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Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400
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Zeitschriftentitel: | FEBS Letters |
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Personen und Körperschaften: | , , , , , , , , , , , |
In: | FEBS Letters, 587, 2013, 22, S. 3722-3728 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Wiley
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Schlagwörter: |
author_facet |
Cameron, Andrew Giacomozzi, Brandy Joyce, John Gray, Audrey Graham, Danielle Ousson, Solenne Neny, Maud Beher, Dirk Carlson, George O'Moore, Jill Shearman, Mark Hering, Heike Cameron, Andrew Giacomozzi, Brandy Joyce, John Gray, Audrey Graham, Danielle Ousson, Solenne Neny, Maud Beher, Dirk Carlson, George O'Moore, Jill Shearman, Mark Hering, Heike |
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author |
Cameron, Andrew Giacomozzi, Brandy Joyce, John Gray, Audrey Graham, Danielle Ousson, Solenne Neny, Maud Beher, Dirk Carlson, George O'Moore, Jill Shearman, Mark Hering, Heike |
spellingShingle |
Cameron, Andrew Giacomozzi, Brandy Joyce, John Gray, Audrey Graham, Danielle Ousson, Solenne Neny, Maud Beher, Dirk Carlson, George O'Moore, Jill Shearman, Mark Hering, Heike FEBS Letters Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
author_sort |
cameron, andrew |
spelling |
Cameron, Andrew Giacomozzi, Brandy Joyce, John Gray, Audrey Graham, Danielle Ousson, Solenne Neny, Maud Beher, Dirk Carlson, George O'Moore, Jill Shearman, Mark Hering, Heike 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2013.09.042 <jats:p>Aggregation of tau into paired helical filaments is a pathological process leading to neurotoxicity in Alzheimer's disease and other tauopathies. Tau is posttranslationally modified by O‐linked <jats:italic>N</jats:italic>‐acetylglucosamine (O‐GlcNAc), and increasing tau O‐GlcNAcylation may protect against its aggregation. Research tools to study the relationship between tau aggregation and tau O‐GlcNAcylation have not been widely available. Here we describe the generation of a rabbit monoclonal antibody specific for tau O‐GlcNAcylated at Ser400 (O‐tau(S400)). We show the utility of this antibody for in vitro and in vivo experiments to investigate the function of O‐GlcNAc modifications of tau at Ser400.</jats:p> Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 FEBS Letters |
doi_str_mv |
10.1016/j.febslet.2013.09.042 |
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Online Free |
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Physik Biologie Chemie und Pharmazie |
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ElectronicArticle |
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Wiley, 2013 |
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Wiley, 2013 |
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2013 |
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Wiley |
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FEBS Letters |
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49 |
title |
Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_unstemmed |
Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_full |
Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_fullStr |
Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_full_unstemmed |
Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_short |
Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_sort |
generation and characterization of a rabbit monoclonal antibody site‐specific for tau o‐glcnacylated at serine 400 |
topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
url |
http://dx.doi.org/10.1016/j.febslet.2013.09.042 |
publishDate |
2013 |
physical |
3722-3728 |
description |
<jats:p>Aggregation of tau into paired helical filaments is a pathological process leading to neurotoxicity in Alzheimer's disease and other tauopathies. Tau is posttranslationally modified by O‐linked <jats:italic>N</jats:italic>‐acetylglucosamine (O‐GlcNAc), and increasing tau O‐GlcNAcylation may protect against its aggregation. Research tools to study the relationship between tau aggregation and tau O‐GlcNAcylation have not been widely available. Here we describe the generation of a rabbit monoclonal antibody specific for tau O‐GlcNAcylated at Ser400 (O‐tau(S400)). We show the utility of this antibody for in vitro and in vivo experiments to investigate the function of O‐GlcNAc modifications of tau at Ser400.</jats:p> |
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author | Cameron, Andrew, Giacomozzi, Brandy, Joyce, John, Gray, Audrey, Graham, Danielle, Ousson, Solenne, Neny, Maud, Beher, Dirk, Carlson, George, O'Moore, Jill, Shearman, Mark, Hering, Heike |
author_facet | Cameron, Andrew, Giacomozzi, Brandy, Joyce, John, Gray, Audrey, Graham, Danielle, Ousson, Solenne, Neny, Maud, Beher, Dirk, Carlson, George, O'Moore, Jill, Shearman, Mark, Hering, Heike, Cameron, Andrew, Giacomozzi, Brandy, Joyce, John, Gray, Audrey, Graham, Danielle, Ousson, Solenne, Neny, Maud, Beher, Dirk, Carlson, George, O'Moore, Jill, Shearman, Mark, Hering, Heike |
author_sort | cameron, andrew |
container_issue | 22 |
container_start_page | 3722 |
container_title | FEBS Letters |
container_volume | 587 |
description | <jats:p>Aggregation of tau into paired helical filaments is a pathological process leading to neurotoxicity in Alzheimer's disease and other tauopathies. Tau is posttranslationally modified by O‐linked <jats:italic>N</jats:italic>‐acetylglucosamine (O‐GlcNAc), and increasing tau O‐GlcNAcylation may protect against its aggregation. Research tools to study the relationship between tau aggregation and tau O‐GlcNAcylation have not been widely available. Here we describe the generation of a rabbit monoclonal antibody specific for tau O‐GlcNAcylated at Ser400 (O‐tau(S400)). We show the utility of this antibody for in vitro and in vivo experiments to investigate the function of O‐GlcNAc modifications of tau at Ser400.</jats:p> |
doi_str_mv | 10.1016/j.febslet.2013.09.042 |
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source_id | 49 |
spelling | Cameron, Andrew Giacomozzi, Brandy Joyce, John Gray, Audrey Graham, Danielle Ousson, Solenne Neny, Maud Beher, Dirk Carlson, George O'Moore, Jill Shearman, Mark Hering, Heike 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2013.09.042 <jats:p>Aggregation of tau into paired helical filaments is a pathological process leading to neurotoxicity in Alzheimer's disease and other tauopathies. Tau is posttranslationally modified by O‐linked <jats:italic>N</jats:italic>‐acetylglucosamine (O‐GlcNAc), and increasing tau O‐GlcNAcylation may protect against its aggregation. Research tools to study the relationship between tau aggregation and tau O‐GlcNAcylation have not been widely available. Here we describe the generation of a rabbit monoclonal antibody specific for tau O‐GlcNAcylated at Ser400 (O‐tau(S400)). We show the utility of this antibody for in vitro and in vivo experiments to investigate the function of O‐GlcNAc modifications of tau at Ser400.</jats:p> Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 FEBS Letters |
spellingShingle | Cameron, Andrew, Giacomozzi, Brandy, Joyce, John, Gray, Audrey, Graham, Danielle, Ousson, Solenne, Neny, Maud, Beher, Dirk, Carlson, George, O'Moore, Jill, Shearman, Mark, Hering, Heike, FEBS Letters, Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
title | Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_full | Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_fullStr | Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_full_unstemmed | Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_short | Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
title_sort | generation and characterization of a rabbit monoclonal antibody site‐specific for tau o‐glcnacylated at serine 400 |
title_unstemmed | Generation and characterization of a rabbit monoclonal antibody site‐specific for tau O‐GlcNAcylated at serine 400 |
topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
url | http://dx.doi.org/10.1016/j.febslet.2013.09.042 |