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See detailPhospholipids quantification in vegetable oil degumming residues by HPLC-ELSD
Pierart, Céline ULg; Danthine, Sabine ULg; Wathelet, B et al

Poster (2008)

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See detailThe phosphoprotein pp135 is an essential constituent of the fibrillar components of nucleoli and of coiled bodies.
Vandelaer, M.; Thiry, Marc ULg

in Histochemistry & Cell Biology (1998), 110(2), 169-77

We examined the distribution of the silver-stainable phosphoprotein, pp135, within Ehrlich tumor and HEp-2 cells by a postembedding Lowicryl immunogold labeling procedure. Identical labeling patterns were ... [more ▼]

We examined the distribution of the silver-stainable phosphoprotein, pp135, within Ehrlich tumor and HEp-2 cells by a postembedding Lowicryl immunogold labeling procedure. Identical labeling patterns were obtained in both cell types. During interphase, gold particles were found not only over the dense fibrillar component but were also evident over the fibrillar centers of nucleoli. By contrast, the granular component did not display any significant label. When rRNA synthesis was inhibited by actinomycin D, the same labeling was observed in segregated nucleoli; both fibrillar components were labeled. Aside from the nucleolar labeling, label was also consistently present in coiled bodies. During metaphase, label was visualized in silver-stainable material of the nucleolus organizing regions. It thus appears that, unlike the two major silver-stained proteins, nucleolin/C23 and B23, pp135 remains located in all major silver-stainable structures during the whole cell cycle. This finding strongly suggests that pp135 could be the component responsible for in situ silver staining. On the other hand, the maintenance of pp135 in the fibrillar centers throughout the cell cycle, like RNA polymerase I, upstream binding factor, and DNA topoisomerase I, suggests that pp135 could be a component involved in transcription of the rRNA genes. [less ▲]

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See detailLe phosphore est-il un facteur de risque cardiovasculaire?
Krzesinski, Jean-Marie ULg; Cohen, Eric P.

in Réalités Cardiologiques (2009), (255), 33-38

Chez l'insuffisant rénal terminal, le phosphore doit être considéré comme un facteur de risque cardiovasculaire. Chez les patients à fonction rénale normale ou subnormale, il peut être surtout le témoin ... [more ▼]

Chez l'insuffisant rénal terminal, le phosphore doit être considéré comme un facteur de risque cardiovasculaire. Chez les patients à fonction rénale normale ou subnormale, il peut être surtout le témoin de ce risque parce qu'il s'associe souvent à d'autres facteurs de risque d'athérosclérose. Il favorise cependant la rigidité artérielle. Le phosphore étant quantitativement élevé dans une alimentation occidentale fort riche, la relation entre cet ion et le risque cardiovasculaire n'est peut-être qu'indirecte. Pour prouver le rôle direct du phosphore sur le risque cardiovasculaire, il est nécessaire d'initier des études à plus grande échelle, prospectives et contrôlées, en connaissant l'alimentation des patients, leurs traitements et comorbidités et divers paramètres biologiques (lipidiques par exemple) à côté de la phosphorémie à déterminer à jeun. [less ▲]

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See detailPhosphorus availability : influence of soil characteristics and fertilization
Renneson, Malorie ULg

Scientific conference (2013, February 04)

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See detailPhosphorus availability in agricultural soils of Wallonia (Belgium) - A modeling approach
Cobert, Florian ULg; Pourret, Olivier; Renneson, Malorie ULg et al

Poster (2013, August)

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See detailPhosphorus intake in preterm babies and variation of tubular reabsorption for phosphate per liter glomerular filtrate
Battisti, Oreste ULg; Langhendries, J. P.; François, A. et al

in Biology of the Neonate (1992), 61

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See detailPhosphorylated HER-2 tyrosine kinase and Her-2/neu gene amplification as predictive factors of response to trastuzumab in patients with HER-2 overexpressing metastatic breast cancer (MBC).
Giuliani, Rosa; Durbecq, Virginie; Di Leo, Angelo et al

in European Journal of Cancer (2007), 43(4), 725-35

AIM: Trastuzumab (T), a humanised monoclonal antibody against HER-2, is active in HER-2-positive MBC patients. However, nearly 60% of the patients do not benefit from T, stressing the need for additional ... [more ▼]

