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1,272 results on '"London, N"'

3. Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases

Author

Shoichet, Brian, Babbitt, Patricia, London, N, Farelli, JD, Brown, SD, Liu, C, Huang, H, Korczynska, M, Al-Obaidi, NF, Babbitt, PC, Almo, SC, and Allen, KN

Abstract

© 2014 American Chemical Society.Enzyme function prediction remains an important open problem. Though structure-based modeling, such as metabolite docking, can identify substrates of some enzymes, it is ill-suited to reactions that progress through a coval

Published
2015

4. Covalent docking of large libraries for the discovery of chemical probes

Author

Shoichet, Brian, Taunton, Jack, London, N, Miller, RM, Krishnan, S, Uchida, K, Irwin, JJ, Eidam, O, Gibold, L, Cimermančič, P, Bonnet, R, and Shoichet, BK

Abstract

Chemical probes that form a covalent bond with a protein target often show enhanced selectivity, potency and utility for biological studies. Despite these advantages, protein-reactive compounds are usually avoided in high-throughput screening campaigns. He

Published
2014

5. Prediction of substrates for glutathione transferases by covalent docking

Author

Babbitt, Patricia, Sali, Andrej, Jacobson, Matthew, Shoichet, Brian, Dong, GQ, Calhoun, S, Fan, H, Kalyanaraman, C, Branch, MC, Mashiyama, ST, London, N, Jacobson, MP, Babbitt, PC, and Shoichet, BK

Abstract

Enzymes in the glutathione transferase (GST) superfamily catalyze the conjugation of glutathione (GSH) to electrophilic substrates. As a consequence they are involved in a number of key biological processes, including protection of cells against chemical d

Published
2014

7. Letter to the Editor Concerning “Common Ophthalmic Preservatives in Soft Contact Lens Care Products: Benefits, Complications, and a Comparison to Non-Preserved Solutions” [Letter]

Author

Erdinest N, London N, and Levinger N

Subjects
mps solutions, preservatives, soft contact lenses, scleral lenses, Ophthalmology, RE1-994
Abstract

Nir Erdinest,1 Naomi London,2 Nadav Levinger1,3 1Department of Ophthalmology, Hadassah-Hebrew University Medical Center, Jerusalem, Israel; 2Private Practice, Jerusalem, Israel; 3Department of Ophthalmology, Enaim Refractive Surgery Center, Jerusalem, IsraelCorrespondence: Naomi LondonNaomi Vision Boutique, 5 Even Israel, Jerusalem, IsraelTel +972 545406646Fax +972 25004333Email imnl4u@gmail.com View the original paper by Dr Bradley and colleagues

Published
2021

8. Letter to the Editor Concerning “Historical Development, Applications and Advances in Materials Used in Spectacle Lenses and Contact Lenses” [Letter]

Author

Erdinest N and London N

Subjects
contact lens materials, advances in lens materials, Ophthalmology, RE1-994
Abstract

Nir Erdinest, 1 Naomi London 2 1Department of Ophthalmology, Hadassah-Hebrew University Medical Center, Jerusalem, Israel; 2Private Practice, Jerusalem, IsraelCorrespondence: Naomi London 5 Even Israel, Jerusalem, IsraelTel +972 545406646Fax +972 25004333Email imnl4u@gmail.com This review on historical developments and advances in spectacle lens and contact lens materials was read with great interest and the authors are to be thanked for encompassing the past, present and possible future materials and their unique coatings.1 In the interest of thoroughness, we would like to add a few fascinating developing materials and coatings for contact lenses in research that were not mentioned. View the original paper by Pillay and colleagues

Published
2020

10. Evaluating the impact of injury prevention interventions in child and adolescent sports using the RE-AIM framework and CERT: A systematic review

Author

Hughes, T, O'Hara, J, Burton, A, London, N, Emmonds, S, Hughes, T, O'Hara, J, Burton, A, London, N, and Emmonds, S

