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Consensus nomenclature for the human ArfGAP domain-containing proteins.

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Date
2008-09-22
Authors
Kahn, Richard A
Bruford, Elspeth
Inoue, Hiroki
Logsdon, John M
Nie, Zhongzhen
Premont, Richard T
Randazzo, Paul A
Satake, Masanobu
Theibert, Anne B
Zapp, Maria L
Cassel, Dan
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Abstract
At the FASEB summer research conference on "Arf Family GTPases", held in Il Ciocco, Italy in June, 2007, it became evident to researchers that our understanding of the family of Arf GTPase activating proteins (ArfGAPs) has grown exponentially in recent years. A common nomenclature for these genes and proteins will facilitate discovery of biological functions and possible connections to pathogenesis. Nearly 100 researchers were contacted to generate a consensus nomenclature for human ArfGAPs. This article describes the resulting consensus nomenclature and provides a brief description of each of the 10 subfamilies of 31 human genes encoding proteins containing the ArfGAP domain.
Type
Journal article
Subject
ADP-Ribosylation Factors
Adaptor Proteins, Signal Transducing
Animals
Cell Cycle Proteins
Cytoskeletal Proteins
GTPase-Activating Proteins
Humans
Microtubule-Associated Proteins
Models, Molecular
Molecular Sequence Data
Multigene Family
Protein Conformation
Terminology as Topic
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https://hdl.handle.net/10161/10774
Published Version (Please cite this version)
10.1083/jcb.200806041
Publication Info
Kahn, Richard A; Bruford, Elspeth; Inoue, Hiroki; Logsdon, John M; Nie, Zhongzhen; Premont, Richard T; ... Cassel, Dan (2008). Consensus nomenclature for the human ArfGAP domain-containing proteins. J Cell Biol, 182(6). pp. 1039-1044. 10.1083/jcb.200806041. Retrieved from https://hdl.handle.net/10161/10774.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
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Scholars@Duke

Premont

Richard Thomas Premont

Associate Professor in Medicine
Critical physiological events throughout the body are controlled by extracellular signals from neurotransmitters and hormones acting on cell surface receptors. Receptors transduce these signals to alter intracellular metabolism and cellular responsiveness through heterotrimeric G protein/second messenger pathways or through small GTP-binding protein/protein kinase cascades. The mechanisms that control the responsiveness of target organ G protein-coupled receptors include receptor ph
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