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Microbiology

D-Index
87
Citations
27402
World Ranking
796
National Ranking
367

Overview

Eric O. Freed is affiliated with the National Institutes of Health in the United States. Their research primarily focuses on infectious diseases, virology, and molecular biology, with a substantial body of work in medicine and immunology and microbiology.

The scientist's research topics include:

  • HIV Research and Treatment
  • HIV/AIDS drug development and treatment
  • Cytomegalovirus and herpesvirus research
  • HIV/AIDS Research and Interventions
  • Bacteriophages and microbial interactions
  • Interferon and immune responses
  • SARS-CoV-2 and COVID-19 Research

Eric O. Freed has contributed to the literature notably in several well-known publication venues, including:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Viruses
  • mBio
  • Science Advances
  • Proceedings of the National Academy of Sciences

Frequent coauthors who have collaborated extensively with this researcher are:

  • Alex B. Kleinpeter
  • Sherimay D. Ablan
  • Yuta Hikichi
  • Abdül Waheed
  • Peijun Zhang

Some recent papers include:

  • HIV-1 Maturation: Lessons Learned from Inhibitors, 2020, Viruses
  • A stable immature lattice packages IP 6 for HIV capsid maturation, 2021, Science Advances
  • PSGL-1 restricts HIV-1 infectivity by blocking virus particle attachment to target cells, 2020, Proceedings of the National Academy of Sciences
  • S-acylation of SARS-CoV-2 spike protein: Mechanistic dissection, in vitro reconstitution and role in viral infectivity, 2021, Journal of Biological Chemistry
  • HIV-1 is dependent on its immature lattice to recruit IP6 for mature capsid assembly, 2023, Nature Structural & Molecular Biology

Best Publications

  • HIV-1 gag proteins: diverse functions in the virus life cycle.

    Eric O. Freed

  • Plasma membrane rafts play a critical role in HIV-1 assembly and release

    Akira Ono;Eric O. Freed

  • HIV sequence compendium 2002

    Carla Kuiken;Brian Foley;Eric Freed;Beatrice Hahn

  • HIV-1 assembly, release and maturation

    Eric O. Freed

  • HIV-1 replication.

    Eric O. Freed

  • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane.

    Akira Ono;Sherimay D. Ablan;Stephen J. Lockett;Kunio Nagashima

  • HIV-1 Envelope Glycoprotein Biosynthesis, Trafficking, and Incorporation

    Mary Ann Checkley;Benjamin G. Luttge;Eric O. Freed

  • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease.

    Mingjun Huang;J. M. Orenstein;M. A. Martin;E. O. Freed

  • Viral Late Domains

    Eric O. Freed

  • PA-457: A potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing

    F. Li;R. Goila-Gaur;K. Salzwedel;N. R. Kilgore

  • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41.

    Eric O. Freed;Dawn J. Myers;Rex Risser

  • Retrovirus budding.

    Unknown

  • DOMAINS OF THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX AND GP41 CYTOPLASMIC TAIL REQUIRED FOR ENVELOPE INCORPORATION INTO VIRIONS

    E O Freed;M A Martin

  • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function

    Dimiter G. Demirov;Akira Ono;Jan M. Orenstein;Eric O. Freed

  • Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix.

    E O Freed;M A Martin

  • Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection.

    E O Freed;G Englund;M A Martin

  • The Role of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in Virus Infection

    Eric O. Freed;Malcolm A. Martin

  • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production.

    E O Freed;J M Orenstein;A J Buckler-White;M A Martin

  • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity.

    Eric O. Freed;Eric L. Delwart;Gary L. Buchschacher;Antonito T. Panganiban

  • Binding of Human Immunodeficiency Virus Type 1 Gag to Membrane: Role of the Matrix Amino Terminus

    Akira Ono;Eric O. Freed

  • Cell-Type-Dependent Targeting of Human Immunodeficiency Virus Type 1 Assembly to the Plasma Membrane and the Multivesicular Body

    Akira Ono;Eric O. Freed

Frequent Co-Authors

Kunio Nagashima
Kunio Nagashima National Institutes of Health
Michael F. Summers
Michael F. Summers University of Maryland, Baltimore County
Abdul Waheed
Abdul Waheed Saint Louis University
Feng Li
Feng Li Shandong University
Jan M. Orenstein
Jan M. Orenstein George Washington University
Robert J. Fisher
Robert J. Fisher Science Applications International Corporation (United States)
Alasdair C. Steven
Alasdair C. Steven National Institutes of Health
Juan S. Bonifacino
Juan S. Bonifacino National Institutes of Health
Shan-Lu Liu
Shan-Lu Liu The Ohio State University
Vinay K. Pathak
Vinay K. Pathak National Institutes of Health

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