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Relevant bibliographies by topics / S244D

Academic literature on the topic 'S244D'

Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

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Journal articles on the topic "S244D"

1

Weng, Leiyun, Yuichi Hirata, Masaaki Arai, Michinori Kohara, Takaji Wakita, Koichi Watashi, Kunitada Shimotohno, Ying He, Jin Zhong, and Tetsuya Toyoda. "Sphingomyelin Activates Hepatitis C Virus RNA Polymerase in a Genotype-Specific Manner." Journal of Virology 84, no. 22 (September 15, 2010): 11761–70. http://dx.doi.org/10.1128/jvi.00638-10.

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ABSTRACT Hepatitis C virus (HCV) replication and infection depend on the lipid components of the cell, and replication is inhibited by inhibitors of sphingomyelin biosynthesis. We found that sphingomyelin bound to and activated genotype 1b RNA-dependent RNA polymerase (RdRp) by enhancing its template binding activity. Sphingomyelin also bound to 1a and JFH1 (genotype 2a) RdRps but did not activate them. Sphingomyelin did not bind to or activate J6CF (2a) RdRp. The sphingomyelin binding domain (SBD) of HCV RdRp was mapped to the helix-turn-helix structure (residues 231 to 260), which was essential for sphingomyelin binding and activation. Helix structures (residues 231 to 241 and 247 to 260) are important for RdRp activation, and 238S and 248E are important for maintaining the helix structures for template binding and RdRp activation by sphingomyelin. 241Q in helix 1 and the negatively charged 244D at the apex of the turn are important for sphingomyelin binding. Both amino acids are on the surface of the RdRp molecule. The polarity of the phosphocholine of sphingomyelin is important for HCV RdRp activation. However, phosphocholine did not activate RdRp. Twenty sphingomyelin molecules activated one RdRp molecule. The biochemical effect of sphingomyelin on HCV RdRp activity was virologically confirmed by the HCV replicon system. We also found that the SBD was the lipid raft membrane localization domain of HCV NS5B because JFH1 (2a) replicon cells harboring NS5B with the mutation A242C/S244D moved to the lipid raft while the wild type did not localize there. This agreed with the myriocin sensitivity of the mutant replicon. This sphingomyelin interaction is a target for HCV infection because most HCV RdRps have 241Q.

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2

Nadeem, Danial, Tenzin Choden, Yiannis Dimopoulos, and Mark C. Mattar. "S2443 Histology Exposes Hidden Histoplasmosis." American Journal of Gastroenterology 116, no. 1 (October 2021): S1033—S1034. http://dx.doi.org/10.14309/01.ajg.0000783304.77699.ee.

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3

Hage, Naim, Tina Howard, Chris Phillips, Claire Brassington, Ross Overman, Judit Debreczeni, Paul Gellert, Snow Stolnik, G. Sebastiaan Winkler, and Franco H. Falcone. "Structural basis of Lewisb antigen binding by the Helicobacter pylori adhesin BabA." Science Advances 1, no. 7 (August 2015): e1500315. http://dx.doi.org/10.1126/sciadv.1500315.

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Helicobacter pylori is a leading cause of peptic ulceration and gastric cancer worldwide. To achieve colonization of the stomach, this Gram-negative bacterium adheres to Lewisb (Leb) antigens in the gastric mucosa using its outer membrane protein BabA. Structural information for BabA has been elusive, and thus, its molecular mechanism for recognizing Leb antigens remains unknown. We present the crystal structure of the extracellular domain of BabA, from H. pylori strain J99, in the absence and presence of Leb at 2.0- and 2.1-Å resolutions, respectively. BabA is a predominantly α-helical molecule with a markedly kinked tertiary structure containing a single, shallow Leb binding site at its tip within a β-strand motif. No conformational change occurs in BabA upon binding of Leb, which is characterized by low affinity under acidic [KD (dissociation constant) of ~227 μM] and neutral (KD of ~252 μM) conditions. Binding is mediated by a network of hydrogen bonds between Leb Fuc1, GlcNAc3, Fuc4, and Gal5 residues and a total of eight BabA amino acids (C189, G191, N194, N206, D233, S234, S244, and T246) through both carbonyl backbone and side-chain interactions. The structural model was validated through the generation of two BabA variants containing N206A and combined D233A/S244A substitutions, which result in a reduction and complete loss of binding affinity to Leb, respectively. Knowledge of the molecular basis of Leb recognition by BabA provides a platform for the development of therapeutics targeted at inhibiting H. pylori adherence to the gastric mucosa.

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4

ANHALT, G. "S244 Autoantigens of oral epithelium." Journal of the European Academy of Dermatology and Venereology 9 (September 1997): S55. http://dx.doi.org/10.1016/s0926-9959(97)89065-4.

