Results 91 to 100 of about 213,935 (349)

Increasing Ciliary ARL13B Expression Drives Active and Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia

Cells, 2023
ADP-ribosylation factor-like protein 13B (ARL13B), a regulatory GTPase and guanine exchange factor (GEF), enriches in primary cilia and promotes tumorigenesis in part by regulating Smoothened (SMO), GLI, and Sonic Hedgehog (SHH) signaling.
Ping Shi, Jia Tian, Julianne C. Mallinger, Dahao Ling, Loic P. Deleyrolle, Jeremy C. McIntyre, Tamara Caspary, Joshua J. Breunig, Matthew R. Sarkisian   +8 more
doaj   +1 more source

Binding of coatomer to Golgi membranes requires ADP-ribosylation factor

Journal of Biological Chemistry, 1993
Coatomer, a complex of seven proteins, appears to be the precursor of the coat structure of non-clathrin-coated Golgi-derived vesicles. Another component of this vesicle coat is the cytosolic protein ADP-ribosylation factor (ARF). Like coatomer, ARF appears to reversibly associate with Golgi membranes.
C. J. M. Beckers, David J. Palmer, L Orci, James E. Rothman, J. B. Helms   +4 more
openaire   +4 more sources

Clinical implication and immunological characterisation of the ARF-GEF family member CYTH4 in ovarian cancer

Autoimmunity, 2020
Background The GTP exchange factors on ADP-ribosylation factor (ARF) mediate the GDP/GTP exchange on ARF, serve as regulators in protein trafficking and membrane dynamics, and play critical roles in various cell processes.
Qinyi Zhang, Qingying Wang, Sufang Wu, Jiawen Zhang   +3 more
doaj   +1 more source

The leishmania ARL-1 and Golgi traffic. [PDF]

PLoS ONE, 2008
We present here the characterisation of the Leishmania small G protein ADP-Ribosylation Factor-Like protein 1 (ARL-1). The ARL-1 gene is present in one copy per haploid genome and conserved among trypanosomatids.
Annelise Sahin, Benoît Espiau, Emmanuel Tetaud, Armelle Cuvillier, Lydia Lartigue, Audrey Ambit, Derrick R Robinson, Gilles Merlin   +7 more
doaj   +1 more source

Guanine Nucleotide Exchange on ADP-ribosylation Factors Catalyzed by Cytohesin-1 and Its Sec7 Domain*

Journal of Biological Chemistry, 1998
ADP-ribosylation factors (ARFs) are 20-kDa guanine nucleotide-binding proteins that require specific guanine nucleotide-exchange proteins (GEPs) to accelerate the conversion of inactive ARF-GDP to active ARF-GTP. Cytohesin-1, a 46-kDa ARF GEP, contains a
G. Pacheco‐Rodriguez, E. Meacci, N. Vitale, J. Moss, M. Vaughan   +4 more
semanticscholar   +1 more source

Coordinated actions of microRNAs with other epigenetic factors regulate skeletal muscle development and adaptation [PDF]

, 2017
Epigenetics plays a pivotal role in regulating gene expression in development, in response to cellular stress or in disease states, in virtually all cell types.
Adamo, Sergio, Bianchi, Marzia, Moresi, Viviana, Renzini, Alessandra   +3 more
core   +1 more source

Composite Quantile Factor Model [PDF]

arXiv, 2023
This paper introduces the method of composite quantile factor model for factor analysis in high-dimensional panel data. We propose to estimate the factors and factor loadings across multiple quantiles of the data, allowing the estimates to better adapt to features of the data at different quantiles while still modeling the mean of the data.
arxiv  

Brefeldin A Inhibited Activity of the Sec7 Domain of p200, a Mammalian Guanine Nucleotide-exchange Protein for ADP-ribosylation Factors*

Journal of Biological Chemistry, 1999
A brefeldin A (BFA)-inhibited guanine nucleotide-exchange protein (GEP) for ADP-ribosylation factors (ARF) was purified earlier from bovine brain cytosol. Cloning and expression of the cDNA confirmed that the recombinant protein (p200) is a BFA-sensitive
N. Morinaga, R. Adamik, J. Moss, M. Vaughan   +3 more
semanticscholar   +1 more source

ADP-Ribosylargininyl reaction of cholix toxin is mediated through diffusible intermediates [PDF]

, 2014
Background: Cholix toxin is an ADP-ribosyltransferase found in non-O1/non-O139 strains of Vibrio cholera. The catalytic fragment of cholix toxin was characterized as a diphthamide dependent ADP-ribosyltransferase.
Sung, Vicky M-H, Tsai, Chia-Lun
core   +1 more source

ADP-ribosylation factor machinery mediates endocytosis in plant cells [PDF]

Proceedings of the National Academy of Sciences, 2010
Endocytosis is crucial for various cellular functions and development of multicellular organisms. In mammals and yeast, ADP-ribosylation factor (ARF) GTPases, key components of vesicle formation, and their regulators ARF-guanine nucleotide exchange factors (GEFs) and ARF-GTPase-activating protein (GAPs) mediate endocytosis.
Stéphanie Robert, Tomasz Paciorek, Jürgen Kleine-Vehn, Jiří Friml, Masaru Fujimoto, Marc Van Montagu, Satoshi Naramoto, Takashi Ueda, Hiroo Fukuda, Akihiko Nakano, Tomoko Dainobu   +10 more
openaire   +3 more sources