AIM: Trastuzumab (T), a humanised monoclonal antibody against HER-2, is active in HER-2-positive MBC patients. However, nearly 60% of the patients do not benefit from T, stressing the need for additional predictive markers. The following markers could be implicated in response to T: (1) the magnitude of Her-2 gene amplification; (2) the co-expression of the other HER family receptors, possibly responsible for HER-2 trans-activation; (3) the activated status of HER-2; (4) the activated status of downstream effectors as mitogen-activated protein kinases (MAPKs), p38 and p27. METHODS: Medical files of patients with MBC treated with T either as a single agent or in combination with chemotherapy (CT) were reviewed. HER family members (EGFR, HER-2, HER-3, HER-4), the phosphorylated forms of EGFR (p-EGFR), HER-2 (p-HER-2) and of the downstream effectors were evaluated in the archival tumours. The correlation between clinical outcome and the expression of these markers was investigated. RESULTS: (1) Increasing values of Her-2 amplification were associated with a higher probability of achieving an objective response; (2) no statistical significant correlation between the expression of the HER family receptors was found; (3) p-HER-2 was predictive of response in patients treated with T+CT; (4) a statistically significant correlation between p-ERK 1/2, p-p38 and p-HER-2 emerged, pointing to the activated vertical pathway p-HER-2-->p-MAPKs. CONCLUSIONS: p-HER-2 and the magnitude of Her-2 amplification were predictive of response to T and their role deserves to be analysed in larger and more homogenous T-treated populations such as those from large phase III trials. [less ▲]

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See detailPhosphorylated Thiamine Derivatives and Cortical Activity in the Baboon Papio Papio: Effect of Intermittent Light Stimulation
Bettendorff, Lucien ULg; Schoffeniels, Ernest; Naquet, R. et al

in Journal of Neurochemistry (1989), 53(1), 80-87

The effect of intermittent light stimulation (ILS) on the distribution of thiamine derivatives in three brain areas (occipital, motor, and premotor) was compared in photosensitive and nonphotosensitive ... [more ▼]

The effect of intermittent light stimulation (ILS) on the distribution of thiamine derivatives in three brain areas (occipital, motor, and premotor) was compared in photosensitive and nonphotosensitive baboons. ILS induces paroxysmal discharges in the motor and premotor areas of photosensitive animals only. In baboons submitted to ILS, thiamine triphosphate (TTP) decreases in both photosensitive and nonphotosensitive animals; thiamine monophosphate (TMP) increases in photosensitive animals, which present ILS-induced paroxysmal discharges, whereas it is unaffected in nonphotosensitive animals. The variations are the most significant in the occipital (visual) cortex. A consumption of TTP may result from electrical activity induced by light stimulation in the occipital area. No correlation between ILS-induced paroxysmal activity and a decrease in TTP contents was found. However, photosensitive animals are affected differently from nonphotosensitive animals, as their content of TMP in the cerebral cortex increases on stimulation. However, as long as the exact role of thiamine compounds in relation to membrane excitability in the nervous system remains unknown, it is impossible to conclude whether the differences observed in the metabolism of thiamine compounds are the cause or the consequence of the photosensitivity in the baboon Papio papio. [less ▲]

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See detailPhosphorylation At Ser244 By Ck1 Determines Nuclear Localization And Substrate Targeting Of Pkd2
Von Blume, J.; Knippschild, U.; Dequiedt, Franck ULg et al

in Embo Journal (2007), 26(22),

Protein kinase D2 (PKD2), a member of the PKD family of serine/threonine kinases, is localized in various subcellular compartments including the nucleus where the kinase accumulates upon activation of G ... [more ▼]

Protein kinase D2 (PKD2), a member of the PKD family of serine/threonine kinases, is localized in various subcellular compartments including the nucleus where the kinase accumulates upon activation of G-protein-coupled receptors. We define three critical post-translational modifications required for nuclear accumulation of PKD2 in response to activation of the CCK2 receptor (CCK2R): phosphorylation at Ser706 and Ser710 within the activation loop by PKC eta leading to catalytic activity and phosphorylation at Ser244 within the zinc-finger domain, which is crucial for blocking nuclear export of active PKD2 by preventing its interaction with the Crm-1 export machinery. We identify CK1delta and epsilon as upstream activated kinases by CCK2R that phosphorylate PKD2 at Ser244. Moreover, nuclear accumulation of active PKD2 is a prerequisite for efficient phosphorylation of its nuclear substrate, HDAC7. Only nuclear, active PKD2 mediates CCK2R-induced HDAC7 phosphorylation and Nur77 expression. Thus, we define a novel, compartment-specific signal transduction pathway downstream of CCK2R that phosphorylates PKD2 at three specific sites, results in nuclear accumulation of the active kinase and culminates in efficient phosphorylation of nuclear PKD2 substrates in human gastric cancer cells. [less ▲]

