23,304 research outputs found

    Alternate title: Ja Da, Ja Da, Jing Jing Jing!

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    First Line: You've heard all about your raggy melodiesFirst Line of Chorus: Ja da, ja da, ja da, ja da, jing, jing, jingKey: F Majo

    Mo he mo ye jing 摩 訶 摩 耶 經[trad. de Tan jing 曇 景].

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    Mahāmāyā-sūtra, cf. Mo he mo ye jing.Mohe mo ye jing 摩 訶 摩 耶 經Mahāmāyā-sūtraNumérisation effectuée à partir d'un document original.J. shang, déb. manque.T . 383, vol. 12, pp. 1005 b5-1010 a. A gauche du titre final, colophon : « Copie duMo he mo ye jing en deux chapitres, due à Peng Puxin 彭 普 信, fidèle ayant reçu les défenses de bodhisattva, le 15e jour du 12emois de la 4e année zhi de des Chen (29 janvier587)... » Repr. partielle (7 dernières col. du texte et colophon) inTKRS , vol. 2, pl. 491-2. Écr. soignée, légèrement empâtée, certains traits descendants trèsaccentués. Encre foncée. 31 col. par f., 17 car. par col. Sur la f. 11, 10fan qie en petits car. sur col. dédoublées. Marges sup. 3,5 à 3,9 cm, inf. 3 à 3,8 cm. Réglure

    [Jin guang ming zui sheng wang jing 金 光 明 最 勝 王 經trad. de Yi jing.]

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    Jin guang ming zuisheng wang jing 金 光 明 最 勝 王 經, trad. Yi jingSuvarṇaprabhāsa-sūtra, trad. Tan wu chan, cf. Jin guang mingjing.Suvarṇaprabhāsottamarāja-sūtra, trad. Yi jing, cf. Jinguang ming zui sheng wang jing.Suvarṇaprabhāsottamarāja-sūtraNumérisation effectuée à partir d'un document original.[J. 6, pin 12,] premières col. etfin manquent. T . 665, vol. 16,pp. 427 b 13-428 a 22. Écr. ordinaire. 1 addition et 1 car. gratté etrécrit. 28 col. (f. 2), 16 à 18 car. par col. Marges sup. 2 à 3 cm, inf. 2,2 à3,1 cm. Réglure

    Jin guang ming zui sheng wang jing 金 光 明 最 勝 王 經[trad. de Yi jing 義 淨].

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    Jin guang mingzui sheng wang jing 金 光 明 最 勝 王 經, trad. Yi jingSuvarṇaprabhāsa-sūtra, trad. Tan wu chan, cf. Jin guang mingjing.Suvarṇaprabhāsottamarāja-sūtra, trad. Yi jing, cf. Jinguang ming zui sheng wang jing.Suvarṇaprabhāsottamarāja-sūtraNumérisation effectuée à partir d'un document original.[J. 7,] déb. manque, dernières col. du pin [14] et pin 15 [1repartie], manque la note finale. T . 665, vol. 16, pp. 434 a 26-437 c. Belle écr.,traits fins légèrement liés, pleins parfois très accentués. Rares additions. 27ou 28 col. par f., 15 à 18 car. par col. Notes et fanqie en petits car. sur col. simples ou dédoublées. Marges sup. 2,6 à 4 cm, inf. 2,8 à 4,1 cm

    Jin guang ming zui sheng wang [jing] 金 光 明 最 勝 王 [經] trad. de Yi jing 義 淨.

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    Jin guang ming zui sheng wang jing 金 光 明 最 勝 王 經Suvarṇa-prabhāsa-uttamarāja-sūtraContient : Acte de promotionNumérisation effectuée à partir d'un document original.[J. 2, pin] 5. Fin manque. T . 665, vol. 16, pp. 413 c 7. 1-414 b 12. 9. Écr. kai. Encre noire. 55 col., 27 et 28 col. par f., 17 car. par col. Marges tracées, sup. 2,7 cm, inf. 2,2 cm. Réglures

    Trachypeplus magnus Jing

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    Trachypeplus magnus Jing Trachypeplus magnus Jing 1981, p. 315 Material examined. 1 M, 1 F, 20 km S, Dalat, 1300 m, 12.IX. 1960, J.L. Gressitt coll. (BPBM). Distribution. This species was known only form China (Yunan) (Jing 1981)Published as part of Guilbert, Eric, 2015, New species and new records of Tingidae (Hemiptera: Heteroptera) from Vietnam, pp. 531-546 in Zootaxa 3956 (4) on page 540, DOI: 10.11646/zootaxa.3956.4.5, http://zenodo.org/record/23784

    Trachypeplus yunnanus Jing

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    Trachypeplus yunnanus Jing Trachypeplus yunnanus Jing 1980, p. 395 Material examined. 1 F, Cuo Phuong, prov. Ninh Binh, N°346. 12/V/ 1966, Leg. Topal, (HMNH). Distribution. This species previously was known from China (Yunan) (Jing 1980) and Laos (Guilbert 2007).Published as part of Guilbert, Eric, 2015, New species and new records of Tingidae (Hemiptera: Heteroptera) from Vietnam, pp. 531-546 in Zootaxa 3956 (4) on page 540, DOI: 10.11646/zootaxa.3956.4.5, http://zenodo.org/record/23784

    Expression and characterization of E-LecEGF for structural study and assay development

