Relevant bibliographies by topics / AMPK signalling

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  1. Journal articles
  2. Dissertations / Theses
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  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'AMPK signalling'

Author: Grafiati
Published: 10 January 2023
Last updated: 28 January 2023

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Journal articles on the topic "AMPK signalling"

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Baumann, Philipp, Sonja Mandl-Weber, Bertold Emmerich, Christian Straka, Daniel Franke, and Ralf Schmidmaier. "Myeloma Cell Proliferation Is Inhibitied by the Activation of Adenosine Monophosphate Activated Protein Kinase (AMPK)." Blood 108, no. 11 (November 16, 2006): 5045. http://dx.doi.org/10.1182/blood.v108.11.5045.5045.

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Abstract In multiple myeloma (MM), a network of cytokines in the bone marrow microenvironment promotes myeloma cell proliferation. Consequent inhibition of intracellular signalling in the myeloma cells seems to be a promising strategy to encounter disease progression. The multiple myeloma cell lines U266, OPM-2, RPMI-8226 and NCI-H929 were incubated with the AMPK activators AICAr and D942. Basal and cytokine stimulated proliferation rates of myeloma cells were measured by the WST-1 assay. Alterations of the cell cycle were determined by flow cytometry after staining with propidium iodide. Intracellular signalling was shown by western blotting. The AMPK activators 5-aminoimidazole-4-carboxamide (AICAr) and D942 induced inhibition of proliferation in multiple myeloma cell lines. AICAr also induced a S-phase cell cycle arrest in all four tested cell lines and led to phosphorylation and herewith activation of AMPK. Furthermore, the inhibition of a nucleoside transporter by nitrobenzyl-thio-9-β-D-ribofuranosylpurine (NBTI), inhibition of the adenosine kinase by iodotubericidine and inhibition of AMPK by AMPKI Compound C reversed AICAr effects, indicating that the cellular effects of AICAr were mediated by AMPK. Activation of AMPK inhibited basal extracellular-signal regulated kinase (ERK), mTOR and P70S6 kinase (P70S6K) signalling and blocked cytokine induced increase of proliferation, which again was due to inhibition of ERK and P70S6K signalling. Troglitazone, a representative of a group of anti-diabetic drugs, similarly inhibited myeloma cell proliferation, activated AMPK and decreased ERK and P70S6K signalling. We demonstrate for the first time that myeloma cell proliferation is controlled by AMPK activity. Consequently, targeting this pathway by inhibitors like glitazones provides a novel strategy in myeloma therapy.
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Shukal, Dhaval K., Pooja B. Malaviya, and Tusha Sharma. "Role of the AMPK signalling pathway in the aetiopathogenesis of ocular diseases." Human & Experimental Toxicology 41 (January 2022): 096032712110631. http://dx.doi.org/10.1177/09603271211063165.

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Background AMP-activated protein kinase (AMPK) plays a precise role as a master regulator of cellular energy homeostasis. AMPK is activated in response to the signalling cues that exhaust cellular ATP levels such as hypoxia, ischaemia, glucose depletion and heat shock. As a central regulator of both lipid and glucose metabolism, AMPK is considered to be a potential therapeutic target for the treatment of various diseases, including eye disorders. Objective To review all the shreds of evidence concerning the role of the AMPK signalling pathway in the pathogenesis of ocular diseases. Method Scientific data search and review of available information evaluating the influence of AMPK signalling on ocular diseases. Results Review highlights the significance of AMPK signalling in the aetiopathogenesis of ocular diseases, including cataract, glaucoma, diabetic retinopathy, retinoblastoma, age-related macular degeneration, corneal diseases, etc. The review also provides the information on the AMPK-associated pathways with reference to ocular disease, which includes mitochondrial biogenesis, autophagy and regulation of inflammatory response. Conclusion The study concludes the role of AMPK in ocular diseases. There is growing interest in the therapeutic utilization of the AMPK pathway for ocular disease treatment. Furthermore, inhibition of AMPK signalling might represent more pertinent strategy than AMPK activation for ocular disease treatment. Such information will guide the development of more effective AMPK modulators for ocular diseases. [Formula: see text]
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Heidorn-Czarna, Malgorzata, Herbert-Michael Heidorn, Sanjanie Fernando, Oana Sanislav, Wieslawa Jarmuszkiewicz, Rupert Mutzel, and Paul R. Fisher. "Chronic Activation of AMPK Induces Mitochondrial Biogenesis through Differential Phosphorylation and Abundance of Mitochondrial Proteins in Dictyostelium discoideum." International Journal of Molecular Sciences 22, no. 21 (October 28, 2021): 11675. http://dx.doi.org/10.3390/ijms222111675.

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Mitochondrial biogenesis is a highly controlled process that depends on diverse signalling pathways responding to cellular and environmental signals. AMP-activated protein kinase (AMPK) is a critical metabolic enzyme that acts at a central control point in cellular energy homeostasis. Numerous studies have revealed the crucial roles of AMPK in the regulation of mitochondrial biogenesis; however, molecular mechanisms underlying this process are still largely unknown. Previously, we have shown that, in cellular slime mould Dictyostelium discoideum, the overexpression of the catalytic α subunit of AMPK led to enhanced mitochondrial biogenesis, which was accompanied by reduced cell growth and aberrant development. Here, we applied mass spectrometry-based proteomics of Dictyostelium mitochondria to determine the impact of chronically active AMPKα on the phosphorylation state and abundance of mitochondrial proteins and to identify potential protein targets leading to the biogenesis of mitochondria. Our results demonstrate that enhanced mitochondrial biogenesis is associated with variations in the phosphorylation levels and abundance of proteins related to energy metabolism, protein synthesis, transport, inner membrane biogenesis, and cellular signalling. The observed changes are accompanied by elevated mitochondrial respiratory activity in the AMPK overexpression strain. Our work is the first study reporting on the global phosphoproteome profiling of D. discoideum mitochondria and its changes as a response to constitutively active AMPK. We also propose an interplay between the AMPK and mTORC1 signalling pathways in controlling the cellular growth and biogenesis of mitochondria in Dictyostelium as a model organism.
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Steinberg, Gregory, R. "Cytokine Regulation of AMPK signalling." Frontiers in Bioscience Volume, no. 14 (2009): 1902. http://dx.doi.org/10.2741/3350.

