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Mechanisms involved in curcumin-induced human neutrophil apoptosis: Evidence that curcumin activates the endoplasmic reticulum stress-induced cell apoptosis pathway.

SAGE open medicine

Antoine F, Girard D.
PMID: 26770672
SAGE Open Med. 2013 Jun 18;1:2050312113488104. doi: 10.1177/2050312113488104. eCollection 2013.

Curcumin was previously reported to accelerate neutrophil apoptosis, but the mechanism is unclear. Herein, we confirmed that curcumin induces human neutrophil apoptosis as assessed by cytology and by increase in the cell surface expression of annexin-V and CD16 shedding....

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Antoine F, Girard D. Mechanisms involved in curcumin-induced human neutrophil apoptosis: Evidence that curcumin activates the endoplasmic reticulum stress-induced cell apoptosis pathway. SAGE Open Med. 2013;1:2050312113488104doi: 10.1177/2050312113488104.
Antoine, F., & Girard, D. (2013). Mechanisms involved in curcumin-induced human neutrophil apoptosis: Evidence that curcumin activates the endoplasmic reticulum stress-induced cell apoptosis pathway. SAGE open medicine, 12050312113488104. https://doi.org/10.1177/2050312113488104
Antoine, Francis, and Girard, Denis. "Mechanisms involved in curcumin-induced human neutrophil apoptosis: Evidence that curcumin activates the endoplasmic reticulum stress-induced cell apoptosis pathway." SAGE open medicine vol. 1 (2013): 2050312113488104. doi: https://doi.org/10.1177/2050312113488104
Antoine F, Girard D. Mechanisms involved in curcumin-induced human neutrophil apoptosis: Evidence that curcumin activates the endoplasmic reticulum stress-induced cell apoptosis pathway. SAGE Open Med. 2013 Jun 18;1:2050312113488104. doi: 10.1177/2050312113488104. eCollection 2013. PMID: 26770672; PMCID: PMC4687759.
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Activation of 5-HT7 receptor stimulates neurite elongation through mTOR, Cdc42 and actin filaments dynamics.

Frontiers in behavioral neuroscience

Speranza L, Giuliano T, Volpicelli F, De Stefano ME, Lombardi L, Chambery A, Lacivita E, Leopoldo M, Bellenchi GC, di Porzio U, Crispino M, Perrone-Capano C.
PMID: 25814944
Front Behav Neurosci. 2015 Mar 11;9:62. doi: 10.3389/fnbeh.2015.00062. eCollection 2015.

Recent studies have indicated that the serotonin receptor subtype 7 (5-HT7R) plays a crucial role in shaping neuronal morphology during embryonic and early postnatal life. Here we show that pharmacological stimulation of 5-HT7R using a highly selective agonist, LP-211,...

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Speranza L, Giuliano T, Volpicelli F, et al. Activation of 5-HT7 receptor stimulates neurite elongation through mTOR, Cdc42 and actin filaments dynamics. Front Behav Neurosci. 2015;9:62doi: 10.3389/fnbeh.2015.00062.
Speranza, L., Giuliano, T., Volpicelli, F., De Stefano, M. E., Lombardi, L., Chambery, A., Lacivita, E., Leopoldo, M., Bellenchi, G. C., di Porzio, U., Crispino, M., & Perrone-Capano, C. (2015). Activation of 5-HT7 receptor stimulates neurite elongation through mTOR, Cdc42 and actin filaments dynamics. Frontiers in behavioral neuroscience, 962. https://doi.org/10.3389/fnbeh.2015.00062
Speranza, Luisa, et al. "Activation of 5-HT7 receptor stimulates neurite elongation through mTOR, Cdc42 and actin filaments dynamics." Frontiers in behavioral neuroscience vol. 9 (2015): 62. doi: https://doi.org/10.3389/fnbeh.2015.00062
Speranza L, Giuliano T, Volpicelli F, De Stefano ME, Lombardi L, Chambery A, Lacivita E, Leopoldo M, Bellenchi GC, di Porzio U, Crispino M, Perrone-Capano C. Activation of 5-HT7 receptor stimulates neurite elongation through mTOR, Cdc42 and actin filaments dynamics. Front Behav Neurosci. 2015 Mar 11;9:62. doi: 10.3389/fnbeh.2015.00062. eCollection 2015. PMID: 25814944; PMCID: PMC4356071.
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The Emerging Role of the Cytoskeleton in Chromosome Dynamics.

