Results 171 to 180 of about 53,577 (232)

AACRNL evolved from virulence factor to epigenetic parasite driving genome expansion in free-living eukaryotes. [PDF]

Nat Commun
Xu T, Geng S, Lv X, Xing Q, Sun Y.
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Metabolites beyond metabolism: Exploring their atypical roles in protein modification and signaling transduction. [PDF]

Chin Med J (Engl)
Yang W, Wu J, Cui G.
europepmc   +1 more source

Targeting MARylation and DePARylation in Cancer Therapy: New Promising Therapeutic Opportunities. [PDF]

Cancers (Basel)
Cabeza-Fernández V, Ríos-Sola FJ, Martín-Oliva D, Borrego-Pérez J, Oliver FJ, YéLamos J, Rodríguez-Vargas JM.   +6 more
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TcArf1: a Trypanosoma cruzi ADP-ribosylation factor

Parasitology Research, 2003
Arfs (ADP-ribosylation factors) are conserved GTP-binding proteins involved in the control of coatomers assembling in budding vesicles in the eukaryotic secretory pathway and during some endocytic events. Here, we describe the gene for an Arf-homologue from the unicellular kinetoplastid parasite Trypanosoma cruzi, named TcArf1.
Alexandre, de Sá-Freire, José Luciano, Nepomuceno-Silva, Júlio César, da Paixão, Sérgio Maurício, de Mendonça, Luiz Dione Barbosa, de Melo, Ulisses Gazos, Lopes   +5 more
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Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors

Molecular and Cellular Biochemistry, 1999
ADP-ribosylation factors (ARFs) are members of a multigene family of 20-kDa guanine nucleotide-binding proteins that are regulatory components in several pathways of intracellular vesicular trafficking. The relatively small (approximately 180-amino acids) ARF proteins interact with a variety of molecules (in addition to GTP/GDP, of course).
J, Moss, M, Vaughan
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Assays of ADP-Ribosylation factor Function

2002
ADP-ribosylation factors (ARFs) comprise a family of 20-kDa GTPases first identified as the protein cofactor required for the ADP ribosylation of the G s α protein, catalyzed by the A 1 subunits of the bacterial toxins cholera toxin (CT) and Escherichia colt heat-labile toxin (UF).
Jun, Kuai, Richard A, Kahn
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Cellular ADP-ribosylation of Elongation Factor 2

Molecular and Cellular Biochemistry, 1994
A cellular ADP-ribosyltransferase activity has been found in a variety of animals and tissues. The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro protein synthesis. Although, the mechanism of action of the cellular enzyme appears similar to diphtheria toxin and Pseudomonas exotoxin A ...
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ADP-ribosylation factor (ARF)

1994
Abstract Cloned ARF cDNA predicts a protein with a glycine at this position. Each of the three human ARF cDNAs hARF11314 (accession number P10947), hARF315 (accession number P16587), and hARF4,3,15 (accession numbers P18085, P21371) encode proteins of 180 or 181 amino acids with predicted molecular masses of 21-22 kDa.
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