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Lim, Chung Thong, Blerina Kola, and Márta Korbonits. "AMPK as a mediator of hormonal signalling." Journal of Molecular Endocrinology 44, no. 2 (July 22, 2009): 87–97. http://dx.doi.org/10.1677/jme-09-0063.

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AMP-activated protein kinase (AMPK) is a key molecular player in energy homeostasis at both cellular and whole-body levels. AMPK has been shown to mediate the metabolic effects of hormones such as leptin, ghrelin, adiponectin, glucocorticoids and insulin as well as cannabinoids. Generally, activated AMPK stimulates catabolic pathways (glycolysis, fatty acid oxidation and mitochondrial biogenesis) and inhibits anabolic pathways (gluconeogenesis, glycogen, fatty acid and protein synthesis), and has a direct appetite-regulating effect in the hypothalamus. Drugs that activate AMPK, namely metformin and thiazolidinediones, are often used to treat metabolic disorders. Thus, AMPK is now recognised as a potential target for the treatment of obesity and associated co-morbidities.
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Okada, Motohiro, Kouji Fukuyama, and Eishi Motomura. "Dose-Dependent Biphasic Action of Quetiapine on AMPK Signalling via 5-HT7 Receptor: Exploring Pathophysiology of Clinical and Adverse Effects of Quetiapine." International Journal of Molecular Sciences 23, no. 16 (August 14, 2022): 9103. http://dx.doi.org/10.3390/ijms23169103.

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Recent pharmacological studies indicated that the modulation of tripartite-synaptic transmission plays important roles in the pathophysiology of schizophrenia, mood disorders and adverse reactions. Therefore, to explore the mechanisms underlying the clinical and adverse reactions to atypical antipsychotics, the present study determined the effects of the sub-chronic administration of quetiapine (QTP: 3~30 μM) on the protein expression of 5-HT7 receptor (5-HT7R), connexin43 (Cx43), cAMP level and intracellular signalling, Akt, Erk and adenosine monophosphate-activated protein kinase (AMPK) in cultured astrocytes and the rat hypothalamus, using ultra-high-pressure liquid chromatography with mass spectrometry and capillary immunoblotting systems. QTP biphasically increased physiological ripple-burst evoked astroglial D-serine release in a concentration-dependent manner, peaking at 10 μM. QTP enhanced the astroglial signalling of Erk concentration-dependently, whereas both Akt and AMPK signalling’s were biphasically enhanced by QTP, peaking at 10 μM and 3 μM, respectively. QTP downregulated astroglial 5-HT7R in the plasma membrane concentration-dependently. Protein expression of Cx43 in astroglial cytosol and intracellular cAMP levels were decreased and increased by QTP also biphasically, peaking at 3 μM. The dose-dependent effects of QTP on the protein expression of 5-HT7R and Cx43, AMPK signalling and intracellular cAMP levels in the hypothalamus were similar to those in astrocytes. These results suggest several complicated pharmacological features of QTP. A therapeutically relevant concentration/dose of QTP activates Akt, Erk and AMPK signalling, whereas a higher concentration/dose of QTP suppresses AMPK signalling via its low-affinity 5-HT7R inverse agonistic action. Therefore, 5-HT7R inverse agonistic action probably plays important roles in the prevention of a part of adverse reactions of QTP, such as weight gain and metabolic complications.
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Strembitska, Anastasiya, Sarah Mancini, Jonathan Gamwell, Timothy Palmer, George Baillie, and Ian Salt. "A769662 Inhibits Insulin-Stimulated Akt Activation in Human Macrovascular Endothelial Cells Independent of AMP-Activated Protein Kinase." International Journal of Molecular Sciences 19, no. 12 (December 5, 2018): 3886. http://dx.doi.org/10.3390/ijms19123886.

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Protein kinase B (Akt) is a key enzyme in the insulin signalling cascade, required for insulin-stimulated NO production in endothelial cells (ECs). Previous studies have suggested that AMP-activated protein kinase (AMPK) activation stimulates NO synthesis and enhances insulin-stimulated Akt activation, yet these studies have largely used indirect activators of AMPK. The effects of the allosteric AMPK activator A769662 on insulin signalling and endothelial function was therefore examined in cultured human macrovascular ECs. Surprisingly, A769662 inhibited insulin-stimulated NO synthesis and Akt phosphorylation in human ECs from umbilical veins (HUVECs) and aorta (HAECs). In contrast, the AMPK activators compound 991 and AICAR had no substantial inhibitory effect on insulin-stimulated Akt phosphorylation in ECs. Inhibition of AMPK with SBI-0206965 had no effect on the inhibition of insulin-stimulated Akt phosphorylation by A769662, suggesting the inhibitory action of A769662 is AMPK-independent. A769662 decreased IGF1-stimulated Akt phosphorylation yet had no effect on VEGF-stimulated Akt signalling in HUVECs, suggesting that A769662 attenuates early insulin/IGF1 signalling. The effects of A769662 on insulin-stimulated Akt phosphorylation were specific to human ECs, as no effect was observed in the human cancer cell lines HepG2 or HeLa, as well as in mouse embryonic fibroblasts (MEFs). A769662 inhibited insulin-stimulated Erk1/2 phosphorylation in HAECs and MEFs, an effect that was independent of AMPK in MEFs. Therefore, despite being a potent AMPK activator, A769662 has effects unlikely to be mediated by AMPK in human macrovascular ECs that reduce insulin sensitivity and eNOS activation.
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Carling, David. "AMPK signalling in health and disease." Current Opinion in Cell Biology 45 (April 2017): 31–37. http://dx.doi.org/10.1016/j.ceb.2017.01.005.

