World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
80
Citations
21662
World Ranking
4113
National Ranking
2020

Overview

Stuart McLaughlin is affiliated with Stony Brook University in the United States and has contributed to research primarily within the field of Biochemistry, Genetics and Molecular Biology. Their work spans topics such as RNA Research and Splicing, Genomics and Chromatin Dynamics, RNA and protein synthesis mechanisms, as well as COVID-19 Impact on Reproduction, Reproductive System and Pregnancy, and Reproductive Biology and Fertility.

Recent publications by McLaughlin include:

  • "Dual role for phosphoinositides in regulation of yeast and mammalian phospholipase D enzymes," 2020, UNC Libraries
  • "REFLECTIONS ON THE CHALLENGES OF HEADSHIP," 2023, The Buckingham Journal of Education
  • "Nucleotide GPT: Sequence-Based Deep Learning Prediction of Nuclear Subcompartment-Associated Genome Architecture," 2024, bioRxiv (Cold Spring Harbor Laboratory)
  • "Paternal SARS-CoV-2 infection impacts sperm small noncoding RNAs and increases anxiety in offspring in a sex-dependent manner," 2025, Nature Communications

McLaughlin's research has appeared in various venues, including:

  • UNC Libraries
  • The Buckingham Journal of Education
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications

Their frequent co-authors include:

  • Vicki A. Sciorra
  • Simon A. Rudge
  • Jiyao Wang
  • Jo Anne Engebrecht
  • Andrew J. Morris

McLaughlin's work engages multidisciplinary subfields such as Molecular Biology, Obstetrics and Gynecology, Immunology, and Public Health, Environmental and Occupational Health. This broad scope reflects an integrated approach to molecular and reproductive biology with implications for health sciences.

Best Publications

  • The electrostatic properties of membranes.

    Stuart McLaughlin

  • Plasma membrane phosphoinositide organization by protein electrostatics

    Stuart McLaughlin;Diana Murray

  • PIP2 and Proteins: Interactions, Organization, and Information Flow

    Stuart McLaughlin;Jiyao Wang;Alok Gambhir;Diana Murray

  • The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions

    Stuart McLaughlin;Alan Aderem

  • Adsorption of monovalent cations to bilayer membranes containing negative phospholipids.

    Moises Eisenberg;Thomas Gresalfi;Thomas Riccio;Stuart McLaughlin

  • Binding of acylated peptides and fatty acids to phospholipid vesicles : pertinence to myristoylated proteins

    Robert M. Peitzsch;Stuart McLaughlin

  • Adsorption of divalent cations to bilayer membranes containing phosphatidylserine

    S McLaughlin;N Mulrine;T Gresalfi;G Vaio

  • Transport of protons across membranes by weak acids.

    S G McLaughlin;J P Dilger

  • THE PLECKSTRIN HOMOLOGY DOMAIN OF PHOSPHOLIPASE C-DELTA 1 BINDS WITH HIGH AFFINITY TO PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE IN BILAYER MEMBRANES

    Pilar Garcia;Rakesh Gupta;Shefali Shah;Andrew J. Morris

  • Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results

    N. Ben-Tal;B. Honig;R.M. Peitzsch;G. Denisov

  • Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins.

    Alok Gambhir;Gyöngyi Hangyás-Mihályné;Irina Zaitseva;David S. Cafiso

  • Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids

    Catherine T. Sigal;Wenjun Zhou;Carolyn A. Buser;Stuart McLaughlin

  • Binding of peptides with basic residues to membranes containing acidic phospholipids

    Jiyun Kim;M. Mosior;L. A. Chung;Hui Wu

  • Binding of neomycin to phosphatidylinositol 4,5-biphosphate (PIP2)

    Eugene Gabev;John Kasianowicz;Tammy Abbott;Stuart McLaughlin

  • The adsorption of divalent cations to phosphatidylcholine bilayer membranes

    Alan McLaughlin;Christoph Grathwohl;Stuart McLaughlin

  • Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions.

    Jiyao Wang;Alok Gambhir;Gyöngyi Hangyás-Mihályné;Diana Murray

  • Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology

    Diana Murray;Nir Ben-Tal;Barry Honig;Stuart McLaughlin

  • Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results.

    G. Denisov;S. Wanaski;P. Luan;M. Glaser

  • Myristoylated Alanine-rich C Kinase Substrate (MARCKS) Produces Reversible Inhibition of Phospholipase C by Sequestering Phosphatidylinositol 4,5-Bisphosphate in Lateral Domains

    Michael Glaser;Stephen Wanaski;Carolyn A. Buser;Valentina Boguslavsky

  • Membrane curvature: how BAR domains bend bilayers.

    Joshua Zimmerberg;Stuart McLaughlin

Frequent Co-Authors

David S. Cafiso
David S. Cafiso University of Virginia
Andrew J. Morris
Andrew J. Morris University of Kentucky
Barry Honig
Barry Honig Columbia University
Wonpil Im
Wonpil Im Lehigh University
Richard W. Pastor
Richard W. Pastor National Institutes of Health
Nir Ben-Tal
Nir Ben-Tal Tel Aviv University
Alan Aderem
Alan Aderem Seattle Children's Hospital
Steven O. Smith
Steven O. Smith Stony Brook University
Roland Benz
Roland Benz Jacobs University
Joachim O. Rädler
Joachim O. Rädler Ludwig-Maximilians-Universität München

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