World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
66
Citations
19183
World Ranking
8535
National Ranking
3837

Overview

Gerd G. Maul was affiliated with The Wistar Institute in the United States. Their research contributions spanned primarily within the fields of Medicine and Biochemistry, Genetics and Molecular Biology.

The subfields of study associated with their work included Epidemiology, Cardiology and Cardiovascular Medicine, and Physiology.

They published at least one recent paper entitled DISC1-PML protein interaction for congenital CMV infection-induced cortical neural progenitor deficit: perturbance of host signaling via viral IE1 in 2025. This paper was published in bioRxiv (Cold Spring Harbor Laboratory).

Their research topics frequently addressed areas related to:

  • Cytomegalovirus and herpesvirus research
  • Viral Infections and Immunology Research
  • Calcium signaling and nucleotide metabolism

Frequent collaborators included:

  • Atsushi Saito
  • Stephanie Tankou
  • Kazuhiro Ishii
  • Makiko Sakao-Suzuki
  • Edwin C. Oh

Their publications were concentrated in venues such as bioRxiv (Cold Spring Harbor Laboratory), where at least one paper was published.

Best Publications

  • SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins

    David C. Schultz;Kasirajan Ayyanathan;Dmitri Negorev;Gerd G. Maul

  • Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1

    Alexander M. Ishov;Alexey G. Sotnikov;Dmitri Negorev;Olga V. Vladimirova

  • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein

    Jacqueline A. Dyck;Jacqueline A. Dyck;Gerd G. Maul;Wilson H. Miller;J.Don Chen

  • BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression

    David E. Jensen;Monja Proctor;Sandra T. Marquis;Heather Perry Gardner

  • Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation

    Kasirajan Ayyanathan;Mark S. Lechner;Peter Bell;Gerd G. Maul

  • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors.

    Ding Yen Lin;Yen Sung Huang;Jen Chong Jeng;Hong Yi Kuo

  • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition.

    A M Ishov;G G Maul

  • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0)

    G. G. Maul;H. H. Guldner;J. G. Spivack

  • PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing.

    Alexey V. Ivanov;Hongzhuang Peng;Vyacheslav Yurchenko;Kyoko L. Yap

  • The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0

    Gerd G. Maul;Roger D. Everett

  • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure.

    V Doucas;A M Ishov;A Romo;H Juguilon

  • Nuclear domain 10, the site of DNA virus transcription and replication

    Gerd G. Maul

  • Review: properties and assembly mechanisms of ND10, PML bodies, or PODs.

    Gerd G. Maul;Dmitri Negorev;Peter Bell;Alexander M. Ishov

  • Identification of a novel nuclear domain.

    Carl A. Ascoli;Gerd G. Maul

  • Differential regulation of sentrinized proteins by a novel sentrin-specific protease.

    Limin Gong;Stefanos Millas;Gerd G. Maul;Edward T.H. Yeh

  • Nuclear Domain 10 as Preexisting Potential Replication Start Sites of Herpes Simplex Virus Type-1

    Gerd G. Maul;Alexander M. Ishov;Roger D. Everett

  • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot.

    Dmitri Negorev;Gerd G Maul

  • THE NUCLEAR DOMAIN 10 (ND10) IS DISRUPTED BY THE HUMAN CYTOMEGALOVIRUS GENE PRODUCT IE1

    Frank Korioth;Gerd G. Maul;Bodo Plachter;Thomas Stamminger

  • Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment.

    Alexander M. Ishov;Richard M. Stenberg;Gerd G. Maul

  • The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain.

    Mark S. Lechner;David C. Schultz;Dmitri Negorev;Gerd G. Maul

Frequent Co-Authors

Frank J. Rauscher
Frank J. Rauscher The Wistar Institute
Peter Bell
Peter Bell University of Pennsylvania
Gerald Schatten
Gerald Schatten University of Pittsburgh
Sergio A. Jimenez
Sergio A. Jimenez Thomas Jefferson University
Dorothee Herlyn
Dorothee Herlyn The Wistar Institute
Meenhard Herlyn
Meenhard Herlyn The Wistar Institute
Louise C. Showe
Louise C. Showe The Wistar Institute
Edward T.H. Yeh
Edward T.H. Yeh University of Missouri
Randall S. Prather
Randall S. Prather University of Missouri
Roger D. Everett
Roger D. Everett University of Glasgow

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Best Scientists Citing Gerd G. Maul