World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
57
Citations
9614
World Ranking
14034
National Ranking
5921

Research.com Recognitions

  • 2018 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Iris Lindberg is affiliated with the University of Maryland, Baltimore, in the United States. Their research contributions span several key areas within biochemistry, genetics, molecular biology, and medicine, focusing primarily on molecular biology, cell biology, surgery, neurology, and physiology.

The scholar's work frequently addresses topics such as endoplasmic reticulum stress and disease, pancreatic function and diabetes, Alzheimer's disease research and treatments, Parkinson's disease mechanisms and treatments, diabetes and associated disorders, S100 proteins and annexins, and cellular transport and secretion.

Recent papers authored or coauthored by Iris Lindberg include:

  • A comprehensive systematic review of CSF proteins and peptides that define Alzheimer's disease, 2020, Clinical Proteomics
  • Secreted Chaperones in Neurodegeneration, 2020, Frontiers in Aging Neuroscience
  • Obesity, POMC, and POMC-processing Enzymes: Surprising Results From Animal Models, 2021, Endocrinology
  • Mouse Models of Human Proprotein Convertase Insufficiency, 2020, Endocrine Reviews
  • Increased expression and retention of the secretory chaperone proSAAS following cell stress, 2020, Cell Stress and Chaperones

Frequent coauthors collaborating with Lindberg include:

  • Timothy S. Jarvela
  • Peter Arvan
  • Manita Shakya
  • Kriti Chaplot
  • Hitoshi Iida

Key venues where Lindberg's research has been published multiple times include bioRxiv (Cold Spring Harbor Laboratory), Endocrinology, Diabetes, Cell Stress and Chaperones, and PLoS ONE.

Lindberg has been recognized as a Fellow of the American Association for the Advancement of Science (AAAS), an honor received in 2018.

Best Publications

  • Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects

    Xiaorong Zhu;An Zhou;Arunangsu Dey;Christina Norrbom

  • The crystal structure of the proprotein processing proteinase furin explains its stringent specificity.

    Stefan Henrich;Angus Cameron;Angus Cameron;Gleb P Bourenkov;Reiner Kiefersauer

  • Polyarginines Are Potent Furin Inhibitors

    Angus Cameron;Jon Appel;Richard A. Houghten;Iris Lindberg

  • The neuroendocrine protein 7B2 is required for peptide hormone processing in vivo and provides a novel mechanism for pituitary Cushing's disease.

    Christoph H Westphal;Laurent Muller;An Zhou;Xiaorong Zhu

  • Purification and characterization of the prohormone convertase PC1(PC3).

    Yi Zhou;I. Lindberg

  • Prodynorphin Processing by Proprotein Convertase 2 CLEAVAGE AT SINGLE BASIC RESIDUES AND ENHANCED PROCESSING IN THE PRESENCE OF CARBOXYPEPTIDASE ACTIVITY

    Robert Day;Claude Lazure;Ajoy Basak;Alain Boudreault

  • Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity.

    Stefan Henrich;Iris Lindberg;Wolfram Bode;Manuel E. Than

  • 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity.

    Xiaorong Zhu;Iris Lindberg

  • The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2

    Gerard J. M. Martens;Joanna A. M. Braks;Douglas W. Eib;Yi Zhou

  • Differential processing of proenkephalin by prohormone convertases 1(3) and 2 and furin.

    M B Breslin;I Lindberg;S Benjannet;J P Mathis

  • The cell biology of the prohormone convertases PC1 and PC2.

    Laurent Muller;I Lindberg

  • Congenital proprotein convertase 1/3 deficiency causes malabsorptive diarrhea and other endocrinopathies in a pediatric cohort

    Martín G. Martín;Iris Lindberg;R. Sergio Solorzano–Vargas;Jiafang Wang

  • Biosynthesis of the prohormone convertase mPC1 in AtT-20 cells.

    Osvaldo Vindrola;Iris Lindberg

  • Inhibition of furin by polyarginine-containing peptides: nanomolar inhibition by nona-D-arginine

    Magdalena M. Kacprzak;Juan R. Peinado;Manuel E. Than;Jon Appel

  • Potent inhibitors of furin and furin-like proprotein convertases containing decarboxylated P1 arginine mimetics.

    Gero L. Becker;Frank Sielaff;Manuel E. Than;Iris Lindberg

  • Specificity of Prohormone Convertase 2 on Proenkephalin and Proenkephalin-related Substrates

    Karla Johanning;Maria A. Juliano;Luiz Juliano;Claude Lazure

  • The Furin Inhibitor Hexa-d-Arginine Blocks the Activation of Pseudomonas aeruginosa Exotoxin A In Vivo

    Miroslav S. Sarac;Angus Cameron;Iris Lindberg

  • Highly potent inhibitors of proprotein convertase furin as potential drugs for treatment of infectious diseases

    Gero L. Becker;Yinghui Lu;Kornelia Hardes;Boris Strehlow

  • Mechanism of the Facilitation of PC2 Maturation by 7B2: Involvement in ProPC2 Transport and Activation but Not Folding

    Laurent Muller;Xiaorong Zhu;Iris Lindberg

  • Internal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: A potential mechanism for its inactivation

    X Zhu;Y Rouille;N S Lamango;D F Steiner

Frequent Co-Authors

Robert Day
Robert Day Université de Sherbrooke
Luiz Juliano
Luiz Juliano Federal University of Sao Paulo
Donald F. Steiner
Donald F. Steiner University of Chicago
Maria A. Juliano
Maria A. Juliano Federal University of Sao Paulo
Claude Lazure
Claude Lazure University of Montreal
Richard A. Houghten
Richard A. Houghten Florida International University
Gerard J. M. Martens
Gerard J. M. Martens Radboud University
Kirsten Sandvig
Kirsten Sandvig Oslo University Hospital
John E. Pintar
John E. Pintar Rutgers, The State University of New Jersey
Wolfgang Garten
Wolfgang Garten Philipp University of Marburg

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