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See detailPhosphorylation of bovine leukemia virus Tax protein is required for in vitro transformation but not for transactivation.
Willems, Luc ULg; Grimonpont, Cathy; Kerkhofs, Pierre et al

in Oncogene (1998), 16(17), 2165-76

The Tax proteins of the oncovirinae viruses are phosphorylated transcriptional activators that exhibit oncogenic potential. The role of phosphorylation in their functional activities remains unknown. As a ... [more ▼]

The Tax proteins of the oncovirinae viruses are phosphorylated transcriptional activators that exhibit oncogenic potential. The role of phosphorylation in their functional activities remains unknown. As a model for the Human T-cell leukemia virus type I (HTLV-I), Bovine Leukemia Virus (BLV) permits the characterization of viral replication and leukemogenesis in vivo. Here, we show that the BLV Tax protein is phosphorylated on serine residues 106 and 293 both in insect and in mammalian cells. These sites can also be efficiently phosphorylated by the cdc2 and MAP kinases in vitro. Mutation of these residues does not affect the capacity of the Tax protein to function as a transactivator. Indeed, the Tax proteins mutated at one or both serines increase LTR-directed viral transcription at levels similar to those obtained with wild-type Tax in cell culture. Moreover, inhibition of Tax phosphorylation by W7, a calmodulin antagonist, does not alter its transactivation activity. Thus, phosphorylation on serines 106 and 293 is not required for transactivation by Tax. However, simultaneous substitution of both serines into alanine residues destroys the capacity of Tax to cooperate with the Ha-ras oncogene to transform primary rat embryo fibroblasts and induce tumors in nude mice. When the serines were replaced with aspartic acid residues, the oncogenic potential of Tax was maintained indicating that the negative charge rather than the phosphate group itself was required for Tax oncogenicity. Finally, to assess the role of the serine residues in vivo, recombinant viruses which express the Tax mutants were constructed and injected into sheep. It appeared that the mutated proviruses replicate at levels similar to the wild-type virus in vivo. We conclude that Tax phosphorylation is dispensable for transactivation and viral replication in vivo but is required for its oncogenic potential in vitro. [less ▲]

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See detailPhosphorylation Of Histone Deacetylase 7 By Protein Kinase D Mediates T Cell Receptor-Induced Nur77 Expression And Apoptosis
Dequiedt, Franck ULg; Van Lint, J.; Lecomte, E. et al

in Journal of Experimental Medicine (2005), 201(5),

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See detailPhosphorylation of huntingtin by cyclin dependent kinase 5.
Godin, Juliette ULg; Anne, Sandrine; Humbert, Sandrine

Poster (2008)

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See detailPhosphorylation of Neurogenin2 specifies the migration properties and the dendritic morphology of pyramidal neurons in the neocortex.
Hand, Randal; Bortone, Dante; Mattar, Pierre et al

in Neuron (2005), 48(1), 45-62

The molecular mechanisms specifying the dendritic morphology of different neuronal subtypes are poorly understood. Here we demonstrate that the bHLH transcription factor Neurogenin2 (Ngn2) is both ... [more ▼]

The molecular mechanisms specifying the dendritic morphology of different neuronal subtypes are poorly understood. Here we demonstrate that the bHLH transcription factor Neurogenin2 (Ngn2) is both necessary and sufficient for specifying the dendritic morphology of pyramidal neurons in vivo by specifying the polarity of its leading process during the initiation of radial migration. The ability of Ngn2 to promote a polarized leading process outgrowth requires the phosphorylation of a single tyrosine residue at position 241, an event that is neither involved in Ngn2 direct transactivation properties nor its proneural function. Interestingly, the migration defect observed in the Ngn2 knockout mouse and in progenitors expressing the Ngn2(Y241F) mutation can be rescued by inhibiting the activity of the small-GTPase RhoA in cortical progenitors. Our results demonstrate that Ngn2 coordinates the acquisition of the radial migration properties and the unipolar dendritic morphology characterizing pyramidal neurons through molecular mechanisms distinct from those mediating its proneural activity. [less ▲]

