Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Jennifer J. Ottesen"'
Autor:
Ziyong Z. Hong, Ruixuan R. Yu, Xiaoyu Zhang, Allison M. Webb, Nathaniel L. Burge, Michael G. Poirier, Jennifer J. Ottesen
Publikováno v:
Peptide Science.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b04357f3b4850d3c51c9c6bf23c5725a
https://doi.org/10.1002/pep2.24323
https://doi.org/10.1002/pep2.24323
Autor:
Nathaniel L. Burge, Jenna L. Thuma, Ziyong Z. Hong, Kevin B. Jamison, Jennifer J. Ottesen, Michael G. Poirier
Publikováno v:
Biochemistry. 61(8)
The linker histone H1 is a highly prevalent protein that compacts chromatin and regulates DNA accessibility and transcription. However, the mechanisms behind H1 regulation of transcription factor (TF) binding within nucleosomes are not well understoo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d1fef477a7a02f918bc2102cc643686
https://pubmed.ncbi.nlm.nih.gov/35377618
https://pubmed.ncbi.nlm.nih.gov/35377618
Autor:
Candice L Wike, Hillary K Graves, Reva Hawkins, Matthew D Gibson, Michelle B Ferdinand, Tao Zhang, Zhihong Chen, Damien F Hudson, Jennifer J Ottesen, Michael G Poirier, Jill Schumacher, Jessica K Tyler
Publikováno v:
eLife, Vol 5 (2016)
Phosphorylation of histone H3 threonine 118 (H3 T118ph) weakens histone DNA-contacts, disrupting the nucleosome structure. We show that Aurora-A mediated H3 T118ph occurs at pericentromeres and chromosome arms during prophase and is lost upon chromos
Externí odkaz:
https://doaj.org/article/48487e7bf0d44c30afc1c804f5cab2f7
Autor:
Sambuddha Sen, Jennifer J. Ottesen, Christine Wachnowsky, Brian Rao, Brian Fries, James A. Cowan, Cecil J. Howard
Publikováno v:
J Biol Inorg Chem
A new class of mitochondrial disease has been identified and characterized as Multiple Mitochondrial Dysfunctions Syndrome (MMDS). Four different forms of the disease have each been attributed to point mutations in proteins involved in iron-sulfur (F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9ae3639ac717b1ac3f759abd8c828bb
https://doi.org/10.1007/s00775-019-01713-x
https://doi.org/10.1007/s00775-019-01713-x
Autor:
Ruixuan R. Yu, Jennifer J. Ottesen, Michael G. Poirier, Xiaoyu Zhang, Allison M. Webb, Ziyong Z. Hong, Nathaniel L. Burge
Simple and efficient total chemical synthesis of large proteins remains a significant challenge. Here, we report development of a convergent hybrid phase native chemical ligation (CHP-NCL) strategy that should be generally applicable for facile prepa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1311ef928b272646fdac22759e8c24f9
https://doi.org/10.1101/661744
https://doi.org/10.1101/661744
Autor:
Michael G. Poirier, Justin A. North, Karolin Luger, Tao Wang, Sarah J. Dreher, John C. Shimko, Jennifer J. Ottesen, Yi Luo, Matthew S. Brehove
Publikováno v:
Journal of Biological Chemistry. 290:22612-22621
Nucleosome unwrapping dynamics provide transient access to the complexes involved in DNA transcription, repair, and replication, whereas regulation of nucleosome unwrapping modulates occupancy of these complexes. Histone H3 is phosphorylated at tyros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f0501caa43f30f27e6e7bde9e7b0cca
https://doi.org/10.1074/jbc.m115.661363
https://doi.org/10.1074/jbc.m115.661363
Autor:
Michelle B. Ferdinand, Alex M. Mooney, Cecil J. Howard, John van Noort, Michael G. Poirier, Justin A. North, Matthew A. Shoffner, Jonathan W. Picking, Marek Simon, Jennifer J. Ottesen
Publikováno v:
Nucleic Acids Research
Nucleosomes contain ∼146 bp of DNA wrapped around a histone protein octamer that controls DNA accessibility to transcription and repair complexes. Posttranslational modification (PTM) of histone proteins regulates nucleosome function. To date, only
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25d3f706a750e867f1b14229345590d2
https://doi.org/10.1093/nar/gku150
https://doi.org/10.1093/nar/gku150
Autor:
Matthew D. Gibson, Candice L Wike, Jennifer J. Ottesen, Tao Zhang, Zhihong Chen, Damien F. Hudson, Jessica K. Tyler, Michael G. Poirier, Reva Hawkins, Michelle B. Ferdinand, Jill M. Schumacher, Hillary K. Graves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::43f58ca3774bedf6ff3f53b471055a2b
https://doi.org/10.7554/elife.11402.029
https://doi.org/10.7554/elife.11402.029
Autor:
Jennifer J. Ottesen, Jill M. Schumacher, Hillary K. Graves, Candice L Wike, Damien F. Hudson, Michelle B. Ferdinand, Matthew D. Gibson, Reva Hawkins, Michael G. Poirier, Tao Zhang, Zhihong Chen, Jessica K. Tyler
Publikováno v:
eLife, Vol 5 (2016)
eLife
eLife
Phosphorylation of histone H3 threonine 118 (H3 T118ph) weakens histone DNA-contacts, disrupting the nucleosome structure. We show that Aurora-A mediated H3 T118ph occurs at pericentromeres and chromosome arms during prophase and is lost upon chromos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6f5c038c7a71c97c2afdf2c76654515
https://elifesciences.org/articles/11402
https://elifesciences.org/articles/11402
Autor:
Jennifer J. Ottesen, Mallory M. Alexander, Santosh K. Mahto, Cecil J. Howard, Kurt Justus, Ruixuan R. Yu
Publikováno v:
Organicbiomolecular chemistry. 14(9)
We introduce a hybrid solid-solution phase ligation approach that combines the efficiency of solid phase ligation with solution phase ligation in the total synthesis of modified histone proteins. A two linker strategy allows analysis throughout work
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0716ab171b91f5162c96e23415910b2
https://pubmed.ncbi.nlm.nih.gov/26821702
https://pubmed.ncbi.nlm.nih.gov/26821702