Relevant bibliographies by topics / Kalmodulin

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'Kalmodulin'

Author: Grafiati
Published: 4 June 2021
Last updated: 3 February 2022

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Journal articles on the topic "Kalmodulin"

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Chubinidze, K., B. Partsvania, A. Khuskivadze, P. Burnadze, G. Petriashvili, D. Dzidziguri, and O. Mukbaniani. "Modeling of calmodulin-mediated processes in tissues using calmodulin-functionalized gold nanoparticles and fluorescent dyes." Materiali in tehnologije 54, no. 2 (April 10, 2020): 211–14. http://dx.doi.org/10.17222/mit.2019.080.

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2

Nuñez, Eider, Arantza Muguruza-Montero, Ainhoa Rodriguez de Yurre, Ariane Araujo, Alvaro Villarroel, and Janire Urrutia. "KV7.2 kanala: estruktura, erregulazioa eta kitzikagarritasun neuronalean duen ekintza." EKAIA Euskal Herriko Unibertsitateko Zientzia eta Teknologia Aldizkaria, October 28, 2020. http://dx.doi.org/10.1387/ekaia.21870.

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Potasio-kanalak ia zelula guztien mintzean agertzen dira eta funtzio biologiko garrantzitsuak betetzen dituzte; besteak beste, korronte elektrikoak kontrolatzen dituzte zelula kitzikagarrietan. KV7 kanalen familia 5 kidez osatuta dago (KV7.1-KV7.5) eta hauek kodetzen dituzten geneak patologia esanguratsuekin erlazionatzen dira. KV7 kanalen estrukturak, zelula-mintzean txertaturiko 6 segmentuz osaturiko ohiko estruktura partekatzen du, N- eta C-muturrak zelula barnekoak izanik. Neuronetan, KV7.2 eta KV7.3 dira nagusiki agertzen diren kanalak, M-korrontea sortuz neuronen kitzikagarritasuna kontrolatzen dutelarik. M-korrontearen erregulazioa konplexua da seinaleztapen-bidezidor desberdinen bidez erregula baitaiteke. Gq/11 proteinari akoplaturiko hartzaileen bidez erregulatzen da, seinaleztapen-bidezidorra desberdina izanik aktibatutako hartzailearen arabera. Horrela, azetilkolinaren M1 hartzaile muskarinikoak KV7.2-aren korrontea inhibituko du PIP2-aren agorpenaren ondorioz. Bradikininaren hartzaileak ordea, IP3-ak eragindako kaltzio kontzentrazioaren igoeraren bidez inhibituko du. Mekanismo hauetan, hainbat proteinek hartzen dute parte, hala nola kalmodulina, proteina kinasak eta aingura proteinak. Berrikuspen honetan KV7.2 kanalari erreparatuko diogu, hainbat gaixotasunen partaide izateagatik eta bere erregulazio konplexuagatik, ikuspuntu farmakologiko batetik itu interesgarria izan baitaiteke.
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Dissertations / Theses on the topic "Kalmodulin"

1

Janoušková, Hana. "Charakterizace kalmodulin vazebných míst TRP kanálů." Master's thesis, 2009. http://www.nusl.cz/ntk/nusl-286920.

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Jarosilová, Kateřina. "Příprava a charakterizace Ca2+/kalmodulin-dependentní protein kinasy kinasy 2 (CaMKK2)." Master's thesis, 2017. http://www.nusl.cz/ntk/nusl-354625.

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Calmodulin kinase cascade is a signaling pathway which is involved in the response to the increasing intracellular calcium levels. Ca2+ is a ubiquitous second messenger which promotes wide-range of cellular signaling events. Many of these signaling pathways start with the binding of Ca2+ to its primary intracellular receptor calmodulin. Calmodulin in turn binds to its downstream targets in the Ca2+ /calmodulin signaling cascade. One of the most important enzymes of this cascade is a Ca2+ /calmodulin-dependent protein kinase kinase 2 (CaMKK2). CaMKK2 is a serine/threonine protein kinase which regulates for example gene transcription or energy homeostasis by phosphorylation of its downstream targets. Catalytic domain (which provides kinase activity) is located in the middle part of the protein and possesses structure typical for kinases. CaMKK2 consists of 588 amino acids but the secondary structure is known only for the region of the kinase domain (298 residues). The rest of the protein is assumed to be unstructured as long as CaMKK2 is not bound to any interaction partner. The aim of this study was to prepare several constructs of human isoform of CaMKK2 for the further structural and activity studies. It is believed that CaMKK2 is regulated by site-specific phosphorylation. Phosphorylation of some...
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3

Bílý, Jan. "Charakterizace vazebných míst na intracelulárních koncích TRPC6 receptoru pro kalmodulin a S100A1." Doctoral thesis, 2016. http://www.nusl.cz/ntk/nusl-353443.

