Výsledky vyhledávání - "R C, Stevens"

Predicting the emergence of antibiotic resistance by directed evolution and structural analysis

Autor: M C, Orencia, J S, Yoon, J E, Ness, W P, Stemmer, R C, Stevens

Publikováno v: Nature structural biology. 8(3)

Directed evolution can be a powerful tool to predict antibiotic resistance. Resistance involves the accumulation of mutations beneficial to the pathogen while maintaining residue interactions and core packing that are critical for preserving function

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::db00216951443baf242d312afa1e1ee4
https://pubmed.ncbi.nlm.nih.gov/11224569

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FDTL phase 3 'project squared': learning through 'electronic projectwork' virtual projects and best practice overview

Autor: E. L. Hines, P. R. C. Stevens, C. B. Thomas, O. J. Downing, D. Morley, D. Downes, R.J. Green

Publikováno v: IEE International Symposium Engineering Education: Innovations in Teaching, Learning and Assessment.

Amongst many schemes to relieve curriculum pressure and to allow delivery of a variety of related personal transferable skills and knowledge has been the development of the project-work theme. Here practice amongst course providers has varied conside

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::976d5f8c61dc13a913fe8e77e315fc2a
https://doi.org/10.1049/ic:20010051

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Automation of X-ray crystallography

Autor: E, Abola, P, Kuhn, T, Earnest, R C, Stevens

Publikováno v: Nature structural biology.

Structure-based biological discovery is entering a new era with the development of industrialized macromolecular structure determination pipelines. Intense, highly focused X-rays from integrated synchrotron radiation beam lines combined with signific

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::20735a89239fd25360137a49fe993960
https://pubmed.ncbi.nlm.nih.gov/11104004

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Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution

Autor: M A, Hanson, R C, Stevens

Publikováno v: Nature structural biology. 7(8)

Botulinum neurotoxin serotype B is a zinc protease that disrupts neurotransmitter release by cleaving synaptobrevin-II (Sb2), one of three SNARE proteins involved in neuronal synaptic vesicle fusion. The three-dimensional crystal structure of the apo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bcb1c7d045519f0b8961bdf61434b60b
https://pubmed.ncbi.nlm.nih.gov/19578378

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Effect of food and pharmacokinetic variability on didanosine systemic exposure in HIV-infected children. Pediatric AIDS Clinical Trials Group Protocol 144 Study Team

Autor: R C, Stevens, J H, Rodman, F H, Yong, V, Carey, C A, Knupp, L M, Frenkel

Publikováno v: AIDS research and human retroviruses. 16(5)

The effect of food on didanosine bioavailability and interpatient pharmacokinetic variability was examined in children infected with human immunodeficiency virus type 1 (HIV-1). Didanosine pharmacokinetics were determined during fasting and fed condi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cad0bd4824529de7355875761bb0a2b7
https://pubmed.ncbi.nlm.nih.gov/10772527

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Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase

Autor: H, Erlandsen, E, Bjørgo, T, Flatmark, R C, Stevens

Publikováno v: Biochemistry. 39(9)

The crystal structure of the dimeric catalytic domain (residues 118-424) of human PheOH (hPheOH), cocrystallized with the oxidized form of the cofactor (7,8-dihydro-L-biopterin, BH(2)), has been determined at 2.0 A resolution. The pterin binds in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::204edd555f921239faf12b4e129c4fba
https://pubmed.ncbi.nlm.nih.gov/10694386

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Structural basis of autoregulation of phenylalanine hydroxylase

Autor: B, Kobe, I G, Jennings, C M, House, B J, Michell, K E, Goodwill, B D, Santarsiero, R C, Stevens, R G, Cotton, B E, Kemp

Publikováno v: Nature structural biology. 6(5)

Phenylalanine hydroxylase converts phenylalanine to tyrosine, a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis. It is tightly regulated by the substrates phenylalanine and tetrahydrobiopterin and by phosp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ab37c0814cf850ccec95435223197205
https://pubmed.ncbi.nlm.nih.gov/10331859

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