Výsledky vyhledávání - "Andrew H. Barratt"

Glycosylation increases active site rigidity leading to improved enzyme stability and turnover

Autor: Krithika Ramakrishnan, Rachel L. Johnson, Samuel D. Winter, Harley L. Worthy, Christopher Thomas, Diana C. Humer, Oliver Spadiut, Sarah H. Hindson, Stephen Wells, Andrew H. Barratt, Georgina E. Menzies, Christopher R. Pudney, D. Dafydd Jones

Publikováno v: The FEBS Journal.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::61d0f7078b1bc8d523de91505d2e4a37
https://doi.org/10.1111/febs.16783

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Author response for 'Glycosylation increases active site rigidity leading to improved enzyme stability and turnover'

Autor: null Krithika Ramakrishnan, null Rachel L. Johnson, null Samuel D. Winter, null Harley L. Worthy, null Christopher Thomas, null Diana C. Humer, null Oliver Spadiut, null Sarah H. Hindson, null Stephen Wells, null Andrew H. Barratt, null Georgina E. Menzies, null Christopher R. Pudney, null D. Dafydd Jones

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce83f8379f1bab935c06bbb0d3205d8b
https://doi.org/10.1111/febs.16783/v3/response1

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Evaluation of the MYCOPLASMA IST3 urogenital mycoplasma assay in an international multicentre trial

Autor: Yohan Bala, Jelena Gluvakov, Laurence Devigne, Ian Boostrom, Kirsty Sands, Lucy C. Jones, Jelena Minic Vasic, Emmanuel Chanard, Edward Portal, Andrew H Barratt, Owen B. Spiller

Publikováno v: Journal of Antimicrobial Chemotherapy

Objectives To evaluate the accuracy, susceptibility and specificity of MYCOPLASMA IST3, the next generation of the most popular culture-based in vitro diagnostic device designed to detect, identify and test the susceptibility of urogenital mycoplasma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a65bb3479e0d40eb673359120c2be656
http://europepmc.org/articles/PMC8678932

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N-linked glycosylation increases horse radish peroxidase rigidity leading to enhanced activity and stability

Autor: Krithika Ramakrishnan, Rachel L. Johnson, Sam D. Winter, Harley L. Worthy, Chris Thomas, Diana Humer, Oliver Spadiut, Sarah H. Hindson, Stephen Wells, Andrew H. Barratt, Georgina E. Menzies, Christopher R. Pudney, D. Dafydd Jones

Glycosylation is the most prevalent protein post-translational modification, with a quarter of glycosylated proteins having enzymatic properties. Yet the full impact of glycosylation on the protein structure-function relationship, especially in enzym

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d3fc9872f8aca3bc8d7fc4e6fc6bd453
https://doi.org/10.1101/2022.09.23.509167

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