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See detailA Namurian A (Silesian) permineralised flora from the "Carrière du Lion" at Engihoul (Belgium).
Gerrienne, Philippe ULg; Fairon-Demaret, Muriel ULg; Galtier, Jean

in Review of Palaeobotany and Palynology (1999), 107

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See detailLe Namurois de la Foire
Ozer, Pierre ULg

Article for general public (2013)

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See detailNancy Huston, Urgence d'écrire
Dor, Juliette ULg

E-print/Working paper (2012)

CR de "Reflets dans un œil d'homme"

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See detailNandrin - Plan communal de mobilité et de sécurité
Hanocq, Philippe ULg; Lacroix, Pascal; Angenot, Etienne ULg

in Croughs, Roger; Jacobs, Chantal; Vermeiren, Benoît (Eds.) le plan communal de mobilité - Evaluation de projets-pilotes wallons - Méthode de conception (1997)

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See detailNandrin - Plan communal de mobilité et de sécurité
Lacroix, Pascal; Hanocq, Philippe ULg; Angenot, Etienne ULg

Report (1996)

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See detailNăng suất chăn nuôi một số gia cấm trong nông hộ tại huyên Phú Xuyên và Chương Mỹ , Hàn ội
Phan Dang, Thang; Bui Huu, Doan; Duquesne, Brigitte ULg et al

in Vietnam Journal of Agriculture and Rural Development = Nông Nghiệp, Công Nghiệp Thục̛ Phâm (2011), (165), 54-59

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See detailNăng suất sinh sản của các tổ hợp lai giữa lợn nái F1(Landrace x Yorkshire) với đực giống (Piétrain x Duroc) có thành phần di truyền Piétrain kháng stress khác nhau
Dao, Pham Thi; Thang, Nguyen Van; Do Duc, Luc ULg et al

in Journal of Animal Husbandry and Technics (2013), (6), 2-9

This study was carried out at 3 pig farm in Hai Duong and Hung Yen provinces from March 2012 to February 2013 to evaluate the reproduction performance of F1(Landrace x Yorkshire) - LY sows mated to three ... [more ▼]

This study was carried out at 3 pig farm in Hai Duong and Hung Yen provinces from March 2012 to February 2013 to evaluate the reproduction performance of F1(Landrace x Yorkshire) - LY sows mated to three different crossbred boars such as Duroc x ( Piétrain x Duroc) - Pi25, Piétrain x Durroc - Pi50 and Piétrain x (Piétrain x Duroc) - Pi75. Results showed that the reproduction performance of three crossbred boars was high: 10.76, 10.50 and 10.97 pigs born alive per litter; 9.90, 9.91 and 10.04 respectively for Pi25, Pi50 and Pi75. Piglet body weights at birth were 1.36, 1.58 and 1.54kg and body weight of pigs at weaning were 6.39, 6.59 and 6.41kg respectively for Pi25 x LY, Pi50 x LY and Pi75 x LY. Pi50 and Pi75 could be used as terminal sires mated to LY to obtain better reproduction performance. [less ▲]

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See detailNăng suất sinh sản của đàn lợn hạt nhân Piétrain kháng stress và Duroc nuôi tại Trung tâm giống lợn chất lượng cao Trường Đại học Nông nghiệp Hà Nội
Do Duc, Luc ULg; Ha Xuan, Bo; Nguyen Chi, Thanh et al

in Journal of Science and Development (2013), 11(1), 30-35

A study was carried out from December 2011 to August 2012 to evaluate reproductive performance of nucleus herd of stress negative Piétrain (Piétrain) and Duroc pigs raised at the experimental farm of ... [more ▼]

A study was carried out from December 2011 to August 2012 to evaluate reproductive performance of nucleus herd of stress negative Piétrain (Piétrain) and Duroc pigs raised at the experimental farm of Hanoi University of Agriculture. A total of 35 gilts, including 21 Piétrain (11 with halothane genotype CC and 10 with CT) and 14 Duroc CC gilts were monitored for their reproductive performance. Piétrain boars (3 CC and 5 CT) were mated to Piétrain and Duroc gilts to produce Piétrain purebred and crossbred Piétrain x Duroc pigs. Results showed that genotype of the boar and the sow affected body weight and litter weight at birth and at weaning (P<0.05). Total number of pigs born, number born alive, number alive to weaning, individual bodyweight at birth, individual bodyweight at weaning, litter weight at birth, litter weight at weaning, survival rate at birth, survival rate to weaning were 9.91, 9.26, 8.11 piglets, 1.4, 6.4, 12.97, 51.96kg, 94.32 and 88.55%, respectively. Body weight and litter weight at birth and at weaning of piglets from Piétrain CC boars were higher than those of piglets from Piétrain CT boars (P<0.05). Reproductive performance was highest for Duroc CC sows, followed by Piétrain CC and lowest for Piétrain CT sows (P<0.05). Reproductive performance of the nucleus herd could be improved by using Piétrain CC boars mated to Piétrain CC sows and Duroc CC sows. [less ▲]

