Work

Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1

Year: 2020

Type: article

Abstract: The ASAP1 PH domain binds to PIP 2 membranes, experiences conformational shifts, and recognizes Arf1 to initiate GTPase activity.

Source: Science Advances

DOI: 10.1126/sciadv.abd1882

Authors: Olivier Soubias, Shashank Pant, Frank Heinrich, Yue Zhang, Neeladri Sekhar Roy, Jess Li, Xiaoying Jian, Marielle E. Yohe, Paul A. Randazzo, Mathias Lösche, Emad Tajkhorshid, R. Andrew Byrd

Institutions: National Cancer Institute, Center for Cancer Research, University of Illinois Urbana-Champaign, National Institute of Standards and Technology, NIST Center for Neutron Research, Carnegie Mellon University, National Institutes of Health

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $4,500

Funders: U.S. Department of Commerce, National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences

Awards: G1104241873, Regulation of ADP-ribosylation factor, G2968100984, Structural Biology of GTPase Activating Proteins, G8709252664, G9000010716, G9000016563, G9000041032, G9000123593

OpenAlex ID: W3091634827

FWCI: 2.28

Cites: 59

Cited by: 36

Related to: 10