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    Human E-selectin (hE-selectin) is a cell adhesion molecule expressed on the membrane of endothelial cells. It is a C-type lectin whose key role is to mediate the initial rolling and adhering of leukocytes in the leukocyte recruitment in inflammation and metastasis of some cancer cells. It is fundamentally involved in many physiological and pathological processes, and hence is an attractive target for developing anti-inflammation drugs. The lectin and EGF domains of hE-selectin (hE-LecEGF) were identified as the minimum functional unit. Crystal structures of hE-LecEGF complexed with its natural ligand, tetrasaccharide sialyl Lewisx (sLex), as well as NMR studies of hE-selectin/IgG bound with this ligand, have been reported and utilized as the structural basis for the development of potent antagonists for hE-selectin. More potent antagonists with better binding affinity than sLex, such as CGP69669, were reported, but their binding modes in hE-LecEGF remain unknown. To obtain the improved structural information of hE-LecEGF complexed with an antagonist and develop more potent antagonists of hE-selectin are challenging tasks. To meet the demands of the protein for the structure determination and the binding assay, a sufficient amount of pure and active hE-LecEGF is needed. In this thesis, insect cell expression systems were initially used to produce the hE-LecEGF protein. hE-LecEGF was cloned, transiently expressed and characterized in Sf9 and High fiveTM cells. The expression plasmid pFastBacYJSE was constructed for expression of the hE-LecEGF protein fused with a N-terminal Flag tag. The recombinant baculovirus was generated and used in the expression of protein in the suspension culture. Pure hE-LecEGF was obtained by anti-Flag M2 affinity chromatography under the optimized condition. The purified protein was active and glycosylated, as identified by mAb 7A9 and glycan detection, respectively. Unfortunately, the homogeneous hE-LecEGF protein was not obtained after the deglycosylation with PNGase F and N-glycosidase A. hE-LecEGF was then cloned, stably expressed and characterized in CHO K1 cells. Stable subclones CHO-YJES and CHO-YJEGS expressing the hE-LecEGF protein with or without a human IgG1 tag were achieved. The CHO-YJES construct was used for production. The monoclonal anti-E-selectin functional blocking antibody 7A9 (mAb 7A9) was produced, purified and coupled to sepharose for functional purification of the hE-LecEGF protein. Highly pure hE-LecEGF protein was obtained in a one-step purification with an mAb 7A9 coupled column. Page, western-blotting, ELISA, MS and NMR were performed to characterize the hE-LecEGF protein. Pure, monomeric and active hE-LecEGF with the molecular weight of 20.444 kDa was obtained. In contrast to the insect cell expression system, pure, active and uniform deglycosylated hE-LecEGF protein was obtained after treatment with PNGase F and purification by a Sepharose Q matrix. A prescreening of the crystallization condition of hE-LecEGF was also performed using a sitting-drop method. Furthermore, a novel cell-free assay “capture-binding assay” was developed with the tag-free hE-LecEGF protein to evaluate the binding activity of the hE-LecEGF protein and the binding affinity of hE-selectin antagonists. The rIC50 of six hE-selectin antagonists was determined. The obtained results were in close agreement with the published results. Compared to the previously unstable polymer assay with hE-selectin/IgG, the capture-binding assay with hE-LecEGF is accurate, sensitive and reproducible. It can correctly evaluate the binding affinities of hE-selectin antagonists. In addition, the antibody BBA1 was used to solve the problem of immobilization of the hE-LecEGF protein on ELISA plates in the assay

    [Guan Mi luo pu sa shang sheng dou shuai tian jing 觀 彌 勒 菩 薩 上 生 兜 率 天 經 trad. de Ju qu Jing sheng 沮 渠 京 聲].

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    Guan Mi le pu sa shang sheng dou shuai tian jing 觀 彌 勒 菩 薩 上 生 兜 率 天 經. Ju Qu Jing sheng 沮 渠 京 聲Numérisation effectuée à partir d'un document original.Déb. et fin manquent. Quelques variantes par rapport à T . 452, vol. 14, pp. 418 b 26. 16-419 b 19. 1. Écr. kai call. Encre foncée. 71 col., 24 col. par f., 17 car. par col. Marges sup. et inf. 3,5 cm. Réglures finement tracées, 1,6 cm

    A Study of the Nian-fo-jing (Buddha-Recitation Mirror)

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    Written by late-Tang Pure Land monks in a question-and-answer format to propagate Pure Land Buddhism, Nian-fo-jing devotes itself to "resolving doubts and arousing faith" and addresses many questions regarding the Pure Land Doctrine, promoting Pure Land teachings and its exceptionality and superiority among other Buddhist practices. This five-chapter thesis focuses on various aspects of Nian-fo-jing, including its title, author, time period written, extant versions, structure, and inherent doctrine. Firstly, the "Introduction" outlines the research purposes and objectives, provides a literature survey, and explains the approach used and the overall structure of the thesis. In the second chapter, "Exploring the text of Nian-fo-jing," extant versions of Nian-fo-jing are juxtaposed for comparison, and the title of the scripture is examined. The identity of author of Nian-fo-jing and the time period in which the scripture was written were also clarified through investigating related studies of modern scholars. The third chapter, "The Structure and Content of Nian-fo-jing," points out the significance of the organization of chapters by employing the Buddhist approach of kepan, or structural analysis of the text, and demonstrating the "text structure of Nian-fo-jing " and the "comprehensive structure of content." The eleven divisions in the scripture are explored for comprehension and interpretation of the doctrine and issues. The fourth chapter, "'Gongde' and Nian-fo-jing," explores gongde, or "merit," in Nian-fo-jing mainly in terms of doctrine, elucidating what the concept of gongde is, how it is understood, and what its meaning is with regard to the Pure Land practice. The background of gongde culture of Nian-fo-jing is also explored to reveal possible reasons leading to the emphasis of gongde as means of propagation and its significance. The concluding chapter briefly summarizes significant findings in this thesis and identifies directions for future research
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