Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Cecil J Howard"'
Autor:
Randi M Mackler, Nathan D Jones, Anne M Gardner, Miguel A Lopez, Cecil J Howard, Richard Fishel, Kristine E Yoder
Publikováno v:
PLoS ONE, Vol 14, Iss 3, p e0212764 (2019)
Eukaryotic DNA binding proteins must access genomic DNA that is packaged into chromatin in vivo. During a productive infection, retroviral integrases (IN) must similarly interact with chromatin to integrate the viral cDNA genome. Here we examine the
Externí odkaz:
https://doaj.org/article/60914d67a03642b5b7b97586bdd57159
Autor:
Edward M. Marcotte, Jagannath Swaminathan, Eric V. Anslyn, Cecil J Howard, Brendan M. Floyd, Angela M. Bardo
Publikováno v:
ACS Chem Biol
The field of proteomics has expanded recently with more sensitive techniques for the bulk measurement of peptides as well as single-molecule techniques. One limiting factor for some of these methods is the need for multiple chemical derivatizations a
Autor:
Alexander V. Kinev, Quanjuan Zhang, P Rogelio Escamilla, Youjun Yang, Cecil J Howard, Eric V. Anslyn, Yanming Shen, Jason B. Shear, Xuhong Qian, Derek S. Hernandez, Daria Y Filonov
Publikováno v:
Chemical Science
Fluorescent probes for nitric oxide (NO), or more frequently for its oxidized surrogate dinitrogen trioxide (N2O3), have enabled scientists to study the contributions of this signaling molecule to many physiological processes. Seeking to improve upon
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
Autor:
Anne M. Gardner, Randi M. Mackler, Kristine E. Yoder, Nathan D. Jones, Miguel Álvarez López, Richard Fishel, Cecil J. Howard
Publikováno v:
PLoS ONE
PLoS ONE, Vol 14, Iss 3, p e0212764 (2019)
PLoS ONE, Vol 14, Iss 3, p e0212764 (2019)
Eukaryotic DNA binding proteins must access genomic DNA that is packaged into chromatin in vivo. During a productive infection, retroviral integrases (IN) must similarly interact with chromatin to integrate the viral cDNA genome. Here we examine the
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
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
Publikováno v:
ChemBioChem. 12:2488-2494
C-terminal peptide thioesters are an essential component of the native chemical ligation approach for the preparation of fully or semisynthetic proteins. However, the efficient generation of C-terminal thioesters by Fmoc solid-phase peptide synthesis
Publikováno v:
Topics in Current Chemistry ISBN: 9783319191881
Eukaryotic chromatin is a complex and dynamic system in which the DNA double helix is organized and protected by interactions with histone proteins. This system is regulated through, a large network of dynamic post-translational modifications (PTMs)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df275bd0a68a20dae6e3738cb5425395
https://europepmc.org/articles/PMC4889135/
https://europepmc.org/articles/PMC4889135/
Publikováno v:
Methods in Molecular Biology ISBN: 9781627033046
The purpose of this chapter is to provide practical chemical ligation procedures to prepare histone proteins suitable for the reconstitution of nucleosomes with specific posttranslational modifications in the nucleosome core. Detailed methods are des