The Fasshauer lab at the Department of Computational Biology in Lausanne strives to understand the mechanisms and evolutionary history of the molecular machine involved in the fusion of transport vesicles with a target compartment.

Research interests

A defining feature of eukaryotic cells is the presence of numerous membrane-bound organelles that subdivide the intracellular space into distinct compartments. Material exchange among most organelles occurs via vesicles that bud off from a source and specifically fuse with a target compartment. How the eukaryotic cell acquired its internal complexity is still poorly understood.

We strive to understand the mechanisms and the evolutionary history of the complex molecular machine that drives this important process. The key factors in vesicle fusion belong to conserved protein families. The core of the machine that drives the fusion of transport vesicles is composed of members of the SNARE protein family. They assemble into tight membrane-bridging complexes to pull two membranes together. Their activity is orchestrated by various other factors including Sec1/Munc18 (SM), Rab, and tethering proteins. Together, they form an ancient molecular machine that diversified during evolution to adapt to the needs of specialized compartments. Rapid exocytosis of neurotransmitters from synaptic vesicles constitutes one of such adaptations, and specific regulatory proteins such as synaptotagmins and complexins evolved in the animal kingdom.

Using biochemical, biophysical, morphological, and bioinformatics approaches we address the following questions:

  • How do SNARE complexes assemble?
  • How is SNARE complex formation controlled by other factors?
  • How are SNARE complexes disassembled after membrane fusion?
  • Do vesicle fusion machines involved in other trafficking steps function in a similar way?
  • How are dysfunctions of the machine linked to disorders?
  • How did vesicle fusion machines of eukaryotes evolve?
  • Is it possible to identify their prokaryotic precursors?
Fasshauer lab secretion

Research technologies

Biochemical & biophysical investigations

To better understand the molecular events underlying vesicular fusion we explore the physicochemical properties of the protein-protein interactions involved. We want to identify the domains involved, locate the binding surfaces and study the affinities, stoichiometries and kinetics of the interactions and their interplay with membranes to disentangle the entire network. For our biochemical studies, we almost exclusively use recombinant proteins. Next to standard biochemical techniques, we employ spectroscopic (circular dichroism and fluorescence spectroscopy) and calorimetric methods. Where feasible we use high-resolution structural techniques.

Munc18 syntaxin complex structure Fasshauer * Munc18 syntaxin 1 complex structure
Munc18 syntaxin interaction Fasshauer * Syntaxin Munc18 interaction by ITC

Bioinformatics investigations

Concomitantly we want to shed light on the evolutionary history of the vesicle fusion machine, which arose from an ancient prototypic mechanism during the rise of the last eukaryotic common ancestor (LECA) from its prokaryotic-like ancestor. We would like to uncover how the mechanism adapted in different eukaryotic lineages and how it was most probably organized in the proto-eukaryotic cell. A particular focus lies on the evolutionary changes of the repertoire of the secretory machine during the rise of animals. Taking advantage of the huge number of available sequence data sets, our group developed a database to store and analyze sequences of the protein families involved in vesicle trafficking. Sequences are analyzed through iterative use of hidden Markov models and tree building.

Four basic types of SNARE proteins Fasshauer * Four basic types of SNARE proteins
EM Monosiga brevicollis Fasshauer * EM Monosiga brevicollis

Morphological & functional investigations

In conjunction, we plan to scrutinize in vivo, the interaction steps that we identified biochemically in vitro. Ultimately we want to correlate the configuration of the (neuro) secretory machinery in the cell with mutations/diseases-related to transport deficiencies. In addition, we are taking a closer look at the very early stages in the evolution of the secretory apparatus by studying the choanoflagellate Monosiga brevicollis and the placozoan Trichoplax adhaerens. Choanoflagellates are a group of mostly single-celled eukaryotes thought to be the closest known sister group to animals; Trichoplax is an animal positioned near the root of the animal tree. It is a simple, free-living marine animal without a nervous system and that glides using cilia to feed on algae. For this, we use, among others, state-of-the-art light and electron microscopy approaches.



