dataesr/scientific-paragraphs-categorization huggingface dataset:
Acknowledgments. We thank  Françoise Guinet ,  Michel Chignard ,  Laurence Arbibe , and  Jean-Marc Cavaillon  for helpful discussions;  G. Cornelis  for kindly providing the YopE-Cya plasmid;  S. Mécheri ,  G. Delespesse , and  W. L. Lathem  for suggestions on the manuscript;  S. Dallongeville  for teaching the ICY software: and  I. Lanctin  for breeding SEG mice. We also acknowledge the  Technology Core of the Center for Translational Science at Institut Pasteur  for support in conducting this study. Financial support. This work was supported  Pasteur Roux  and  Carnot-Pasteur Maladies Infectieuses (postdoctoral fellowships  to H. O. ) and the  Philippe Foundation  (international mobility support to H. O. ). Potential conflicts of interest. All authors: No reported conflicts of interest. All authors have submitted the  ICMJE Form for Disclosure of Potential Conflicts of Interest.
PET scans and data acquisition Cerebral ischemia studies. PET scans were repeatedly performed before reperfusion (day 0) and at 1, 3, 7, 14, 21 and 28 days afterwards using a General Electric eXplore Vista CT camera (GE Healthcare). Scans were performed in rats anaesthetized with 4% isofluorane and maintained by 2-2. 5% of isofluorane in 100% O 2. The tail vein was catheterized with a 24-gauge catheter for intravenous administration of the radiotracer. Animals were placed into a rat holder compatible with PET acquisition system and maintained normothermic using a water-based heating blanket. Animals were subjected to PET scans to assess CB2 receptors ([ 11 C]A-836339) at each time point (before and after ischemia onset). For longitudinal imaging evaluation of CB2 receptors, $70 MBq of [ 11 C]A-836339 was injected at the start of the PET acquisition.
5 mm À1. LPS and AMPA studies. [ 11 C]A-836339 dynamic PET scans were acquired two days (LPS) or seven days (AMPA) after intrastriatal injection using a Siemens Inveon Õ small animal PET or PET-CT scanner. Both scanners were used in parallel in order to assure a high specific radioactivity at the time of injection. The imaging time points were chosen based on previous studies that demonstrated different dynamics of the models which indicated strong neuroinflammation at early times (16-72 h) after LPS injection  26, 32  compared to seven days post AMPA injection. 33 Animals were anaesthetized with isoflurane (induction: 4%, maintenance: 2-2. 5%) in oxygen. The radiolabeled compound was injected in the caudal vein through a 24-gauge catheter at the start of the PET acquisition. The mean injected doses were $40 MBq and PET data were acquired during 60 min.
PET image analysis Cerebral ischemia studies. PET images were analyzed using PMOD image analysis software (PMOD Technologies Ltd, Zu¨rich, Switzerland). To verify the anatomical location of the signal, PET images were coregistered to the anatomical data of an MRI rat brain template. VOIs were manually drawn in the entire ipsilateral hemisphere that contained the area supplied by the MCA on slices of a MRI (T 2 W) rat brain template from the PMOD software to study the [ 11 C]A-836339 and [ 18 F]DPA-714 PET signal. For quantification of radiotracers uptake, the last three ([ 11 C]A-836339) or four frames ([ 18 F]DPA-714) in steady state were used to calculate the summed PET binding during the last 15 min of acquisition. PET signal uptake was averaged in each ROI and expressed as percentage of injected dose per cubic centimetre (% ID/cc).
LPS and AMPA studies. PET image analysis was performed using VINCI, a fast graphical image analysis package  34  with image co-registration tools. PET images were co-registered to an MRI template. 35 The Anatomist BrainVISA software package (http://www. brainvisa. info) was also used for data evaluation. For quantitative analysis, a volume-of-interest (VOI) analysis was performed on kinetic image data sets. Two VOIs were manually delineated, one around the injection site in the ipsilateral and one control VOI in the contralateral hemisphere. The time activity curves extracted from these VOIs were obtained from dynamic PET data and normalized by the injected dose (% ID). Immunohistochemistry and cell counts. Immunohistochemistry staining was performed at control (day 0), day 7 and day 28 after cerebral ischemia.