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Ahwazi, Danial, Katyayanee Neopane, Greg R. Markby, Franziska Kopietz, Ashley J. Ovens, Morten Dall, Anna S. Hassing, et al. "Investigation of the specificity and mechanism of action of the ULK1/AMPK inhibitor SBI-0206965." Biochemical Journal 478, no. 15 (August 10, 2021): 2977–97. http://dx.doi.org/10.1042/bcj20210284.

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SBI-0206965, originally identified as an inhibitor of the autophagy initiator kinase ULK1, has recently been reported as a more potent and selective AMP-activated protein kinase (AMPK) inhibitor relative to the widely used, but promiscuous inhibitor Compound C/Dorsomorphin. Here, we studied the effects of SBI-0206965 on AMPK signalling and metabolic readouts in multiple cell types, including hepatocytes, skeletal muscle cells and adipocytes. We observed SBI-0206965 dose dependently attenuated AMPK activator (991)-stimulated ACC phosphorylation and inhibition of lipogenesis in hepatocytes. SBI-0206965 (≥25 μM) modestly inhibited AMPK signalling in C2C12 myotubes, but also inhibited insulin signalling, insulin-mediated/AMPK-independent glucose uptake, and AICA-riboside uptake. We performed an extended screen of SBI-0206965 against a panel of 140 human protein kinases in vitro, which showed SBI-0206965 inhibits several kinases, including members of AMPK-related kinases (NUAK1, MARK3/4), equally or more potently than AMPK or ULK1. This screen, together with molecular modelling, revealed that most SBI-0206965-sensitive kinases contain a large gatekeeper residue with a preference for methionine at this position. We observed that mutation of the gatekeeper methionine to a smaller side chain amino acid (threonine) rendered AMPK and ULK1 resistant to SBI-0206965 inhibition. These results demonstrate that although SBI-0206965 has utility for delineating AMPK or ULK1 signalling and cellular functions, the compound potently inhibits several other kinases and critical cellular functions such as glucose and nucleoside uptake. Our study demonstrates a role for the gatekeeper residue as a determinant of the inhibitor sensitivity and inhibitor-resistant mutant forms could be exploited as potential controls to probe specific cellular effects of SBI-0206965.
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Neumann, Dietbert, and Benoit Viollet. "AMP-Activated Protein Kinase Signalling." International Journal of Molecular Sciences 20, no. 3 (February 12, 2019): 766. http://dx.doi.org/10.3390/ijms20030766.

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Dissertations / Theses on the topic "AMPK signalling"

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Mancini, Sarah J. "Regulation of inflammatory signalling in adipocytes by AMPK." Thesis, University of Glasgow, 2014. http://theses.gla.ac.uk/5130/.

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AMP-activated protein kinase (AMPK) has been proposed to be a potential therapeutic target for patients with Type 2 diabetes and the metabolic syndrome. While the role of AMPK in muscle and liver is relatively well-characterised, less is known about the role of AMPK in the other principal metabolic tissue, adipose. Obesity is associated with the chronic, sub-clinical inflammation of adipose tissue. Characteristic hypertrophic adipocytes and the elevated infiltration and activation of macrophages stimulate production of cytokines and chemokines, including tumour necrosis factor-alpha (TNF-a), interleukin-1 beta (IL-1beta), interleukin-6 (IL-6) and monocyte chemoattractant protein-1 (MCP-1). These have autocrine, paracrine and endocrine effects which have been suggested to play a key role in the development of peripheral insulin resistance. Increasing evidence suggests that AMPK has anti-inflammatory actions, independent of its effect on carbohydrate and lipid metabolism. Previous work in our laboratory has demonstrated that AMPK inhibits TNF-alpha-stimulated MCP-1 secretion and monocyte adhesion in endothelial cells. The role of AMPK in the regulation of inflammatory signalling in adipocytes is currently poorly characterised. To address this, the effect of AMPK activation on the phosphorylation of TNF-alpha/IL-1beta and IL-6 signalling pathway intermediates was initially assessed in cultured 3T3-L1 adipocytes. Furthermore, the molecular mechanism by which AMPK elicits these effects was investigated. In addition, the effect of AMPK activation on downstream functional consequences of proinflammatory signalling in 3T3-L1 adipocytes and RAW 264.7 macrophages were examined. Finally, the effect of macrophage AMPK activation on inflammation-induced insulin resistance in 3T3-L1 adipocytes was also investigated. A769662 and infection with adenovirus expressing a constitutively active AMPK mutant suppressed IL-1beta-stimulated NFkappaB nuclear translocation in 3T3-L1 adipocytes. Conversely, this was abrogated upon adenoviral expression of a dominant negative AMPK mutant. In line with this, phosphorylation of upstream IkappaBalpha and IKK were also ameliorated upon AMPK activation. In parallel, A769662-mediated AMPK activation inhibited TNF-alpha/IL-1beta-stimulated phosphorylation of JNK, ERK1/2 and p38 MAPKs in 3T3-L1 adipocytes. Furthermore, A769662-mediated inhibition of TNF-alpha/IL-1beta proinflammatory signalling was likely to be independent of endothelial nitric oxide synthase (eNOS) activation and subsequent nitric oxide production. The target of AMPK may be downstream of TAK1, as IKK, JNK and p38 are inhibited in response to both TNF-alpha and IL-1beta; however the mechanism by which AMPK elicits these effects remains to be elucidated. A769662-mediated AMPK activation inhibited phosphorylation of IL-6-stimulated STAT3 (signal transducer and activator of transcription 3) in 3T3-L1 adipocytes independently of phosphatase action, yet A769662 was unable to inhibit constitutive Janus kinase (JAK)-mediated phosphorylation of STAT3, suggesting AMPK may inhibit JAK activity. Inhibition of mTOR was found to suppress STAT3 phosphorylation in a manner mutually exclusive with A769662 stimulation, potentially via activation of T cell protein tyrosine phosphatase (TC-PTP). Adipose tissue from AMPKalpha1-/- mice demonstrated increased basal JNK and STAT3 phosphorylation, further providing evidence for an anti-inflammatory role for AMPK in adipose tissue. In 3T3-L1 adipocytes, A769662 abrogated cytokine-stimulated MCP-1 gene expression, and secretion of chemokines IP-10 (CXCL10), KC (CXCL1) and MCP-1. Furthermore, AMPK activation reduced secretion of IL-5, MCP-1 and MIP-1alpha, but not TNF-alpha, from proinflammatory RAW 264.7 macrophages. Preliminary results indicated that chronic IL-6 and acute TNF-alpha or IL-1beta exposure suppressed insulin-stimulated glucose transport in 3T3-L1 adipocytes. Conditioned medium from activated RAW 264.7 macrophages also inhibited 3T3-L1 adipocyte insulin sensitivity; however, prior AMPK activation failed to attenuate this, potentially as a result of the presence of TNF-alpha. Overall these results suggest that activation of AMPK inhibits activation of multiple distinct proinflammatory signalling pathways in adipocytes and macrophages. AMPK activation may suppress IL-6 signalling via regulation of JAK, while the AMPK-mediated inhibition of IKK and concomitant suppression of MAPKs in response to TNF-alpha/IL-1beta suggests TAK1 as a potential AMPK target. Finally, proinflammatory stimuli induce insulin resistance in adipocytes, however whether this can be rescued by AMPK activation remains to be fully elucidated.
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Ovens, Ashley John. "Moving towards isoform-specific AMPK activation." Phd thesis, Australian Catholic University, 2021. https://acuresearchbank.acu.edu.au/download/368ef3f9b6ef00c34227af8bea2a17693253138f442217dfd893f8986519d895/36925900/Ovens_2021_Moving_towards_isoform-specific_AMPK_activation.pdf.

