Roland Lill

Professor and Chair

Philipps-Universität Marburg

Germany

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Professor Roland Lill serves as the Chair at Philipps-Universität Marburg in Germany. His research focuses on the biogenesis and function of iron-sulfur proteins, as reflected in his recent publications which explore topics such as mitochondrial and cytosolic systems of iron-sulfur protein biogenesis. He has also contributed to the understanding of iron-sulfur cluster assembly mechanisms and their implications in various biological systems.

Articles (19)

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2025

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2020

Collaborators (10)

Vladimir Hampl

Charles University

CZECH REPUBLIC

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Lars-Oliver Essen

Prof.

GERMANY

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Heather W. Pinkett

Northwestern University

UNITED STATES

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Stephen G. Aller

The University of Alabama

UNITED STATES

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Hiroaki Kato

Professor

Kyoto University

JAPAN

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Konstantinos Beis

Imperial College London

UNITED KINGDOM

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Christiane Wolz

Eberhard Karls Universität Tübingen

GERMANY

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Miroslaw Cygler

Professor

University of Saskatchewan

CANADA

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Satoshi Murakami

Professor

Tokyo Institute of Technology

JAPAN

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Antonio J. Pierik

Full Professor

Technische Universität Kaiserslautern

GERMANY

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Roland Lill

Research Interests

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About

Articles (19)

The cytochrome oxidase defect in ISC‐depleted yeast is caused by impaired iron–sulfur cluster maturation of the mitoribosome assembly factor Rsm22

Editorial for the BBA-MCR Special Issue on “Biogenesis and Function Iron-sulfur Proteins”

Mitochondriale und zytosolische Systeme der Eisen-Schwefel-Proteinbiogenese

Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol

Mechanism and structural dynamics of sulfur transfer during de novo [2Fe-2S] cluster assembly on ISCU2

Two-stage binding of mitochondrial ferredoxin-2 to the core iron-sulfur cluster assembly complex

WITHDRAWN: Editorial for the BBA-MCR special issue on “biogenesis and function Iron-sulfur proteins”

Characterization of the SUF FeS cluster synthesis machinery in the amitochondriate eukaryote Monocercomonoides exilis.

Functional spectrum and specificity of mitochondrial ferredoxins FDX1 and FDX2

Hsp90 and metal‐binding J‐protein family chaperones are not critically involved in cellular iron–sulfur protein assembly and iron regulation in yeast

Mitochondrial [2Fe‐2S] ferredoxins: new functions for old dogs

A novel IBA57 variant is associated with mitochondrial iron–sulfur protein deficiency and necrotizing myelopathy in dogs

The iron-sulfur cluster assembly (ISC) protein Iba57 executes a tetrahydrofolate-independent function in mitochondrial [4Fe-4S] protein maturation.

N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization

Conformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle

The alarmone (p)ppGpp confers tolerance to oxidative stress during the stationary phase by maintenance of redox and iron homeostasis in Staphylococcus aureus

Structural and functional diversity calls for a new classification of ABC transporters

Do FeS clusters rule bacterial iron regulation?

Glutaredoxins and iron-sulfur protein biogenesis at the interface of redox biology and iron metabolism.

Collaborators (10)

Vladimir Hampl

Lars-Oliver Essen

Heather W. Pinkett

Stephen G. Aller

Hiroaki Kato

Konstantinos Beis

Christiane Wolz

Miroslaw Cygler

Satoshi Murakami

Antonio J. Pierik

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