Stefani I, Iwaszkiewicz J, Fasshauer D.

Exploring the conformational changes of the Munc18-1/syntaxin 1a complex.

bioRxiv, 2022 Nov


Khalifeh D, Neveu E, Fasshauer D.

Megaviruses contain various genes encoding for eukaryotic vesicle trafficking factors.

Traffic. 2022 Aug; 23(8): 414–425



Donkervoort S, Krause N, Dergai M, Yun P, Koliwer J, Gorokhova S, Geist Hauserman J, Cummings BB, Hu Y, Smith R, Uapinyoying P, Ganesh VS, Ghosh PS, Monaghan KG, Edassery SL, Ferle PE, Silverstein S, Chao KR, Snyder M, Ellingwood S, Bharucha-Goebel D, Iannaccone ST, Dal Peraro M, Reghan Foley A, Savas JN, Bolduc V, Fasshauer D, Bönnemann CG, Schwake M.

BET1 variants establish impaired vesicular transport as a cause for muscular dystrophy with epilepsy

EMBO Mol Med (2021)13:e13787


Romanova DY, Varoqueaux F, Daraspe J, Nikitin MA, Eitel M, Fasshauer D, Moroz LL.

Hidden cell diversity in Placozoa: ultrastructural insights from Hoilungia hongkongensis.

Cell Tissue Res. 2021 Apr 19;10.1007/s00441-021-03459-y


McGrath K, Agarwal S, Tonelli M, Dergai M, Gaeta AL, Shum AK, Lacoste J, Zhang Y, Wen W, Chung D, Wiersum G, Shevade A, Zaichick S, van Rossum DB, Shuvalova L, Savas JN, Kuchin S, Taipale M, Caldwell KA, Caldwell GA, Fasshauer D, Caraveo G.

A conformational switch driven by phosphorylation regulates the activity of the evolutionarily conserved SNARE Ykt6.

Proc Natl Acad Sci U S A. 2021 Mar 23;118(12):e2016730118


Göhde R, Naumann B, Laundon D, Imig C, McDonald K, Cooper BH, Varoqueaux F, Fasshauer D, Burkhardt P.

Choanoflagellates and the ancestry of neurosecretory vesicles.

Philos Trans R Soc Lond B Biol Sci. 2021 Mar 29;376(1821):20190759



Moroz LL, Romanova DY, Nikitin MA, Sohn D, Kohn AB, Neveu E, Varoqueaux F, Fasshauer D.

The diversification and lineage-specific expansion of nitric oxide signaling in Placozoa: insights in the evolution of gaseous transmission.

Sci Rep. 2020 Aug 3;10(1):13020


Kondratiuk I, Jakhanwal S, Jin J, Sathyanarayanan U, Kroppen B, Pobbati AV, Krisko A, Ashery U, Meinecke M, Jahn R, Fasshauer D., Milosevic I.

PI(4,5)P2-dependent regulation of exocytosis by amisyn, the vertebrate-specific competitor of synaptobrevin 2

Proc Natl Acad Sci U S A. 2020 Jun 16;117(24):13468-13479


Neveu E, Khalifeh D, Salamin N, Fasshauer D.

Prototypic SNARE Proteins Are Encoded in the Genomes of Heimdallarchaeota, Potentially Bridging the Gap between the Prokaryotes and Eukaryotes.

Curr Biol. 2020 Jul 6;30(13):2468-2480.e5


Romanova DY, Heyland A, Sohn D, Kohn AB, Fasshauer D, Varoqueaux F, Moroz LL.

Glycine as a signaling molecule and chemoattractant in Trichoplax (Placozoa): insights into the early evolution of neurotransmitters.

Neuroreport. 2020 Apr 8;31(6):490-497



Varoqueaux F, Williams EA, Grandemange S, Truscello L, Kamm K, Schierwater B, Jékely G, Fasshauer D.

High Cell Diversity and Complex Peptidergic Signaling Underlie Placozoan Behavior.

