Výsledky vyhledávání - "Rachel H. Watkins"

Oxidation of the Yeast Mitochondrial Thioredoxin Promotes Cell Death

Autor: Rachel H. Watkins, Jill Parkin, Paraskevi Kritsiligkou, Darren Greetham, Chris M. Grant, Zorana Carter

Publikováno v: Antioxidants & Redox Signaling. 18:376-385

Yeast, like other eukaryotes, contains a complete mitochondrial thioredoxin system comprising a thioredoxin (Trx3) and a thioredoxin reductase (Trr2). Mitochondria are a main source of reactive oxygen species (ROS) in eukaryotic organisms, and this s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8df18802a1dda6e58119d619db5e87d6
https://doi.org/10.1089/ars.2012.4597

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Direct and Absolute Quantification of over 1800 Yeast Proteins via Selected Reaction Monitoring

Autor: Karin Lanthaler, Chris M. Grant, Victoria M. Harman, Paul F. G. Sims, Simon J. Hubbard, Robert J. Beynon, Craig Lawless, Dean E. Hammond, Rachel H. Watkins, Rebecca L. Miller, Claire E. Eyers, Philip Brownridge, Stephen W. Holman

Publikováno v: Molecular and Cellular Proteomics
Lawless, C, Holman, S W, Brownridge, P, Lanthaler, K, Harman, V M, Watkins, R, Hammond, D E, Miller, R L, Sims, P F G, Grant, C, Eyers, C E, Beynon, R J & Hubbard, S 2016, ' Direct and Absolute Quantification of over 1800 Yeast Proteins via Selected Reaction Monitoring. ', Molecular and Cellular Proteomics, vol. 15, no. 4, pp. 1309-1322 . https://doi.org/10.1074/mcp.M115.054288
Molecular & Cellular Proteomics : MCP

Defining intracellular protein concentration is critical in molecular systems biology. Although strategies for determining relative protein changes are available, defining robust absolute values in copies per cell has proven significantly more challe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e08430dd8363cdb7f183992c61a8a44f

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Global absolute quantification of a proteome: Challenges in the deployment of a QconCAT strategy

Autor: Philip Brownridge, Ronan O’Cualain, Robert J. Beynon, Rachel H. Watkins, Karin Lanthaler, Chris M. Grant, Simon J. Hubbard, Simon J. Gaskell, Stephen W. Holman, Paul F. G. Sims, Craig Lawless, Victoria M. Harman

Publikováno v: PROTEOMICS. 11:2957-2970

In this paper, we discuss the challenge of large-scale quantification of a proteome, referring to our programme that aims to define the absolute quantity, in copies per cell, of at least 4000 proteins in the yeast Saccharomyces cerevisiae. We have ba

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::164f2c2e242e34bfbb8e77cd7eb28f46
https://doi.org/10.1002/pmic.201100039

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Rat Primary Hepatocytes and H4 Hepatoma Cells Display Differential Sensitivity to Cyclic AMP at the Level of Expression of Tyrosine Aminotransferase

Autor: Alan J. Dickson, Rachel H. Watkins, Clive S. Pickering

Publikováno v: Biochemical and Biophysical Research Communications. 252:764-769

We have shown that the sensitivity of isolated hepatocytes and H4 hepatoma cells to cyclic AMP is different. In terms of activation of tyrosine aminotransferase at mRNA and activity level in response to cyclic AMP, isolated hepatocytes are 10-fold mo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::822b65a250d69f35f6dbe945fb69f457
https://doi.org/10.1006/bbrc.1998.9735

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Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins

Autor: Neil J. Bulleid, Jennifer J. Simmons, Catherine E. Jessop, Rachel H. Watkins, Mohammed Tasab

At least 17 members of the protein disulphide isomerase (PDI) family of oxidoreductases are present in the endoplasmic reticulum (ER) of mammalian cells. They are thought to catalyse disulphide formation to aid folding or to regulate protein function

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0c7a49e9fc8888ab703bd65f7bfb7bc
https://europepmc.org/articles/PMC2779130/

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Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin

Autor: Joseph E. Chambers, Catherine E. Jessop, Rachel H. Watkins, Neil J. Bulleid, Timothy J. Tavender

Publikováno v: The Journal of Biological Chemistry

The formation of disulfides within proteins entering the secretory pathway is catalyzed by the protein disulfide isomerase family of endoplasmic reticulum localized oxidoreductases. One such enzyme, ERp57, is thought to catalyze the isomerization of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd8a2ab1245aac988935fc5f65252739
https://pubmed.ncbi.nlm.nih.gov/19054761

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Oxidative protein folding in the mammalian endoplasmic reticulum

Autor: Catherine E. Jessop, Rachel H. Watkins, Neil J. Bulleid, Seema Chakravarthi

Publikováno v: Biochemical Society transactions. 32(Pt 5)

Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4689c6b161fb279e42eba1b21e57536
https://pubmed.ncbi.nlm.nih.gov/15493980

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