World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
49
Citations
8985
World Ranking
18004
National Ranking
1238

Research.com Recognitions

  • 1969 - Fellow of Alfred P. Sloan Foundation

Overview

Roland Brandt is affiliated with Osnabrück University in Germany and specializes in biochemistry, genetics, and molecular biology. Their research encompasses a strong focus on molecular biology, physiology, and cell biology, with additional interest in cellular and molecular neuroscience and computational theory and mathematics.

The scientist's work spans several key topics, including:

  • Alzheimer's disease research and treatments
  • Microtubule and mitosis dynamics
  • Mitochondrial function and pathology
  • Computational drug discovery methods
  • Neuroscience and neuropharmacology research
  • Advanced fluorescence microscopy techniques
  • RNA research and splicing

Brandt has published extensively in various venues, with frequent contributions to:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Frontiers in Synaptic Neuroscience
  • Nature Communications
  • Brain Research Bulletin
  • BIOspektrum

Their notable recent papers include:

  • Much More Than a Cytoskeletal Protein: Physiological and Pathological Functions of the Non-microtubule Binding Region of Tau (2020, Frontiers in Neurology)
  • Caspase-cleaved tau is senescence-associated and induces a toxic gain of function by putting a brake on axonal transport (2022, Molecular Psychiatry)
  • Early Effects of Aβ Oligomers on Dendritic Spine Dynamics and Arborization in Hippocampal Neurons (2020, Frontiers in Synaptic Neuroscience)
  • Quantitative live cell imaging of a tauopathy model enables the identification of a polypharmacological drug candidate that restores physiological microtubule interaction (2024, Nature Communications)
  • Super-resolution imaging and quantitative analysis of microtubule arrays in model neurons show that epothilone D increases the density but decreases the length and straightness of microtubules in axon-like processes (2022, Brain Research Bulletin)

Frequent co-authors in their research include:

  • Lidia Bakota
  • Nataliya I. Trushina
  • Christian Conze
  • Nanci Monteiro-Abreu
  • Nicolo Bisi

Roland Brandt's productivity is reflected by prolific output in the field of molecular biology and related disciplines. The interdisciplinary nature of their work integrates experimental and computational approaches, particularly applied to neurodegenerative diseases such as Alzheimer's disease and the dynamics of the cytoskeleton.

They were recognized early in their career as a Fellow of the Alfred P. Sloan Foundation in 1969.

Best Publications

  • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.

    R Brandt;J Léger;G Lee

  • CD95 ligand (Fas-L/APO-1L) and tumor necrosis factor-related apoptosis-inducing ligand mediate ischemia-induced apoptosis in neurons.

    Ana Martin-Villalba;Ingrid Herr;Irmela Jeremias;Michael Hahne

  • Molecular Interactions among Protein Phosphatase 2A, Tau, and Microtubules IMPLICATIONS FOR THE REGULATION OF TAU PHOSPHORYLATION AND THE DEVELOPMENT OF TAUOPATHIES

    Estelle Sontag;Viyada Nunbhakdi-Craig;Gloria Lee;Roland Brandt

  • Tau alteration and neuronal degeneration in tauopathies: mechanisms and models

    Roland Brandt;Monika Hundelt;Neelam Shahani

  • Process Outgrowth of Oligodendrocytes Is Promoted by Interaction of Fyn Kinase with the Cytoskeletal Protein Tau

    Corinna Klein;Eva-Maria Krämer;Anne-Marie Cardine;Burkhardt Schraven

  • Tau Binds to the Distal Axon Early in Development of Polarity in a Microtubule- and Microfilament-Dependent Manner

    Martina Kempf;Albrecht Clement;Andreas Faissner;Gloria Lee

  • Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro.

    R. Brandt;G. Lee

  • Tau-Mediated Cytotoxicity in a Pseudohyperphosphorylation Model of Alzheimer's Disease

    Thomas Fath;Jochen Eidenmüller;Roland Brandt;Roland Brandt

  • Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments.

    Thorsten Maas;Jochen Eidenmüller;Roland Brandt

  • Functions and malfunctions of the tau proteins

    N. Shahani;R. Brandt

  • Tau Biology and Tau-Directed Therapies for Alzheimer’s Disease

    Lidia Bakota;Roland Brandt

  • Divergent pathways mediate spine alterations and cell death induced by amyloid-beta, wild-type tau, and R406W tau

    Christian Tackenberg;Roland Brandt

  • Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau.

    Jocelyne Léger;Martina Kempf;Gloria Lee;Roland Brandt

  • Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons

    Dennis Janning;Maxim Igaev;Frederik Sündermann;Jörg Brühmann

  • The frontotemporal dementia mutation R406W blocks tau’s interaction with the membrane in an annexin A2–dependent manner

    Anne Gauthier-Kemper;Carina Weissmann;Nataliya Golovyashkina;Zsofia Sebö-Lemke

  • Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein.

    Jochen Eidenmüller;Thomas Fath;Thorsten Maas;Madeline Pool

  • Structural and Functional Implications of Tau Hyperphosphorylation: Information from Phosphorylation-Mimicking Mutated Tau Proteins†

    Jochen Eidenmuller;Thomas Fath;Andrea Hellwig;Jennifer Reed

  • A Caenorhabditis elegans model of tau hyperphosphorylation: Induction of developmental defects by transgenic overexpression of Alzheimer's disease-like modified tau

    Roland Brandt;Aikaterini Gergou;Irene Wacker;Thomas Fath;Thomas Fath

  • NMDA receptor subunit composition determines beta-amyloid-induced neurodegeneration and synaptic loss.

    C Tackenberg;S Grinschgl;A Trutzel;A C Santuccione

  • Stabilization of hyperdynamic microtubules is neuroprotective in amyotrophic lateral sclerosis.

    Patrizia Fanara;Jayee Banerjee;Rommel V. Hueck;Macha R. Harper

Frequent Co-Authors

Gloria Lee
Gloria Lee University of Iowa
Marc K. Hellerstein
Marc K. Hellerstein University of California, Berkeley
Wolfgang Junge
Wolfgang Junge Osnabrück University
Heinz-Jürgen Steinhoff
Heinz-Jürgen Steinhoff Osnabrück University
Jürgen Götz
Jürgen Götz University of Queensland
Christian Ungermann
Christian Ungermann Osnabrück University
Volker Gerke
Volker Gerke University of Münster
Hannah Monyer
Hannah Monyer German Cancer Research Center
Andreas Faissner
Andreas Faissner Ruhr University Bochum
Christian Schultz
Christian Schultz Heidelberg University

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