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5

Powell, Charleston, Emily Wichersham, and Phillip Lindholm. "S2440 Hemochromatosis Secondary to Acute, Severe Parvovirus Infection." American Journal of Gastroenterology 115, no. 1 (October 2020): S1292—S1293. http://dx.doi.org/10.14309/01.ajg.0000711808.10950.62.

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6

Samuel, Shirly, Arvin J. Mallari, and Nicole Gentile. "S2448 Acute Esophageal Necrosis From Trimethoprim-Sulfamethoxazole Use." American Journal of Gastroenterology 117, no. 10S (October 2022): e1634-e1635. http://dx.doi.org/10.14309/01.ajg.0000866432.58109.bd.

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7

Naffouj, Sandra, Elie Ghoulam, Meredith Yellen, and Robert E. Carroll. "S2442 A Rare Finding of a Common Disorder." American Journal of Gastroenterology 117, no. 10S (October 2022): e1630-e1631. http://dx.doi.org/10.14309/01.ajg.0000866408.29285.d6.

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8

Rosner, M., N. Siegel, A. Valli, C. Fuchs, and M. Hengstschläger. "mTOR phosphorylated at S2448 binds to raptor and rictor." Amino Acids 38, no. 1 (January 15, 2009): 223–28. http://dx.doi.org/10.1007/s00726-008-0230-7.

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9

Raza, Syed Musa, Daniyal Raza, Nazar Hafiz, Maryam Mubashir, Shazia Rashid, Anush Vasikaran, and Sudha Pandit. "S2443 Achalasia in a 16-Year-Old: Diagnostic Dilemma." American Journal of Gastroenterology 117, no. 10S (October 2022): e1631-e1631. http://dx.doi.org/10.14309/01.ajg.0000866412.29351.fe.

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10

Che Omar, Siti Nurhadis, Janna Ong Abdullah, Khairul Anuar Khairoji, Sieo Chin Chin, and Muhajir Hamid. "Effects of Flower and Fruit Extracts ofMelastoma malabathricumLinn. on Growth of Pathogenic Bacteria:Listeria monocytogenes, Staphylococcus aureus, Escherichia coli,andSalmonella typhimurium." Evidence-Based Complementary and Alternative Medicine 2013 (2013): 1–11. http://dx.doi.org/10.1155/2013/459089.

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Melastoma malabathricumLinn. is a shrub that comes with beautiful pink or purple flowers and has berries-like fruits rich in anthocyanins. This study was carried out with the aim to evaluate the inhibitory activities of different concentrations of theM. malabathricumLinn. flower and fruit crude extracts againstListeria monocytogenesIMR L55,Staphylococcus aureusIMR S244,Escherichia coliIMR E30, andSalmonella typhimuriumIMR S100 using the disc diffusion method. The lowest concentrations of the extracts producing inhibition zones against the test microorganisms were used to determine their minimum inhibitory concentrations (MICs) and minimum bactericidal concentrations (MBCs). In addition, the growth ofListeria monocytogenesIMR L55 andStaphylococcus aureusIMR S244 grown in medium supplemented with the respective extracts at different temperatures (4°C, 25°C, and 37°C) and pHs (4, 6, 7, and 8) was determined.

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Dissertations / Theses on the topic "S244D"

1

L'Homme, Denis. "La fonction de luminosité et la fonction de masse initiale de l'amas d'étoiles S247D." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/MQ56755.pdf.

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2

Sallah, Tijan M. "Agricultural tenancy and contracts: an economic analysis of the strange farmer system in the Gambia." Diss., Virginia Polytechnic Institute and State University, 1987. http://hdl.handle.net/10919/49884.

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This dissertation explores, both theoretically and empirically, the role of strange farmers in the Gambia's mono-cash crop economy and analyzes the structure of strange farmer contracts within the context of rural production relations; ie. the relations of economic agents to resources of production in terms of their use and ownership rights and the relations between economic agents as principals (ie. landlords) and agents (ie. workers; strange farmers). Strange farmers, the migrant laborers who come from the West African hinterland to farm in the coastal areas of the Senegambia region due to certain transaction cost advantages, constitute a dynamic population adjustment to West Africa's spatial, unequal spread of resources. It is argued in this study that the reason "strange farming" has continued to persist is because it is flexible and adaptable to the prevailing agroclimatic conditions and endowments of the West Africa region, and to the economic changes induced by the interplay of internal (the government; technology) and external (e.g., world primary commodity markets) institutional and market forces. Detailed analysis of the strange farmer contract (a contract of "input sharing"), as contrasted with wage, fixed-rent, and sharecropping, is presented; and emphasis is placed on the "strangeness" of the strange farmers (the fact that they are non-residents of their farming areas) as the distinguishing feature of the contract. Our analysis considers how environmental and idiosyncratic factors such as information, risk, and incentive constraints impinge on agents in this environment and how alternative models of the strange farmer system explain how such problems are circumvented. The study concludes by examining the efficiency and (briefly) the equity implications of strange farming, and argues that strange farming performs the vital economic role of providing otherwise labor deficient landlords with a steady and timely supply of labor throughout the farming season and indeed circumvents the contract enforcement and shirking problems posed by a second-best environment.
Ph. D.
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3

