Results 161 to 170 of about 7,868 (194)

Whole genome sequence meta-analyses reveal common and rare genetic associations with critical COVID-19

Kousathanas A, Rawlik K, Pairo-Castineira E, Griffiths F, Oosthuyzen W, Hendry SC, Malinauskas T, Butler-Laporte G, Arumugam P, Begg C, Chadeau-Hyam M, Chan G, Cooke G, Donovan S, Elgar G, Fowler TA, Goddard P, Hinds C, Horby P, Ling L, Magavern EF, Maleady-Crowe F, Montgomery H, Odhams CA, Openshaw PJ, Patch C, Rendon A, Salehi S, Scott RH, Semple MG, Shankar-Hari M, Siddiq A, Stuckey A, Summers C, Todd L, Walker S, Walsh T, Ward H, Zainy T, GenOMICC Investigators, ISARIC4C Investigators, BQC19 Investigators, GENCOVID Investigators, DeCOI Investigators, POLCOVID Investigators, PMBB Investigators, Fawkes A, Murphy L, Law A, Vitart V, Chinnery PF, Wilson JF, Brown MA, Elliott P, Moutsianas L, Caulfield MJ, Baillie JK.   +56 more
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ARF1 and SAR1 GTPases in Endomembrane Trafficking in Plants [PDF]

International Journal of Molecular Sciences, 2013
Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics.
Birsen Cevher-Keskin
exaly   +5 more sources

Structural basis for activation of Arf1 at the Golgi complex

Cell Reports, 2022
Summary The Golgi complex is the central sorting station of the eukaryotic secretory pathway. Traffic through the Golgi requires activation of Arf GTPases that orchestrate cargo sorting and vesicle formation by recruiting an array of effector proteins.
J Christopher Fromme
exaly   +3 more sources

The p24 Complex Contributes to Specify Arf1 for COPI Coat Selection [PDF]

International Journal of Molecular Sciences, 2021
Golgi trafficking depends on the small GTPase Arf1 which, upon activation, drives the assembly of different coats onto budding vesicles. Two related types of guanine nucleotide exchange factors (GEFs) activate Arf1 at different Golgi sites.
Susana Sabido-Bozo, Javier Manzano-Lopez, Sofia Rodriguez-Gallardo   +2 more
exaly   +3 more sources

Multiple activities for Arf1 at the Golgi complex

Biochimica Et Biophysica Acta - Molecular Cell Research, 2005
The Arf family of GTPases regulates membrane traffic and organelle structure. At the Golgi complex, Arf proteins facilitate membrane recruitment of many cytoplasmic coat proteins to allow sorting of membrane proteins for transport, stimulate the activity of enzymes that modulate the lipid composition of the Golgi, and assemble a cytoskeletal scaffold ...
Julie G Donaldson, Roberto Weigert
exaly   +3 more sources

Dissection of COPI and Arf1 dynamics in vivo and role in Golgi membrane transport

Nature, 2002
Cytosolic coat proteins that bind reversibly to membranes have a central function in membrane transport within the secretory pathway. One well-studied example is COPI or coatomer, a heptameric protein complex that is recruited to membranes by the GTP ...
John F Presley, Theresa H Ward, Eric D Siggia   +2 more
exaly   +2 more sources

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Preparation of Myristoylated Arf1 and Arf6

2005
Arf proteins are members of the Arf family of small Ras-like GTP binding proteins. Six Arfs, grouped into three classes, have been identified in mammalian cells and three members have been identified in yeasts. Arf1 and Arf6, more extensively studied than other Arfs, have been found to affect membrane traffic and actin remodeling.
Vi Luan, Ha, Geraint M H, Thomas, Stacey, Stauffer, Paul A, Randazzo   +3 more
openaire   +2 more sources

Integrating Three Views of Arf1 Activation Dynamics

Journal of Molecular Biology, 2004
The proteins Arno and Gea2 of the Sec7 family can promote GDP-GTP exchange on Arf1, a small GTP-binding protein, which coordinates coated vesicle formation for protein transport within the cell. Crystal structures of the essential Sec7 domain (Sec7d) of Gea2 in the free and Arf1-bound forms suggest that conformational dynamics of the Sec7d as well as ...
Charles H Robert, Jacqueline Cherfils, Liliane Mouawad   +2 more
exaly   +3 more sources

Arf1

1995
Abstract Bovine ARF1 was cloned by screening a bovine adrenal chromaffin cDNA library with an oligonucleotide probe, derived from partial protein sequencing of purified bovine brain ARF (Sewell and Kahn 1988; accession number J03275).
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In Vitro Assays of Arf1 Interaction with GGA Proteins

2005
ADP-ribosylation factor 1 (Arf1) is a GTP-binding protein that regulates membrane traffic. This function of Arf1 is, at least in part, mediated by Arf1 x GTP binding to coat proteins such as coatomer, clathrin adaptor protein (AP) complexes 1 and 3, and gamma-adaptin homology-Golgi associated Arf-binding (GGA) proteins.
Hye-Young, Yoon, Juan S, Bonifacino, Paul A, Randazzo   +2 more
openaire   +2 more sources