Reinhard Jahn

ORCID: 0000-0003-1542-3498
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Cellular transport and secretion
  • Lipid Membrane Structure and Behavior
  • Neuroscience and Neuropharmacology Research
  • Erythrocyte Function and Pathophysiology
  • Photoreceptor and optogenetics research
  • Endoplasmic Reticulum Stress and Disease
  • Ion channel regulation and function
  • Botulinum Toxin and Related Neurological Disorders
  • Calcium signaling and nucleotide metabolism
  • Retinal Development and Disorders
  • Neurological disorders and treatments
  • Microtubule and mitosis dynamics
  • Pancreatic function and diabetes
  • Receptor Mechanisms and Signaling
  • Biochemical and Structural Characterization
  • Biotin and Related Studies
  • Force Microscopy Techniques and Applications
  • RNA and protein synthesis mechanisms
  • Mitochondrial Function and Pathology
  • Glycosylation and Glycoproteins Research
  • Supramolecular Self-Assembly in Materials
  • Photosynthetic Processes and Mechanisms
  • Advanced biosensing and bioanalysis techniques
  • Advanced Fluorescence Microscopy Techniques
  • RNA Interference and Gene Delivery

Max Planck Institute for Biophysical Chemistry
2016-2025

Massachusetts Institute of Technology
2025

Health Net
2025

Max Planck Society
2008-2024

Max Planck Institute for Multidisciplinary Sciences
2021-2024

University of Göttingen
1980-2023

Nanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103
2023

Friedrich Schiller University Jena
2023

Tissue Dynamics (Israel)
2021

Max Planck Institute of Experimental Medicine
2016-2017

SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] proteins are essential for membrane and conserved from yeast to humans. Sequence alignments of the most regions were mapped onto recently solved crystal structure heterotrimeric synaptic complex. The association four alpha-helices in complex produces highly layers interacting amino acid side chains center four-helix bundle. Mutations these reduce stability cause defects traffic even distantly related...

10.1073/pnas.95.26.15781 article EN Proceedings of the National Academy of Sciences 1998-12-22

Neurons release neurotransmitters by calcium-dependent exocytosis of synaptic vesicles. However, the molecular steps transducing calcium signal into membrane fusion are still an enigma. It is reported here that synaptotagmin, a highly conserved vesicle protein, binds at physiological concentrations in complex with negatively charged phospholipids. This binding specific for and involves cytoplasmic domain synaptotagmin. Calcium dependent on intact oligomeric structure synaptotagmin (it...

10.1126/science.1589771 article EN Science 1992-05-15

A protein with an apparent molecular mass of 38,000 daltons designated p38 was found in synaptic vesicles from rat brain. The subcellular distribution and some its properties were determined the aid polyclonal monoclonal antibodies. similar to that synapsin I, a synaptic-vesicle specific phosphoprotein. vesicle fraction purified by controlled-pore glass bead chromatography showed enrichment more than 20-fold over crude homogenate. Immunostaining sections through various brain regions...

10.1073/pnas.82.12.4137 article EN Proceedings of the National Academy of Sciences 1985-06-01

Using quick-freeze/deep-etch electron microscopy of recombinant proteins adsorbed to mica, we show that NSF, the oligomeric ATPase involved in membrane fusion, is a hollow 10 × 16 nm cylinder whose conformation depends upon nucleotide binding. Depleted nucleotide, NSF converts "splayed" protease-sensitive reveals its subunit composition. NSF's synaptic substrate, ternary SNARE complex containing syntaxin, SNAP-25, and synaptobrevin, 4 14 rod with "tail" at one end, corresponding N-terminus...

10.1016/s0092-8674(00)80512-7 article EN cc-by-nc-nd Cell 1997-08-01

We present video-rate (28 frames per second) far-field optical imaging with a focal spot size of 62 nanometers in living cells. Fluorescently labeled synaptic vesicles inside the axons cultured neurons were recorded stimulated emission depletion (STED) microscopy 2.5-micrometer by 1.8-micrometer field view. By reducing cross-sectional area about factor 18 below diffraction limit (260 nanometers), STED allowed us to map and describe vesicle mobility within highly confined space boutons....

10.1126/science.1154228 article EN Science 2008-02-22

An intrinsic membrane protein of brain synaptic vesicles with Mr 38,000 (p38, synaptophysin) has recently been partially characterized (Jahn, R., W. Schiebler, C. Ouimet, and P. Greengard, 1985, Proc. Natl. Acad. Sci. USA, 83:4137-4141; Wiedenmann, B., Franke, Cell, 41:1017-1028). We have now studied the presence p38 in a variety tissues by light electron microscopy immunocytochemistry immunochemistry. Our results indicate that, within nervous system, p38, like neuron-specific phosphoprotein...

10.1083/jcb.103.6.2511 article EN The Journal of Cell Biology 1986-12-01

We demonstrate far-field fluorescence microscopy with a focal-plane resolution of 15–20 nm in biological samples. The 10- to 12-fold multilateral increase below the diffraction barrier has been enabled by elimination molecular triplet state excitation as major source photobleaching number dyes stimulated emission depletion microscopy. Allowing for relaxation between subsequent excitation–depletion cycles yields an up 30-fold total signal compared reported illumination schemes. Moreover, it...

10.1073/pnas.0604965103 article EN Proceedings of the National Academy of Sciences 2006-07-25
Coming Soon ...