Acknowledgements The authors would like to thank  L Colas ,  Dr. B Sczcupak ,  L Morales ,  A Leukona ,  V Salinas ,  A Arrieta  and  A Cano  for technical support in the immunohictochemistry, radiosynthesis and technical assistance in the PET studies,  Dr. C Wimberley  for English language editing and  Prof. M Higuchi  for the gift of the NP155 antibody.
Funding The author(s) disclosed receipt of the following financial support for the research, authorship, and/or publication of this article: This study was funded by the  Department of Industry of the Basque Government  and  Spanish Ministry of Economy and Competitiveness  through grant  SAF2014-54070-JIN , the  EU   7th Framework Programme  ( FP7/2007-2013)  under grant agreement n  278850  ( INMiND ) and the  France Life Imaging  under grant agreement  ANR-11-INBS-0006  (FLI).
Minimum clinically important difference analysis confirms the efficacy of IgPro10 in CIDP: the PRIMA trial Dear Editor, The PRIMA (PRivigen Impact on Mobility and Autonomy, NCT01184846) trial, a prospective, multi-center, single-arm, open-label, phase III trial, was designed to assess efficacy and safety of IgPro10 (10% liquid IVIG formulated with L-proline, Privigen ® , CSL Behring, Berne, Switzerland) in patients with chronic inflammatory demyelinating polyneuropathy (CIDP)  (Léger et al. , 2013). The primary outcome of the PRIMA study was the responder rate by the 10-point adjusted Inflammatory Neuropathy Cause and Treatment (INCAT) disability score (responders defined as showing an INCAT score improvement ≥1 vs baseline). The success criterion (responder rate ≥35%) was met, making IgPro10 the second IgG product with demonstrated efficacy in CIDP (after IGIV-C)  (Hughes et al.
Acknowledgements The authors would like to thank  Alphonse Hubsch  from  CSL Behring AG, Berne, Switzerland  for the critical review of this Letter. The authors acknowledge the editorial support of  Emiliana Jelezarova, PhD , from  Fishawack Communications GmbH , a member of the  Fishawack Group of Companies , supported by  CSL Behring. Sincerely,  Ingemar S. J. Merkies  1 , John-Philip Lawo 2 ,  Jonathan M. Edelman 3  ,  Jan L. De Bleecker 4  ,  Claudia Sommer 5  ,  Wim Robberecht 6  ,  Mika Saarela 7  ,  Jerzy Kamienowski  8 , Zbigniew Stelmasiak 9 , Orell Mielke 2 ,  Björn Tackenberg 10  ,  Jean-Marc Léger   11  , and on behalf of the PRIMA trial investigators † 1  Spaarne Hospital, Hoofddorp , and  Maastricht University Medical Centre , Maastricht, The Netherlands ; 2  CSL Behring GmbH, Marburg, Germany ; 3  CSL Behring LLC, King of Prussia, PA, USA ; 4 AZ St-Lucas, Gent, Belgium; 5  Department of Neurology, Universitätsklinikum Würzburg, Würzburg, Germany ; 6  UZ Leuven, Leuven, Belgium; 7 Department of Neurology, Helsinki University Central Hospital, Helsinki , Finland; 8  Dolno śl aski Szpital Specjalistyczny , Wroclaw, Poland; 9  Samodzielny Publiczny Szpital Kliniczny, Lublin , Poland; 10  Department of Neurology, Philipps University, Marburg, Germany ; and 11 Reference Center for  Rare Neuromuscular Diseases, Hôpital Pitié-Salpêtrière , and  University Paris VI, Paris ,  France † See Appendix  for complete list of Study group members.
