Stephan Nußberger

ORCID: 0000-0003-3619-4452
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About
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Research Areas
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • RNA and protein synthesis mechanisms
  • Photosynthetic Processes and Mechanisms
  • Lipid Membrane Structure and Behavior
  • Amino Acid Enzymes and Metabolism
  • Neuroscience and Neuropharmacology Research
  • Drug Transport and Resistance Mechanisms
  • Protein Structure and Dynamics
  • RNA modifications and cancer
  • Molecular Sensors and Ion Detection
  • Nanopore and Nanochannel Transport Studies
  • Ion channel regulation and function
  • Cancer, Hypoxia, and Metabolism
  • Metabolism and Genetic Disorders
  • Enzyme Structure and Function
  • DNA and Nucleic Acid Chemistry
  • Mass Spectrometry Techniques and Applications
  • Ion Transport and Channel Regulation
  • RNA Interference and Gene Delivery
  • Autophagy in Disease and Therapy
  • Advanced biosensing and bioanalysis techniques
  • Biological Research and Disease Studies
  • Metabolomics and Mass Spectrometry Studies
  • Genetics, Bioinformatics, and Biomedical Research

University of Stuttgart
2016-2025

Ludwig-Maximilians-Universität München
1998-2005

Institut für Urheber- und Medienrecht
2002

Harvard University
1994-1997

Brigham and Women's Hospital
1994-1997

Harvard University Press
1994-1996

Yale University
1996

Czech Academy of Sciences, Institute of Analytical Chemistry
1996

Northeastern University
1996

Kyorin University
1994

Abstract The shape of biological matter is central to cell function at different length scales and determines how cellular components recognize, interact respond one another. However, their shapes are often transient hard reprogramme. Here we construct a synthetic model composed signal-responsive DNA nanorafts, biogenic pores giant unilamellar vesicles (GUVs). We demonstrate that reshaping rafts the nanoscale can be coupled GUVs microscale. nanorafts collectively undergo reversible...

10.1038/s41563-024-02075-9 article EN cc-by Nature Materials 2025-01-13

Translocation of nuclear-encoded preproteins across the outer membrane mitochondria is mediated by multicomponent transmembrane TOM complex. We have isolated core complex Neurospora crassa removing receptors Tom70 and Tom20 from holo treatment with detergent dodecyl maltoside. It consists Tom40, Tom22, small Tom components, Tom6 Tom7. This was also purified directly after solubilization The has characteristics general insertion pore; it contains high-conductance channels binds preprotein in...

10.1083/jcb.147.5.959 article EN The Journal of Cell Biology 1999-11-29

Active ion-coupled glutamate transport is of critical importance for excitatory synaptic transmission, normal cellular function, and epithelial amino acid metabolism. We previously reported the cloning rabbit intestinal high affinity transporter EAAC1 (Kanai, Y., Hediger, M. A.(1992) Nature 360, 467-471), which [Medline] expressed in numerous tissues including intestine, kidney, liver, heart, brain. Here, we report a detailed stoichiometric kinetic analysis Xenopus laevis oocytes. Uptake...

10.1074/jbc.270.28.16561 article EN cc-by Journal of Biological Chemistry 1995-07-01

Tom40 is the main component of preprotein translocase outer membrane mitochondria (TOM complex). We have isolated Neurospora crassa by removing receptor Tom22 and small Tom components Tom6 Tom7 from purified TOM core complex. organized in a high molecular mass complex ∼350 kD. It forms conductance channel. Mitochondrial presequence peptides interact specifically with reconstituted into planar lipid membranes decrease ion flow through pores voltage-dependent manner. The secondary structure...

10.1083/jcb.153.6.1151 article EN The Journal of Cell Biology 2001-06-04

High affinity transport of glutamate across plasma membranes brain neurons and epithelia is mediated by a Na+-and K'-coupled electrogenic transporter.Here we report the primary structure functional characterization human high transporter (HEAACl).A unique characteristic HEAAC1mediated that for maximal rate are strongly dependent on membrane potential.Our data provide new insights into individual steps show mechanism distinct from y-aminobutyric acid GAT-1 Na+/glucose SGLTl.Under voltage...

10.1016/s0021-9258(17)32035-5 article EN cc-by Journal of Biological Chemistry 1994-08-01

Abstract Background Poly(3-hydroxybutyrate) (PHB) granules are important storage compounds of carbon and energy in many prokaryotes which allow survival the cells absence suitable sources. Formation subcellular localization PHB was previously assumed to occur randomly cytoplasm accumulating bacteria. However, contradictionary results on Ralstonia eutropha were published, recently. Results Here, we provide evidence by transmission electron microscopy that localized close contact nucleoid...