Curr Biol. 2018 Nov 5;28(21):3495-3501.e2



Morey C, Kienle CN, Klöpper TH, Burkhardt P, Fasshauer D.

Evidence for a conserved inhibitory binding mode between the membrane fusion assembly factors Munc18 and syntaxin in animals.

J Biol Chem. 292(50):20449-60


Völker J.M., Dergai M., Abriata L.A., Mingard Y., Ysselstein D., Krainc D., Dal Peraro M., Fischer von Mollard G., Fasshauer D., Koliwer J., Schwake M.

Functional assays for the assessment of the pathogenicity of variants of GOSR2, an ER-to-Golgi SNARE involved in progressive myoclonus epilepsies.

Dis Model Mech. 10(12):1391-1398


Varoqueaux F, Fasshauer D.

Getting Nervous: An Evolutionary Overhaul for Communication.

Annu Rev Genet. 51:455-476

DOI / PMID / Serval


Kienle N., Kloepper T.H., Fasshauer D.

Shedding light on the expansion and diversification of the Cdc48 protein family during the rise of the eukaryotic cell.

BMC Evol Biol. Oct 18;16(1):215

DOI / PMID / AAA Database


Demircioglu F.E., Burkhardt P., Fasshauer D.

The SM protein Sly1 accelerates assembly of the ER–Golgi SNARE complex.

PNAS 111:13828-33


Smith C.L., Varoqueaux F., Kittelmann M., Azzam R.N., Cooper B., Winters C.A., Eitel M., Fasshauer D.*, Reese T.S.*

Novel cell types, neurosecretory cells, and body plan of the early-diverging metazoan Trichoplax adhaerens.

Curr Biol. 24:1565-72. (* co-last authors)

DOI / PMID / UNIL News / Comment in DOI / PMID


Colbert K.N., Hattendorf D.A., Weiss T.M., Burkhardt P., Fasshauer D., Weis W.I.

Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation.

PNAS. 110:12637-42


Honigmann A., van den Bogaart G., Iraheta E., Risselada H.J., Milovanovic D., Mueller V., Müllar S., Diederichsen U., Fasshauer D., Grubmüller H., Hell S.W., Eggeling C., Kühnel K., Jahn R

Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.

Nat Struct Mol Biol. 20:679-86



Jahn R. & Fasshauer D.

Molecular machines governing exocytosis of synaptic vesicles.

Nature 490: 201-7


Klöpper T.H., Kienle N., Fasshauer D., Munro S.

Untangling the evolution of Rab G proteins: implications of a comprehensive genomic analysis.

BMC Biol. 10:71

DOI / PMID / Rab Database

Meijer M.1, Burkhardt P.1, de Wit H., Toonen R.F., Fasshauer D.2, Verhage M.2

Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.

EMBO J. 31(9):2156-68 (1: equally contributing authors; 2: corresponding authors)



Burkhardt P., Stegmann C.M., Cooper B., Kloepper T.H., Imig C., Varoqueaux F., Wahl M.C., Fasshauer D.

Primordial neurosecretory apparatus identified in the choanoflagellate Monosiga brevicollis.

PNAS. 108(37):15264-9

DOI / PMID / New Scientist


Wiederhold K., Kloepper T.H., Walter A.M., Stein A., Kienle N., Sorensen J.B., and Fasshauer D.

A coiled-coil trigger site is essential for rapid binding of synaptobrevin to the SNARE acceptor complex.

J Biol Chem. 285:21549-59


Walter A.M., Wiederhold K., Bruns D., Fasshauer D., and Sørensen J.B.

Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis.

Cell Biol. 188(3):401-13



Winter U., Chen X., Fasshauer D.

A conserved membrane attachment site in α-SNAP facilitates NSF-driven SNARE complex disassembly.

J Biol Chem. 284(46):31817-26


Domanska M.K., Kiessling V., Stein A., Fasshauer D., Tamm L.K.

Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion.

