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Biology and Biochemistry

D-Index
57
Citations
10506
World Ranking
13952
National Ranking
5894

Overview

Paul A. Randazzo is affiliated with the National Institutes of Health in the United States. Their research spans several topics and fields within biochemistry and molecular biology, with a significant focus on cell biology and immunology. The primary areas of study include cellular transport and secretion, sarcoma diagnosis and treatment, protein kinase regulation and GTPase signaling, lipid membrane structure and behavior, cell adhesion molecules research, cellular mechanics and interactions, and retinal diseases and treatments.

Randazzo's contributions are documented in multiple research papers published in recognized scientific journals. Notable recent publications include:

  • "CIB2 regulates mTORC1 signaling and is essential for autophagy and visual function," 2021, Nature Communications
  • "Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1," 2020, Science Advances
  • "Control of cell signaling by Arf GTPases and their regulators: Focus on links to cancer and other GTPase families," 2021, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
  • "Rigosertib Induces Mitotic Arrest and Apoptosis in RAS-Mutated Rhabdomyosarcoma and Neuroblastoma," 2020, Molecular Cancer Therapeutics
  • "Small GTPase ARF6 Is a Coincidence-Detection Code for RPH3A Polarization in Neutrophil Polarization," 2020, The Journal of Immunology

Their frequent collaborators appear across a spectrum of research areas, enhancing the interdisciplinary nature of the work. Frequent co-authors include Xiaoying Jian, Olivier Soubias, Eric Rosenberg, R. Andrew Byrd, and Rebekah Jackson.

Randazzo has contributed extensively to scientific journals known for publishing research in biophysics and molecular biology. The most common publication venues for their work include:

  • Biophysical Journal
  • Journal of Biological Chemistry
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Cancer Research

The body of their research fits predominantly within the broad fields of Biochemistry, Genetics and Molecular Biology as well as Medicine. Within these, the subfields of Molecular Biology, Cell Biology, Immunology, Pulmonary and Respiratory Medicine, and Physiology feature prominently. This cross-disciplinary presence indicates a breadth of research interest with a special emphasis on signaling pathways, cellular mechanisms, and disease-related cellular functions.

Best Publications

  • The GGAs Promote ARF-Dependent Recruitment of Clathrin to the TGN

    Rosa Puertollano;Paul A Randazzo;John F Presley;Lisa M Hartnell

  • 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

  • Arf and its many interactors

    Zhongzhen Nie;Dianne S Hirsch;Paul A Randazzo

  • 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

  • The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton.

    Paul A. Randazzo;Josefa Andrade;Koichi Miura;Megan T. Brown

  • Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4.

    Jana Mazelova;Lisa Astuto-Gribble;Hiroki Inoue;Beatrice M Tam

  • Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling

    Paul A Randazzo;Dianne S Hirsch

  • 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

  • ARAP1: a point of convergence for Arf and Rho signaling.

    Koichi Miura;Kerry M. Jacques;Stacey Stauffer;Atsutaka Kubosaki

  • Identification of a New Pyk2 Target Protein with Arf-GAP Activity

    J Andreev;J P Simon;D D Sabatini;J Kam

  • Acaps Are Arf6 Gtpase-Activating Proteins That Function in the Cell Periphery

    Trevor R. Jackson;Fraser D. Brown;Zhongzhen Nie;Koichi Miura

  • ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat

    Jia-Shu Yang;Stella Y. Lee;Minggeng Gao;Sylvain Bourgoin

  • Arf GAPs and their interacting proteins.

    Hiroki Inoue;Paul A. Randazzo

  • Arf GAPs and membrane traffic.

    Zhongzhen Nie;Paul A. Randazzo

  • Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes.

    P. A. Randazzo;Yun Chung Yang;C. Rulka;R. A. Kahn

  • Semaphorin 3E Initiates Antiangiogenic Signaling through Plexin D1 by Regulating Arf6 and R-Ras

    Atsuko Sakurai;Julie Gavard;Yuliya Annas-Linhares;John R. Basile

  • The Myristoylated Amino Terminus of ADP-ribosylation Factor 1 Is a Phospholipid- and GTP-sensitive Switch

    Paul A. Randazzo;Takeshi Terui;Stacey Sturch;Henry M. Fales

  • Consensus nomenclature for the human ArfGAP domain-containing proteins

    Richard A. Kahn;Elspeth Bruford;Hiroki Inoue;John M. Logsdon

  • Small-molecule synergist of the Wnt/β-catenin signaling pathway

    Qisheng Zhang;Michael B. Major;Shinichi Takanashi;Nathan D. Camp

  • ARF GTPases and their GEFs and GAPs: concepts and challenges

    Elizabeth Sztul;Pei Wen Chen;James E. Casanova;Jacqueline Cherfils

Frequent Co-Authors

Richard A. Kahn
Richard A. Kahn Emory University
John K. Northup
John K. Northup National Institutes of Health
Elizabeth Sztul
Elizabeth Sztul University of Alabama at Birmingham
Richard T. Premont
Richard T. Premont University Hospitals of Cleveland
Mathias Lösche
Mathias Lösche Carnegie Mellon University
Henry M. Fales
Henry M. Fales National Institutes of Health
Victor W. Hsu
Victor W. Hsu Brigham and Women's Hospital
Peter P. Roller
Peter P. Roller National Institutes of Health
J. Silvio Gutkind
J. Silvio Gutkind University of California, San Diego
Juan S. Bonifacino
Juan S. Bonifacino National Institutes of Health

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