Results 121 to 130 of about 77,829 (292)

Unfolding of core nucleosomes by PARP-1 revealed by spFRET microscopy

AIMS Genetics, 2017
DNA accessibility to various protein complexes is essential for various processes in the cell and is affected by nucleosome structure and dynamics. Protein factor PARP-1 (poly(ADP-ribose) polymerase 1) increases the accessibility of DNA in chromatin to ...
Daniel Sultanov, Nadezhda Gerasimova, Kseniya Kudryashova, Natalya Maluchenko, Elena Kotova, Marie-France Langelier, John Pascal, Mikhail Kirpichnikov, Alexey Feofanov, Vasily Studitsky   +9 more
doaj   +1 more source

Calcium-regulated exocytosis of dense-core vesicles requires the activation of ADP-ribosylation factor (ARF)6 by ARF nucleotide binding site opener at the plasma membrane

Journal of Cell Biology, 2002
The ADP ribosylation factor (ARF) GTP binding proteins are believed to mediate cytoskeletal remodeling and vesicular trafficking along the secretory pathway.
N. Vitale, S. Chasserot-Golaz, Y. Bailly, N. Morinaga, M. Frohman, M. Bader   +5 more
semanticscholar   +1 more source

AGAP1, an Endosome-associated, Phosphoinositide-dependent ADP-ribosylation Factor GTPase-activating Protein That Affects Actin Cytoskeleton*

Journal of Biological Chemistry, 2002
We have identified three members of the AGAP subfamily of ASAP family ADP-ribosylation factor GTPase-activating proteins (Arf GAPs). In addition to the Arf GAP domain, these proteins contain GTP-binding protein-like, ankyrin repeat and pleckstrin ...
Z. Nie, K. T. Stanley, S. Stauffer, Kerry M. Jacques, D. Hirsch, J. Takei, P. Randazzo   +6 more
semanticscholar   +1 more source

Phages carry orphan antitoxin-like enzymes to neutralize the DarTG1 toxin-antitoxin defense system

Nature Communications
The astounding number of anti-phage defenses encoded by bacteria is countered by an elaborate set of phage counter-defenses, though their evolutionary origins are often unknown. Here, we report the discovery of an orphan antitoxin counter-defense element
Anna Johannesman, Leila C. Awasthi, Nico Carlson, Michele LeRoux   +3 more
doaj   +1 more source

Overexpression of an ADP-ribosylation Factor-Guanine Nucleotide Exchange Factor, BIG2, Uncouples Brefeldin A-induced Adaptor Protein-1 Coat Dissociation and Membrane Tubulation*

Journal of Biological Chemistry, 2002
BIG2 is a guanine nucleotide exchange factor (GEF) for the ADP-ribosylation factor (ARF) family of small GTPases, which regulate membrane association of COPI and adaptor protein (AP)-1 coat protein complexes.
C. Shinotsuka, Yusaku Yoshida, Kazumasa Kawamoto, H. Takatsu, K. Nakayama   +4 more
semanticscholar   +1 more source

Class II ADP-ribosylation Factors Are Required for Efficient Secretion of Dengue Viruses [PDF]

, 2011
Mateusz Kudelko, Jean‐Baptiste Brault, Kevin Kwok, Ming Yuan Li, Nathalie Pardigon, Malik Peiris, Roberto Bruzzone, Philippe Desprès, Béatrice Nal, Peigang Wang   +9 more
openalex   +1 more source

Hit and run versus long-term activation of PARP-1 by its different domains fine-tunes nuclear processes. [PDF]

, 2019
Poly(ADP-ribose) polymerase 1 (PARP-1) is a multidomain multifunctional nuclear enzyme involved in the regulation of the chromatin structure and transcription.
Ampofo, Michelle, Boyle, Cody, Currie, Michelle, Datz, Haily, Harbin, Jonathan, Ji, Yingbiao, Johnson, Sarah J., Lodhi, Niraj, MacLeod, Brett, Patel, Shri, Pechenkina, Kate, Thomas, MD, Colin, Tulin, Alexei V., Wu, Chao   +13 more
core   +1 more source

Poly(ADP-ribose) Polymerase-1 (PARP1) in Atherosclerosis: From Molecular Mechanisms to Therapeutic Potential [PDF]

, 2014
Poly(ADP-ribosyl)ation reactions, carried out by poly(ADP-ribose) polymerases (PARPs/ARTDs), are reversible posttranslational modifications impacting on numerous cellular processes (e.g., DNA repair, transcription, metabolism, or immune functions). PARP1
Bay, Péter, Little, P., Liu, P., Xu, S.
core   +1 more source

The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. [PDF]

, 1996
Andrea S. Dittié, Nasser Hajibagheri, Sharon A. Tooze   +2 more
openalex   +1 more source

Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites [PDF]

, 2017
Poly(ADP-ribose) polymerase 1 (PARP1) synthesizes poly(ADP-ribose) (PAR) using nicotinamide adenine dinucleotide (NAD) as a substrate. Despite intensive research on the cellular functions of PARP1, the molecular mechanism of PAR formation has not been ...
Altmeyer, Matthias, Fey, Monika, Hassa, Paul O., Hottiger, Michael O., Messner, Simon   +4 more
core