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Biology and Biochemistry

D-Index
78
Citations
20765
World Ranking
4563
National Ranking
2219

Overview

Louis B. Hersh is affiliated with the University of Kentucky in the United States and has contributed extensively to research in biochemistry, genetics, molecular biology, immunology, microbiology, and medicine. Their scientific work covers multiple interconnected disciplines, focusing notably on molecular biology and parasitology.

Their research spans a variety of topics, including:

  • Protein Tyrosine Phosphatases
  • Glycosylation and Glycoproteins Research
  • Galectins and Cancer Biology
  • Toxoplasma gondii Research Studies
  • Parasitic Infections and Diagnostics
  • Cytomegalovirus and Herpesvirus Research
  • Peptidase Inhibition and Analysis

Several frequent co-authors appear repeatedly in their work, highlighting collaborative efforts in various studies:

  • K. Martin Chow
  • Caroline N. Smith
  • Jessica S. Blackburn
  • Daniel Deredge
  • Eun Suk Song

Louis B. Hersh's publications have appeared in a range of scientific journals. The most frequent venues for their research include:

  • Cancer Research
  • bioRxiv (Cold Spring Harbor Laboratory)
  • PLoS ONE
  • mSphere
  • Communications Materials

A selection of recent papers demonstrates the breadth of their work:

  • Toxoplasma gondii Toxolysin 4 Contributes to Efficient Parasite Egress from Host Cells, 2021, mSphere
  • Aerosol capture and coronavirus spike protein deactivation by enzyme functionalized antiviral membranes, 2022, Communications Materials
  • Structure of puromycin-sensitive aminopeptidase and polyglutamine binding, 2023, PLoS ONE
  • Development and characterization of nanobodies that specifically target the oncogenic Phosphatase of Regenerating Liver-3 (PRL-3) and impact its interaction with a known binding partner, CNNM3, 2023, PLoS ONE
  • Abstract 672: Development and validation of nanobodies specific to the oncogenic phosphatase protein tyrosine phosphatase 4A3 (PTP4A3 or PRL-3), 2022, Cancer Research

Their research addresses specific biochemical mechanisms such as protein tyrosine phosphatases, along with infectious disease studies focused on parasitic organisms including Toxoplasma gondii. Additionally, work on nanobodies highlights a concentration on targeted molecular interactions in oncology and enzymology.

Best Publications

  • Environmental Enrichment Reduces Aβ Levels and Amyloid Deposition in Transgenic Mice

    Orly Lazarov;John Robinson;Ya Ping Tang;Ilana S. Hairston

  • Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation.

    Wei Qiao Qiu;Dominic M. Walsh;Zhen Ye;Konstantinos Vekrellis

  • Neprilysin Gene Transfer Reduces Human Amyloid Pathology in Transgenic Mice

    Robert A. Marr;Edward Rockenstein;Atish Mukherjee;Mark S. Kindy

  • Amyloid-β peptide levels in brain are inversely correlated with insulysin activity levels in vivo

    Bonnie C. Miller;Elizabeth A. Eckman;Kumar Sambamurti;Kumar Sambamurti;Nicole Dobbs

  • Human kidney "enkephalinase", a neutral metalloendopeptidase that cleaves active peptides.

    John T. Gafford;Randal A. Skidgel;Ervin G. Erdos;Louis B. Hersh

  • Preservation of nucleus basalis neurons containing choline acetyltransferase and the vesicular acetylcholine transporter in the elderly with mild cognitive impairment and early Alzheimer's disease.

    Michelle L. Gilmor;Jeffrey D. Erickson;Hélène Varoqui;Louis B. Hersh

  • Human reticular formation: Cholinergic neurons of the pedunculopontine and laterodorsal tegmental nuclei and some cytochemical comparisons to forebrain cholinergic neurons

    M. Marsel Mesulam;Changiz Geula;Mark A. Bothwell;Louis B. Hersh

  • Two new proteases in the MHC class I processing pathway

    Lars Stoltze;Markus Schirle;Gerold Schwarz;Christian Schröter

  • Effects of Estrogen Replacement on the Relative Levels of Choline Acetyltransferase, trkA, and Nerve Growth Factor Messenger RNAs in the Basal Forebrain and Hippocampal Formation of Adult Rats

    Robert B. Gibbs;Donghai Wu;Louis B. Hersh;Donald W. Pfaff

  • The hydrolysis of endothelins by neutral endopeptidase 24.11 (enkephalinase).

    J. Vijayaraghavan;A. G. Scicli;O. A. Carretero;Clive A. Slaughter

  • Puromycin-sensitive aminopeptidases

    Adriano Fontana;Daniel Beat Constam;Andreas Rudolf Tobler;Karl-Heinz Altmann

  • An atlas of the regional and laminar distribution of choline acetyltransferase immunoreactivity in rat cerebral cortex

    A. Lysakowski;B. H. Wainer;Gordon Bruce;L. B. Hersh

  • CD10/neutral endopeptidase 24.11 hydrolyzes bombesin-like peptides and regulates the growth of small cell carcinomas of the lung

    Margaret A. Shipp;George E. Tarr;Chang-Yan Chen;Stephanie N. Switzer

  • Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 (enkephalinase): direct evidence by cDNA transfection analysis

    Margaret A. Shipp;Jayanthi Vijayaraghavan;Emmett V. Schmidt;Emma L. Masteller

  • Nerve growth factor receptor immunoreactive profiles in the normal, aged human basal forebrain: Colocalization with cholinergic neurons

    Elliott J. Mufson;Mark Bothwell;Louis B. Hersh;Jeffrey H. Kordower

  • Heterogeneity and selectivity of the degeneration of cholinergic neurons in the basal forebrain of patients with Alzheimer's disease

    S Lehéricy;E C Hirsch;P Cervera-Piérot;L B Hersh

  • Differential cholinergic innervation within functional subdivisions of the human cerebral cortex: A choline acetyltransferase study

    M. ‐Marsel Mesulam;Louis B. Hersh;Deborah C. Mash;Changiz Geula

  • Immunoaffinity purification of human choline acetyltransferase: comparison of the brain and placental enzymes.

    Gordon Bruce;Bruce H. Wainer;Louis B. Hersh

  • Neprilysin regulates amyloid Beta peptide levels.

    Robert A. Marr;Hanjun Guan;Edward Rockenstein;Mark Kindy

  • Choline Acetyltransferase: Celebrating Its Fiftieth Year

    Donghai Wu;Louis B. Hersh

Frequent Co-Authors

Luiz Juliano
Luiz Juliano Federal University of Sao Paulo
Maria A. Juliano
Maria A. Juliano Federal University of Sao Paulo
Donghai Wu
Donghai Wu Cornell University
David M. Armstrong
David M. Armstrong National Institutes of Health
Fred H. Gage
Fred H. Gage Salk Institute for Biological Studies
Yves Agid
Yves Agid Institut du Cerveau
Clifford B. Saper
Clifford B. Saper Beth Israel Deaconess Medical Center
Etienne C. Hirsch
Etienne C. Hirsch Sorbonne University
Bruce H. Wainer
Bruce H. Wainer Emory University
Craig Gerard
Craig Gerard Boston Children's Hospital

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