Frontiers in genetics

Spichal M, Fabre E.
PMID: 28580009
Front Genet. 2017 May 19;8:60. doi: 10.3389/fgene.2017.00060. eCollection 2017.

Chromosomes underlie a dynamic organization that fulfills functional roles in processes like transcription, DNA repair, nuclear envelope stability, and cell division. Chromosome dynamics depend on chromosome structure and cannot freely diffuse. Furthermore, chromosomes interact closely with their surrounding nuclear...

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Spichal M, Fabre E. The Emerging Role of the Cytoskeleton in Chromosome Dynamics. Front Genet. 2017;8:60doi: 10.3389/fgene.2017.00060.
Spichal, M., & Fabre, E. (2017). The Emerging Role of the Cytoskeleton in Chromosome Dynamics. Frontiers in genetics, 860. https://doi.org/10.3389/fgene.2017.00060
Spichal, Maya, and Fabre, Emmanuelle. "The Emerging Role of the Cytoskeleton in Chromosome Dynamics." Frontiers in genetics vol. 8 (2017): 60. doi: https://doi.org/10.3389/fgene.2017.00060
Spichal M, Fabre E. The Emerging Role of the Cytoskeleton in Chromosome Dynamics. Front Genet. 2017 May 19;8:60. doi: 10.3389/fgene.2017.00060. eCollection 2017. PMID: 28580009; PMCID: PMC5437106.
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The effect of microbial challenge on the intestinal proteome of broiler chickens.

Proteome science

O'Reilly EL, Burchmore RJ, Sparks NH, Eckersall PD.
PMID: 28572745
Proteome Sci. 2017 May 30;15:10. doi: 10.1186/s12953-017-0118-0. eCollection 2016.

BACKGROUND: In poultry production intestinal health and function is paramount to achieving efficient feed utilisation and growth. Uncovering the localised molecular mechanisms that occur during the early and important periods of growth that allow birds to grow optimally is...

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O'Reilly EL, Burchmore RJ, Sparks NH, et al. The effect of microbial challenge on the intestinal proteome of broiler chickens. Proteome Sci. 2017;15:10doi: 10.1186/s12953-017-0118-0.
O'Reilly, E. L., Burchmore, R. J., Sparks, N. H., & Eckersall, P. D. (2016). The effect of microbial challenge on the intestinal proteome of broiler chickens. Proteome science, 1510. https://doi.org/10.1186/s12953-017-0118-0
O'Reilly, Emily L, et al. "The effect of microbial challenge on the intestinal proteome of broiler chickens." Proteome science vol. 15 (2016): 10. doi: https://doi.org/10.1186/s12953-017-0118-0
O'Reilly EL, Burchmore RJ, Sparks NH, Eckersall PD. The effect of microbial challenge on the intestinal proteome of broiler chickens. Proteome Sci. 2017 May 30;15:10. doi: 10.1186/s12953-017-0118-0. eCollection 2016. PMID: 28572745; PMCID: PMC5450085.
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Fluorescence Localization of Cytoskeletal Proteins in Fibrin-Trapped Cells.

The Biological bulletin

Lee KG, Mohan N, Koroleva Z, Huang LF, Cohen WD.
PMID: 28570182
Biol Bull. 1998 Oct;195(2):211-212. doi: 10.2307/1542844.

No abstract available.

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Lee KG, Mohan N, Koroleva Z, et al. Fluorescence Localization of Cytoskeletal Proteins in Fibrin-Trapped Cells. Biol Bull. 1998;195(2):211-212doi: 10.2307/1542844.
Lee, K. G., Mohan, N., Koroleva, Z., Huang, L. F., & Cohen, W. D. (1998). Fluorescence Localization of Cytoskeletal Proteins in Fibrin-Trapped Cells. The Biological bulletin, 195(2), 211-212. https://doi.org/10.2307/1542844
Lee, K G, et al. "Fluorescence Localization of Cytoskeletal Proteins in Fibrin-Trapped Cells." The Biological bulletin vol. 195,2 (1998): 211-212. doi: https://doi.org/10.2307/1542844
Lee KG, Mohan N, Koroleva Z, Huang LF, Cohen WD. Fluorescence Localization of Cytoskeletal Proteins in Fibrin-Trapped Cells. Biol Bull. 1998 Oct;195(2):211-212. doi: 10.2307/1542844. PMID: 28570182.
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Effect of Rapid Chilling on Beef Quality and Cytoskeletal Protein Degradation in M. longissimus of Chinese Yellow Crossbred Bulls.

Asian-Australasian journal of animal sciences

Mao Y, Zhang Y, Liang R, Ren L, Zhu H, Li K, Zhu L, Luo X.
PMID: 25049681
Asian-Australas J Anim Sci. 2012 Aug;25(8):1197-204. doi: 10.5713/ajas.2012.12055.

The objective of this study was to investigate the effect of rapid chilling (RC) on beef quality and the degradation of cytoskeletal proteins. Twenty Chinese Yellow crossbred bulls were selected and randomly divided into two groups. RC and conventional...

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Mao Y, Zhang Y, Liang R, et al. Effect of Rapid Chilling on Beef Quality and Cytoskeletal Protein Degradation in M. longissimus of Chinese Yellow Crossbred Bulls. Asian-Australas J Anim Sci. 2012;25(8):1197-204doi: 10.5713/ajas.2012.12055.
Mao, Y., Zhang, Y., Liang, R., Ren, L., Zhu, H., Li, K., Zhu, L., & Luo, X. (2012). Effect of Rapid Chilling on Beef Quality and Cytoskeletal Protein Degradation in M. longissimus of Chinese Yellow Crossbred Bulls. Asian-Australasian journal of animal sciences, 25(8), 1197-204. https://doi.org/10.5713/ajas.2012.12055
Mao, Yanwei, et al. "Effect of Rapid Chilling on Beef Quality and Cytoskeletal Protein Degradation in M. longissimus of Chinese Yellow Crossbred Bulls." Asian-Australasian journal of animal sciences vol. 25,8 (2012): 1197-204. doi: https://doi.org/10.5713/ajas.2012.12055
Mao Y, Zhang Y, Liang R, Ren L, Zhu H, Li K, Zhu L, Luo X. Effect of Rapid Chilling on Beef Quality and Cytoskeletal Protein Degradation in M. longissimus of Chinese Yellow Crossbred Bulls. Asian-Australas J Anim Sci. 2012 Aug;25(8):1197-204. doi: 10.5713/ajas.2012.12055. PMID: 25049681; PMCID: PMC4092990.
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Molecular phylogeny of sequenced saccharomycetes reveals polyphyly of the alternative yeast codon usage.

Genome biology and evolution

Mühlhausen S, Kollmar M.
PMID: 25053656
Genome Biol Evol. 2014 Jul 22;6(5). doi: 10.1093/gbe/evu093. Epub 2014 Jul 22.

The universal genetic code defines the translation of nucleotide triplets, called codons, into amino acids. In many Saccharomycetes a unique alteration of this code affects the translation of the CUG codon, which is normally translated as leucine. Most of...

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Mühlhausen S, Kollmar M. Molecular phylogeny of sequenced saccharomycetes reveals polyphyly of the alternative yeast codon usage. Genome Biol Evol. 2014;6(5)doi: 10.1093/gbe/evu093.
Mühlhausen, S., & Kollmar, M. (2014). Molecular phylogeny of sequenced saccharomycetes reveals polyphyly of the alternative yeast codon usage. Genome biology and evolution, 6(5), . https://doi.org/10.1093/gbe/evu093
Mühlhausen, Stefanie, and Kollmar, Martin. "Molecular phylogeny of sequenced saccharomycetes reveals polyphyly of the alternative yeast codon usage." Genome biology and evolution vol. 6,5 (2014). doi: https://doi.org/10.1093/gbe/evu093
Mühlhausen S, Kollmar M. Molecular phylogeny of sequenced saccharomycetes reveals polyphyly of the alternative yeast codon usage. Genome Biol Evol. 2014 Jul 22;6(5). doi: 10.1093/gbe/evu093. Epub 2014 Jul 22. PMID: 25053656.
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Evaluating Inhibition of the Epidermal Growth Factor (EGF)-Induced Response of Mutant MCF10A Cells with an Acoustic Sensor.