Abstract

Background Participation in sport is a popular pastime for children and adolescents that improves their physical health, mental health and motor skills. Musculoskeletal injuries are a relatively common downside of sports participation and can have negative long-term consequences. Injury prevention programmes have demonstrated effectiveness in child and adolescent sports, provided compliance is adequate. However, little is known about the factors which relate to their impact on the wider community and whether the prevention programmes have been adopted and maintained in the long-term. The objective of this review was to assess the current literature on exercise-based injury prevention interventions in child and adolescent sports (aged under 19 years) against the ‘Reach’, ‘Effectiveness’, ‘Adoption’, ‘Implementation’, ‘Maintenance’ (RE-AIM) framework and Consensus of Exercise Reporting Template (CERT), to ascertain level of reporting for the components which relate to external validity. Methods Seven electronic databases; PubMed, Medline, SPORTDiscus, PsycINFO, CINAHL, Scopus and The Cochrane Library, were searched from date of inception to July 2022 using the themes of: ‘Child and Adolescent’, ‘Sport’, ‘Injury’ and ‘Prevention’. Eligibility criteria included: Experimental trial design, exercise-based intervention programmes, primary outcome of injury incidence and participants aged under 19 years. Two reviewers assessed each trial independently against the RE-AIM model dimension items checklist (RE-AIM MDIC) and Consensus on Exercise Reporting Template (CERT) before reaching a consensus on reporting. Results Forty-five unique trials met the eligibility criteria. Mean reporting level for all studies across the whole RE-AIM MDIC was 31% (SD ± 16.2%, Range 7–77%). The domain of ‘effectiveness’ was the most comprehensively reported (60%), followed by ‘implementation’ (48%), ‘reach’ (38%), ‘adoption’ (26%) and ‘maintenance’ (7%). The mean reporting score for the CERT was

