World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
50
Citations
10656
World Ranking
17539
National Ranking
336

Overview

Eric G. Berger is affiliated with the University of Zurich in Switzerland. Their research primarily intersects the fields of Biochemistry, Genetics and Molecular Biology, and Medicine. Within these broad domains, Berger has focused extensively on subfields such as Molecular Biology, Physiology, Epidemiology, Biomedical Engineering, and Cancer Research.

Berger's scientific work addresses various topics, including:

  • Adipose Tissue and Metabolism
  • Adipokines, Inflammation, and Metabolic Diseases
  • Extracellular vesicles in disease
  • Metabolism, Diabetes, and Cancer
  • Lipid metabolism and disorders
  • Liver Disease Diagnosis and Treatment
  • Peroxisome Proliferator-Activated Receptors

Notable papers by Eric G. Berger include:

  • Use of Nanovesicles from Orange Juice to Reverse Diet-Induced Gut Modifications in Diet-Induced Obese Mice (2020) published in Molecular Therapy - Methods & Clinical Development
  • FABP4 Controls Fat Mass Expandability (Adipocyte Size and Number) through Inhibition of CD36/SR-B2 Signalling (2023) published in International Journal of Molecular Sciences
  • Insulin prevents fatty acid induced increase of adipocyte size (2022) published in Adipocyte

Frequent co-authors of Berger include:

  • Alain Géloën
  • Audrey Jalabert
  • Emmanuelle Meugnier
  • Sophie Rome
  • Jennifer Rieusset

Berger's publications have appeared in various scientific venues, highlighting a multidisciplinary research approach. These venues include:

  • Molecular Therapy - Methods & Clinical Development
  • International Journal of Molecular Sciences
  • Scientific Reports
  • Life
  • Adipocyte

Best Publications

  • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway.

    Jennifer Lippincott-Schwartz;Julie G. Donaldson;Anja Schweizer;Eric G. Berger

  • Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae.

    J Roth;E G Berger

  • Golgi-disturbing agents.

    André Dinter;E. G. Berger

  • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides.

    Catherine Rabouille;Norman Hui;Felicia Hunte;Regina Kieckbusch

  • Kin recognition between medial Golgi enzymes in HeLa cells.

    T Nilsson;M H Hoe;P Slusarewicz;C Rabouille

  • Structure, biosynthesis and functions of glycoprotein glycans

    Eric G. Berger;Eckhart Buddecke;Johannis P. Kamerling;Akira Kobata

  • Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway.

    John M Lucocq;Eric G. Berger;Graham Warren

  • The molecular and cell biology of glycosyltransferases

    Ralf Kleene;Eric G. Berger

  • Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae

    Alexander A. Mironov;Galina V. Beznoussenko;Paolo Nicoziani;Oliviano Martella

  • GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum

    Olivier Martinez;Claude Antony;Gérard Pehau-Arnaudet;Eric G. Berger

  • Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie

    Timo Imbach;Barbara Schenk;Els Schollen;Patricie Burda

  • The Golgi apparatus remains associated with microtubule organizing centers during myogenesis.

    A M Tassin;M Paintrand;E G Berger;M Bornens

  • MPDU1 mutations underlie a novel human congenital disorder of glycosylation, designated type If

    Barbara Schenk;Timo Imbach;Christian G. Frank;Claudia E. Grubenmann

  • Deficiency of UDP-galactose:N-acetylglucosamine β-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId

    Bengt Hanßke;Christian Thiel;Torben Lübke;Martin Hasilik

  • Carbohydrate-deficient glycoprotein syndromes become congenital disorders of glycosylation: an updated nomenclature for CDG. First International Workshop on CDGS.

    M Aebi;A Helenius;B Schenk;R Barone

  • A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic

    Timo Imbach;Patricie Burda;Peter Kuhnert;Ron A. Wevers

  • Genomic Cloning and Expression of Three Murine UDP-galactose: β-N-Acetylglucosamine β1,3-Galactosyltransferase Genes *

    Thierry Hennet;André Dinter;Peter Kuhnert;Taj S. Mattu

  • A NOVEL CARBOHYDRATE-DEFICIENT GLYCOPROTEIN SYNDROME CHARACTERIZED BY A DEFICIENCY IN GLUCOSYLATION OF THE DOLICHOL-LINKED OLIGOSACCHARIDE

    P Burda;L Borsig;J de Rijk-van Andel;R Wevers

  • A β-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to β-1,3-galactosyltransferases

    Dapeng Zhou;André Dinter;Ricardo Gutiérrez Gallego;Johannis P. Kamerling

  • Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik

    Claudia E. Grubenmann;Christian G. Frank;Andreas J. Hülsmeier;Els Schollen

Frequent Co-Authors

Thierry Hennet
Thierry Hennet University of Zurich
Markus Aebi
Markus Aebi ETH Zurich
Gert Matthijs
Gert Matthijs KU Leuven
Christian Wandrey
Christian Wandrey Forschungszentrum Jülich
Johannis P. Kamerling
Johannis P. Kamerling Utrecht University
Lubor Borsig
Lubor Borsig University of Zurich
Johannes F.G. Vliegenthart
Johannes F.G. Vliegenthart Utrecht University
Ron A. Wevers
Ron A. Wevers Radboud University
Martin Thurnher
Martin Thurnher Innsbruck Medical University
Jaak Jaeken
Jaak Jaeken KU Leuven

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