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 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
facet_avail Online
Free
finc_class_facet Physik
Biologie
Chemie und Pharmazie
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAxNi9qLmZlYnNsZXQuMjAxMy4wOS4wNDI
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAxNi9qLmZlYnNsZXQuMjAxMy4wOS4wNDI
institution DE-105
DE-14
DE-Ch1
DE-L229
DE-D275
DE-Bn3
DE-Brt1
DE-Zwi2
DE-D161
DE-Gla1
DE-Zi4
DE-15
DE-Pl11
DE-Rs1
imprint Wiley, 2013
imprint_str_mv Wiley, 2013
issn 1873-3468
0014-5793
issn_str_mv 1873-3468
0014-5793
language English
mega_collection Wiley (CrossRef)
match_str cameron2013generationandcharacterizationofarabbitmonoclonalantibodysitespecificfortauoglcnacylatedatserine400
publishDateSort 2013
publisher Wiley
recordtype ai
record_format ai
series FEBS Letters
source_id 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>
container_issue 22
container_start_page 3722
container_title FEBS Letters
container_volume 587
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792343173941428228
geogr_code not assigned
last_indexed 2024-03-01T16:47:28.792Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Generation+and+characterization+of+a+rabbit+monoclonal+antibody+site%E2%80%90specific+for+tau+O%E2%80%90GlcNAcylated+at+serine+400&rft.date=2013-11-15&genre=article&issn=1873-3468&volume=587&issue=22&spage=3722&epage=3728&pages=3722-3728&jtitle=FEBS+Letters&atitle=Generation+and+characterization+of+a+rabbit+monoclonal+antibody+site%E2%80%90specific+for+tau+O%E2%80%90GlcNAcylated+at+serine+400&aulast=Hering&aufirst=Heike&rft_id=info%3Adoi%2F10.1016%2Fj.febslet.2013.09.042&rft.language%5B0%5D=eng
SOLR
_version_ 1792343173941428228
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
facet_avail Online, Free
finc_class_facet Physik, Biologie, Chemie und Pharmazie
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAxNi9qLmZlYnNsZXQuMjAxMy4wOS4wNDI
imprint Wiley, 2013
imprint_str_mv Wiley, 2013
institution DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1
issn 1873-3468, 0014-5793
issn_str_mv 1873-3468, 0014-5793
language English
last_indexed 2024-03-01T16:47:28.792Z
match_str cameron2013generationandcharacterizationofarabbitmonoclonalantibodysitespecificfortauoglcnacylatedatserine400
mega_collection Wiley (CrossRef)
physical 3722-3728
publishDate 2013
publishDateSort 2013
publisher Wiley
record_format ai
recordtype ai
series FEBS Letters
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