Read the abstract, see who wrote it and who cites it, and get the citation in APA, MLA, Chicago or Harvard.
About 10,000 papers for “Signalling pathways”
Birgit E. J. Teunissen, Habo J. Jongsma, Marti F. A. Bierhuizen · 2004
Cardiac hypertrophy is characterised by an increase in cardiomyocyte size, enhanced protein synthesis and a higher sarcomere organization, which are all preceded and accompanied by a reactivation of several foetal
Cited by 0
F Damiani, M Gianguzza, G Dolcemascolo · 2009
We studied the effects of various TBT concentrations by assaying the activity of ERK 1/2 (p44/42) and phospho-ERK1/2 (phospho-p44/42), proteins with a key role in ascidian development, and tyrosine kinase-dependent pathway. The effects of this xenobiotic and the role of some signalling mechanisms on ascidian embryos were examined by using Western immunoblotting. The tyrosine phosphorylation pattern in the ascidians Ciona intestinalis and Phallusia mammillata development was examined and different levels of protein phosphorylation were found as a response to TBT at µM range. To determine whether another key signalling pathway was activated, the effects of TBT on the phosphorylation state of a component of tyrosine kinase-mediated signal transduction MAPK, ERK 1/2 (p44/42) were evaluated. Embryos of Ciona intestinalis exposed to 0.1, 0.25 and 0.5 µM TBT showed a slight decrement in the level of phosphorylated ERK, while a remarkable decrement in level of phopshorylated ERK were observed at higher TBT concentrations (0.5 µM to 10 µM). These data indicated that exposures to TBT induced changes in the total pattern of phosphotyrosine and in the phosphorylation levels of ERK 1/2 but there were no changes on the overall level of total ERK in ascidian embryos. Key words: tributyltin-induced effect; tyrosine kinase signalling; MAPK; ERK (p44/42); ascidian embryos
Cited by 0
E Horner-glister, M Maleki-dizaji, C J Guerin et al. · 2014
Influence of oestradiol and tamoxifen on oestrogen receptors- and- protein degradation and non-genomic
Cited by 0
Yvette W. J. Paulis, Henk M. W. Verheul , et al. · 2010
Cited by 0
Harry C. Blair, Lisa Robinson, Mone Zaidi · Biochemical and Biophysical Research Communications · 2004
Cited by 156
Zubair Ahmed, Roy Bicknell · Methods in molecular biology · 2008
Hypoxia is widely recognised as a key driving force for tumor angiogenesis by its induction of vascular endothelial growth factor (VEGF) and other direct-acting angiogenic factors. We describe the effect of hypoxia on gene expression and downstream angiogenic signalling; however, the angiogenic process is complex, and many other signalling pathways beyond VEGF are implicated in the formation of new vessels. These include extra-cellular signalling pathways such as the notch/delta, ephrin/Eph receptor, roundabout/slit, and netrin/UNC (uncoordinated) receptor families as well as intracellular proteins such as hedgehog and sprouty. The remarkable diversity in angiogenic signalling pathways provides many opportunities for therapeutic intervention, and anti-angiogenesis is currently a major area of oncology research.