10.1186/1471-2180-12-262 article EN cc-by BMC Microbiology 2012-11-16

Three-dimensional (3D) bioprinting promises to change future lifestyle and the way we think about aging, field of medicine, clinicians treat ailing patients. In this brief review, attempt give a glimpse into how recent developments in 3D are going impact vast research ranging from complex functional organ transplant toxicology studies printed organ-like spheroids. The techniques were successfully applied reconstructed tissue for implantation, application-based high-throughput (HTP) platforms...

10.3390/app9040811 article EN cc-by Applied Sciences 2019-02-25

Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein are limited by sample consumption or compatibility with buffer components. Here we describe how miniaturized measurement intrinsic tryptophan fluorescence (NanoDSF assay) combination simplified description unfolding can be used to interrogate sample. We demonstrate that improved measures, such as apparent Gibbs free energy unfolding, rather than...

10.1002/pro.3986 article EN cc-by Protein Science 2020-11-03

1. The intestinal H(+)-coupled peptide transporter PepT1, displays a broad substrate specificity and accepts most charged neutral di- tripeptides. To study the proton-to-peptide stoichiometry dependence of kinetic parameters on extracellular pH (pHo), rabbit PepT1 was expressed in Xenopus laevis oocytes used for uptake studies radiolabelled dipeptides, voltage-clamp analysis intracellular measurements. 2. did not display substrate-gated anion conductances that have been found to be...

10.1113/jphysiol.1997.sp021883 article EN The Journal of Physiology 1997-02-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSpectroscopic characterization of three different monomeric forms the main chlorophyll a/b binding protein from chloroplast membranesStephan Nussberger, Jan P. Dekker, Werner Kuehlbrandt, Bauke M. van Bolhuis, Rienk Grondelle, and Herbert AmerongenCite this: Biochemistry 1994, 33, 49, 14775–14783Publication Date (Print):December 1, 1994Publication History Published online1 May 2002Published inissue 1 December...

10.1021/bi00253a016 article EN Biochemistry 1994-12-01

The intrinsic pathway of apoptotic cell death is mainly mediated by the BCL-2-associated X (BAX) protein through permeabilization mitochondrial outer membrane (MOM) and concomitant release cytochrome c into cytosol. In healthy, non-apoptotic cells, BAX predominantly localized in cytosol exhibits a dynamic shuttle cycle between mitochondria. Thus, initial association with mitochondria represents critical regulatory step enabling to insert MOMs, promoting ultimately resulting apoptosis....

10.1038/cddis.2014.17 article EN cc-by Cell Death and Disease 2014-02-13

The TOM complex is the main entry point for precursor proteins (preproteins) into mitochondria. Preproteins containing targeting sequences are recognized by and imported We have determined structure of core from

10.1073/pnas.2301447120 article EN cc-by Proceedings of the National Academy of Sciences 2023-08-14

Precursor proteins of the solute carrier family and channel forming Tim components are imported into mitochondria in two main steps. First, they translocated through TOM complex outer membrane, a process assisted by Tim9/Tim10 complex. They passed on to TIM22 complex, which facilitates their insertion inner membrane. In present study, we have analyzed function translocation substrates across membrane mitochondria. The purified core was reconstituted lipid vesicles entrapped. precursor...

10.1091/mbc.e03-05-0272 article EN Molecular Biology of the Cell 2003-12-16

Ion-coupled solute transporters exhibit pre-steady-tate currents that resemble those of voltage-dependent ion channels. These were assumed to be mostly due binding and dissociation the coupling near extracellular transporter surface. Little attention was given analogous events may occur at intracellular To address this issue, we performed voltage clamp studies Xenopus oocytes expressing intestinal H+-coupled peptide cotransporter PepT1 recorded dependence transient charge movements in...

10.1074/jbc.272.12.7777 article EN cc-by Journal of Biological Chemistry 1997-03-01

Abstract Control of extrasynaptic glutamate concentration in the central nervous system is an important determinant neurotransmission and excitotoxicity. Mechanisms that modulate transporter function are therefore critical factors these processes. The redox modulation uptake was examined by measuring transporter‐mediated electrical currents radiolabelled amino acid influx voltage‐clamped Xenopus oocytes expressing human neuronal EAAC1. Up down changes response to treatment with...

10.1111/j.1460-9568.1997.tb01388.x article EN European Journal of Neuroscience 1997-10-01

Transport of nuclear encoded proteins into mitochondria is mediated by multisubunit translocation machineries in the outer and inner membranes mitochondria. The TOM complex contains receptor pore components that facilitate recognition preproteins their transfer through membrane. In addition, a set small proteins. Tom7 Tom6 have been found Neurospora yeast, Tom5 has so far only latter organism. present study, we identified analyzed its function comparison to yeast Tom5, which proposed play...

10.1074/jbc.m413667200 article EN cc-by Journal of Biological Chemistry 2005-02-09
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