A5036116391- Heat shock proteins research
- Enzyme Structure and Function
- Signaling Pathways in Disease
- Protein Structure and Dynamics
- Photosynthetic Processes and Mechanisms
- Endoplasmic Reticulum Stress and Disease
- Biochemical and Molecular Research
- Metabolism and Genetic Disorders
- Algal biology and biofuel production
- Viral Infectious Diseases and Gene Expression in Insects
- Computational Drug Discovery Methods
- ATP Synthase and ATPases Research
- Toxin Mechanisms and Immunotoxins
- Amino Acid Enzymes and Metabolism
- Mitochondrial Function and Pathology
- RNA and protein synthesis mechanisms
- Viral Infections and Outbreaks Research
- Cellular transport and secretion
- Lipid Membrane Structure and Behavior
- Receptor Mechanisms and Signaling
- Hepatitis B Virus Studies
- Bacterial Genetics and Biotechnology
- Inorganic Chemistry and Materials
- RNA modifications and cancer
- Glycosylation and Glycoproteins Research
Max Planck Institute of Biochemistry
2014-2024
Max Planck Society
2002-2015
Medical University of Vienna
2009-2012
University of Alabama at Birmingham
2011-2012
European Molecular Biology Laboratory
2000-2004
Technical University of Munich
1996-2003
European Bioinformatics Institute
2000-2002
Institute of Molecular Biology, Academia Sinica
2002
Heidelberg University
1996
Institut für Zeitgeschichte München–Berlin
1996
The identification of proximate amino acids by chemical cross-linking and mass spectrometry (XL-MS) facilitates the structural analysis homogeneous protein complexes. We gained distance restraints on a modular interaction network complexes affinity-purified from human cells applying an adapted XL-MS protocol. Systematic phosphatase 2A (PP2A) identified 176 interprotein 570 intraprotein cross-links that link specific trimeric PP2A to multitude adaptor proteins control their cellular...
A biotech tour de force RuBisCo, the key enzyme of photosynthesis, is a complex eight large and small subunits. It mediates fixation atmospheric CO 2 in Calvin-Benson-Bassham cycle. In addition to being enzymatically inefficient, RuBisCo has problem with distinguishing between O . The results energetically wasteful reaction photorespiration. Thus, there strong incentive improve RuBisCo's catalytic properties by engineering. However, for decades, it been impossible express from plants an...
After folding, many proteins must assemble into oligomeric complexes to become biologically active. Here we describe the role of RbcX as an assembly chaperone ribulose-bisphosphate carboxylase/oxygenase (Rubisco), enzyme responsible for fixation atmospheric carbon dioxide. In cyanobacteria and plants, Rubisco is approximately 520 kDa complex composed eight large subunits (RbcL) small (RbcS). We found that cyanobacterial functions downstream chaperonin-mediated RbcL folding in promoting...
Proteasomes execute the degradation of most cellular proteins. Although 20S core particle (CP) has been studied in great detail, structure 19S regulatory (RP), which prepares ubiquitylated substrates for degradation, remained elusive. Here, we report crystal one RP subunits, Rpn6, and describe its integration into cryo-EM density map 26S holocomplex at 9.1 Å resolution. Rpn6 consists an α-solenoid-like fold a proteasome COP9/signalosome eIF3 (PCI) module right-handed suprahelical...
Significance The 26S proteasome is a multiprotein complex that degrades proteins marked for destruction by the covalent attachment of polyubiquitin chains. Proteasome activity essential removal damaged, potentially toxic and regulation numerous cellular processes. Multiple crystal structures Rpn8-Rpn11 heterodimer, which responsible tags before substrate degradation in proteasome, provide insight into how unfolding isopeptide bond cleavage might be coupled, premature activation this module...
The immunosuppressant and anticancer drug rapamycin works by inducing inhibitory protein complexes with the kinase mTOR, an important regulator of growth proliferation. obligatory accessory partner is believed to be FK506-binding 12 (FKBP12). Here we show that larger FKBP family members can tightly bind mTOR potently inhibit its activity. Cocrystal structures FKBP51 FKBP52 reveal modified molecular binding mode these alternative ternary in detail. In cellular model systems, FKBP12...
Molecular chaperones contribute to the maintenance of cellular protein homoeostasis through assisting de novo folding and preventing amyloid formation. Chaperones Hsp70 family can further disaggregate otherwise irreversible aggregate species such as α-synuclein fibrils, which accumulate in Parkinson's disease. However, mechanisms kinetics this key functionality are only partially understood. Here, we combine microfluidic measurements with chemical study disaggregation. We show that Hsc70...