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See detailNăng suất sinh trưởng, thân thịt và chất lượng thịt của các tổ hợp lai giữa lợn nái F1(landrace x Yorkshire) với đực giống (Piétrain x Duroc) có thành phần Piétrain kháng stress khác nhau
Pham Thi, Dao; Nguyen Van, Thang; Vu Dinh, Ton et al

in Journal of Science and Development (2013), 11(2), 200-208

The study was carried out at 3 pig farms in Hai Duong and Hung Yen from March 2011 to January 2013 to evaluate growth rate and carcass quality of F1(Landrace x Yorkshire) (F1(L x Y)) sows mated with F1 ... [more ▼]

The study was carried out at 3 pig farms in Hai Duong and Hung Yen from March 2011 to January 2013 to evaluate growth rate and carcass quality of F1(Landrace x Yorkshire) (F1(L x Y)) sows mated with F1(Piétrain x Duroc) (PiDu) boars with Pietrain ReHal genetic constitution (25, 50 and 50%: PiDu25, PiDu50, PiDu75). The results showed that these crossbreds obtained high growth rates and low feed conversion ratio (FCR) (829.42 g/day and 2.31 kg/kg; 797.78 g/day and 2.33 kg/kg; 765.79 g/day and 2.38 kg feed/kg weight gain, respectively). Lean meat percentage of PiDu25 x F1(L x Y), PiDu50 x F1(L x Y) và PiDu75 x F1(L x Y) were 54.66, 56.32 and 59.97%, respectively. Lean meat percentage of PiDu75 x F1(L x Y) was higher than that of PiDu25 x F1(L x Y) and PiDu50 x F1(L x Y). The meat quality traits in terms of pH, colour drip loss, and firmness of 3 crossbreds were normal. Crude protein of musculus longissimus dorsi of crossbreds was 21.53, 22.18 and 22.63%. The research suggests that using crossbed boars PiDu25, PiDu50, PiDu75 to mate with F1(L x Y) sows helps to obtain high performance in pig farms [less ▲]

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See detailNani in Festa
Moret, Jean-Marc; Morard, Thomas ULg

Conference given outside the academic context (2009)

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See detail"Nano-imaginaries" in a Future Smart Environment: Breakdown of a Three Round Delphi Study
Van Oudheusden, Michiel ULg; Evers, Johan; Deblonde, Marian et al

Report (2007)

This report summarizes the key findings of a three round Delphi study involving nanotechnologists, Technology Assessment experts, and citizens in Flanders, on the future of a nanotechnology-enabled smart ... [more ▼]

This report summarizes the key findings of a three round Delphi study involving nanotechnologists, Technology Assessment experts, and citizens in Flanders, on the future of a nanotechnology-enabled smart environment. First it lays out the conceptual basis and methodological design of the Delphi study from the perspective of the Flemish Interactive Technology Assessment project ‘Nanotechnologies for Tomorrow’s Society’, which the authors coordinate. It then discerns respondents’ envisaged solutions or responses to key issues or problems in relation to nanotechnology’s emergence, thereby identifying recurrent themes in respondents’ narratives, including personalization, user convenience, and prevention, which, it is argued, are all concerned with the more fundamental issues of human control over nature and human destiny. The report also gives a brief impression of the resultant ‘nano-imaginaries’ which emerged in the final round and concludes with a critical afterthought in view of the objectives which the Delphi study sought to achieve. [less ▲]

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See detailNano-sized drug carriers and their interactions with biomimetic model membranes
Frost, R; Cerda, B; Grandfils, Christian ULg et al

Poster (2009, September 28)

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See detailNano-ultrasonics sensors
Arca, Ahmet; Dispas, Amandine ULg; Jamie, Twycross et al

Poster (2010, November)

Ultrasound is a powerful tool for diagnosing medical and mechanical problems. Conventional ultrasonics work at megahertz frequencies and with wavelengths of 1-2mms to 10’s mm. This means it cannot "see ... [more ▼]

