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Search results 101 to 116 out of 116 for Gbf1

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0.019s

Type

Details

Score

Publication

25008939 | J:214631

First Author:	Ford Siltz LA
Year:	2014
Journal:	J Virol
Title:	New small-molecule inhibitors effectively blocking picornavirus replication.
Volume:	88
Issue:	19
Pages:	11091-107

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Publication

11950392 | -

First Author:	Takatsu H
Year:	2002
Journal:	Biochem J
Title:	GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.
Volume:	365
Issue:	Pt 2
Pages:	369-78

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Publication

15979507 | -

First Author:	Donaldson JG
Year:	2005
Journal:	Biochim Biophys Acta
Title:	Multiple activities for Arf1 at the Golgi complex.
Volume:	1744
Issue:	3
Pages:	364-73

•

Publication

15728366 | -

First Author:	Deretic D
Year:	2005
Journal:	Proc Natl Acad Sci U S A
Title:	Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4).
Volume:	102
Issue:	9
Pages:	3301-6

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Publication

16030262 | -

First Author:	Volpicelli-Daley LA
Year:	2005
Journal:	Mol Biol Cell
Title:	Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic.
Volume:	16
Issue:	10
Pages:	4495-508

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Publication

12446727 | -

First Author:	Kim SW
Year:	2003
Journal:	J Biol Chem
Title:	ADP-ribosylation factor 4 small GTPase mediates epidermal growth factor receptor-dependent phospholipase D2 activation.
Volume:	278
Issue:	4
Pages:	2661-8

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Protein Domain

IPR045872 | Arf1-5-like

Type:

Family

Description:

Arf GTPases are involved in the formation of coated carrier vesicles by recruiting coat proteins. This entry includes Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned []. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins []. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor []. Arf4 has also been shown to recognise the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialised post-Golgi rhodopsin transport carriers (RTCs) []. There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs) [].

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Protein

P61750

Organism:	Mus musculus/domesticus
Length:	180
Fragment?:	false

•

Protein

P84084

Organism:	Mus musculus/domesticus
Length:	180
Fragment?:	false

•

Protein

Q8BSL7

Organism:	Mus musculus/domesticus
Length:	181
Fragment?:	false

•

Protein

P61205

Organism:	Mus musculus/domesticus
Length:	181
Fragment?:	false

•

Protein

P84078

Organism:	Mus musculus/domesticus
Length:	181
Fragment?:	false

•

Protein

Q9DD04

Organism:	Mus musculus/domesticus
Length:	181
Fragment?:	false

•

Protein

Q3U344

Organism:	Mus musculus/domesticus
Length:	181
Fragment?:	false

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Protein

Q14BR4

Organism:	Mus musculus/domesticus
Length:	180
Fragment?:	false

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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