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D-Index & Metrics

Biology and Biochemistry

D-Index
44
Citations
6025
World Ranking
19326
National Ranking
174

Overview

Peter Loidl is affiliated with Innsbruck Medical University in Austria. Their research spans several fields of study, predominantly in Medicine and Biochemistry, Genetics, and Molecular Biology. Within these areas, their work focuses on oncology, molecular biology, and ophthalmology as subfields.

The scientist's main topics of research include cancer-related molecular pathways, ubiquitin and proteasome pathways, and ocular oncology and treatments. These areas reflect a concentration on molecular mechanisms underlying cancer and eye diseases.

Peter Loidl has coauthored publications with several researchers, including Farman Ullah, Nadia Khurshid, Qaiser Fatimi, and Muhammad Saeed.

The scientist has published in venues such as PLoS ONE.

One of the recent publications is:

  • Mutations in the acetylation hotspots of Rbl2 are associated with increased risk of breast cancer, 2022, PLoS ONE

Best Publications

  • Inhibition of maize histone deacetylases by HC toxin, the host-selective toxin of Cochliobolus carbonum.

    Gerald Brosch;Richard Ransom;Thomas Lechner;Jonathan D. Walton

  • Identification of Maize Histone Deacetylase HD2 as an Acidic Nucleolar Phosphoprotein

    Alexandra Lusser;Gerald Brosch;Adele Loidl;Hubertus Haas

  • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation.

    Manfred Jung;Gerald Brosch;Doris Kölle;Hans Scherf

  • Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides.

    Antonello Mai;Silvio Massa;Riccardo Pezzi;Silvia Simeoni

  • Histone acetylation: facts and questions.

    P. Loidl

  • A plant dialect of the histone language.

    Peter Loidl

  • Histone modifications and chromatin dynamics: a focus on filamentous fungi

    Gerald Brosch;Peter Loidl;Stefan Graessle

  • Histone acetylation: lessons from the plant kingdom

    Alexandra Lusser;Doris Kölle;Peter Loidl

  • 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-alkylamides as a new class of synthetic histone deacetylase inhibitors. 1. Design, synthesis, biological evaluation, and binding mode studies performed through three different docking procedures

    Antonello Mai;Silvio Massa;Rino Ragno;Ilaria Cerbara

  • Biochemical methods for analysis of histone deacetylases.

    Doris Kölle;Gerald Brosch;Thomas Lechner;Alexandra Lusser

  • Towards an understanding of the biological function of histone acetylation

    Peter Loidl

  • Analogues of trichosтatin a and trapoxin B as histone deacetylase inhibitors

    Manfred Jung;Katharina Hoffmann;Gerald Brosch;Peter Loidl

  • Cell growth inhibition by the Mad/Max complex through recruitment of histone deacetylase activity

    Anette Sommer;Stefanie Hilfenhaus;Annette Menkel;Elisabeth Kremmer

  • A non-isotopic assay for histone deacetylase activity

    Katharina Hoffmann;Manfred Jung;Gerald Brosch;Peter Loidl

  • 3-(4-aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors.

    Silvio Massa;Antonello Mai;Gianluca Sbardella;Monica Esposito

  • Comparative analysis of HD2 type histone deacetylases in higher plants.

    Markus Dangl;Gerald Brosch;Hubertus Haas;Peter Loidl

  • Different types of maize histone deacetylases are distinguished by a highly complex substrate and site specificity.

    Doris Kölle;Gerald Brosch;Thomas Lechner;Alexandra Pipal

  • Histone deacetylases in fungi: novel members, new facts

    Patrick Trojer;Eva M. Brandtner;Gerald Brosch;Peter Loidl

  • Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin.

    Gerardo López-Rodas;Gerald Brosch;Elena I. Georgieva;Elena I. Georgieva;Ramón Sendra;Ramón Sendra

  • Structure-activity relationships on phenylalanine-containing inhibitors of histone deacetylase: in vitro enzyme inhibition, induction of differentiation, and inhibition of proliferation in Friend leukemic cells.

    Sybille Wittich;Hans Scherf;Changping Xie;Gerald Brosch

Frequent Co-Authors

Gerald Brosch
Gerald Brosch Innsbruck Medical University
Antonello Mai
Antonello Mai Sapienza University of Rome
Hubertus Haas
Hubertus Haas Innsbruck Medical University
Jonathan D. Walton
Jonathan D. Walton Michigan State University
Herbert Lindner
Herbert Lindner Innsbruck Medical University
Manfred Jung
Manfred Jung University of Freiburg
Bernhard Lüscher
Bernhard Lüscher RWTH Aachen University
Sergio Valente
Sergio Valente Sapienza University of Rome
Dietmar Fuchs
Dietmar Fuchs Innsbruck Medical University
Dante Rotili
Dante Rotili Sapienza University of Rome

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