the unfolded protein response (UPR) pathway activators in the endoplasmic reticulum (ER) that subsequently augments the ER quality control systems to remove these aberrant proteins. ER resident chaperones, folding enzymes and other proteins serve as part of the ER quality control machinery in restoring nascent protein folding. These ER chaperones are crucial for ER function aiding in native protein folding, maintaining calcium homeostasis, as sensors of ER stress and also as immune modulators. Consequently, ER chaperones seems to be involved in many cellular processes, yet the association is expanding to be explored. Understanding the role and mechanism of ER chaperones in regulating protein misfolding and aggregation would provide new avenues for therapeutic intervention as well as for the development of new diagnostic approaches.
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Koch, Christof. "Diffusion, Buffering, and Binding." In Biophysics of Computation. Oxford University Press, 1998. http://dx.doi.org/10.1093/oso/9780195104912.003.0017.

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In Chap. 9 we introduced calcium ions and alluded to their crucial role in regulating the day-to-day life of neurons. The dynamics of the free intracellular calcium is controlled by a number of physical and chemical processes, foremost among them diffusion and binding to a host of different proteins, which serve as calcium buffers and as calcium sensors or triggers. Whereas buffers simply bind Ca2+ above some critical concentration, releasing it back into the cytoplasm when [Ca2+]i has been reduced below this level, certain proteins— such as calmodulin—change their conformation when they bind with Ca2+ ions, thereby activating or modulating enzymes, ionic channels, or other proteins. The calcium concentration inside the cell not only determines the degree of activation of calcium-dependent potassium currents but—much more importantly—is relevant for determining the changes in structure expressed in synaptic plasticity. As discussed in Chap. 13, it is these changes that are thought to underlie learning. Given the relevance of second messenger molecules, such as Ca2+, IP3, cyclic AMP and others, for the processes underlying growth, sensory adaptation, and the establishment and maintenance of synaptic plasticity, it is crucial that we have some understanding of the role that diffusion and chemical kinetics play in governing the behavior of these substances. Today, we have unprecedented access to the spatio-temporal dynamics of intracellular calcium in individual neurons using fluorescent calcium dyes, such as fura-2 or fluo-3, in combination with confocal or two-photon microscopy in the visible or in the infrared spectrum (Tsien, 1988; Tank et al., 1988; Hernández-Cruz, Sala, and Adams, 1990; Ghosh and Greenberg, 1995).
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"Protein-Based Calcium Sensors." In Optical Probes in Biology, 96–111. CRC Press, 2016. http://dx.doi.org/10.1201/b18007-10.

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Thestrup, Thomas, and Oliver Griesbeck. "Protein-Based Calcium Sensors." In Optical Probes in Biology, 73–88. CRC Press, 2015. http://dx.doi.org/10.1201/b18007-6.

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Weiss, Jamie L., and Robert D. Burgoyne. "EF-Hand Proteins and Calcium Sensing: The Neuronal Calcium Sensors." In Handbook of Cell Signaling, 79–82. Elsevier, 2003. http://dx.doi.org/10.1016/b978-012124546-7/50497-6.

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Large, Charles H. "Genetic association of voltage-gated ion channels with psychotic disorders." In Psychotic Disorders, edited by Michael A. P. Bloomfield and Oliver D. Howes, 335–40. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780190653279.003.0037.

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A goal for the treatment of psychotic disorders, such as schizophrenia and bipolar disorder, is to correct the function of neural circuits that have been implicated in the range of symptoms from altered sensory perception to impaired cognition. However, this goal is complicated by the absence of an obvious lesion, genetic mutation, or even a clear disease process. The brains of people with psychotic illness just appear to work differently. Dopamine receptor blocking strategies repress the more florid symptoms of psychosis, but appear to do little to influence the underlying dysfunction of brain circuits, and they do not improve the patient’s cognition. Voltage-gated ion channels (VGICs) are proteins that define neurons: they are required for all aspects of neural processing and signaling. Could modulation of these highly dynamic proteins be useful in the treatment of psychosis? This chapter reviews examples of VGICs that have been linked to psychosis and that may take us toward the goal of better treatments for these devastating disorders. This chapter covers specific examples of chloride, calcium, potassium and VGIC channel pathology associated with psychosis.
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Conference papers on the topic "Calcium sensor proteins"