Cited by 77
Hiroshi Fukasawa, Koichi Shudo · PubMed · 1993
Retinoids, all-trans-retinoic acid (AT-RA) and its bioisters, exert diverse and profound effects on the growth and differentiation of normal and malignant cells, vertebrate development, and homeostasis. Since their nuclear receptors (RARs: alpha, beta and gamma) were cloned, extensive studies on retinoid signalling at molecular level have elucidated its elaborate mechanisms, by which the expression of a variety of retinoid responsive genes are regulated. Furthermore, discoveries of the second receptor system of retinoid (RXRs: alpha, beta and gamma) and their substantial ligand, 9-cis-retinoic acid (9C-RA), were recently reported. The heterodimer formation between RXR and RAR or other members of the steroid/thyroid hormone receptor superfamily gave us a new aspect of hormonal gene control including retinoids, thyroid hormone, vitamin D3 and others. These heterodimers were showed to bind specific response elements consisted of the direct repeat of consensus sequence (AGATTC) or its related sequences. Differential regulation of retinoid responsive gene by RARs or/and RXRs in vivo is an ongoing subject and the combinatory outcome of subtypes or isotypes of receptors, natural response elements, natural ligands (AT-RA, 9C-RA, or their metabolites) owing to pleiotropic effects of retinoids is being revealed. The anti-malignant effect of retinoids is another important theme. The report of prominent therapeutic effect of AT-RA against APL patients was sensational. In many APL patients, translocation between RAR alpha gene and an oncogenic gene, PML, can be detected, although the roles of their fusion products (RAR alpha-PML and PML-RAR alpha) in APL induction have not been understood. Furthermore, the cross-talk between RAR and AP-1 is thought to give an explanation for the suppressive effects of retinoids against tumor promoters (TPA and others). In those contexts, synthetic retinoids specific for each subtype of RAR or RXR, which will be useful reagents for biological studies and/or excellent therapeutic agents, are being developed. Some RAR subtype-selective compounds including antagonists have been already reported.
Cited by 1
Natalie Charnley, Stephanie B. Donaldson, Pat Price · Methods in molecular biology · 2008
There is a need for direct imaging of effects on tumor vasculature in assessment of response to antiangiogenic drugs and vascular disrupting agents. Imaging tumor vasculature depends on differences in permeability of vasculature of tumor and normal tissue, which cause changes in penetration of contrast agents. Angiogenesis imaging may be defined in terms of measurement of tumor perfusion and direct imaging of the molecules involved in angiogenesis. In addition, assessment of tumor hypoxia will give an indication of tumor vasculature. The range of imaging techniques available for these processes includes positron emission tomography (PET), dynamic contrast-enhanced magnetic resonance imaging (DCE-MRI), perfusion computed tomography (CT), and ultrasound (US).
Cited by 26
Banteiskhem Kharwanlang, Ramesh Sharma · 2015
Cited by 0
Marie Vognstoft Hjortbak (4884811), Thomas Skjærlund Grønnebæk (9569046), Nichlas Riise Jespersen (4884814) et al. · Figshare · 2020
<p>(A) Representative blots, (B) Phosphorylation of AMPK, (C) Phosphorylation of ACC, (D) Phosphorylation of GS, (E) levels of PHB1 and (F) Levels of VDAC. LCR: Low capacity runners, HCR: High capacity runners, CON: Control, IPC: Local ischemic preconditioning, RIC: Remote ischemic preconditioning, AMPK: AMP-activated Kinase, ACC: Acetyl-CoA Carboxylase, GS: Glycogen Synthase, PHB1: Prohibitin-1, VDAC: Voltage-dependent anion channel, COX IX: Cytochrome c oxidase IX, β-HAD: β-hydroxyacyl-CoA dehydrogenase and CS: Citrate synthase. Values are presented as mean ± SEM. N = 5–8.</p>
Cited by 0Open access
Dianne Watters, Martin F. Lavin · 1999