The fluorescent intensity was determined by a Perkin Elmer LS55 spectrofluorimeter (Becton Dickinson, San Jose, CA, USA) with excitation at 530 nm and emission at 590 nm. The cytotoxic concentration which kill 50% of cells (CC 50 ) was determined by nonlinear regression analysis of the logarithm of concentration in function of the normalized response (percentage of cell viability) using the software GraphPad Prism 6. 0 (GPW6-242831-RBMZ-03274). Each experiment was performed in triplicate and repeated three times.
Cell Death Mechanism by Cytometry For the evaluation of cell death (necrosis/apoptosis) mechanism, cells were labeled with Annexin FITC-conjugated (1:500) and propidium iodide (PI) fluorochrome. Briefly, MCF-7 and MDA-MB-231 cells (3. 5 × 10 5 cells/mL) were plated in a 12-well plate and treated with F. umbellata MeOH extract at 45, 90 and 180 µg/mL or solvent control (DMSO) for 24 h. Further, cells were washed twice with cold PBS (500 mL/well) and resuspended in the binding buffer. The pellets were stained with the fluorescent probe solution (50 mg/mL PI and 1 mg/mL Annexin in PBS) on ice in dark for 15 min. Cells were analyzed by flow cytometer BD DACS Verse (Becton Dickinson, Franklin Lakes, NJ, USA) and the results were analyzed using WinMDI 2. 9 software. Each experiment was repeated three times.
Wound-Healing Assay This assay was performed to assess the ability of F. umbellata constituents to inhibit MDA-MB-231 cells migration using the scratch method. Briefly, cells were plated in the 12-well plates at a density of 3 × 10 5 cells/mL in DMEM with 10% FBS. Twenty-four hours after, the cell layer was scratched with a sterile plastic tip and then washed twice with PBS to remove cells mechanically detached. The cells were then maintained in DMEM for 48 h with F. umbellata MeOH extract at 45, 90 and 180 µg/mL or solvent control (DMSO). The cell migration was recorded using a light microscopy Nikon Eclise TS100 (Melville, NY, USA), photographed every 12 h and area of wound healing was evaluated by image editor software (ImageJ ® ). Each experiment was repeated three times.
5%. Further, the membranes were washed four times with TBS-T and incubated with anti-mouse IgG peroxidase secondary antibody (1:10,000) (Sigma Aldrich, St. Louis, MO, USA). Immune complexes were visualized by chemiluminescent detection using Amersham ECL™ (GE Healthcare, UK) detected by ChemiDoc MP (Bio-Rad, CA, USA). Proteins were quantified on Bio-Rad image analysis software (Bio-Rad, Hercules, CA, USA) and β-actin was used to ensure equal loading of proteins and normalize the proteins content.
Histological Analysis Histomorphological changes in mammary glands, ovaries, uterus, brain and liver were determined by using 5 µm tissue sections of paraffin-embedded organs stained with hematoxylin and eosin. Histological sections were observed and images were captured using the complete Zeiss equipment consisting of a microscope Axioskop 40 connected to a computer where the images were transferred and analyzed with the MRGrab 1. 0 and Axio Vision 3. 1 softwares, all provided by Zeiss (Hallbermoos, Germany). The mammary tumors were classified using the well characterized criteria  [40].
Statistical Analysis For in vitro experiments, the results were presented as mean ± standard error of mean (SEM) of triplicates from three-independent experiments. For in vivo experiment, the data from each experimental group was expressed as mean ± SEM. One-way analysis of variance (ANOVA) followed by Dunnett's post-hoc test for multiple comparisons were used for statistical analysis of data using GraphPad Prism software version 6. 00. Differences were considered significant at a probability level of 5% (p < 0. 05).