Bejaoui, Noureddine. "Structure primaire de la ß-lactamase CARB-4 et génétique atomique des acides aminés R234 à S244 dans l'hydrolyse des antibiotiques." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1996. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq25381.pdf.

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4

Salles, Paulo Afonso de Almeida. "Hydrodynamic controls on multiple tidal inlet persistence." Thesis, Massachusetts Institute of Technology, 2001. http://hdl.handle.net/1721.1/84213.

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Thesis (Ph.D.)--Joint Program in Oceanography (Massachusetts Institute of Technology, Dept. of Civil and Environmental Engineering, and the Woods Hole Oceanographic Institution), 2001.
Includes bibliographical references.
by Paulo Salles.
Ph.D.

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5

Safewright, Marcia Porter. "Dimensions of the interorganizational relationship between Area Agencies on Aging and Social Services Block Grant Agencies." Diss., This resource online, 1990. http://scholar.lib.vt.edu/theses/available/etd-08232007-112149/.

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6

Chao, Rebecca. "Utilising CYP199A4 from Rhodopseudomonas palustris HaA2 for biocatalysis and mechanistic studies." Thesis, 2016. http://hdl.handle.net/2440/102745.

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The cytochrome P450 enzyme CYP199A4 from Rhodopseudomonas palustris strain HaA2 is highly specific for the regioselective oxidation of para-substituted benzoic acids. A selection of these compounds was tested with the enzyme with the aim of investigating the mechanism of different P450-catalysed reactions. These studies revealed that the binding affinity and oxidative activity of CYP199A4 is influenced by the substituent at the para-position, and that to the enzyme’s known oxidative activities (demethylation, hydroxylation, heteroatom oxidation and desaturation) can be added alkene epoxidation, alkyne oxidation and aldehyde oxidation. The active oxidants involved in these CYP199A4-catalysed oxidations were investigated using two active site mutants at the conserved acid-alcohol pair, T252A CYP199A4 [CYP199A4 subscript] and D251N CYP199A4 [CYP199A4 subscript], which should disrupt different steps of the catalytic cycle. There was a general increase in hydrogen peroxide uncoupling in the T252A CYP199A4 [CYP199A4 subscript] mutant but significant levels of product formation were observed with each substrate. The D251N mutation reduced the activity of the enzyme dramatically in all but one case, suggesting that this mutation interferes with proton delivery as expected. The elevated rate of 4-ethynylbenzoic acid oxidation by T252A CYP199A4 [CYP199A4 subscript] when compared to the wild-type enzyme suggested the involvement of Cpd 0 in alkyne oxidation, while a reduction in activity with 4-methoxybenzoic acid implicated Cpd I in demethylation. Additionally, the notable increase in product formation and coupling efficiency of D251N CYP199A4 [CYP199A4 subscript] with 4-formylbenzoic acid suggested the involvement of the peroxo-anion in aldehyde oxidation. Larger cinnamic acids and closely related substrates were also investigated with CYP199A4. The binding affinity and oxidative activity of the enzyme decreased in the order 4-methoxybenzoic acid > 4-methoxycinnamic acid > 3-(4- methoxyphenyl)propionic acid > 4-methoxyphenylacetic acid, highlighting its selectivity for a planar, benzoic acid- or cinnamic acid-like framework. The exclusive oxidation of cinnamic acids and related derivatives at the para-position further demonstrated the high regioselectivity of CYP199A4. While CYP199A4 exhibited low oxidation activity towards para-methoxy substituted benzene derivatives, considerably higher levels of activity reminiscent of the demethylation of 4-methoxybenzoic acid were observed for the Ser244 → Asp244 (S244D) mutant of CYP199A4. The exclusive demethylation of the para-methoxy substituted benzenes by S244D revealed that the regioselectivity of CYP199A4 oxidation is maintained in this mutant. The regioselectivity of the S244D mutant was further investigated using a selection of methyl- and ethyl-substituted derivatives. The methyl analogues were exclusively oxidised at the para-position to a single α-hydroxylation product. α-Hydroxylation and Cα [α subscript] -Cᵦ desaturation products were generated in the turnovers of the ethyl derivatives. The alcohol was formed with high stereoselectivity. The electronic properties of the ethyl substrates were found to influence the ratio of hydroxylation/desaturation product, with the more electron donating substrates giving rise to a greater proportion of the latter. This suggested the involvement of a cationic intermediate in CYP199A4- catalysed desaturation.
Thesis (M.Phil.) -- University of Adelaide, School of Physical Sciences, 2016.

