The Experts below are selected from a list of 258 Experts worldwide ranked by ideXlab platform
Martin J Cann - One of the best experts on this subject based on the ideXlab platform.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Annmarie C. O'donoghue, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Martin J CannAbstract:Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO2 interactions.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Annmarie C. O’donoghue, Martin J CannAbstract:Carbon dioxide can interact with proteins to form carbamate post-translational modifications. Here, the authors developed a strategy to identify carbamate post-translational modifications by trapping carbon dioxide and subsequently identifying the carbamylated proteins. Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO_2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO_2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO_2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO_2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO_2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO_2 interactions.
Victoria L. Linthwaite - One of the best experts on this subject based on the ideXlab platform.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Annmarie C. O'donoghue, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Martin J CannAbstract:Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO2 interactions.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Annmarie C. O’donoghue, Martin J CannAbstract:Carbon dioxide can interact with proteins to form carbamate post-translational modifications. Here, the authors developed a strategy to identify carbamate post-translational modifications by trapping carbon dioxide and subsequently identifying the carbamylated proteins. Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO_2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO_2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO_2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO_2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO_2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO_2 interactions.
Achim Treumann - One of the best experts on this subject based on the ideXlab platform.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Annmarie C. O'donoghue, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Martin J CannAbstract:Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO2 interactions.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Annmarie C. O’donoghue, Martin J CannAbstract:Carbon dioxide can interact with proteins to form carbamate post-translational modifications. Here, the authors developed a strategy to identify carbamate post-translational modifications by trapping carbon dioxide and subsequently identifying the carbamylated proteins. Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO_2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO_2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO_2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO_2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO_2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO_2 interactions.
Adrian P. Brown - One of the best experts on this subject based on the ideXlab platform.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Annmarie C. O'donoghue, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Martin J CannAbstract:Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO2 interactions.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Annmarie C. O’donoghue, Martin J CannAbstract:Carbon dioxide can interact with proteins to form carbamate post-translational modifications. Here, the authors developed a strategy to identify carbamate post-translational modifications by trapping carbon dioxide and subsequently identifying the carbamylated proteins. Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO_2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO_2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO_2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO_2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO_2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO_2 interactions.
David Wong-pascua - One of the best experts on this subject based on the ideXlab platform.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Annmarie C. O'donoghue, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Martin J CannAbstract:Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO2 interactions.
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The identification of carbon dioxide mediated protein post-translational modifications
Nature Communications, 2018Co-Authors: Victoria L. Linthwaite, Adrian P. Brown, David Wong-pascua, Achim Treumann, Joanna M. Janus, Andrew Porter, David R. W. Hodgson, Annmarie C. O’donoghue, Martin J CannAbstract:Carbon dioxide can interact with proteins to form carbamate post-translational modifications. Here, the authors developed a strategy to identify carbamate post-translational modifications by trapping carbon dioxide and subsequently identifying the carbamylated proteins. Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO_2 is generally unreactive but can combine with neutral amines to form Carbamates on proteins under physiological conditions. The most widely known examples of this are CO_2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO_2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein Carbamates using triethyloxonium tetrafluoroborate to covalently trap CO_2, allowing for downstream proteomic analysis. This report describes the systematic identification of Carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO_2 can impact protein biochemistry through carbamate formation. The ability to identify protein Carbamates will significantly advance our understanding of cellular CO_2 interactions.