J Biol Chem. 284(46):32158-66


Radhakrishnan A., Stein A., Jahn R., Fasshauer D.

The Ca2+ affinity of synapto-tagmin 1 is markedly increased by a specific interaction of its C2B domain with phosphatidylinositol 4,5-bisphosphate.

J Biol Chem. 284:25749-60


Kienle N., Kloepper T.H., and Fasshauer D.

Differences in the SNARE evolution of fungi and metazoa.

Biochem Soc Trans 37:787-91


Wiederhold K., Fasshauer D.

Is assembly of the SNARE complex enough to fuel membrane fusion?

J Biol Chem. 284:13143-52

DOI / PMID / Comment in DOI / PMID

Kienle N., Kloepper T.H., and Fasshauer D.

Phylogeny of the SNARE vesicle fusion machinery yields insights into the conservation of the secretory pathway in fungi.

BMC Evolutionary Biology 9:19

DOI / PMID / SNARE Database


Bar-On, D., Winter,U., Nachliel, E., Gutman, M., Fasshauer, D., Lang, T., and Ashery, U.

Imaging the assembly and disassembly kinetics of cis-SNARE complexes on native plasma membranes.

FEBS Letters, 582:3563-8


Kloepper T.H., Kienle C.N., and Fasshauer D.

SNAREing the basis of multicellularity: Consequences of protein family expansion during evolution.

Mol.Biol.Evol. 25:2055-68

DOI / PMID / SNARE Database

Burkhardt P., Hattendorf D. A., Weis W. I., Fasshauer D.

Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide.

EMBO J. 27: 923-33


Barszczewski M., Chua J., Stein A., Winter U., Heintzmann R., Zilly F.E., Fasshauer D., Lang T., and Jahn R.

Binding of α-SNAP to syntaxin 1 blocks SNARE-dependent exocytosis.

Mol. Biol. Cell 19:776-84



Stein, A., Radhakrishnan, A., Riedel, D., Fasshauer, D., and Jahn, R

Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids.

Nat. Struct. Mol. Biol. 14: 904-11


Fasshauer, D. & Jahn, R.

Budding insights on cell polarity (News & Views).

Nature Structural & Molecular Biology 14: 360-2


Kloepper, T.H., Kienle, C.N., and Fasshauer, D.

An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system.

Mol. Biol. Cell 18: 3463-71

DOI / PMID / InCytes / SNARE Database

Siddiqui, T.J., Vites, O., Stein, A., Heintzmann, R. Jahn, R., and Fasshauer, D.

Determinants of Synaptobrevin regulation in Membranes.

Mol. Biol. Cell 18: 2037-46

DOI / PMID / InCytes

Zwilling, D., Cypionka, A., Pohl, W., Fasshauer, D., Walla, P.J., Wahl, M.C., and Jahn R.

Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies.

EMBO J. 26: 9-18



Pobbati, A., Stein, A., and Fasshauer, D.

N- to C-terminal SNARE complex assembly promotes rapid membrane fusion.

Science 313: 673-6


Holt, M., Varoqueaux, F., Wiederhold, K., Takamori, S., Urlaub, H., and Fasshauer, D. and Jahn, R.

Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous expression.

J. Biol. Chem. 281: 17076-83


Sorensen JB., Wiederhold, K., Müller EM., Milosevic, I., Nagy, G., de Groot, BL., Grubmüller, H., and Fasshauer, D

Sequential N- to C-terminal ‘zipping-up’ of the SNARE complex drives priming and fusion of secretory vesicles.

EMBO J. 25:955-66



Nagy G., Milosevic I., Fasshauer D., Müller EM., de Groot BL., Lang T., Wilson MC., Sørensen JB.

Alternative Splicing of SNAP-25 Regulates Secretion through Nonconservative Substitutions in the SNARE Domain.

Mol. Biol. Cell 12: 5675-85



Pobbati A., Razeto A., Böddener M., Becker S., Fasshauer D.

A structural basis for the inhibitory role of tomosyn in exocytosis.