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Books on the topic "S244D"

1

Dark Galaxies and Lost Baryons (IAU S244) (Proceedings of the International Astronomical Union Symposia and Colloquia). Cambridge University Press, 2008.

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Conference papers on the topic "S244D"

1

Skriver, L., L. C. Petersen, L. R. Lund, L. S. Nielsen, and K. Danø. "SINGLE-CHAIN UROKINASE TYPE PLASMINOGEN ACTIVATOR (SCU-PA) FROM HT-1080 HUMAN FIBROSARCOMA CELLS IS A GENUINE PROENZYME." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644394.

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U-PA is released from many cells as a single polypeptide chain (scu-PA) that is converted into its active two-chain form (tcu-PA) by limited proteolysis with plasmin. There is general agreement that scu-PA has an extremely low amidolytic activity, but different oppinions exist, as to whether scu-PA itself can activate plasminogen. We have reinvestigated the plasminogen activating activity of our scu-PA preparations by means of a direct [125]I-plasminogen conversion assay and two amidolytic assays for plasmin and u-PA activity. In the [125]I-plasminogen conversion assay in the presence of bovine pancreatic trypsin inhibitor (BPTI) the subsequent plasmin catalyzed conversion of scu-PA is blocked while the plasminogen activation is unaffected. In this assay with 3oo nM Glu-plasminogen and 15 pM BPTI, 4o nM scu-PA caused a low but significant plasminogen conversion, which could be fully inhibited by pretreatment of scu-PA with diisopropylfluorophos-phate (DFP). DFP-treated scu-PA was convertible to fully active tcu-PA. Rates of plasminogen activation in this type of assay for scu-PA activity was at least 4oo fold slower than that measured for tcu-PA. A coupled amidolytic assay with Lys-plasminogen, scuPA or tcu-PA, BPTI, and the high affinity plasmin substrate H-D-Val-Phe-LyspNA (S2390) was performed under conditions that ensures a low steady state concentration of free plasmin. In this assay the initial rate of Lys-plasminogen activation by DFP-treated scu-PA was at least 25o fold slower than that measured for tcu-PA. Finally, u-PA activity was measured in an assay with the chromogenic substrate <Glu-Gly-ArgpNA (S2444) (o.8mM) in the presence of highly purified Glu-plasminogen (3oonM) and DFP-treated scu-PA (2nM) in the absence of BPTI. Within the initial 15 min of incubation no detectable hydrolysis of S2444 occurred. Addition of tcu-PA (2pM) or plasmin (o.lnM) to the scu-PA/Glu-plasminogen mixture caused a significant reduction of the lag period before onset of the cascade reaction leading to scu-PA conversion and subsequent hydrolysis of S2444. We conclude that the low rates of plasminogen activation measured in these assays by scu-PA might be accounted for by the presence of trace amounts of tcu-PA in the scu-PA preparations, and that scu-PA meets the requirements for a genuine proenzyme

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2

VOVIS, G. F., J. MAO, R. BROEZE, D. ABERCROMBIE, P. PUMA, K. HSAIO, and S. ALMEDA. "AMINO ACID CHANGES AT LYS-158 THAT ALTER THE SENSITIVITY OF SCUPA TO CLEAVAGE BY PLASMIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644417.

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Plasmin converts Scu-PA to two-chain urokinase by hydrolyzing the lys-158/ile-159 peptide bond. Using site directed mutagenesis, the codon at amino acid position 158 was changed from one that codes for lysine to one that codes for either alanine, glutamic acid, or methionine. These DNA constructions were expressed and amplified in Chinese hamster ovary cells. The resulting protein products were isolated and characterized ip vitro. Under conditions where Scu-PA is completely converted by plasmin to two chain urokinase, none of these derivatives were cleaved by plasmin. However, all of these molecules, including Scu-PA, were cleaved by thrombin. These derivatives exhibited low amidolytic activity as determined by using the chromogenic substrate S2444 and low fibrinolytic activity as determined by using fibrin plates. All three derivatives activated either glu-plasminogen or lys-plasminogen to plasmin ip vitro but at rates significantly slower than that seen with Scu-PA.

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