Of note, the importance of M +… Cπ(arene) in biological structures, supramolecular assemblies, and catalytic and ion transportation processes has long been established  [8] [9] [10] [11] [12] [13] [14]. Many such complexes have been structurally characterized; there are nearly 300 referenced X-ray structures to date in the Cambridge Structural Database (CSD) for  6 -coordinated K +… Cπ(arene) compounds alone. As part of our program aimed at implementing the large alkaline earths (Ae = Ca, Sr, Ba) in molecular catalysis, we prepared some time ago several heteroleptic amido-Ae aryloxides and fluoroalkoxides stabilized by secondary interactions, in particular intramolecular Ae 2+… F contacts and β-Si-H … Ae 2+ agostic distortions when using the N(SiMe2H)  amido co-ligand  [15] [16] [17] [18].
System control and data processing were carried out using MassLynx software version 4. 1. Spray voltage was 3. 0 kV, and sheath and auxiliary gas pressures were 50 and 15 (arbitrary units), respectively. The insource CID energy was fixed at 12 V, and capillary temperature was 350 °C. Tube lens and collision energy values were optimized for insulin. Multiple reaction monitoring was used for the detection of the ion transitions. The multiple reaction monitoring transitions for analytes was as follows: m/z insulin 709. 805 N 731. 76, m/z insulin 1284. 73 N 1104. 60. Analytes were quantified by means of calibration curves using insulin as internal standard. The standard curves showed linearity for creatine over a range of 0. 025-10 μg mL -1 for insulin. The methodology for this assay involves reduction with dithiolthreitol 45 mM and alkylation with 100 mM of iodoacetamide 100 mM of intact insulin for measurement of the free B chain.
Colloidal stability of insulin-loaded PARG NCs during storage Insulin-loaded PARG NCs were stored, as a suspension, at room temperature (~25 °C). The particle size and count rate were monitored up to 45 days (supporting materials Fig. S1 ), and the results showed that these PARG NCs remained stable over this period of time. In addition, insulin content in these NCs was determined at 0, 1, 3, and 15 days, and the insulin remaining unmodified. These positive preliminary stability data are in good agreement with the stabilization strategy defined in the formulation process of NCs.
Toxicity of PARG NCs on Caco-2 cells The cytotoxicity of insulin loaded PARG NCs was evaluated in the Caco-2 model using the LDH and NRU assays. The results of the DHL assay shown in Fig. 9A , indicate that PARG NCs induced a dose-dependent toxicity after a 2 h incubation. LDH release from the damaged cells was observed when the concentration of NCs tested was 1. 48 mg/mL or higher. Very similar results were observed when using the NRU assay (Fig. 9B ). In this case, the cytotoxicity of PARG NCs was compared with that of the control nanoemulsion (same constituents as the NCs except PARG). The conclusion from these data was that the toxicity of the NC and NE was very similar, showing a significant toxicity only at the concentration of 1. 48 mg/mL. On the other hand, the results shown in Fig.
B oth were then tested for inhibition of LecA showing ac omparable diastereoselectivity as observed for the unsubstituted phenyl derivatives 2 and 3 before:6 d epoxide 15 inhibited LecA with an IC 50 of 109 mm,w hereas the diastereomeric 6l epoxide 14 was inactive (IC 50 > 3mm). The stereochemistry of 14 and 15 was unambiguously assigned by combining the activity data and NMR chemical shift and coupling constant analysis and comparison with analogues 2 and 3. T he active diasteromer 15 was then coupled in ac opper(II)-catalyzed click reaction to the azide 16  [17]  to give fluorescent probe 17 in good yields. Thec ovalent nature of the binding of fluoresceinederivative 17 was then further studied by incubation with LecA. Complexes of LecA with 17 or with an on-covalent analogue 18 were performed as observed by high fluorescence polarization.
Figure1. A) Galactoside recognition by the bacterial lectin LecA (pdb: 3ZYF [15]  ); B) Electrophilic epoxide derivatives 2 and 3 for the targeting of Cys62. The distances from Cys62-S to C6 and O6 of 1 are between 4. 1 and 4. 3. (sc = side chain, bb = backbone).