Ultrasound is a powerful tool for diagnosing medical and mechanical problems. Conventional ultrasonics work at megahertz frequencies and with wavelengths of 1-2mms to 10’s mm. This means it cannot "see" very small objects at the nanoscale. Our new transducers are so small it is impractical to communicate with them electrically. Instead we have devised a non contact method of talking to them using short pulses of laser light. We have adopted two approaches for producing these transducers, one method builds plates devices the other uses self assembled nanoparticles. The transducers are made from alternating metal and soft transparent layers. They have optical and mechanical resonances and so the devices have to be made such that they work well both mechanically and optically [less ▲]

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See detailNanoblock coupling effect in iodine intercalated [Bi0.82CaO 2]2[CoO2]1.69 layered cobaltite
Guilmeau, E.; Pollet, M.; Grebille, D. et al

in Inorganic Chemistry (2007), 46(6), 2124-2131

We report on the structural, microstructural, and electronic properties of iodine intercalated [Bi0.82CaO2]2[CoO 2]1.69 misfit cobaltite. We first prove through a detailed and careful structural study ... [more ▼]

We report on the structural, microstructural, and electronic properties of iodine intercalated [Bi0.82CaO2]2[CoO 2]1.69 misfit cobaltite. We first prove through a detailed and careful structural study that the block layer structure can be modified in the desired way. Iodine enters the material between the [BiO] double layers, and the c-cell parameter of the pristine compound is elongated by 3.6 Å. On the basis of this result, we point out the coupling between the block-layer structure and the transport properties. Additionally, we provide in-depth commentary and discussion of some extra results, clarifying some doping effects in the quasi-2D studied phase. Finally, we also propose some expressions that might be useful to material scientists for the tuning of the properties of such compounds. © 2007 American Chemical Society. [less ▲]

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See detailNanobodies as structural probes to investigate the mechanism of fibril formation by the amyloidogenic variants of human lysozyme
Dumont, Janice ULg; pardon, Els; Aumont-Nicaise, Magali et al

Poster (2012, June)

Six variants of human lysozyme (single-point mutatants I56T, F57I, W64R, D67H and double mutants F57I/T70N, W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidosis. These ... [more ▼]

Six variants of human lysozyme (single-point mutatants I56T, F57I, W64R, D67H and double mutants F57I/T70N, W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidosis. These proteins form extracellular amyloid fibrils that deposit in a wide range of tissues and organs such as liver, spleen and kidneys where they cause damages [1]. It was shown that the D67H and I56T mutations cause a loss in stability and more particularly a loss of global cooperativity of protein [1]. Consequently, under physiologically relevant conditions, these variants can transiently populate a partially unfolded state in which the beta-domain and the C-helix are cooperatively unfolded while the rest of the protein remains native like [1]. The formation of intermolecular interactions between the regions that are unfolded in this intermediate state is likely to be a fundamental trigger of the aggregation process that ultimately leads to the formation and deposition of fibrils in tissues. We have also shown that the binding of three variable domain of camelid antibodies (VHHs) - raised against the wild type human lysozyme inhibit in vitro the formation of amyloid fibrils by the lysozyme variants. These three VHHs bind on different regions of lysozyme and act as amyloid fibril inhibitor through different mechanisms [2, 3, and unpublished results]. In the present work, sixteen new VHHs specific of human lysozyme have been generated. Competition experiments have shown that they bind to five non-overlapping epitopes. We have demonstrated that five of these VHHs are able to bind lysozyme in conditions used for amyloid fibril formation, and interestingly two of them recognize two epitopes that are different from those of the three VHHs previously characterized [2, 3, and unpublished results]. The effects of these new VHHs on the properties of lysozyme variants such as stability, cooperativity and aggregation will be discussed. [1] Dumoulin, M., J.R. Kumita, and C.M. Dobson, Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants. Acc Chem Res, 2006, 39(9), 603-610. [2] Dumoulin, M., et al., A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature, 2003, 424, 783-788. [3] Chan, P.H., et al., Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils. Biochemistry, 2008, 47, 11041-11054. [less ▲]

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See detailNanobodies as structural probes to investigate the mechanism of fibril formation by the amyloidogenic variants of human lysozyme
Dumont, Janice ULg; Pardon, Els; Aumont-Nicaise, Magalie et al

Poster (2011)