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The AMP-activated protein kinase (AMPK) αβγ heterotrimer is a highly conserved serine/threonine protein kinase that acts as a metabolic fuel sensor and is crucial for maintaining cellular energy homeostasis. Mammalian AMPK forms complexes in a 1:1:1 ratio made of unique subunit isoform variations (α1, α2, β1, β2, γ1, γ2, γ3) that allow for 12 distinct AMPK complexes to form, where each complex is subject to a range of modifications such as phosphorylation. Each isoform exhibits distinct tissue-expression signatures, α2 and β2 are expressed in a range of tissues but display high expression in skeletal muscle and γ3 shows the highest selectivity being exclusively expressed in skeletal muscle with small amounts recently found in brown adipose tissue. The majority of direct allosteric AMPK activators bind at a hydrophobic binding pocket formed between the α and β subunits, termed the allosteric drug and metabolite site (ADaM site). AMPK is capable of stimulating glucose uptake independently of insulin signalling, where activating AMPK using ADaM site activators has been shown to improve key hallmarks of type 2 diabetes mellitus (T2DM). Despite this, recent studies show that chronically stimulating all 12 AMPK complexes (pan activation) is detrimental as it can lead to hypertrophic cardiomyopathy. This precludes pan activators from progressing to clinical trials. The current direction for the field is to develop isoform-specific activators that target AMPK expressed in select tissues. For the treatment of T2DM it is beneficial to target skeletal muscle as it is the primary site for glucose disposal, hence, α2, β2, and γ3 isoforms are the most favourable to target. This can be achieved by developing α2β2-specific ADaM site compounds or with novel drugs targeting γ3 directly. Despite this, the current knowledge on isoform-specific AMPK regulation is limited, in particular the regulation by a range of phosphorylation sites across each subunit, the functional role of an NH2-terminal extension (NTE) unique to the γ3 subunit, and the structural mechanism for the isoform specificity of the currently limited range of direct allosteric activators. Therefore, the goal of this thesis is to tackle each of these questions to ultimately aid the field in the development of isoform-specific AMPK activators. Our lab recently characterised the ADaM site activator SC4 as not only α2-selective, but also as a potent β2 activator. In Chapter 2 I perform structure/function analysis of SC4 by substituting the 2-hydroxyphenyl group with polar-substituted cyclohexene-based probes. This resulted in the formation of two compounds, MSG010 and MSG011, that do not display α2-selectivity and are hence classified as pan activators. A crystal structure of MSG011 complexed to AMPK α2β1γ1 revealed a similar binding mode to SC4. Interestingly, it highlighted the absence of an interaction that we saw in the SC4/α2β1γ1 crystal structure between the SC4 2-hydroxyphenyl group and α2K31, which may be important for directing α2-selectivity. These findings will guide future design of α2β2-selective AMPK activators. In addition, MSG010 and MSG011 will serve as important tool compounds in AMPK research as they are most potent pan activators available to date. In Chapter 3 I use a targeted mass spectrometry approach to generated precise phosphorylation stoichiometry profiles of 18 phosphorylation sites across all 12 AMPK complexes. This uncovered important isoform-specific differences, particularly in the basal level of βS108 phosphorylation which is located in the ADaM site and dictates the potency of most activators. Mechanistic target of rapamycin complex 1 (mTORC1) is a nutrient-sensitive protein kinases that governs cell growth and proliferation. It has been known for some time that AMPK inhibits mTORC1 activity by phosphorylation, and our lab recently discovered AMPK is directly phosphorylated by mTORC1 on α2S345 to suppress activity, forming a fundamental negative feedback loop. I found seven phosphorylation sites on AMPK were sensitive to pharmacological mTORC1 inhibition, including four in the unique γ2-NTE and α2S377 which is located in the nucleotide-sensing motif. In particular, β1S182 and β2S184 were found to be mTORC1 substrates in vitro and near-maximally phosphorylated under cellular growth conditions. Lastly, I identify two phosphorylation sites on the γ3-NTE. Despite γ3 being a promising therapeutic target, it is yet to undergo rigorous biochemical characterisation leaving it without a solved crystal or cryoEM structure and the function of its NTE remains unknown. In Chapter 4 I discover that removal of the γ3-NTE results in elevated AMPK activity, suggesting it contains an autoinhibitory region. Furthermore, I detected a direct interaction between the γ3-NTE and the α2 kinase domain which may partly explain the mechanism for AMPK autoinhibition. I characterise one of the γ3-NTE phosphorylation sites I discovered in Chapter 3, γ3S14, identifying it as an autophosphorylation site in vitro and in cellulo with the potential for alternative upstream kinases in cellulo.
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Dandapani, Madhumita. "The AMPK signalling pathway in cancer and DNA damage." Thesis, University of Dundee, 2013. https://discovery.dundee.ac.uk/en/studentTheses/9a3ca91b-dd8b-4407-bed2-cd9dd4c00ca7.

