Results 21 to 30 of about 91,412 (386)

Exploring the role of N-acetyltransferases in diseases: a focus on N-acetyltransferase 9 in neurodegeneration. [PDF]

Neural Regen Res
Acetyltransferases, required to transfer an acetyl group on protein are highly conserved proteins that play a crucial role in development and disease.
Deshpande P, Chimata AV, Singh A.
europepmc   +2 more sources

A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii

Nature Communications, 2023
Acinetobacter baumannii is a nosocomial pathogen highly resistant to environmental changes and antimicrobial treatments. Regulation of cellular motility and biofilm formation is important for its virulence, although it is poorly described at the ...
Julija Armalytė, Albinas Čepauskas, Gabija Šakalytė, Julius Martinkus, Jūratė Skerniškytė, Chloé Martens, Edita Sužiedėlienė, Abel Garcia-Pino, Dukas Jurėnas   +8 more
doaj   +1 more source

A synopsis of eukaryotic N^α-terminal acetyltransferases: nomenclature, subunits and substrates [PDF]

BMC Proceedings, 2009
We have introduced a consistent nomenclature for the various subunits of the NatA-NatE N-terminal acetyltransferases from yeast, humans and other eukaryotes.
Polevoda Bogdan, Arnesen Thomas, Sherman Fred   +2 more
doaj   +1 more source

Garcinol and Anacardic Acid, Natural Inhibitors of Histone Acetyltransferases, Inhibit Rhabdomyosarcoma Growth and Proliferation

Molecules, 2023
Rhabdomyosarcoma (RMS) is a malignant tumour of the soft tissues. There are two main histopathological types: alveolar and embryonal. RMS occurs mainly in childhood and is a result of the deregulation of growth and differentiation of muscle cell ...
Patrycja Tomasiak, Joanna Janisiak, Dorota Rogińska, Magdalena Perużyńska, Bogusław Machaliński, Maciej Tarnowski   +5 more
doaj   +1 more source

Structural and molecular rationale for the diversification of resistance mediated by the Antibiotic_NAT family

Communications Biology, 2022
A comprehensive functional and structural study of the Antibiotic_NAT family of aminoglycoside acetyltransferases provides new insight into the molecular mechanisms underlying resistance to existing and emerging aminoglycoside antibiotics.
Peter J. Stogios, Emily Bordeleau, Zhiyu Xu, Tatiana Skarina, Elena Evdokimova, Sommer Chou, Luke Diorio-Toth, Alaric W. D’Souza, Sanket Patel, Gautam Dantas, Gerard D. Wright, Alexei Savchenko   +11 more
doaj   +1 more source

Illuminating the impact of N-terminal acetylation: from protein to physiology. [PDF]

Nat Commun
N-terminal acetylation is a highly abundant protein modification in eukaryotic cells. This modification is catalysed by N-terminal acetyltransferases acting co- or post-translationally. Here, we review the eukaryotic N-terminal acetylation machinery: the
McTiernan N, Kjosås I, Arnesen T.
europepmc   +2 more sources

Structural insights into WcbI, a novel polysaccharide-biosynthesis enzyme

IUCrJ, 2014
Capsular polysaccharides (CPSs) are protective structures on the surfaces of many Gram-negative bacteria. The principal CPS of the human pathogen and Tier 1 select agent Burkholderia pseudomallei consists of a linear repeat of –3)-2-O-acetyl-6-deoxy-β-d ...
Mirella Vivoli, Emily Ayres, Edward Beaumont, Michail N. Isupov, Nicholas J. Harmer   +4 more
doaj   +1 more source

MORF and MOZ acetyltransferases target unmethylated CpG islands through the winged helix domain

Nature Communications, 2023
Human acetyltransferases MOZ and MORF mediate development programs and are dysregulated in diseases. Here the authors identified two winged helix (WH) domains in MORF/MOZ and characterized their DNA binding functions, including targeting of CpG by WH1.
Dustin C. Becht, Brianna J. Klein, Akinori Kanai, Suk Min Jang, Khan L. Cox, Bing-Rui Zhou, Sabrina K. Phanor, Yi Zhang, Ruo-Wen Chen, Christopher C. Ebmeier, Catherine Lachance, Maxime Galloy, Amelie Fradet-Turcotte, Martha L. Bulyk, Yawen Bai, Michael G. Poirier, Jacques Côté, Akihiko Yokoyama, Tatiana G. Kutateladze   +18 more
doaj   +1 more source

Transcription shapes genome-wide histone acetylation patterns

Nature Communications, 2021
Histone acetylation is a ubiquitous hallmark of transcription. Here the authors provide evidence that the majority of histone acetylation is dependent on transcription, specifically due to the requirement of RNAPII for the recruitment and activity of ...
Benjamin J. E. Martin, Julie Brind’Amour, Anastasia Kuzmin, Kristoffer N. Jensen, Zhen Cheng Liu, Matthew Lorincz, LeAnn J. Howe   +6 more
doaj   +1 more source

MOZ/ENL complex is a recruiting factor of leukemic AF10 fusion proteins

Nature Communications, 2023
Altered transcriptional machinery promotes aberrant self-renewal of non-stem hematopoietic progenitors. Here the authors show that AF10 fusion proteins cause aberrant self-renewal via ENL, which promotes leukemic transformation by binding to MOZ/MORF ...
Yosuke Komata, Akinori Kanai, Takahiro Maeda, Toshiya Inaba, Akihiko Yokoyama   +4 more
doaj   +1 more source