His scientific interests lie mostly in Cell biology, ADP ribosylation factor, GTPase-activating protein, Actin cytoskeleton and Biochemistry. As part of his studies on Cell biology, he often connects relevant areas like Cytoskeleton. His ADP ribosylation factor research integrates issues from Phospholipase D and GTP'.
The various areas that Paul A. Randazzo examines in his GTPase-activating protein study include COP-Coated Vesicles and Vesicle. His Actin cytoskeleton research includes elements of Guanine nucleotide exchange factor, Conformational change and Pleckstrin homology domain. His biological study spans a wide range of topics, including Binding protein and Filopodia.
His primary scientific interests are in Cell biology, ADP ribosylation factor, Biochemistry, GTPase-activating protein and GTP'. In his study, Actin is inextricably linked to Actin cytoskeleton, which falls within the broad field of Cell biology. His ADP ribosylation factor study combines topics from a wide range of disciplines, such as Actin remodeling, Phospholipase D, Vesicle, Guanine nucleotide exchange factor and Endocytic cycle.
His GTPase-activating protein study combines topics from a wide range of disciplines, such as Plasma protein binding, Signal transducing adaptor protein and Endosome. He interconnects Mutant and Effector in the investigation of issues within GTP'. His Golgi apparatus research is multidisciplinary, incorporating perspectives in Transport protein and G protein.
Paul A. Randazzo mostly deals with Biophysics, Pleckstrin homology domain, Cell biology, Small GTPase and Integrin. His Biophysics research integrates issues from Membrane surface, Membrane, GTPase, Actin remodeling and SH3 domain. His research in GTPase focuses on subjects like GTP', which are connected to Guanosine.
His studies examine the connections between SH3 domain and genetics, as well as such issues in Actin cytoskeleton, with regards to ADP ribosylation factor, Phosphatidylinositol, Microtubule, Motor protein and Filamentous actin. His studies in Pleckstrin homology domain integrate themes in fields like Protein kinase B, Cooperative binding, GTPase-activating protein and Stereochemistry. His Cell biology study frequently links to related topics such as Cytoskeleton.
Paul A. Randazzo spends much of his time researching Cell biology, GTPase-activating protein, Focal adhesion, Pleckstrin homology domain and Biochemistry. Paul A. Randazzo has researched Cell biology in several fields, including BAR domain, Gene knockdown and Cytoskeleton. Paul A. Randazzo combines subjects such as Golgi apparatus, Heterotrimeric G protein, G protein-coupled receptor and Signal transducing adaptor protein with his study of GTPase-activating protein.
His Pleckstrin homology domain study deals with Cooperative binding intersecting with Phospholipid Binding, Phospholipid, Vesicle and A-site. His study brings together the fields of Biophysics and Biochemistry. His Collagen receptor research is multidisciplinary, incorporating elements of Guanine nucleotide exchange factor and ADP ribosylation factor.
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The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport.
R A Kahn;P Randazzo;T Serafini;O Weiss.
Journal of Biological Chemistry (1992)
Arf and Its Many Interactors
Zhongzhen Nie;Dianne S Hirsch;Paul A Randazzo.
Current Opinion in Cell Biology (2003)
The GGAs Promote ARF-Dependent Recruitment of Clathrin to the TGN
Rosa Puertollano;Paul A Randazzo;John F Presley;Lisa M Hartnell.
Cell (2001)
Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4
Jana Mazelova;Lisa Astuto-Gribble;Hiroki Inoue;Beatrice M Tam.
The EMBO Journal (2009)
ASAP1, a Phospholipid-Dependent Arf GTPase-Activating Protein That Associates with and Is Phosphorylated by Src
Megan T. Brown;Josefa Andrade;Harish Radhakrishna;Julie G. Donaldson.
Molecular and Cellular Biology (1998)
The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton.
Paul A. Randazzo;Josefa Andrade;Koichi Miura;Megan T. Brown.
Proceedings of the National Academy of Sciences of the United States of America (2000)
GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids.
P A Randazzo;R A Kahn.
Journal of Biological Chemistry (1994)
Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling
Paul A Randazzo;Dianne S Hirsch.
Cellular Signalling (2004)
ARAP1: a point of convergence for Arf and Rho signaling.
Koichi Miura;Kerry M. Jacques;Stacey Stauffer;Atsutaka Kubosaki.
Molecular Cell (2002)
Acaps Are Arf6 Gtpase-Activating Proteins That Function in the Cell Periphery
Trevor R. Jackson;Fraser D. Brown;Zhongzhen Nie;Koichi Miura.
Journal of Cell Biology (2000)
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