Biosensors

Garcia MP, Shahid A, Chen JY, Xi J.
PMID: 25586035
Biosensors (Basel). 2012 Nov 13;2(4):448-64. doi: 10.3390/bios2040448.

Many cancer treatments rely on inhibition of epidermal growth factor (EGF)-induced cellular responses. Evaluating drug effects on such responses becomes critical to the development of new cancer therapeutics. In this report, we have employed a label-free acoustic sensor, the...

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Garcia MP, Shahid A, Chen JY, et al. Evaluating Inhibition of the Epidermal Growth Factor (EGF)-Induced Response of Mutant MCF10A Cells with an Acoustic Sensor. Biosensors (Basel). 2012;2(4):448-64doi: 10.3390/bios2040448.
Garcia, M. P., Shahid, A., Chen, J. Y., & Xi, J. (2012). Evaluating Inhibition of the Epidermal Growth Factor (EGF)-Induced Response of Mutant MCF10A Cells with an Acoustic Sensor. Biosensors, 2(4), 448-64. https://doi.org/10.3390/bios2040448
Garcia, Marcela P, et al. "Evaluating Inhibition of the Epidermal Growth Factor (EGF)-Induced Response of Mutant MCF10A Cells with an Acoustic Sensor." Biosensors vol. 2,4 (2012): 448-64. doi: https://doi.org/10.3390/bios2040448
Garcia MP, Shahid A, Chen JY, Xi J. Evaluating Inhibition of the Epidermal Growth Factor (EGF)-Induced Response of Mutant MCF10A Cells with an Acoustic Sensor. Biosensors (Basel). 2012 Nov 13;2(4):448-64. doi: 10.3390/bios2040448. PMID: 25586035; PMCID: PMC4263556.
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Stepping Out of the Shade: Control of Neuronal Activity by the Scaffold Protein Kidins220/ARMS.

Frontiers in cellular neuroscience

Scholz-Starke J, Cesca F.
PMID: 27013979
Front Cell Neurosci. 2016 Mar 14;10:68. doi: 10.3389/fncel.2016.00068. eCollection 2016.

The correct functioning of the nervous system depends on the exquisitely fine control of neuronal excitability and synaptic plasticity, which relies on an intricate network of protein-protein interactions and signaling that shapes neuronal homeostasis during development and in adulthood....

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Scholz-Starke J, Cesca F. Stepping Out of the Shade: Control of Neuronal Activity by the Scaffold Protein Kidins220/ARMS. Front Cell Neurosci. 2016;10:68doi: 10.3389/fncel.2016.00068.
Scholz-Starke, J., & Cesca, F. (2016). Stepping Out of the Shade: Control of Neuronal Activity by the Scaffold Protein Kidins220/ARMS. Frontiers in cellular neuroscience, 1068. https://doi.org/10.3389/fncel.2016.00068
Scholz-Starke, Joachim, and Cesca, Fabrizia. "Stepping Out of the Shade: Control of Neuronal Activity by the Scaffold Protein Kidins220/ARMS." Frontiers in cellular neuroscience vol. 10 (2016): 68. doi: https://doi.org/10.3389/fncel.2016.00068
Scholz-Starke J, Cesca F. Stepping Out of the Shade: Control of Neuronal Activity by the Scaffold Protein Kidins220/ARMS. Front Cell Neurosci. 2016 Mar 14;10:68. doi: 10.3389/fncel.2016.00068. eCollection 2016. PMID: 27013979; PMCID: PMC4789535.
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Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously.

