World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
71
Citations
17086
World Ranking
6692
National Ranking
3110

Overview

Robert Blumenthal is affiliated with the National Institutes of Health in the United States. Their career centers on scientific research within this prominent government institution.

While comprehensive details on publications, specific research fields, and co-authors are not provided, Blumenthal's position at the NIH suggests involvement in biomedical or health-related research. The NIH is well-known for supporting diverse scientific investigations ranging from molecular biology and genetics to public health and clinical studies.

There is no listed record of recent papers or frequent publication venues attributed to Blumenthal in the available data. Likewise, no book publications or awards have been documented. However, the NIH affiliation typically signifies engagement in collaborative projects and multidisciplinary research endeavors.

The absence of information on main fields of study, subfields, or research topics precludes detailing specific areas of scientific focus. Nonetheless, working at a national research institution implies exposure to cutting-edge studies and potential contributions to advancing knowledge in the biomedical sciences.

Given the limited data, no further elaboration on collaborative networks or citation impact can be made. The profile reflects the current scope of publicly available information on Robert Blumenthal's academic and research activities.

Best Publications

  • Design of liposomes for enhanced local release of drugs by hyperthermia

    Milton B. Yatvin;John N. Weinstein;Warren H. Dennis;Robert Blumenthal

  • Liposome-Cell Interaction: Transfer and Intracellular Release of a Trapped Fluorescent Marker

    J. N. Weinstein;S. Yoshikami;P. Henkart;R. Blumenthal

  • Membrane asymmetry in epithelia: is the tight junction a barrier to diffusion in the plasma membrane?

    Paul R. Dragsten;Paul R. Dragsten;Robert Blumenthal;Joseph S. Handler

  • The structure of human beta-defensin-2 shows evidence of higher order oligomerization.

    David M. Hoover;Kanaghalagatta R. Rajashankar;Kanaghalagatta R. Rajashankar;Robert Blumenthal;Anu Puri

  • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41.

    Isabel Muñoz-Barroso;Stewart Durell;Kazuyasu Sakaguchi;Ettore Appella

  • Human beta-defensins suppress human immunodeficiency virus infection: potential role in mucosal protection.

    Lingling Sun;Catherine M. Finnegan;Tina Kish-Catalone;Robert Blumenthal

  • Carboxyfluorescein as a probe for liposome-cell interactions effect of impurities, and purification of the dye

    Evelyn Ralston;Leonard M. Hjelmeland;Richard D. Klausner;John N. Weinstein

  • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (Review)

    Stewart R. Durell;Isabelle Martin;Jean-Marie Ruysschaert;Yechiel Shai

  • Conformational Changes in Cell Surface HIV-1 Envelope Glycoproteins Are Triggered by Cooperation between Cell Surface CD4 and Co-receptors

    Philip L. St. J. Jones;Thomas Korte;Robert Blumenthal

  • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events.

    R Blumenthal;D P Sarkar;S Durell;D E Howard

  • HIV Entry and Envelope Glycoprotein-mediated Fusion

    Robert Blumenthal;Stewart Durell;Mathias Viard

  • Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage.

    Yossef Kliger;Stephen A. Gallo;Sergio G. Peisajovich;Isabel Muñoz-Barroso

  • Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell Fusion. Structure-function study.

    Yossef Kliger;Amir Aharoni;Doron Rapaport;Philip Jones

  • The block to HIV-1 envelope glycoprotein-mediated membrane fusion in animal cells expressing human CD4 can be overcome by a human cell component(s).

    Christopher C. Broder;Dimiter S. Dimitrov;Robert Blumenthal;Edward A. Berger

  • Phase transition release, a new approach to the interaction of proteins with lipid vesicles. Application to lipoproteins.

    John N. Weinstein;Richard D. Klausner;Thomas Innerarity;Evelyn Ralston

  • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process.

    Stephen A. Gallo;and Anu Puri;Robert Blumenthal

  • Light-sensitive lipid-based nanoparticles for drug delivery: design principles and future considerations for biological applications

    Amichai Yavlovich;Brandon Smith;Kshitij Gupta;Robert Blumenthal

  • Anticancer β-Hairpin Peptides: Membrane-Induced Folding Triggers Activity

    Chomdao Sinthuvanich;Ana Salomé Veiga;Kshitij Gupta;Diana Gaspar

  • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion.

    J Zimmerberg;R Blumenthal;D P Sarkar;M Curran

  • Regulation of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Fusion by a Membrane-Interactive Domain in the gp41 Cytoplasmic Tail

    Stéphanie Wyss;Antony S. Dimitrov;Frédéric Baribaud;Terri G. Edwards

Frequent Co-Authors

John N. Weinstein
John N. Weinstein The University of Texas MD Anderson Cancer Center
Pierre A. Henkart
Pierre A. Henkart National Institutes of Health
Yechiel Shai
Yechiel Shai Weizmann Institute of Science
Dimiter S. Dimitrov
Dimiter S. Dimitrov University of Pittsburgh
Andreas Herrmann
Andreas Herrmann Humboldt-Universität zu Berlin
Susan O. Sharrow
Susan O. Sharrow National Institutes of Health
Abraham Loyter
Abraham Loyter Hebrew University of Jerusalem
Timothy D. Veenstra
Timothy D. Veenstra Lake Erie College of Osteopathic Medicine
Joshua Zimmerberg
Joshua Zimmerberg National Institutes of Health

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