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Forster, Thilo, Christof Strohhofer, Karlheinz Bock, Peter Kasak, Martin Danko, Zuzana Kronekova, Tomas Nedelcev, Igor Krupa, and Igor Lacik. "Biosensor for calcium based on a hydrogel optical waveguide with integrated sensor proteins." In TRANSDUCERS 2009 - 2009 International Solid-State Sensors, Actuators and Microsystems Conference. IEEE, 2009. http://dx.doi.org/10.1109/sensor.2009.5285877.

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Udomsom, Suruk, Punramon Rattakorn, Ukrit Mankong, Toshimasa Umezawa, Atsushi Matsumoto, Atsushi Kanno, Naokatsu Yamamoto, et al. "Detection of S100 Calcium Binding Protein A6 by Silicon Nitride Photonic Sensor." In 2022 International Electrical Engineering Congress (iEECON). IEEE, 2022. http://dx.doi.org/10.1109/ieecon53204.2022.9741660.

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Reynolds, Stephanie, Jon Onativia, Caroline S. Copeland, Simon R. Schultz, and Pier Luigi Dragotti. "Spike detection using FRI methods and protein calcium sensors: Performance analysis and comparisons." In 2015 International Conference on Sampling Theory and Applications (SampTA). IEEE, 2015. http://dx.doi.org/10.1109/sampta.2015.7148948.

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Reports on the topic "Calcium sensor proteins"

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Yalovsky, Shaul, and Julian Schroeder. The function of protein farnesylation in early events of ABA signal transduction in stomatal guard cells of Arabidopsis. United States Department of Agriculture, January 2002. http://dx.doi.org/10.32747/2002.7695873.bard.

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Loss of function mutations in the farnesyltransferase β subunit gene ERA1 (enhanced response to abscisic acid), cause abscisic acid hypersensitivity in seedlings and in guard cells. This results in slowed water loss of plants in response to drought. Farnesyltransferase (PFT) catalyses the attachment of the 15-carbon isoprenoid farnesyl to conserved cysteine residues located in a conserved C-terminal domain designated CaaX box. PFT is a heterodimeric protein comprised of an a and b sununits. The a subunit is shared between PFT and geranylgeranyltransferase-I (PGGTI) which catalyses the attachemt of the 20-carbon isoprenoid geranylgeranyl to CaaX box proteins in which the last amino acid is almost always leucine and in addition have a polybasic domain proximal to the CaaL box. Preliminary data presented in the proposal showed that increased cytoplasmic Ca2+ concentration in stomal guard cells in response to non-inductive ABA treatements. The goals set in the proposal were to characterize better how PFT (ERA1) affects ABA induced Ca2+ concentrations in guard cells and to identify putative CaaX box proteins which function as negative regulators of ABA signaling and which function is compromised in era1 mutant plants. To achieve these goals we proposed to use camelion Ca2+ sensor protein, high throughput genomic to identify the guard cell transcriptome and test prenylation of candidate proteins. We also proposed to focus our efforts of RAC small GTPases which are prenylated proteins which function in signaling. Our results show that farnesyltransferaseprenylates protein/s that act between the points of ABA perception and the activation of plasma membrane calcium influx channels. A RAC protein designated AtRAC8/AtRop10 also acts in negative regulation of ABA signaling. However, we discovered that this protein is palmitoylated and not prenylated although it contains a C-terminal CXXX motif. We further discovered a unique C-terminal sequence motif required for membrane targeting of palmitoylatedRACs and showed that their function is prenylation independent. A GC/MS based method for expression in plants, purification and analysis of prenyl group was developed. This method would allow highly reliable identification of prenylated protein. Mutants in the shared α subunit of PFT and PGGT-I was identified and characterized and was shown to be ABA hypersensitive but less than era1. This suggested that PFT and PGGT-I have opposing functions in ABA signaling. Our results enhanced the understanding of the role of protein prenylation in ABA signaling and drought resistance in plants with the implications of developing drought resistant plants. The results of our studies were published 4 papers which acknowledge support from BARD.
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