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Narbonne, Patrick. "Roles of LKB1/AMPK signalling in the «C.elegans» dauer larva." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=32247.

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Many organisms can execute a dormant state or diapause to survive harsh environmental conditions for extended durations. When Caenorhabditis elegans larvae enter the dauer diapause, they completely arrest development and feeding, but remain active and motile, yet become stress-resistant and extremely long-lived. Entry into dauer is associated with a reduction in insulin-like signalling, the establishment of a generalized cell cycle arrest, the accumulation of nutritive resources and a concomitant global change in metabolism. The precise molecular and physiological processes that induce cell cycle quiescence and enable long-term survival in the absence of caloric intake however remain largely unknown. I show here that the C. elegans orthologs of PTEN, STRAD, LKB1 and AMPK (α1, α2, β1, β2 subunits) cooperate to establish quiescence in the germline stem cell population during dauer development. Interestingly, germline mutations in LKB1 cause predisposition to cancer in humans, while mutations in STRAD or AMPK subunits do not seem to cause cancer. In C. elegans, LKB1 also regulates embryonic polarity, while STRAD and AMPK are dispensable for this process. Thus, my data suggest that LKB1/STRAD regulate cell growth/proliferation through AMPK, while LKB1 also acts independently to regulate polarity, and that this function may be critical for tumor suppression in human. In addition, I show that C. elegans larvae that lack LKB1/AMPK signalling rapidly consume their stored energy and prematurely expire following vital organ failure. This signalling pathway acts in adipose-like tissues to downregulate triglyceride hydrolysis so that these fat reserves are rationed to last the
Plusieurs organismes peuvent entrer en dormance, ou diapause, pour survivre à des conditions environnementales précaires pour une durée prolongée. Lorsque des larves de Caenorhabditis elegans entrent en diapause dauer, elles cessent complètement de se développer ainsi que de se nourrir, cependant elles demeurent actives et mobiles, tout en acquérant une résistance au stress et une longévité extrême. L'entrée en stade dauer est accompagnée d'une réduction de signalisation par l'insuline, de l'établissement d'un arrêt généralisé du cycle cellulaire, de l'accumulation de ressources nutritives et d'un changement global au niveau du métabolisme. Les processus physiologiques et moléculaires précis qui induisent la quiescence cellulaire et permettent la survie prolongée en l'absence de tout apport calorique, demeurent toutefois essentiellement inconnus. Je montre ici que les orthologues de PTEN, STRAD, LKB1 et de AMPK (sous-unités α1, α2, β1, β2) chez C. elegans coopèrent dans l'optique d'établir la quiescence cellulaire dans la population de cellules germinales souches durant le développement de la larve dauer. Il est intéressant de préciser que chez l'humain, une mutation de LKB1 dans la lignée germinale provoque une prédisposition au cancer, tandis qu'une mutation dans une sous-unité de STRAD ou d'AMPK ne semble pas causer de cancer. Chez C. elegans, LKB1 régule aussi la polarité embryonnaire, tandis que STRAD et AMPK sont dispensables pour ce processus. Donc, mes données suggèrent que LKB1/STRAD régulent la croissance et la prolifération des cellules à travers AMPK, tandis que LKB1 fonctionne aussi indépendamment pour contrôler
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Hinchy, Elizabeth. "How cellular ATP/ADP ratios and reactive oxygen species affect AMPK signalling." Thesis, University of Cambridge, 2017. https://www.repository.cam.ac.uk/handle/1810/270029.

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Mitochondria are key generators of cellular ATP, vital to complex life. Historically, mitochondrial generation of reactive oxygen species (ROS) was considered to be an unregulated process, produced by dysfunctional mitochondria. More recently, mitochondrial ROS generated by complex I, particularly by the process of reverse electron transfer (RET), has emerged as a potentially biologically relevant signal that is tightly-regulated and dependent on mitochondrial status. ROS production by RET is reported to play a role in the innate immune response and lifespan extension in fruit flies. One way in which mitochondrial ROS may behave as a signal is by altering the activity of AMP-activated protein kinase (AMPK), a key metabolic sensor and regulator of cell metabolism, which is activated when cellular ATP levels decrease during energy demand. Mitochondria can signal to AMPK via the magnitude of the cellular ATP/AMP and ATP/ADP ratios, which alter in response to mitochondrial function. Our view is mitochondria may also signal to AMPK via ROS. Important studies have helped to clarify the role of exogenous or cytosolic ROS in AMPK regulation. However, the effects of mitochondrial ROS on AMPK activity, specifically that generated by complex I, remain unclear and is the main focus of this thesis. I characterized the effects of exogenous H2O2 on cellular AMPK activity, ATP/ADP ratios and cellular redox state in a cell model. I then compounded this with selective mitochondria generated ROS by the mitochondria-targeted redox-cycler, MitoParaquat (MPQ). AMPK activity appeared to correlate with decreasing cell ATP/ADP ratios, indicating that both sources of ROS primarily activate AMPK in an AMP/ADP-dependent mechanism. In parallel, I developed an approach for analyzing the redox state of candidate proteins, an important step in determining if a protein is directly regulated by ROS. I also initiated development of a cell model for studying the downstream effects of mitochondrial ROS production by RET, by expressing alternative respiratory enzymes in a mammalian cell line.
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Speirs, Claire. "Examination of potential mechanisms linking AMPK to inhibition of IL-6 signalling." Thesis, University of Glasgow, 2017. http://theses.gla.ac.uk/8185/.