Published
2023

11. Open science discovery of potent noncovalent SARS-CoV-2 main protease inhibitors.

Author

Boby, M.L., Fearon, D., Ferla, M., Filep, M., Koekemoer, L., Robinson, M.C., Chodera, J.D., Lee, A.A., London, N., Delft, A. von, Delft, F. von, Achdout, H., Aimon, A., Alonzi, D.S., Arbon, R., Aschenbrenner, J.C., Balcomb, B.H., Bar-David, E., Barr, H., Ben-Shmuel, A., Bennett, J., Bilenko, V.A., Borden, B., Boulet, P., Bowman, G.R., Brewitz, L., Brun, J., Bvnbs, S., Calmiano, M., Carbery, A., Carney, D.W., Cattermole, E., Chang, E., Chernyshenko, E., Clyde, A., Coffland, J.E., Cohen, G., Cole, J.C., Contini, A., Cox, L., Croll, T.I., Cvitkovic, M., Jonghe, S. De, Dias, A., Donckers, K., Dotson, D.L., Douangamath, A., Duberstein, S., Dudgeon, T., Dunnett, L.E., Eastman, P., Erez, N., Eyermann, C.J., Fairhead, M., Fate, G., Fedorov, O., Fernandes, R.S., Ferrins, L., Foster, R., Foster, H., Fraisse, L., Gabizon, R., García-Sastre, A., Gawriljuk, V.O., Gehrtz, P., Gileadi, C., Giroud, C., Glass, W.G., Glen, R.C., Glinert, I., Godoy, A.S., Gorichko, M., Gorrie-Stone, T., Griffen, E.J., Haneef, A., Hassell Hart, S, Heer, J., Henry, M., Hill, M., Horrell, S., Huang, Q.Y.J., Huliak, V.D., Hurley, M.F.D., Israely, T., Jajack, A., Jansen, J, Jnoff, E., Jochmans, D., John, T., Kaminow, B., Kang, L., Kantsadi, A.L., Kenny, P.W., Kiappes, J.L., Kinakh, S.O., Kovar, B., Krojer, T., La, V.N.T., Laghnimi-Hahn, S., Lefker, B.A., Levy, H., Lithgo, R.M., Logvinenko, I.G., Lukacik, P., Macdonald, H.B., MacLean, E.M., Makower, L.L., Malla, T.R., Marples, P.G., Matviiuk, T., McCorkindale, W., McGovern, B.L., Melamed, S., Melnykov, K.P., Michurin, O., Miesen, P., Mikolajek, H., Milne, B.F., Minh, D., Morris, A., Morris, G.M., Morwitzer, M.J., Moustakas, D., Mowbray, C.E., Nakamura, A.M., Neto, J.B., Neyts, J., Nguyen, L, Noske, G.D., Oleinikovas, V., Oliva, G., Overheul, G.J., Owen, C.D., Pai, R., Pan, J., Paran, N., Payne, A.M., Perry, B., Pingle, M., Pinjari, J., Politi, B., Powell, A., Pšenák, V., Pulido, I., Puni, R., Rangel, V.L., Reddi, R.N., Rees, P., Reid, S.P., Reid, L., Resnick, E., Ripka, E.G., Robinson, R.P., Rodriguez-Guerra, J., Rosales, R., Rufa, D.A., Saar, K., Saikatendu, K.S., Salah, E., Schaller, D., Scheen, J., Schiffer, C.A., Schofield, C.J., Shafeev, M., Shaikh, A., Shaqra, A.M., Shi, J., Shurrush, K., Singh, S., Sittner, A., Sjö, P., Skyner, R., Smalley, A., Smeets, B., Smilova, M.D., Solmesky, L.J., Spencer, J., Strain-Damerell, C., Swamy, V., Tamir, H., Taylor, J.C., Tennant, R.E., Thompson, W., Thompson, A., Tomásio, S., Tomlinson, C.W.E., Tsurupa, I.S., Tumber, A., Vakonakis, I., Rij, R.P. van, Vangeel, L., Varghese, F.S., Vaschetto, M., Vitner, E.B., Voelz, V., Volkamer, A., Walsh, M.A., Ward, W., Weatherall, C., Weiss, S., White, K.M., Wild, C.F., Witt, K.D., Wittmann, M., Wright, N., Yahalom-Ronen, Y., Yilmaz, N.K., Zaidmann, D., Zhang, I., Zidane, H., Zitzmann, N., Zvornicanin, S.N., Boby, M.L., Fearon, D., Ferla, M., Filep, M., Koekemoer, L., Robinson, M.C., Chodera, J.D., Lee, A.A., London, N., Delft, A. von, Delft, F. von, Achdout, H., Aimon, A., Alonzi, D.S., Arbon, R., Aschenbrenner, J.C., Balcomb, B.H., Bar-David, E., Barr, H., Ben-Shmuel, A., Bennett, J., Bilenko, V.A., Borden, B., Boulet, P., Bowman, G.R., Brewitz, L., Brun, J., Bvnbs, S., Calmiano, M., Carbery, A., Carney, D.W., Cattermole, E., Chang, E., Chernyshenko, E., Clyde, A., Coffland, J.E., Cohen, G., Cole, J.C., Contini, A., Cox, L., Croll, T.I., Cvitkovic, M., Jonghe, S. De, Dias, A., Donckers, K., Dotson, D.L., Douangamath, A., Duberstein, S., Dudgeon, T., Dunnett, L.E., Eastman, P., Erez, N., Eyermann, C.J., Fairhead, M., Fate, G., Fedorov, O., Fernandes, R.S., Ferrins, L., Foster, R., Foster, H., Fraisse, L., Gabizon, R., García-Sastre, A., Gawriljuk, V.O., Gehrtz, P., Gileadi, C., Giroud, C., Glass, W.G., Glen, R.C., Glinert, I., Godoy, A.S., Gorichko, M., Gorrie-Stone, T., Griffen, E.J., Haneef, A., Hassell Hart, S, Heer, J., Henry, M., Hill, M., Horrell, S., Huang, Q.Y.J., Huliak, V.D., Hurley, M.F.D., Israely, T., Jajack, A., Jansen, J, Jnoff, E., Jochmans, D., John, T., Kaminow, B., Kang, L., Kantsadi, A.L., Kenny, P.W., Kiappes, J.L., Kinakh, S.O., Kovar, B., Krojer, T., La, V.N.T., Laghnimi-Hahn, S., Lefker, B.A., Levy, H., Lithgo, R.M., Logvinenko, I.G., Lukacik, P., Macdonald, H.B., MacLean, E.M., Makower, L.L., Malla, T.R., Marples, P.G., Matviiuk, T., McCorkindale, W., McGovern, B.L., Melamed, S., Melnykov, K.P., Michurin, O., Miesen, P., Mikolajek, H., Milne, B.F., Minh, D., Morris, A., Morris, G.M., Morwitzer, M.J., Moustakas, D., Mowbray, C.E., Nakamura, A.M., Neto, J.B., Neyts, J., Nguyen, L, Noske, G.D., Oleinikovas, V., Oliva, G., Overheul, G.J., Owen, C.D., Pai, R., Pan, J., Paran, N., Payne, A.M., Perry, B., Pingle, M., Pinjari, J., Politi, B., Powell, A., Pšenák, V., Pulido, I., Puni, R., Rangel, V.L., Reddi, R.N., Rees, P., Reid, S.P., Reid, L., Resnick, E., Ripka, E.G., Robinson, R.P., Rodriguez-Guerra, J., Rosales, R., Rufa, D.A., Saar, K., Saikatendu, K.S., Salah, E., Schaller, D., Scheen, J., Schiffer, C.A., Schofield, C.J., Shafeev, M., Shaikh, A., Shaqra, A.M., Shi, J., Shurrush, K., Singh, S., Sittner, A., Sjö, P., Skyner, R., Smalley, A., Smeets, B., Smilova, M.D., Solmesky, L.J., Spencer, J., Strain-Damerell, C., Swamy, V., Tamir, H., Taylor, J.C., Tennant, R.E., Thompson, W., Thompson, A., Tomásio, S., Tomlinson, C.W.E., Tsurupa, I.S., Tumber, A., Vakonakis, I., Rij, R.P. van, Vangeel, L., Varghese, F.S., Vaschetto, M., Vitner, E.B., Voelz, V., Volkamer, A., Walsh, M.A., Ward, W., Weatherall, C., Weiss, S., White, K.M., Wild, C.F., Witt, K.D., Wittmann, M., Wright, N., Yahalom-Ronen, Y., Yilmaz, N.K., Zaidmann, D., Zhang, I., Zidane, H., Zitzmann, N., and Zvornicanin, S.N.