Six variants of human lysozyme (single-point mutations I56T, F57I, W64R, D67H and double mutations F57I/T70N, W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidose. These ... [more ▼]

Six variants of human lysozyme (single-point mutations I56T, F57I, W64R, D67H and double mutations F57I/T70N, W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidose. These proteins form extracellular amyloid fibrils that deposit in a wide range of tissues and organs such as liver, spleen and kidneys where they cause damages [1]. It was shown that the D67H and I56T mutations cause a loss in stability and more particularly a loss of global cooperativity of protein [1]. Consequently, under physiologically relevant conditions, these variants can transiently populate a partially unfolded state in which the beta-domain and the C-helix are cooperatively unfolded while the rest of the protein remains native like [1]. The formation of intermolecular interactions between the regions that are unfolded in this intermediate state is likely to be a fundamental trigger of the aggregation process that ultimately leads to the formation and deposition of fibrils in tissues. We have also shown that the binding of three variable domain of camelid antibodies or (VHHs) - raised against the wild type human lysozyme inhibit in vitro the formation of amyloid fibrils by the lysozyme variants. These three VHHs bind on different regions of lysozyme and act as amyloid fibrils inhibitor through different mechanisms [2, 3, and unpublished results]. In the present work, sixteen new VHHs specific of human lysozyme have been generated. Competition experiments have shown that they bind to five non overlapping epitopes. We have demonstrated that five of these new VHHs are able to bind lysozyme in conditions used for amyloid fibril formation, and interestingly two of them recognize two epitopes that are different from those of the three VHHs previously characterized [2, 3, and unpublished results]. The effects of these new VHHs on the properties of lysozyme variants such as activity, stability, cooperativity and aggregation will be discussed. [less ▲]

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See detailNanobodies as structural probes to investigate the mechanism of fibril formation by the amyloidogenic variants of human lysozyme.
Dumont, Janice ULg; Menzer, Linda ULg; Pardon, Els et al

Poster (2010)

Six variants of human lysozyme (single-point mutations I56T, F57I, W64R, D67H and double mutations F57I/T70N, W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidose. These ... [more ▼]

Six variants of human lysozyme (single-point mutations I56T, F57I, W64R, D67H and double mutations F57I/T70N, W112R/T70N) are associated with a hereditary non-neuropathic systemic amyloidose. These proteins form extracellular amyloid fibrils that deposit in a wide range of tissues and organs such as liver, spleen and kidneys where they cause damages [1]. It was shown that the D67H and I56T mutations cause a loss in stability and more particularly a loss of global cooperativity of protein [1]. Consequently, under physiologically relevant conditions, these variants can transiently populate a partially unfolded state in which the beta-domain and the C-helix are cooperatively unfolded while the rest of the protein remains native like [1]. The formation of intermolecular interactions between the regions that are unfolded in this intermediate state is likely to be a fundamental trigger of the aggregation process that ultimately leads to the formation and deposition of fibrils in tissues. The binding of three variable domain of camelid antibodies – also named nanobodies - (cAb-HuL 6 [2], cAb-HuL 5 and cAb-HuL 22 [3]) raised against the wild type human lysozyme inhibit in vitro the formation of amyloid fibrils by the lysozyme variants. These three nanobodies bind on different regions of lysozyme and act as Amyloid fibrils inhibitor through different mechanisms. On one hand, cAb-HuL 6 and cAb-HuL 22 stabilize the native state of the lysozyme variants thus restoring the global cooperativity characteristic of the wild-type protein. On the other, cAb-HuL 5 probably acts by binding soluble prefibrillar aggregates. In the present work, sixteen other nanobodies specific of human lysozyme have been generated. Competition experiments have shown that they bind to five non overlapping epitopes. The effects of the binding of these nanobodies on the stability of the D67H variant of human lysozyme and on its aggregation into amyloid fibrils will be discussed. [less ▲]

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See detailNanobodies as tools to investigate the mechanism of aggregation of chimeric proteins made by the insertion of polyglutamine stretches into the beta-lactamase BlaP
Pain, Coralie ULg

Doctoral thesis (2014)

Among the neurodegenerative amyloidoses, ten disorders, referred to as polyglutamine (polyQ) diseases and including Huntington's disease and several spinocerebellar ataxias, are associated with ten ... [more ▼]

