Julia Weigand

Professor

Philipps-Universität Marburg

Germany

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Julia Weigand is a Professor at Philipps-University Marburg, Germany. Her research focuses on the structural and functional analysis of RNA-binding proteins and their interactions with RNA. Recent articles include work on chemical probes for SARS-CoV-2, Roquin binding preferences, and the structure of RNA motifs. She is also involved in collaborations to study the implications of these interactions on gene regulation and disease mechanisms.

Articles (18)

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2025

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2024

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2024

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2024

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2024

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2021

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2021

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2021

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2020

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2020

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2020

Collaborators (11)

Michaela Müller-McNicoll

W2 Professor

Goethe University Frankfurt

GERMANY

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Oliver Binas

Goethe University Frankfurt

GERMANY

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Katja Petzold

Karolinska Institutet

SWEDEN

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David Mathews

Professor

University of Rochester Medical Center

UNITED STATES

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Sabine Müller

GERMANY

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Andreas Schlundt

GERMANY

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José Gallego

Universidad Católica de Valencia San Vicente Mártir

SPAIN

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Boris Fürtig

GERMANY

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Rolf Backofen

Full Professor

GERMANY

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Josef Wachtveitl

Full Professor for Biophysics and Physical Chemistry (C4)

Goethe University Frankfurt

GERMANY

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Verena Linhard

Goethe University Frankfurt

GERMANY

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Julia Weigand

Research Interests

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About

Articles (18)

Optimization of Structure-Guided Development of Chemical Probes for the Pseudoknot RNA of the Frameshift Element in SARS-CoV-2.

Heterogenous nuclear ribonucleoprotein D-like controls endothelial cell functions

Comprehensive Profiling of Roquin Binding Preferences for RNA Stem‐Loops

Detaillierte Analyse der Bindepräferenz von Roquin an RNA‐Stammschleifen

Structure and RNA-binding of the helically extended Roquin CCCH-type zinc finger

Arid5a uses disordered extensions of its core ARID domain for distinct DNA- and RNA-recognition and gene regulation

Structure of an internal loop motif with three consecutive U•U mismatches from stem–loop 1 in the 3′-UTR of the SARS-CoV-2 genomic RNA

Magnesium Ion-Driven Folding and Conformational Switching Kinetics of Tetracycline Binding Aptamer: Implications for in vivo Riboswitch Engineering

Das COVID19‐NMR‐Konsortium: Ein öffentlicher Bericht über den Einfluss dieser neuen globalen Kollaboration

The COVID19‐NMR Consortium: A Public Report on the Impact of this New Global Collaboration

1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10

Correction to ‘Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy’

1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein

A Novel, Universally Active C-terminal Protein Degradation Signal Generated by Alternative Splicing.

<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N chemical shift assignment of the stem-loop 5a from the 5'-UTR of SARS-CoV-2.

1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b

Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy

1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e.

Collaborators (11)

Michaela Müller-McNicoll

Oliver Binas

Katja Petzold

David Mathews

Sabine Müller

Andreas Schlundt

José Gallego

Boris Fürtig

Rolf Backofen

Josef Wachtveitl

Verena Linhard

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