Martin Luther University Halle-Wittenberg

„Tanfords Garten“: Der Leipziger Künstler Timm Kregel hat die Kunst am Bau des Proteinzentrums gestaltet. (Foto: Maike Glöckner)

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Research Groups CTP

Prof. Mechthild Hatzfeld    

Division for Pathobiochemistry
Prof. Dr. Mechthild Hatzfeld

Connections between the cytoskeleton and intercellular junctions profoundly influence cell shape and motility. It is becoming increasingly clear that in addition to structural functions, components of the adhesion apparatus also possess signalling capabilities. Recent studies suggest that proteins with such dual functions may provide the means to integrate changes in morphology and gene expression during tissue and organ development. Our research focuses on the molecular analysis of signalling through junction-associated proteins. In the previous years, we have defined the p120ctn family of armadillo related proteins that includes the prototype p120ctn, p0071, δ-catenin/NPRAP, ARVCF and the more distantly related plakophilins 1-3...

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Head: Jun.-Prof. Dr. Tony Gutschner

Junior Research Group “RNA biology and pathogenesis”
Prof. Dr. Tony Gutschner

The research projects in our lab aim to unravel the molecular function and regulatory principles applied by non-coding RNAs (ncRNAs) and RNA-binding proteins (RBPs) in cancer cells. We develop novel genome engineering and gene targeting strategies, which we combine with classical cell biology and biochemical approaches to dissect molecular pathways and interaction networks of these important regulators in the context of tumor biology.

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Das Institut für Molekulare Medizin, Sektion Molekulare Zellbiologie 
ist ein Forschungsinstitut und beschäftigt sich mit Zellbiologischen 

Institut für Molekulare Medizin, Sektion Molekulare Zellbiologie
Prof. Dr. Stefan Hüttelmaier

Our lab is interested in the characterization of regulatory mechanisms directing the cytoplasmic fate of specific mRNAs and how this posttranscriptional control of gene expression modulates cell function and pathogenesis, in particular tumor progression.

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The Core Facilty Imaging

Core Facility — Proteomic Mass Spectrometry (CFP)
Dr. Matt Fuszard

The Core Facility - Proteomic Mass Spectrometry at Weinberg Campus is a collaboration between the Faculty I of Natural Science - Biological Science and the Zentrum für Medizinische Grundlagenforschung (ZMG) within theMedical Faculty and will provide a full proteomic infrastructure for identification and characterization of proteins and peptides.

Signal computation and signaling defect heterogeneity in human cancers

Tumor Biology
Prof. Stephan M. Feller, PhD

Many human cancers are difficult or impossible to cure, in no small part because each human cancer essentially presents a unique disease at the molecular level. We are using a wide range of biochemical and cell biology methods to gain insight into the molecular diversity and functions of cancer cell proteins. A second focus of our research is on understanding how complex signals in normal cells and cancer cells are molecularly computed in order to drive decision-making regarding important cell actions like proliferation, migration and invasion. For this we employ various biophysical tools, as well as biochemical and cell biological assays. We have recently developed a novel, internationally recognized hypothesis of how complex signal computation is accomplished on large, intrinsically disordered proteins (IDPs) and how this may potentially be exploited for future disease treatments. Last not least, we are also engaged in the education of medical students, politicians, pupils and the general public regarding addiction and disease prevention, since prevention is frequently more effective than even the best of therapies.

The Core Facilty Imaging

Core Facility Imaging (CFI)
Dr. Nadine Bley

The Core Facilty Imaging is registered as a Research Infrastructure of the Deutsche Forschungsgemeinschaft (DFG) and is available at the RIsources portal and part of the German BioImaging Netzwerks.

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Pharmaceutical Chemistry and Bioanalytics

Department of Pharmaceutical Chemistry and Bioanalytics
Prof. Dr. Andrea Sinz

The research interest of our group is the advancement of the chemical cross-linking/MS strategy for elucidating protein 3D-structures and for mapping protein-protein interactions. We are currently exploring the development and application of novel MS/MS cleavable cross-linkers as well as the incorporation of photo-reactive amino acids. Analysis of the cross-linked products is performed by theStavroX    software developed by Michael Götze. Our lab is equipped with two Orbitrap mass spectrometers (LTQ-Orbitrap XL and Orbitrap Fusion Tribrid, Thermo Fisher Scientific), both coupled to nano-HPLC systems, a MALDI-TOF/TOFmass spectrometer (Ultraflex III, Bruker Daltonik), and a High-Mass Q-TOF mass spectrometer (Micromass/MS Vision).