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Considerable recent evidence supports the role of AMP-activated protein kinase (AMPK) as an anti-inflammatory mediator, yet the mechanisms of its anti-inflammatory actions are only starting to be unravelled. Inappropriate cytokine stimulated Janus kinase (JAK)-signal transducer and activator of transcription (STAT) signalling is a key feature of many pro-inflammatory events, including atherogenesis. Previous unpublished studies in our group have investigated whether AMPK modifies cytokine stimulation of JAK-STAT signalling in HUVECs. These preliminary investigations demonstrated that pre-treatment of HUVECs with AMPK activator, A769662, significantly inhibits both sIL-6Rα/IL-6 and IFN-α stimulation of STAT3 Tyr705 phosphorylation in HUVECs. IFN-α activates STATs via an IFNα/β receptor 1 (IFNAR1/IFNAR2) complex which is distinct from the sIL-6Rα/IL-6/gp130 complex. The studies in this thesis therefore tested the hypothesis that AMPK was exerting its inhibitory effects at one or more common signalling loci downstream of IFNAR1/IFNAR2 and gp130 at a post-receptor level. First, it was investigated whether AMPK exerts its inhibitory effects on JAK-STAT signalling via a known regulator of JAK or STAT, or an AMPK downstream target known to either directly or indirectly impact on JAK-STAT signalling. A combination of genetic and pharmacological approaches was utilised to assess the role of each of the following AMPK targets: TC-PTP, SHP2, eNOS, PKCλ, SIRT1, CPT1 and mTOR. It was demonstrated that activation of AMPK in HUVECs inhibited sIL-6Rα/IL-6 stimulated STAT3 Tyr705 phosphorylation via a mechanism independent of TC-PTP, eNOS, PKC, SIRT1 and mTOR. Furthermore, inhibition of mTOR and eNOS reduced sIL-6Rα/IL-6 stimulated STAT3 Tyr705 phosphorylation, independent of AMPK activation by A769662. Next, it was investigated whether AMPK acts directly on a signalling component of the JAK-STAT pathway. Specifically, it was hypothesised that AMPK could directly phosphorylate serine or threonine residues within JAK to inhibit IL-6 signalling. siRNA-mediated downregulation of JAK isoforms demonstrated that IL-6 induced STAT3 Tyr705 phosphorylation predominantly via JAK1 in human umbilical vein endothelial cells (HUVECs). In vitro kinase assays of JAK1-derived peptides demonstrated that AMPK can directly phosphorylate two residues, Ser515 and Ser518, within the JAK1 SH2 domain. Subsequently, a GST- 14-3-3 pull down assay of cell lysates produced from A769662 treated JAK1- defcient U4C cells transiently expressing either wild type or S515A/S518A double mutant JAK1 demonstrated that pharmacological activation of AMPK promotes 14-3-3 binding of JAK1 via a mechanism requiring Ser515 and Ser518. Furthermore, mutation of Ser515 and Ser518 abolishes the ability of AMPK to inhibit JAK-STAT signalling by an IL-6 trans-signalling complex and from a constitutively active Val658Phe-mutated JAK1. In this study it is proposed that AMPK phosphorylation of JAK1 at Ser515 and Ser518 inhibits IL-6 stimulated JAK1 phosphorylating STAT3 by interfering with the ability of JAK1 to interact and phosphorylate the GP130 receptor and /or STAT3 and STAT1. Therefore, AMPK phosphorylation of JAK1 could potentially be a novel regulatory mechanism that could be developed as a therapy for treating chronic inflammatory diseases such as atherosclerosis.
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Raja, Erna. "Cross-regulation between TGFβ/BMP Signalling and the metabolic LKB1 pathway." Doctoral thesis, Ludwig Institute for Cancer Research, Faculty of Medicine, Uppsala University, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-178181.

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Cell signalling determines physiological responses to many cellular stimuli and environmental changes. The transforming growth factor-beta (TGFβ)/bone morphogenetic protein (BMP) signalling pathways begin by binding of ligand to the heterodimeric receptor complex, followed by activation of Smads that translocate to the nucleus to regulate transcription of genes that further mediate cellular physiology. The TGFβ/BMP pathways are very important for proper tissue development and homeostasis, thus precise spatial and temporal regulation of the signalling pathway is required and achieved by many positive and negative signalling regulators. This thesis work identified the liver kinase B1 (LKB1) pathway as a negative regulator of TGFβ/BMP signalling pathways. In the first paper, we established LKB1 as a negative regulator of TGFβ signalling and TGFβ-induced epithelial to mesenchymal transition (EMT). LKB1 impairs Smad4 binding capacity to DNA leading to suppressed TGFβ-activated gene transcription. The second paper describes further the mechanism of LKB1 negative regulation on BMP signalling, by mediating BMP type I receptor degradation resulting in inhibition of BMP-induced cell differentiation. Downstream of LKB1, salt inducible kinase 1 (SIK1) is a TGFβ target gene and its expression is up-regulated by Smad2/3/4-mediated gene transcription. The third paper elucidates the mechanism of SIK1 transcriptional induction via an enhancer element located 3’ of the gene and SIK1-mediated type I TGFβ receptor degradation, which requires the activity of Smad7 and of the Smurf2 ubiquitin ligase. The fourth manuscript finds sucrose non-fermenting (SNF) 1-like kinase 2 (NUAK2) as another TGFβ target gene and its up-regulation results in modification of the mammalian target of rapamycin (mTOR) pathway that controls protein synthesis. NUAK2 cooperates with LKB1 leading to Raptor phosphorylation and inhibition of mTOR-mediated protein synthesis. Collectively, this thesis work has provided a functional link between two important signalling pathways, the metabolic LKB1 pathway and TGFβ/BMP pathway.
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Bacon, Sandra. "Investigation of plant derived compounds mediating cell signalling effects on FOXO1a and AMPK." Thesis, University of Dundee, 2012. https://discovery.dundee.ac.uk/en/studentTheses/b6abc6a4-de82-430a-ad30-015e8f69c8e8.