1. The Role of Sphigolipids in Stress Responses and Apoptosis in Eukaryotes 2. Radiation Response Pathways and Apoptosis 3. Apoptosis in Drosophila 4. Baculoviral Lessons in Apoptosis 5. The Mitochondrion: Decisive for Cell Death Control? 6. Caspases and the Commitment to Death 7. Killer Cells - Deliverers of Exogenous Death Proteases 8. Protein Kinase C Isoenzymes: Evidence for Selectivity in the Regulation of Apoptosis 9, The Death Receptors 10. Kinase Cascades and Apoptosis 11. Caspases: The Molecular Effectors of Apoptosis 12. Substrates of Cell Death Proteases and Their Role in Apoptosis
Cited by 14
Celso Henrique Alves (493802), Koen Bossers (135792), Rogier M. Vos (243202) et al. · Figshare · 2015
<p>Transcript levels measured by quantitative real time PCR at P3 (A) and P10 (B) in 5-6 control and Crb2 cKO retinas showed only changes in Hey1 (<i>P</i> = 0.041). P3: <i>Notch1 </i><i>P</i> = 0.144, <i>Kaiso </i><i>P</i> = 0.440, β-catenin <i>P</i> = 0.082, c-myc <i>P</i> = 0.711, cyclin D1 <i>P</i> = 0.226, Cyr61 <i>P</i> = 0.4687, <i>Shh </i><i>P</i> = 0.411. P10: <i>Smo </i><i>P</i> = 0.182, <i>gli1 </i><i>P</i> = 0.262, <i>P120-catenin </i><i>P</i> = 0.228, β-catenin <i>P</i> = 0.837, Hey2 <i>P</i> = 0.472, <i>elF4E </i><i>P</i> = 0.236, RPS6 <i>P</i> = 0.196, <i>PIK3K1 </i><i>P</i> = 0.375. Data are presented as mean ± SEM *<i>P</i><0.05; **<i>P</i><0.01.</p>
Cited by 0Open access
Thomas P. Prescott (733335), Moritz Lang (733336), Antonis Papachristodoulou (221915) · Figshare · 2015
<p>This figure shows two signalling pathways, with two crosstalk mechanisms. Functionality <i>F</i><sup>1</sup> = {<i>R</i><sub>1</sub>, <i>R</i><sub>2</sub>, <i>R</i><sub>3</sub>} is the <i>X</i> pathway; <i>F</i><sup>2</sup> = {<i>R</i><sub>4</sub>, <i>R</i><sub>5</sub>, <i>R</i><sub>6</sub>} is the <i>Y</i> pathway; the mutually inhibiting crosstalk <i>F</i><sup>3</sup> = {<i>R</i><sub>7</sub>, <i>R</i><sub>8</sub>}; and the mutually excitatory crosstalk <i>F</i><sup>4</sup> = {<i>R</i><sub>9</sub>, <i>R</i><sub>10</sub>}. Model adopted from [<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1004235#pcbi.1004235.ref008" target="_blank">8</a>].</p>
Cited by 0Open access
Vahri Beaumont, Glantschnig Helmut, Ignacio Muñoz-Sanjuán et al. · Europe PMC (PubMed Central) · 2006
Cited by 0
Martin F. Lavin, Herston, Australia · 1952
Cited by 2
Graeme S. Cottrell · Handbook of experimental pharmacology · 2018
Cited by 42
凯铭 张 · Advances in Clinical Medicine · 2024
Cited by 0
Tony Pawson · PubMed · 1994
Protein-tyrosine kinases act as receptors for a wide range of external signals that control the growth and differentiation of normal cells. Additionally, many retroviral and cellular oncogenes encode tyrosine kinase variants that are constitutively active. Recent evidence suggests that the intracellular targets of tyrosine kinases contain a protein module of approximately 100 amino acids, the Src homology 2 (SH2) domain. SH2 domains directly recognize tyrosine phosphorylation sites, and are thereby recruited to activated, autophosphorylated growth factor receptors. These interactions, in turn, stimulate the biochemical signalling pathways that control gene expression, cytoskeletal architecture, and cell metabolism. SH2-containing proteins frequently contain a distinct element of approximately 50 residues, the SH3 domain, that recognizes proline-rich motifs. Proteins with SH2 and SH3 domains can act as adaptors to couple tyrosine kinases to downstream targets with SH3-binding sites. A specific example of the synergistic action of SH2 and SH3 domains involves regulation of the Ras pathway by the adaptor protein Sem-5/drk/Grb2, which links tyrosine kinases to the Ras guanine nucleotide releasing protein Sos, which converts Ras to the active GTP-bound state.
Cited by 32
Vilmantė Borutaitė · Lithuanian University of Health Sciences · 2007
Bibliogr.: 3 pavad.
Cited by 0
Rainer Breitling, David Gilbert, Monika Heiner et al. · 2008
Cited by 0