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Institute of Molecular Medicine, Martin Luther University - Medical Faculty, CTP - 1st floor

NWG Köhn

Nora Hase, Marcel Köhn, Peter Zorn

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Cryo-Electron microscopy of membrane protein complexes    

Cryo-Electron microscopy of membrane protein complexes
Jun.-Prof. Dr. Panagiotis L. Kastritis

Our aim is to analyze the molecular architecture of enzymatic supercomplexes, ideally within their native cellular context. We combine cryo-electron microscopy and computational structural biology approaches, two methods that are at the forefront of biological research. Our integrative findings will provide a whole new avenue for targeted drug design. Rather than targeting the active sites of individual subunits -which share many physical and chemical characteristics thus compromising specificity- we envisage a therapeutic strategy that targets the interface between proteins in the supercomplex that are likely to be unique.

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Allgemeine Biochemie

Abteilung Allgemeine Biochemie
Prof. Dr. Elmar Wahle

Die Arbeitsgruppe interessiert sich in erster Linie für die mRNA-Prozessierung, die Regulation der Translation und den mRNA-Abbau in Eukaryoten. Ein weiteres Thema ist die posttranslationale Modifikation von Proteinen durch die Methylierung von Argininseitenketten.

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ZIK HALOmem - membrane structure and dynamics

Abteilung Biophysikalische Charakterisierung medizinisch relevanter
Jun.-Prof. Dr. Carla Schmidt

We employ various mass spectrometric techniques to study structure and dynamics of protein-lipid complexes. Our main research focus is the investigation of protein-lipid interactions in synaptic vesicles and in the neuronal synapse. This research project is part of the BMBF-funded  interdisciplinary research center „HALOmem: membrane structure and dynamics“

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Department of Enzymology

Abteilung Enzymologie
Prof. Dr. Mike Schutkowski

Die Forschung der Arbeitgruppe konzentriert sich auf zwei dominante Themen:

  1. Untersuchung posttranslationaler Modifikationen von Proteinen und deren Auswirkungen unter Nutzung von Peptid-Chips
  2. Strukturelle und enzymkinetische Charakterisierung von Thiamindiphosphat-abhängigen Enzymen

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§%%§%%§%%de%##%##%##Startseite der Abt. Mikrobielle Biotechnologie

Abteilung Mikrobielle Biotechnologie
Prof. Dr. Sven-Erik Behrens

Die Abteilung Mikrobielle Biotechnologie hat zwei dominante Forschungsinteressen:
1. Die Identifizierung und Charakterisierung essentieller Faktoren des Lebenszyklus’ verschiedener RNA-Viren (bekanntestes Beispiel: Hepatitis C Virus).
2. Die Entwicklung von Applikationsformen von RNA-Viren zu Genexpressions- und Vakzinierungszwecken.

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§%%§%%§%%en%##%##%##Abteilung Physikalische Biotechnologie

Abteilung Physikalische Biotechnologie
Prof. Dr. Milton T. Stubbs

Unsere Arbeitsgruppe beschäftigt sich mit der Strukturanalyse biologischer Makromoleküle. Durch verschiedenste Projekte ist eine übergeordnete Fragestellung unserer Arbeiten entstanden – wie sich Proteine an ihrer Umgebung durch konformationelle Umwandlungen anpassen.

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§%%§%%§%%de%##%##%##Abteilung Naturstoffbiochemie

Abteilung Naturstoffbiochemie
Prof. Dr. Frank Bordusa

Im Fokus des Interesses unserer Abteilung steht die Etablierung neuer Strategien zur Semisynthese und ortsspezifischen Modifizierung von Proteinen durch artifiziell adaptierte Enzymkatalysatoren. Methodische Einzelaktivitäten umfassen insbesondere das rationale und evolutive Enzymdesign, die chemische und kombinatorische Peptidsynthese und Reaktionen in ionischen Flüssigkeiten.

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