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In recent years there has been a considerable increase in human obesity levels with an associated increase in the incidence of type 2 diabetes mellitus (T2DM), a disorder of glucose metabolism characterised by insulin resistance. It is unclear why obesity and insulin resistance should frequently exist comorbidly but the current prevalence of polypharmacy suggests the underlying mechanisms may be multifactorial in origin. This project has highlighted plant compounds and extracts with: Insulin-like properties in cell culture experiments in that they induce phosphorylation and therefore inactivation of the transcription factor FOXO1a, which is a major downstream effector insulin and Properties similar to the T2D drugs metformin and pioglitazone, which both activate AMOK signalling and reduce phosphorylation of the ribosomal protein S6. The project began with an analysis of plant extracts which can mediate intracellular cell signalling effects on FOXO1a and AMPK. The pilot data established that one extract (grape seed, GSE) induces regulation of AMPK and FOXO1a much more readily than another (pine bark, PBE). GSE and PBE were subjected to multiple fractionation methods and mass spectrometry to learn more about the active agent(s) in the extracts. Another chapter adopted a candidate-approach, investigating effects of the plant compound gallic acid (GA) on AMPK. Although GA cannot explain the effects of GSE on AMPK, the availability of a variety of analogues of GA allowed investigation of structural requirements for cell responses. Two more extracts, cranberry and lingonberry, were then investigated using the techniques established earlier with GSE and PBE. These studies discovered that fractions containing B-type linkages were more effective at phosphorylating of FOXO1a than those containing A-type linkages, suggesting B-type linkages may be required for these effects. Metformin itself is a synthetic analogue of a plant compound and metformin analogues known as diguanides were synthesised and structure/activity relationships were assessed. Diguanides and biguanides were found ti induce similar responses but diguanides were much more toxic than biguanides, suggesting they may be less specific in their mechanism of action, or alternatively that they have different intramitochondrial targets. The aims of this project were 1. To extract polyphenolic compounds from grape seed, pine bark and berries using chromatography techniques and to characterise these compound using liquid chromatography/mass spectrometry 2. To exclude or confirm insulin-like or metformin-like properties by application to cell culture models to assess effects on regulation of glucose and energy homeostasis by measuring phosphorylation of the transcription factor FOXO1a, AMPK and the ribosomal protein S6.
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To, Truc. "AMPK Promotes Xenophagy Through ‘Priming’ of Autophagic Kinases upon Detection of Salmonella Outer Membrane Vesicles." Thesis, Université d'Ottawa / University of Ottawa, 2019. http://hdl.handle.net/10393/38764.

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The autophagy pathway is an essential component of the innate immune response, capable of rapidly targeting intracellular bacteria, which are subsequently degraded by lysosomal enzymes. Recent work has begun to elucidate the regulatory signalling for autophagy induction in response to pathogenic bacteria. However, the initial signalling regulating autophagy induction in response to the detection of pathogens remains largely unclear. Here we report that AMPK, an important upstream activator of the autophagy pathway, is rapidly stimulated upon detection of pathogenic bacteria, prior to bacterial invasion. Bacterial recognition is initially achieved through detection of outer membrane vesicles (OMVs). Additionally, we show that AMPK signalling relieves mTORC1-mediated repression of the autophagy pathway in response to Salmonella infection, positioning the cell for a rapid induction of autophagy. Surprisingly, we found that the activation of AMPK and inhibition of mTORC1 in response to extracellular Salmonella are not accompanied by an induction of bulk autophagy. However, upon Salmonella invasion AMPK signalling is required for efficient and selective targeting of bacteria-containing vesicles by the autophagy pathway through activation of pro-autophagic kinase complexes. Collectively, these results demonstrate a key role for AMPK signalling in coordinating the rapid autophagic response prior to invasion of pathogenic bacteria.
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Green, Charlotte. "Insulin sensitivity and fatty acid induced lipotoxicity : The role of PKB and AMPK signalling." Thesis, University of Dundee, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.510657.

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Books on the topic "AMPK signalling"

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AMP-Activated Protein Kinase Signalling. MDPI, 2019. http://dx.doi.org/10.3390/books978-3-03897-663-9.

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Book chapters on the topic "AMPK signalling"

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Evans, A. Mark, Sophronia A. Lewis, Oluseye A. Ogunbayo, and Javier Moral-Sanz. "Modulation of the LKB1-AMPK Signalling Pathway Underpins Hypoxic Pulmonary Vasoconstriction and Pulmonary Hypertension." In Advances in Experimental Medicine and Biology, 89–99. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-18440-1_11.

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Evans, A. Mark, Chris Peers, Christopher N. Wyatt, Prem Kumar, and D. Grahame Hardie. "Ion Channel Regulation by the LKB1-AMPK Signalling Pathway: The Key to Carotid Body Activation by Hypoxia and Metabolic Homeostasis at the Whole Body Level." In Advances in Experimental Medicine and Biology, 81–90. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4584-1_11.

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Menegollo, Michela, Isabella Tessari, Luigi Bubacco, and Gyorgy Szabadkai. "Determination of ATP, ADP, and AMP Levels by Reversed-Phase High-Performance Liquid Chromatography in Cultured Cells." In Calcium Signalling, 223–32. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9018-4_19.

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Duarte, Carlos B., Ana L. Carvalho, and Arsélio P. Carvalho. "Modulation of the Ampa/Kainate Receptors by Protein Kinase C." In Signalling Mechanisms — from Transcription Factors to Oxidative Stress, 115–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79675-3_11.

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Evans, A. Mark, D. Grahame Hardie, Antony Galione, Chris Peers, Prem Kumar, and Christopher N. Wyatt. "AMP-Activated Protein Kinase Couples Mitochondrial Inhibition by Hypoxia to Cell-Specific Ca2+ Signalling Mechanisms in Oxygensensing Cells." In Signalling Pathways in Acute Oxygen Sensing, 234–58. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/9780470035009.ch18.