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Identification of the binding sites on transient receptor potential cation channel TRPC6 for Calmodulin and S100A1 The TRP (transient receptor potential) group of ion channels represents a large subset of membrane receptors. A part of this supergroup are canonical TRPC channels with a sequence homology analogical to TRP receptor first discovered at fruit fly (Drosophila melanogaster). These membrane channels are involved in a variety of physiological functions in different cell types and tissues. TRPC6 is a non-selective cation channel that modulates the calcium level in eukaryotic cells (including sensory receptor cells) in response to external signals. TRPC6 channel contains binding domain CIBR (Calmodulin inositol binding region), which is also able to adapt to calcium binding protein S100A1. Characterisation of the integrative binding site for calmodulin (CaM) and S100A1 at the C-tail of TRPC6 is presented in this work. Using site-directed mutagenesis, soluble protein fragments TRPC6 CT (801-787) were prepared with intentional changes in amino acid sequence. Several positively charged amino acid residues (Arg852, Lys856, Lys859, Arg860 and Arg864) were determined by measurement of fluorescence anisotropy influence and their participation in the calcium-dependent binding of CaM and/or S100A1 to...
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4

Gerych, Tomáš. "Studium vlivu sarkosinu na kalmodulinem-zprostředkovanou vnitrobuněčnou signalizaci." Master's thesis, 2019. http://www.nusl.cz/ntk/nusl-427871.

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The following diploma thesis titled Effects of sarcosine on calmodulin-dependent intracellular signalization is dedicated to analyzation of current findings in the area of increased sarcosine levels effects to calmodulin and calmodulin dependent kinases mediated intracellular signalization and experimental verification of these findings on malignant and non-malignant cell cultures of prostate origin. Use of sarcosine as a possible marker of prostate cancer is an assumption for elaboration of this diploma thesis. Diagnostics of prostate cancer could be simpler and more effective in case of its confirmation as a usable marker by availability of simple home-testing kits reacting on sarcosine level in urine of tested individual.
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5

Mikulů, Martina. "Studium struktury komplexů proteinu 14-3-3 s CaMKK1 a CaMKK1:Ca2+/CaM." Master's thesis, 2020. http://www.nusl.cz/ntk/nusl-434037.

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The Ca2+ -signaling pathway is an important mechanism of cell signaling. Ca2+ /Cal- modulin (CaM)-dependent protein kinases (CaMKs) are members of Ser/Thr protein kinase family. CaMKs are regulated by Ca2+ /CaM binding in response to increase in intracellular level of Ca2+ . An important member of this protein family is Ca2+ /CaM- dependent protein kinase kinase (CaMKK), which is an upstream activator of CaMKI and CaMKIV. There are two isoforms of CaMKK, CaMKK1 and CaMKK2. CaMKK1 is regulated not only by Ca2+ /CaM-binding, but also by phosphorylation by cAMP-dependent protein kinase A (PKA). PKA phosphorylation induces inter- action with the 14-3-3 proteins. Previous studies of interaction between CaMKK1 and 14-3-3 proteins suggested, that the interaction with 14-3-3 proteins keeps CaMKK1 in the PKA-induced inhibited state and blocks its active site. However, the exact mecha- nism of this inhibition is still unclear mainly due to the absence of structural data. Main aim of this diploma thesis was to characterize the protein complexes between CaMKK1, Ca2+ /CaM and 14-3-3γ using analytical ultracentrifugation, small angle X-ray scattering, and chemical cross-linking coupled to mass spectrometry. Analytical ultracentrifugation revealed concentration-dependent dimerization of CaMKK1, which is...
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Koupilová, Nicola. "Strukturní charakterizace lidské proteinkinasy CaMKK2 a jejích interakcí s vazebnými partnery." Master's thesis, 2021. http://www.nusl.cz/ntk/nusl-448762.

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5 Abstract Ca2+/calmodulin-dependent protein kinase kinase 2 (CaMKK2) belongs to the serine/ threonine protein kinase family, which is involved in the calcium signaling pathway. The increase of intracellular calcium concentration induces the activation of calmodulin (CaM), which then activates its binding partners including CaMKII, CaMKIII, CaMKK1 and CaMKK2. CaMKK2 activates CaMKI, CaMKIV and AMP-dependent kinase, AMPK, by phosphorylation. CaMKK2 is naturally present in cells in an autoinhibited state, which is caused by the steric hindrance of the active site by the autoinhibitory domain. When calmodulin binds to the calmodulin-binding domain, the autoinhibitory domain is removed and the active site becomes accessible. Upon activation, CaMKK2 undergoes autophosphorylation, which increases its enzyme activity. Negative regulation of CaMKK2 is mediated by cAMP-dependent protein kinase A (PKA)- and GSK3-dependent phosphorylation. Sites phosphorylated by PKA have been identified for both CaMKK1 and CaMKK2. Two of them are also motifs recognized by scaffolding 14-3-3 proteins. Previous studies have shown that the 14-3-3 protein binding maintains phosphorylated CaMKK2 in an inhibited state by blocking the dephosphorylation of S495, which prevents the binding to calmodulin. However, it is unclear if it is the...
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