Abstract

Item does not contain fulltext, We report the results of the COVID Moonshot, a fully open-science, crowdsourced, and structure-enabled drug discovery campaign targeting the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease. We discovered a noncovalent, nonpeptidic inhibitor scaffold with lead-like properties that is differentiated from current main protease inhibitors. Our approach leveraged crowdsourcing, machine learning, exascale molecular simulations, and high-throughput structural biology and chemistry. We generated a detailed map of the structural plasticity of the SARS-CoV-2 main protease, extensive structure-activity relationships for multiple chemotypes, and a wealth of biochemical activity data. All compound designs (>18,000 designs), crystallographic data (>490 ligand-bound x-ray structures), assay data (>10,000 measurements), and synthesized molecules (>2400 compounds) for this campaign were shared rapidly and openly, creating a rich, open, and intellectual property-free knowledge base for future anticoronavirus drug discovery.

Published
2023

21. Crystal Structure of SARS-CoV-2 main protease in complex with LON-WEI-adc59df6-47

Author

Fearon, D., primary, Douangamath, A., additional, Aimon, A., additional, Brandao-Neto, J., additional, Dias, A., additional, Dunnett, L., additional, Gehrtz, P., additional, Gorrie-Stone, T.J., additional, Lukacik, P., additional, Powell, A.J., additional, Skyner, R., additional, Strain-Damerell, C.M., additional, Zaidman, D., additional, London, N., additional, Walsh, M.A., additional, von Delft, F., additional, and Covid Moonshot Consortium, ., additional

Published
2021
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23. Linkage analysis using direct and indirect counting and relative efficiencies for codominant and dominant loci

Author

Da, Y., Garbe, J., London, N., and Xu, J.

Subjects
Animal breeding, Genetic engineering, Zoology and wildlife conservation
Abstract

A method based on direct and indirect counting is developed for rapid and accurate linkage analysis for codominant and dominant loci. Methods for estimating gender-specific recombination frequencies are available for cases where at least one of the two loci is multiallelic and for biallelic loci with mixed parental linkage phases where at least one locus is codominant. Most of the estimates of gender-average and gender-specific recombination frequencies required iterative solutions. The new method makes use of the full data set, yields exact estimates of the recombination frequencies when the observed and expected genotypic frequencies are equal, and are computationally efficient. Relative efficiency of various data types is affected by the inheritance mode and by parental linkage phases of biallelic loci, but unaffected by the locus polymorphism when using the full data set for linkage analysis. The ability to determine parental linkage phases is affected by the locus polymorphism as well as inheritance mode. Intercross (or F-2 design) is more efficient for mapping codominant loci, whereas backcross is more efficient if dominance is involved. Mixed parental linkage phases of biallelic loci are less efficient than coupling or repulsion linkage phases. Ignoring noninformative offspring results in biased estimates of recombination frequency for biallelic loci only and reduced LOD scores for all cases. Key Words: Codominance, Dominance, Linkage Analysis, Loci

Published
2002

28. PanDDA analysis group deposition of computational designs of SARS-CoV-2 main protease covalent inhibitors -- Crystal Structure of SARS-CoV-2 main protease in complex with LON-WEI-adc59df6-27 (Mpro-x3113)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Zaidman, D., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Gorie-Stone, T.J., additional, Skyner, R., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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29. PanDDA analysis group deposition of computational designs of SARS-CoV-2 main protease covalent inhibitors -- Crystal Structure of SARS-CoV-2 main protease in complex with LON-WEI-adc59df6-30 (Mpro-x3359)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Zaidman, D., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Gorie-Stone, T.J., additional, Skyner, R., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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30. DnaJB1 JD-GF

Author

Avraham-Abayev, M., primary, London, N., additional, and Rosenzweig, R., additional

Published
2020
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31. PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with Cov_HetLib030 (Mpro-x2097)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, Keeley, A., additional, Keseru, G.M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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32. PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with PG-COV-42 (Mpro-x2052)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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33. PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with SF013 (Mpro-x2193)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, Keeley, A., additional, Keseru, G.M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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34. PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with PG-COV-34 (Mpro-x2754)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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35. PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2010253653 (Mpro-x2643)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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36. PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102628 (Mpro-x0771)

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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37. PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with NCL-00025412

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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38. PanDDA analysis group deposition of ground-state model of SARS-CoV-2 main protease screened against DSI poised (Enamine), Fraglites and Peplites (Newcastle university), Mini Frags (Astex), York 3D (York university), electrophile cysteine covalent (Weizman institute) fragment libraries

Author

Fearon, D., primary, Owen, C.D., additional, Douangamath, A., additional, Lukacik, P., additional, Powell, A.J., additional, Strain-Damerell, C.M., additional, Resnick, E., additional, Krojer, T., additional, Gehrtz, P., additional, Wild, C., additional, Aimon, A., additional, Brandao-Neto, J., additional, Carbery, A., additional, Dunnett, L., additional, Skyner, R., additional, Snee, M., additional, London, N., additional, Walsh, M.A., additional, and von Delft, F., additional

Published
2020
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