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Rasmussen, Howard, Carlos Isales, Shridar Ganesan, Roberto Calle, and Walter Zawalich. "Ca2+-Cyclic AMP Interactions in Sustained Cellular Responses." In Ciba Foundation Symposium 164 - Interactions Among Cell Signalling Systems, 98–112. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514207.ch7.

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Grassie, Morag A., and Graeme Milligan. "The Use of Stably Transfected Cell Lines in the Analysis of Functional Interactions between Goα1 & Giα2 and the α2C10 Adrenoceptor." In Signalling Mechanisms — from Transcription Factors to Oxidative Stress, 99–113. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79675-3_10.

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Piazza, Francesco, and Gianpietro Semenzato. "Signalling Molecules as Selective Targets for Therapeutic Strategies in Multiple Myeloma." In Cell Signaling & Molecular Targets in Cancer, 87–108. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4614-0730-0_5.

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Rutherford, Claire, and Timothy M. Palmer. "Molecular Basis of Protective Anti-Inflammatory Signalling by Cyclic AMP in the Vascular Endothelium." In Systems Biology for Signaling Networks, 561–87. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-5797-9_23.

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Santarelli, Enrico. "Asset Specificity, R&D Financing and the Signalling Properties of the Firm’s Finance Structure." In Finance and Technological Change, 39–58. London: Palgrave Macmillan UK, 1995. http://dx.doi.org/10.1057/9780230375031_4.

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Conference papers on the topic "AMPK signalling"

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Chang, Jae Won, Seung-Nam Jung, Lihua Liua, Jin Man Kim, Myung Jin Ban, Yeon Soo Kim, Bok-Soon Lee, et al. "Abstract 843: CLDN1 mediates tumor invasion in HNSCC by regulation of EMT through AMPK-TGF-β signalling." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-843.

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Celestini, V., T. Tezil, L. Russo, C. Fasano, P. Sanese, G. Forte, A. Peserico, M. Lepore Signorile, V. Grossi, and C. Simone. "PO-161 The AMPK and MEK/ERK signalling pathways regulate mitochondrial FOXO3A import through phosphorylation of serine 12 and serine 30." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.683.

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Marriot, D. "Installation & testing of the signalling system." In 11th IET Professional Development Course on Railway Signalling and Control Systems. Institution of Engineering and Technology, 2006. http://dx.doi.org/10.1049/ic.2006.0695.

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Nicholson, T. J. "Train equipment & interfaces." In IET Professional Development Course on Railway Signalling and Control Systems (RSCS 2010). IET, 2010. http://dx.doi.org/10.1049/ic.2010.0097.

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Nicholson, T. J. "Train equipment & interfaces." In IET Professional Development Course on Railway Signalling and Control Systems (RSCS 2012). IET, 2012. http://dx.doi.org/10.1049/ic.2012.0053.

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Nicholson, T. J. "Total automation: impacts & systems." In IET Professional Development Course on Railway Signalling and Control Systems (RSCS 2010). IET, 2010. http://dx.doi.org/10.1049/ic.2010.0105.

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Nicholson, T. J. "Total automation: impacts & systems." In IET Professional Development Course on Railway Signalling and Control Systems (RSCS 2012). IET, 2012. http://dx.doi.org/10.1049/ic.2012.0058.

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McKendrick, B. "Asset management standards & practice." In IET Professional Development Course on Railway Signalling and Control Systems (RSCS 2010). IET, 2010. http://dx.doi.org/10.1049/ic.2010.0087.

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Clark, G. E. "Supervision & operation of mass transit systems." In 11th IET Professional Development Course on Railway Signalling and Control Systems. Institution of Engineering and Technology, 2006. http://dx.doi.org/10.1049/ic.2006.0691.

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Brook, B., and P. R. Munthe. "The NRM Lancashire & Yorkshire Railway School of Signalling." In IET History of Technology Network 36th Annual Weekend Meeting. IET, 2009. http://dx.doi.org/10.1049/cp.2009.1242.

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Reports on the topic "AMPK signalling"

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Yuval, Boaz, and Todd E. Shelly. Lek Behavior of Mediterranean Fruit Flies: An Experimental Analysis. United States Department of Agriculture, July 2000. http://dx.doi.org/10.32747/2000.7575272.bard.

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The Mediterranean fruit fly, Ceratitis capitata (Diptera: Tephritidae), is a ubiquitous pest of fruit trees, causing significant economic damage both in the U.S. and in Israel. Control efforts in the future will rely heavily on the sterile insect technique (SIT). Success of such operations hinges on the competitive ability of released males. The mating system of the medfly is based on leks. These are aggregations of sexually signaling males that attract females (who then select and copulate a courting male). A major component of male competitiveness is their ability to join existing leks or establish leks that are attractive to wild females. Accordingly, we identified leks and the behaviors associated with them as critical for the success of SIT operations. The objectives of this proposal were to determine 1. what makes a good lek site, 2. what are the energetic costs of lekking, 3. how females choose leks, and finally 4. whether the copulatory success of sterile males may be manipulated by particular pre-release diets and judicious spatial dispersal. We established that males choose lek sites according to their spatial location and penological status, that they avoid predators, and within the lek tree choose the perch that affords a compromise between optimal signalling, micro-climatic conditions and predation risk (Kaspi & Yuval 1999 a&b; Field et al 2000; Kaspi & Yuval submitted). We were able to show that leks are exclusive, and that only males with adequate protein and carbohydrate reserves can participate (Yuval et al 1998; Kaspi et al 2000; Shelly et al 2000). We determined that females prefer leks formed by protein fed, sexually experienced males (Shelly 2000). Finally, we demonstrated that adding protein to the diet of sterile males significantly enhances their probability of participating in leks and copulating wild females (Kaspi & Yuval 2000).
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