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See detailPhosphorylation of NF-kappa B and I kappa B proteins: implications in cancer and inflammation
Viatour, Patrick ULg; Merville, Marie-Paule ULg; Bours, Vincent ULg et al

in Trends in Biochemical Sciences (2005), 30(1), 43-52

Nuclear factor-kappaB (NF-kappaB) is a transcription factor that has crucial roles in inflammation, immunity, cell proliferation and apoptosis. Activation of NF-kappaB mainly occurs via IkappaB kinase ... [more ▼]

Nuclear factor-kappaB (NF-kappaB) is a transcription factor that has crucial roles in inflammation, immunity, cell proliferation and apoptosis. Activation of NF-kappaB mainly occurs via IkappaB kinase (IKK)-mediated phosphorylation of inhibitory molecules, including IkappaBalpha. Optimal induction of NF-kappaB target genes also requires phosphorylation of NF-kappaB proteins, such as p65, within their transactivation domain by a variety of kinases in response to distinct stimuli. Whether, and how, phosphorylation modulates the function of other NF-kappaB and IkappaB proteins, such as B-cell lymphoma 3, remains unclear. The identification and characterization of all the kinases known to phosphorylate NF-kappaB and IkappaB proteins are described here. Because deregulation of NF-kappaB and IkappaB phosphorylations is a hallmark of chronic inflammatory diseases and cancer, newly designed drugs targeting these constitutively activated signalling pathways represent promising therapeutic tools. [less ▲]

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See detailPhosphorylation of p65(RelA) on Ser547 by ATM represses NF-κB-dependent transcription of specific genes after genotoxic stress.
Sabatel, Hélène ULg; Di Valentin, Emmanuel ULg; Gloire, Geoffrey ULg et al

in PLoS ONE (2012)

The NF-κB pathway is involved in immune and inflammation responses, proliferation, differentiation and cell death or survival. It is activated by many external stimuli including genotoxic stress. DNA ... [more ▼]

The NF-κB pathway is involved in immune and inflammation responses, proliferation, differentiation and cell death or survival. It is activated by many external stimuli including genotoxic stress. DNA double-strand breaks activate NF-κB in an ATM-dependent manner. In this manuscript, a direct interaction between p65(RelA) and the N-terminal extremity of ATM is reported. We also report that only one of the five potential ATM-(S/T)Q target sites present in p65, namely Ser547, is specifically phosphorylated by ATM in vitro. A comparative transcriptomic analysis performed in HEK-293 cells expressing either wild-type HA-p65 or a non-phosphorylatable mutant HA-p65S547A identified several differentially transcribed genes after an etoposide treatment (e.g. IL8, A20, SELE). The transcription of these genes is increased in cells expressing the mutant. Substitution of Ser547 to alanine does not affect p65 binding abilities on the κB site of the IL8 promoter but reduces p65 interaction with HDAC1. Cells expressing p65S547A have a higher level of histone H3 acetylated on Lys9 at the IL8 promoter, which is in agreement with the higher gene induction observed. These results indicate that ATM regulates a sub-set of NF-κB dependent genes after a genotoxic stress by direct phosphorylation of p65. [less ▲]

Detailed reference viewed: 44 (17 ULg)
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See detailPhosphorylation of Proteins Induced in a Murine Pre-T Cell Line by Neurohypophysial Peptides
Martens, Henri ULg; Kecha, O.; Charlet-Renard, C. et al

in Advances in Experimental Medicine and Biology (1998), 449

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See detailPhosphorylation of proteins induced in a murine pre-T cell line by neurohypophysial peptides
Martens, Henri ULg; Kecha, Ouafae; Brilot, Fabienne et al

in Zingg, Hans H.; Bourque, Charles W.; Bichet, Daniel (Eds.) Vasopressin and Oxytocin: Molecular, Cellular, and Clinical Advances (1998)

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See detailPhosphorylation of SCG10/stathmin-2 determines multipolar stage exit and neuronal migration rate
Westerlund, N.; Zdrojewska, J.; Padzik, A. et al

in Nature Neuroscience (2011)

Detailed reference viewed: 21 (2 ULg)
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See detailPhosphorylation of the Bovine Leukemia Virus transactivator p34Tax is required for transformation but not for transactivation.
Kettmann, Richard ULg; Grimonpont, C.; Kerkhofs, Pierre et al

in FASEB Journal (1997), 11(9), 1179

Detailed reference viewed: 7 (1 ULg)