Acknowledgements Theauthors acknowledge the continuous support of  Prof. R olf W. Hartmann  (HIPS). We are further grateful to  Prof. B odo Philipp  ( University of Münster ) and  Prof. A rthur F. J. Ram  ( Leiden University ) for providing bacterial strains and plasmids used in this study,t oS arah Henrikus ( Saarland University ) for the synthesis of 16 and to  Laura Becker  ( University of Konstanz ) for initial synthetic experiments towards the galactose-derived epoxides and  Dr. Josef Zapp  ( Saarland University ) for acquisition of NMR spectra. Emilie Gillon prepared LecA  for crystallization and performed some crystallization trials. A. I. and A. V. acknowledge support from the  ANR  projects  Glyco@Alps  ( ANR-15-IDEX-02 ) and  Labex ARCANE  ( ANR-11-LABX-003 ). A. V. acknowledges financial support from the  European CommunitysS eventh Framework Programme  (FP7/2007-2013) under BioStruct-X (grant agreement No.
All patients who used dental prostheses were required to wear them during measurement. The saliva produced during a period of 5 minutes was collected and measured in a container graduated at 0. 05ml. The volume of salivary flow was calculated in ml/min (millimiter per minute). The patient was instructed not to swallow any amount of saliva that was being produced. Additionally, the patient should keep the body tilted forward in order to avoid saliva swallowing. Sialometric values were given according to standards established by the Brazilian Association of Halitosis (ABHA): 0. 00-0. 049 ml/min-asialia; 0. 05-0. 5 ml/min-severe hyposalivation; 0. 51-0. 9 ml/min-moderate hyposalivation; 0. 91-1. 19 ml/min-mild hyposalivation; 1. 2-2. 5 ml/min-ideal salivation; > 2. 5 ml/min-sialorrhea  [13]. Data were tabulated and statistical calculations were performed using the Statistical Package for the Social Sciences (SPSS), version 22.
With the authorization from the Commission Nationale de l'Informatique et des Libertés (CNIL), data were anonymized prior to analyses. All volunteers provided informed consent for the use of all their recorded variables. Dental and periodontal examination. The participants received a full-mouth clinical examination from one of five trained dental examiners. A simplified plaque index based on that developed by Silness and Loe  21  was used and included the following ratings: low (plaque cannot be seen with the naked eye), moderate (limited quantity of plaque can be seen), and high amount (abundance of soft matter within tooth and/or gingival margin). Similarly, the calculus index was rated: low (supragingival calculus covering no more than one-third of the tooth surface), moderate (supragingival calculus covering more than one-third but not more than two-thirds of the tooth surface and/or the presence of individual flecks of subgingival calculus around the cervical portion of the tooth), and high amount (supragingival calculus covering more than two-thirds of the tooth surface).
Mortality ascertainment. For each screened subject, vital status was obtained from the "Institut National de Statistiques et d'Etudes Economiques" (INSEE, Paris, France). Causes of mortality, taken from death certificates, were provided by INSERM's Department of Mortality Studies ("Institut National de la Santé et de la Recherche Médicale", Unit SC8). Causes of death were codified according to the International Classification of Disease (8th revision until 1978 and 9th revision until 2000 and 10 thereafter). To validate this procedure, in 2012 we compared a random sample of 364 subjects considered as deceased from our database and compared the mortality data with those provided by city hall registries for every candidate. Discordance was found in only two cases (0. 55%). Furthermore, subjects with a personal medical history of cancer or cardiovascular disease and death by casualty were excluded from the analysis, representing 3079 subjects.
To generate propensity scores, multivariate logistic models were run in which each single oral health variable was the dependent variables (high dental plaque, high dental calculus, high gingival inflammation, number of teeth ≤ 10, number of functional occlusal units < 5) and all others confounders (age, gender, body mass index, current smokers, diabetes, hypertension, gamma-glutamyl transferase (gamma_GT), cholesterol, and education level) were the independent variables. Scores were then calculated for each oral variables for each participant. The C-statistics for the propensity models are reported in Supplemental Data Table A. For each model, the C-statistic p-values were higher than 0. 7 suggesting a high predictive value of the model. The second stage was to evaluate mortality risk using Cox regression model including the propensity score for each dental exposure.
