Výsledky vyhledávání - "Richard D. Hutton"

Mapping the Topography of a Protein Energy Landscape

Autor: Pierpaolo Bruscolini, James Wilkinson, Laura S. Itzhaki, Alan R. Lowe, Mauro Faccin, Alessandro Pelizzola, Richard D. Hutton, Elin M. Sivertsson

Publikováno v: Journal of the American Chemical Society. 137:14610-14625

Protein energy landscapes are highly complex, yet the vast majority of states within them tend to be invisible to experimentalists. Here, using site-directed mutagenesis and exploiting the simplicity of tandem-repeat protein structures, we delineate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f3042d4c351006bb9b4f1ccbabda237
https://doi.org/10.1021/jacs.5b07370

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Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both

Autor: Melissa N. Webby, Ali Reza Nazmi, Emily J. Parker, Nicola J. Blackmore, Geoffrey B. Jameson, Richard D. Hutton, Edward N. Baker

Publikováno v: Journal of Biological Chemistry. 290:18187-18198

Allostery, where remote ligand binding alters protein function, is essential for the control of metabolism. Here, we have identified a highly sophisticated allosteric response that allows complex control of the pathway for aromatic amino acid biosynt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1d5dd54e8904549950300bb669e2b2eb
https://doi.org/10.1074/jbc.m115.638700

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Single-molecule characterization of Fen1 and Fen1/PCNA complexes acting on flap substrates

Autor: J. Carlos Penedo, Timothy D. Craggs, Richard D. Hutton, Malcolm F. White, Alfonso Brenlla

Publikováno v: Nucleic Acids Research

This article was made OA through RCUK block grant funds. Flap endonuclease 1 (Fen1) is a highly conserved structure-specific nuclease that catalyses a specific incision to remove 5′ flaps in double-stranded DNA substrates. Fen1 plays an essential r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdef06d45edbf1d7ac7db7f7dc42e535
https://doi.org/10.1093/nar/gkt1116

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Dynamic Cross-Talk among Remote Binding Sites: The Molecular Basis for Unusual Synergistic Allostery

Autor: Emily J. Parker, Geoffrey B. Jameson, Penelope J. Cross, Richard D. Hutton, Wanting Jiao

Publikováno v: Journal of Molecular Biology. 415:716-726

Allosteric regulation of protein function is critical for metabolic control. Binding of allosteric effectors elicits a functional change in a remote ligand binding site on a protein by altering the equilibrium between different forms in the protein e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0dc712b8e4d54a72d1013110178bbe1
https://doi.org/10.1016/j.jmb.2011.11.037

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Potent Inhibitors of a Shikimate Pathway Enzyme from Mycobacterium tuberculosis

Autor: Emily J. Parker, Richard D. Hutton, Sebastian Reichau, Edward N. Baker, Scott Walker, Wanting Jiao

Publikováno v: Journal of Biological Chemistry. 286:16197-16207

Tuberculosis remains a serious global health threat, with the emergence of multidrug-resistant strains highlighting the urgent need for novel antituberculosis drugs. The enzyme 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAH7PS) catalyzes t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::be5d1e2844af293388cdb5968c3cae02
https://doi.org/10.1074/jbc.m110.211649

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Targeting the Role of a Key Conserved Motif for Substrate Selection and Catalysis by 3-Deoxy-d-manno-octulosonate 8-Phosphate Synthase

Autor: Richard D. Hutton, Fiona C. Cochrane, Geoffrey B. Jameson, Jeffrey A. Yeoman, Emily J. Parker, Timothy M. Allison

Publikováno v: Biochemistry. 50:3686-3695

3-Deoxy-D-manno-octulosonate 8-phosphate synthase (KDO8PS) catalyzes the reaction between three-carbon phosphoenolpyruvate (PEP) and five-carbon d-arabinose 5-phosphate (A5P), generating KDO8P, a key intermediate in the biosynthetic pathway to 3-deox

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45c76483205c49dc98a84a717f00d785
https://doi.org/10.1021/bi200251f

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Synergistic Allostery, a Sophisticated Regulatory Network for the Control of Aromatic Amino Acid Biosynthesis in Mycobacterium tuberculosis

Autor: Richard D. Hutton, Celia J. Webby, Geoffrey B. Jameson, Nicola J. Blackmore, Emily J. Parker, Edward N. Baker, Heather M. Baker, Wanting Jiao

Publikováno v: Journal of Biological Chemistry. 285:30567-30576

The shikimate pathway, responsible for aromatic amino acid biosynthesis, is required for the growth of Mycobacterium tuberculosis and is a potential drug target. The first reaction is catalyzed by 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8814ede7c7befb8cd425b23579d4717
https://doi.org/10.1074/jbc.m110.111856

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Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both: AN EXAMPLE OF MOLECULAR SYMBIOSIS

Autor: Nicola J, Blackmore, Ali Reza, Nazmi, Richard D, Hutton, Melissa N, Webby, Edward N, Baker, Geoffrey B, Jameson, Emily J, Parker

Publikováno v: The Journal of biological chemistry. 290(29)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::11e1ec2fbc5e4c0fb20346fbfb1a96b3
https://pubmed.ncbi.nlm.nih.gov/26032422

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General Motors Increases Its Production Throughput

Autor: Jeffrey M. Alden, Mark A. Turnquist, Theodore Costy, Kevin A. Kohls, David S. Kim, Lawrence D. Burns, David J. Vander Veen, Richard D. Hutton, Craig A. Jackson, Jonathan H. Owen

Publikováno v: Interfaces. 36:6-25

In the late 1980s, General Motors Corporation (GM) initiated a long-term project to predict and improve the throughput performance of its production lines to increase productivity throughout its manufacturing operations and provide GM with a strategi

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https://doi.org/10.1287/inte.1050.0181

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Three sites and you are out: ternary synergistic allostery controls aromatic amino acid biosynthesis in Mycobacterium tuberculosis

Autor: Wanting Jiao, Geoffrey B. Jameson, Edward N. Baker, Richard D. Hutton, Nicola J. Blackmore, Sebastian Reichau, Emily J. Parker

Publikováno v: Journal of molecular biology. 425(9)

3-Deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAH7PS) catalyzes the first step in the shikimate pathway, the pathway responsible for the biosynthesis of the aromatic amino acids Trp, Phe, and Tyr. Unlike many other organisms that produce up t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::545b7661882006d5afcbd327f77dca6f
https://pubmed.ncbi.nlm.nih.gov/23274137

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