Results 61 to 70 of about 213,935 (349)

A phosphatidylinositol-3-kinase-dependent signal transition regulates ARF1 and ARF6 during Fcgamma receptor-mediated phagocytosis. [PDF]

open access: yesPLoS Biology, 2006
Fcgamma receptor (FcgammaR)-mediated phagocytosis of IgG-coated particles is regulated by 3'-phosphoinositides (3'PIs) and several classes of small GTPases, including ARF6 from the ADP Ribosylation Factor subfamily.
Peter Beemiller   +2 more
doaj   +1 more source

Attenuated SIRT1 Activity Leads to PER2 Cytoplasmic Localization and Dampens the Amplitude of Bmal1 Promoter-Driven Circadian Oscillation

open access: yesFrontiers in Neuroscience, 2021
The circadian clock possesses robust systems to maintain the rhythm approximately 24 h, from cellular to organismal levels, whereas aging is known to be one of the risk factors linked to the alternation of circadian physiology and behavior. The amount of
Atsushige Ashimori   +11 more
doaj   +1 more source

ATM induces MacroD2 nuclear export upon DNA damage [PDF]

open access: yes, 2016
ADP-ribosylation is a dynamic post-translation modification that regulates the early phase of various DNA repair pathways by recruiting repair factors to chromatin.
Golia, Barbara   +8 more
core   +1 more source

Activation of rat brain phospholipase D by ADP-ribosylation factors 1,5, and 6: separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes.

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1994
Two major forms of phospholipase D (PLD) activity, solubilized from rat brain membranes with Triton X-100, were separated by HPLC on a heparin-5PW column with buffer containing octyl glucoside.
D. Massenburg   +6 more
semanticscholar   +1 more source

APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells [PDF]

open access: yes, 2008
APLF is a novel protein of unknown function that accumulates at sites of chromosomal DNA strand breakage via forkhead-associated (FHA) domain-mediated interactions with XRCC1 and XRCC4.
Caldecott, Keith W   +4 more
core   +3 more sources

Arf GTPase-activating proteins SMAP1 and AGFG2 regulate the size of Weibel-Palade bodies and exocytosis of von Willebrand factor

open access: yesBiology Open, 2021
Arf GTPase-Activating proteins (ArfGAPs) mediate the hydrolysis of GTP bound to ADP-ribosylation factors (Arfs), which are critical to form transport intermediates.
Asano Watanabe   +13 more
doaj   +1 more source

Similarities in Function and Gene Structure of Cytohesin-4 and Cytohesin-1, Guanine Nucleotide-exchange Proteins for ADP-ribosylation Factors*

open access: yesJournal of Biological Chemistry, 2000
Activation of ADP-ribosylation factors (ARFs), ∼20-kDa GTPases that are inactive in the GDP-bound form, depends on guanine nucleotide-exchange proteins (GEPs) to accelerate GTP binding.
M. Ogasawara   +8 more
semanticscholar   +1 more source

Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors.

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1998
The Saccharomyces cerevisiae Sec7 protein (ySec7p), which is an important component of the yeast secretory pathway, contains a sequence of approximately 200 amino acids referred to as a Sec7 domain.
M. Sata   +3 more
semanticscholar   +1 more source

Mutational Analysis of the Poly(ADP-Ribosyl)ation Sites of the Transcription Factor CTCF Provides an Insight into the Mechanism of Its Regulation by Poly(ADP-Ribosyl)ation [PDF]

open access: yes, 2009
Poly(ADP-ribosyl)ation of the conserved multifunctional transcription factor CTCF was previously identified as important to maintain CTCF insulator and chromatin barrier functions.
Chernukhin, Igor   +8 more
core   +2 more sources

GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids.

open access: yesJournal of Biological Chemistry, 1994
ADP-ribosylation factor (ARF) is a 21-kDa GTP binding protein that regulates eukaryotic membrane traffic. Both the binding and hydrolysis of GTP by ARF have been shown to be necessary for this function. However, purified mammalian ARF lacks intrinsic GTPase activity (< 0.0015 min-1). We document the presence, in bovine brain extracts, of a protein with
Paul A. Randazzo, Richard A. Kahn
openaire   +3 more sources

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