The link between food choices and masticatory efficiency is well established  14. It has been shown that dietary fiber intake was lower among subjects with reduced masticatory function  23. Therefore, it could be that tooth loss impairs masticatory function and this leads to poor diet. On the other hand, it has been demonstrated that lifestyle habits in particular dietary are strongly related to lifetime mortality  24. This may explain the relationship between poor masticatory function and mortality. In the IPC cohort study 0. 5% of study members had dies (n = 370). This is in accordance with the most recent data on the premature causes of death in France. In addition, subjects included in the IPC cohort are volunteers, and have a healthcare insurance that cover free follow-up medical examination every 5 years.
Acknowledgements We thank the  Caisse Nationale d' Assurance Maladie des Travailleurs Salariés  ( CNAM-TS, France ) and the  Caisse Primaire d' Assurance Maladie de Paris (CPAM-P, France)  for their help in making this study possible. We also thank  Dr. Catherine FERRE  (coordinator),  Dr. François VIZLER ,  Dr. Marie-Hélène ROUAUD ,  Dr. Yves DAMOTTE ,  Dr. Anne-Marie BEAUCIRE ,  Dr Aleksandar DAKIC  for their contributions to this study.
ABSTRACT Maltose and maltodextrins are formed during the degradation of starch or glycogen. Maltodextrins are composed of a mixture of maltooligosaccharides formed by ␣-1,4but also some ␣-1,6-linked glucosyl residues. The ␣-1,6-linked glucosyl residues are derived from branching points in the polysaccharides. In Enterococcus faecalis, maltotriose is mainly transported and phosphorylated by a phosphoenolpyruvate:carbohydrate phosphotransferase system. The formed maltotriose-6Љ-phosphate is intracellularly dephosphorylated by a specific phosphatase, MapP. In contrast, maltotetraose and longer maltooligosaccharides up to maltoheptaose are taken up without phosphorylation via the ATP binding cassette transporter MdxEFG-MsmX. We show that the maltose-producing maltodextrin hydrolase MmdH (GenBank accession no.
EFT41964) in strain JH2-2 catalyzes the first catabolic step of ␣-1,4-linked maltooligosaccharides. The purified enzyme converts even-numbered ␣-1,4-linked maltooligosaccharides (maltotetraose, etc. ) into maltose and odd-numbered (maltotriose, etc. ) into maltose and glucose. Inactivation of mmdH therefore prevents the growth of E. faecalis on maltooligosaccharides ranging from maltotriose to maltoheptaose. Surprisingly, MmdH also functions as a maltogenic ␣-1,6-glucosidase, because it converts the maltotriose isomer isopanose into maltose and glucose. In addition, E. faecalis contains a glucose-producing ␣-1,6specific maltodextrin hydrolase (GenBank accession no. EFT41963, renamed GmdH). This enzyme converts panose, another maltotriose isomer, into glucose and maltose. A gmdH mutant had therefore lost the capacity to grow on panose.
The genes mmdH and gmdH are organized in an operon together with GenBank accession no. EFT41962 (renamed mmgT). Purified MmgT transfers glucosyl residues from one ␣-1,4-linked maltooligosaccharide molecule to another. For example, it catalyzes the disproportionation of maltotriose by transferring a glucosyl residue to another maltotriose molecule, thereby forming maltotetraose and maltose together with a small amount of maltopentaose. IMPORTANCE The utilization of maltodextrins by Enterococcus faecalis has been shown to increase the virulence of this nosocomial pathogen. However, little is known about how this organism catabolizes maltodextrins. We identified two enzymes involved in the metabolism of various ␣-1,4and ␣-1,6-linked maltooligosaccharides. We found that one of them functions as a maltose-producing ␣-glucosidase with relaxed linkage specificity (␣-1,4 and ␣-1,6) and exo-and endoglucosidase activities.