Zobrazeno 1 - 10
of 135
pro vyhledávání: '"Kyle K Biggar"'
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e68830 (2013)
One of the most adaptive facultative anaerobes among vertebrates is the freshwater turtle, Trachemys scripta elegans. Upon a decrease in oxygen supply and oxidative phosphorylation, these turtles are able to reduce their metabolic rate and recruit an
Externí odkaz:
https://doaj.org/article/a52e52cf2fcf498ea4930dbd4cd24464
Publikováno v:
Biomolecules, Vol 14, Iss 10, p 1303 (2024)
The expansive field of drug discovery is continually seeking innovative approaches to identify and develop novel peptide-based therapeutics. With the advent of artificial intelligence (AI), there has been a transformative shift in the generation of n
Externí odkaz:
https://doaj.org/article/f9e03f85439f43b3abd31ad77890d42a
Autor:
Mullen Boulter, Kyle K. Biggar
Publikováno v:
Biomolecules, Vol 14, Iss 9, p 1112 (2024)
The dual methyltransferase methyltransferase-like protein 13, also referred to as METTL13, or formerly known as FEAT (faintly expressed in healthy tissues, aberrantly overexpressed in tumors), has garnered attention as a significant enzyme in various
Externí odkaz:
https://doaj.org/article/bcae9e1029984d6099a3e6b7e01f64f8
Publikováno v:
PeerJ, Vol 9, p e11117 (2021)
Background Understanding the disease pathogenesis of the novel coronavirus, denoted SARS-CoV-2, is critical to the development of anti-SARS-CoV-2 therapeutics. The global propagation of the viral disease, denoted COVID-19 (“coronavirus disease 2019
Externí odkaz:
https://doaj.org/article/807a8a338ea045fa9d86ec7bf5ef90bf
Publikováno v:
STAR Protocols, Vol 1, Iss 3, Pp 100135- (2020)
Summary: Protein lysine methylation mediates a variety of biological processes, and their dysregulation has been established to play pivotal roles in human disease. A number of these sites constitute attractive drug targets. However, systematic ident
Externí odkaz:
https://doaj.org/article/dcb604d600654c2d99d0fbd76e759a70
Publikováno v:
Biomolecules, Vol 12, Iss 5, p 641 (2022)
Jumonji C (JmjC) lysine demethylases (KDMs) catalyze the removal of methyl (-CH3) groups from modified lysyl residues. Several JmjC KDMs promote cancerous properties and these findings have primarily been in relation to histone demethylation. However
Externí odkaz:
https://doaj.org/article/44cb37f32494409d887cd64c8ec52349
Publikováno v:
The Journal of Biochemistry. 173:31-42
The KDM5/JARID1 sub-family are 2-oxoglutarate and Fe(II)-dependent lysine-specific histone demethylases that are characterized by their Jumonji catalytic domains. The KDM5 family is known to remove tri-/di-methyl modifications from lysine-4 of histon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3717f70209b3bb75b7e162d839da77a
https://doi.org/10.1093/jb/mvac081
https://doi.org/10.1093/jb/mvac081
Autor:
Coen M. Adema, LaDeana W. Hillier, Catherine S. Jones, Eric S. Loker, Matty Knight, Patrick Minx, Guilherme Oliveira, Nithya Raghavan, Andrew Shedlock, Laurence Rodrigues do Amaral, Halime D. Arican-Goktas, Juliana G. Assis, Elio Hideo Baba, Olga L. Baron, Christopher J. Bayne, Utibe Bickham-Wright, Kyle K. Biggar, Michael Blouin, Bryony C. Bonning, Chris Botka, Joanna M. Bridger, Katherine M. Buckley, Sarah K. Buddenborg, Roberta Lima Caldeira, Julia Carleton, Omar S. Carvalho, Maria G. Castillo, Iain W. Chalmers, Mikkel Christensens, Sandra Clifton, Celine Cosseau, Christine Coustau, Richard M. Cripps, Yesid Cuesta-Astroz, Scott F. Cummins, Leon di Stefano, Nathalie Dinguirard, David Duval, Scott Emrich, Cédric Feschotte, Rene Feyereisen, Peter FitzGerald, Catrina Fronick, Lucinda Fulton, Richard Galinier, Sandra G. Gava, Michael Geusz, Kathrin K. Geyer, Gloria I. Giraldo-Calderón, Matheus de Souza Gomes, Michelle A. Gordy, Benjamin Gourbal, Christoph Grunau, Patrick C. Hanington, Karl F. Hoffmann, Daniel Hughes, Judith Humphries, Daniel J. Jackson, Liana K. Jannotti-Passos, Wander de Jesus Jeremias, Susan Jobling, Bishoy Kamel, Aurélie Kapusta, Satwant Kaur, Joris M. Koene, Andrea B. Kohn, Dan Lawson, Scott P Lawton, Di Liang, Yanin Limpanont, Sijun Liu, Anne E. Lockyer, TyAnna L. Lovato, Fernanda Ludolf, Vince Magrini, Donald P. McManus, Monica Medina, Milind Misra, Guillaume Mitta, Gerald M. Mkoji, Michael J. Montague, Cesar Montelongo, Leonid L. Moroz, Monica C. Munoz-Torres, Umar Niazi, Leslie R. Noble, Francislon S. Oliveira, Fabiano S. Pais, Anthony T. Papenfuss, Rob Peace, Janeth J. Pena, Emmanuel A. Pila, Titouan Quelais, Brian J. Raney, Jonathan P. Rast, David Rollinson, Izinara C. Rosse, Bronwyn Rotgans, Edwin J. Routledge, Kathryn M. Ryan, Larissa L. S. Scholte, Kenneth B. Storey, Martin Swain, Jacob A. Tennessen, Chad Tomlinson, Damian L. Trujillo, Emanuela V. Volpi, Anthony J. Walker, Tianfang Wang, Ittiprasert Wannaporn, Wesley C. Warren, Xiao-Jun Wu, Timothy P. Yoshino, Mohammed Yusuf, Si-Ming Zhang, Min Zhao, Richard K. Wilson
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Biomphalaria glabrata is a fresh water snail that acts as a host for trematode Schistosoma mansoni that causes intestinal infection in human. This work describes the genome and transcriptome analyses from 12 different tissues of B glabrata, and ident
Externí odkaz:
https://doaj.org/article/8e37a8f501a642c1ba7af6bed39bfe44
Autor:
Kyle K. Biggar, Cheng-Wei Wu, Shannon N. Tessier, Jing Zhang, Fabien Pifferi, Martine Perret, Kenneth B. Storey
Publikováno v:
Genomics, Proteomics & Bioinformatics, Vol 13, Iss 2, Pp 111-118 (2015)
A variety of mammals employ torpor as an energy-saving strategy in environments of marginal or severe stress either on a daily basis during their inactive period or on a seasonal basis during prolonged multi-day hibernation. Recently, a few Madagasca
Externí odkaz:
https://doaj.org/article/393fc69b6a1146c6b011a75bd6360a0c
Publikováno v:
BioTechniques, Vol 62, Iss 1, p xiii (2017)
Protocol Summary Here we present a new protocol to analyze protein unfolding kinetics using a quantified real-time thermocycler. This technique enables the analysis of a wide range of denaturants (and their interactions with temperature change) on pr
Externí odkaz:
https://doaj.org/article/deb20695c62a438982f1036d13333283