Nature microbiology

Cho H, Wivagg CN, Kapoor M, Barry Z, Rohs PDA, Suh H, Marto JA, Garner EC, Bernhardt TG.
PMID: 27643381
Nat Microbiol. 2016 Sep 19;1:16172. doi: 10.1038/nmicrobiol.2016.172.

Multi-protein complexes organized by cytoskeletal proteins are essential for cell wall biogenesis in most bacteria. Current models of the wall assembly mechanism assume that class A penicillin-binding proteins (aPBPs), the targets of penicillin-like drugs, function as the primary cell...

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Cho H, Wivagg CN, Kapoor M, et al. Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nat Microbiol. 2016;1:16172doi: 10.1038/nmicrobiol.2016.172.
Cho, H., Wivagg, C. N., Kapoor, M., Barry, Z., Rohs, P. D. A., Suh, H., Marto, J. A., Garner, E. C., & Bernhardt, T. G. (2016). Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nature microbiology, 116172. https://doi.org/10.1038/nmicrobiol.2016.172
Cho, Hongbaek, et al. "Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously." Nature microbiology vol. 1 (2016): 16172. doi: https://doi.org/10.1038/nmicrobiol.2016.172
Cho H, Wivagg CN, Kapoor M, Barry Z, Rohs PDA, Suh H, Marto JA, Garner EC, Bernhardt TG. Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nat Microbiol. 2016 Sep 19;1:16172. doi: 10.1038/nmicrobiol.2016.172. PMID: 27643381; PMCID: PMC5030067.
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Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles.

Frontiers in neuroscience

Haase G, Rabouille C.
PMID: 26696811
Front Neurosci. 2015 Dec 08;9:448. doi: 10.3389/fnins.2015.00448. eCollection 2015.

Pathological alterations of the Golgi apparatus, such as its fragmentation represent an early pre-clinical feature of many neurodegenerative diseases and have been widely studied in the motor neuron disease amyotrophic lateral sclerosis (ALS). Yet, the underlying molecular mechanisms have...

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Haase G, Rabouille C. Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles. Front Neurosci. 2015;9:448doi: 10.3389/fnins.2015.00448.
Haase, G., & Rabouille, C. (2015). Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles. Frontiers in neuroscience, 9448. https://doi.org/10.3389/fnins.2015.00448
Haase, Georg, and Rabouille, Catherine. "Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles." Frontiers in neuroscience vol. 9 (2015): 448. doi: https://doi.org/10.3389/fnins.2015.00448
Haase G, Rabouille C. Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles. Front Neurosci. 2015 Dec 08;9:448. doi: 10.3389/fnins.2015.00448. eCollection 2015. PMID: 26696811; PMCID: PMC4672084.
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Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.

Science advances

Shi C, Fricke P, Lin L, Chevelkov V, Wegstroth M, Giller K, Becker S, Thanbichler M, Lange A.
PMID: 26665178
Sci Adv. 2015 Dec 04;1(11):e1501087. doi: 10.1126/sciadv.1501087. eCollection 2015 Dec.

Bactofilins are a recently discovered class of cytoskeletal proteins of which no atomic-resolution structure has been reported thus far. The bacterial cytoskeleton plays an essential role in a wide range of processes, including morphogenesis, cell division, and motility. Among...

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Shi C, Fricke P, Lin L, et al. Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR. Sci Adv. 2015;1(11):e1501087doi: 10.1126/sciadv.1501087.
Shi, C., Fricke, P., Lin, L., Chevelkov, V., Wegstroth, M., Giller, K., Becker, S., Thanbichler, M., & Lange, A. (2015). Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR. Science advances, 1(11), e1501087. https://doi.org/10.1126/sciadv.1501087
Shi, Chaowei, et al. "Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR." Science advances vol. 1,11 (2015): e1501087. doi: https://doi.org/10.1126/sciadv.1501087
Shi C, Fricke P, Lin L, Chevelkov V, Wegstroth M, Giller K, Becker S, Thanbichler M, Lange A. Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR. Sci Adv. 2015 Dec 04;1(11):e1501087. doi: 10.1126/sciadv.1501087. eCollection 2015 Dec. PMID: 26665178; PMCID: PMC4672760.
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Showing 1 to 12 of 339 entries