Among the neurodegenerative amyloidoses, ten disorders, referred to as polyglutamine (polyQ) diseases and including Huntington's disease and several spinocerebellar ataxias, are associated with ten proteins within which a polyQ tract is expanded above a threshold of typically 35-45 glutamine residues. Such expanded polyQ tracts lead to the aggregation of the host protein into amyloid fibrils that accumulate in the nucleus of some populations of neurons; these aggregates or some of their precursors are thought to contribute to neuronal death. So far, no preventive or curative treatment exists for these devastating pathologies. While the expansion of the polyQ tract above the threshold is the determinant factor for aggregation, recent studies suggest that non-polyQ regions of these proteins can play a significant role, either preventative or facilitative, in the aggregation process. The general principles governing the complex interplay between the role of the expanded polyQ tract and the role of the non-polyQ regions in the aggregation process are not well understood yet. In order to develop therapeutic strategies, it is important to better understand this complex interplay. To contribute to this aim, we have engineered chimeric proteins via the insertion of polyQ repeats of various lengths (23, 30, 55 and 79Q) into two sites (197 and 216) of the BlaP beta-lactamase from Bacillus licheniformis 749/C. The properties of these chimeric proteins recapitulate the characteristic features of the disease-associated polyQ proteins, i.e. (i) there is a minimum number of inserted glutamines (threshold) required to trigger the aggregation of the chimeras into amyloid fibrils, and (ii) above the threshold, the longer the polyQ tract, the faster the aggregation. Interestingly, for the same polyQ length, the chimeras with insertions in position 216 have an increased propensity to form amyloid fibrils compared to their counterparts with insertions in position 197. These findings highlight the strong influence of the overall protein context on aggregation triggered by expanded polyQ tracts. This thesis addresses the use of the variable domains of camelid heavy-chain antibodies, referred to as nanobodies or VHHs, as structural and mechanistic probes to better understand the different aggregating properties of the two sets of BlaP-polyQ chimeras (197 and 216). We have also performed limited proteolysis experiments and transglutaminase-mediated reactions on the monomeric form of the BlaP-polyQ chimeras to further investigate the effects of the polyQ insertions on the structure and dynamics of the BlaP moiety, as well as the structure of the polyQ tract itself. From the blood of a llama immunised with BlaP197(Gln)55, we isolated more than 60 VHHs specific to the BlaP-polyQ chimeras. Twenty eight of them were produced, purified and characterised. These VHHs were found to be all specific to the BlaP moiety and could be classified into four different groups recognising distinct epitopes on the surface of BlaP. One representative VHH of each group (i.e. cAb-A3S, cAb-H7S, cAb-F11N and cAb-G10S) was selected as probe to investigate the mechanism of aggregation of the BlaP-polyQ chimeras. The epitope of three of them was determined by X-ray diffraction and/or by NMR spectroscopy. Although they recognise distinct epitopes and exhibit different affinities for BlaP, the binding of the four VHHs significantly slows down the aggregation of all the BlaP-polyQ chimeras investigated (i.e. BlaP197(Gln)55, BlaP197(Gln)79 and BlaP216(Gln)79). The extent of inhibition depends however on the chimera and on the experimental conditions. We show that the inhibition of the aggregation of BlaP197(Gln)55 and BlaP197(Gln)79 upon binding of the four VHHs is correlated with the stabilisation of their native state. In the case of BlaP216(Gln)79, the extent of inhibition could not be only correlated to the stabilisation of its native state; the location of the epitope of the VHH is instead also determinant. This observation demonstrates that the lower thermodynamic stability of BlaP216(Gln)79 is not the unique factor responsible for its increased aggregation propensity. It also further highlights the complexity of the aggregation mechanism of polyQ proteins and the strong influence of the non-polyQ regions on the amyloid fibril formation triggered by the expanded polyQ tract. All together our results suggest that antibodies or antibody fragments raised against the non-polyQ regions of polyQ proteins associated with diseases could constitute a relevant therapeutic strategy. They also further demonstrate the power of nanobodies as probes to get a deeper knowledge of the underlying mechanisms of amyloid fibril formation. The preliminary limited proteolysis and transglutamination experiments obtained suggest that the polyQ tracts are all flexible, except that of 23 glutamines inserted in position 197 of BlaP, which seems to be more rigid than the others. The results obtained confirm that, globally, the structure of BlaP is not significantly modified by the insertions while the 216 chimeras seem more dynamic than the 197 chimeras. [less ▲]

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See detailA Nanobody Binding to Non-amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril Formation.
de Genst, EJ; Chan, PH; Pardon, Els et al

in Journal of Physical Chemistry B (2013)

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