J. Biol. Chem. 279: 47192-200 “JBC Paper of the week”


Fasshauer, D. and Margittai, M.

A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly.

J. Biol. Chem. 279: 7613-21



Margittai, M., Widengren, J., Schweinberger, E., Schröder, G.F., Felekyan, E., Haustein, E., König, M., Fasshauer, D., Grubmüller, H., Jahn, R., Seidel, C.A.M.

Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin-1.

PNAS 100: 15516-21


Fasshauer D.

Structural insights into the SNARE mechanism.

BBA - Molecular Cell Research. Special Issue: Membrane Fusion, 1641: 87-97


Hatsuzawa. K., Lang, T., Fasshauer, D., Bruns, D., and Jahn, R.

The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis.

J. Biol. Chem. 278: 31159-66


Reidt, U., Wahl, M.C., Fasshauer, D., Horowitz, D.S., Lührmann, R., and Ficner, R.

Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide.

J. Mol. Biol., 331: 45-56


Margittai, M., Fasshauer, D., Jahn, R., and Langen R.

Habc Domain and SNARE Core Complex Are Connected by a Flexible Linker.

Biochemistry, 42: 4009-14



Fasshauer, D., Antonin, W., Subramaniam, V., and Jahn, R.

SNARE assembly and disassembly exhibit a pronounced hysteresis.

Nat. Struct. Biol. 9: 144-151

DOI / PMID / Commented in DOI / PMID

Antonin, W., Fasshauer, D., Becker, S., Jahn, R., and Schneider, T.R.

Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs.

Nat. Struct. Biol. 9: 107-111


Pabst, S., Margittai, M., Vainius, D., Langen, R., Jahn, R., and Fasshauer, D.

Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis.

J. Biol. Chem. 277: 7838-48



Margittai, M., Fasshauer, D., Pabst, S., Jahn, R., and Langen, R.

Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling.

J. Biol. Chem. 276: 13169-77



Antonin, W, Holroyd, C, Fasshauer, D, Pabst, S, Fischer Von Mollard, G, Jahn, R.

A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function.

EMBO J. 19:6453-64


Pabst, S., Hazzard, J.W., Antonin, W., Südhof, T.C., Jahn, R., Rizo, J., Fasshauer, D.

Selective interaction of complexin with the neuronal SNARE complex: determination of the binding regions.

J. Biol. Chem. 275:19808-18



Davis, A.F., Bai, J., Fasshauer, D., Wolowick, M.J., Lewis, J.L., and Chapman, E.R.

Kinetics of Synaptotagmin Respones to Ca2+ and Assembly with the Core SNARE Complex onto Membranes.

Neuron 24: 363-76


Fasshauer, D., Antonin, W., Margittai, M., Pabst, S., and Jahn, R.

Mixed and non-cognate SNARE complexes.

J. Biol. Chem. 274: 15440-46



Fasshauer, D., Sutton, R.B., Brünger, A.T. and Jahn, R.

Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs.

Proc. Natl. Acad. Sci. USA 95: 15781-86


Sutton, R.B., Fasshauer, D., Jahn, R., and Brünger, A.T.

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution.

Nature 395: 347-353

DOI / PMID / Comment in DOI / PMID

Fasshauer, D., Eliason, W.K., Brünger, A.T., and Jahn, R.

Identification of a minimal core of the synaptic SNARE-complex sufficient for reversible assembly and disassembly.

Biochemistry 37: 10345-55



Fasshauer, D., Otto, H., Eliason, W. K., Jahn, R., and Brünger, A.T.

Structural changes are associated with SNARE complex formation.

J. Biol. Chem. 272, 28036-41


Fasshauer, D., Bruns, D., Shen, B., Jahn, R., and Brünger, A.T.

A structural change occurs upon binding of syntaxin to SNAP-25.

J. Biol. Chem. 272: 4582-90



Nickel W, Kipper N, Barthel A, Kahn RA, Fasshauer D, Söling HD

ARF and VAPP14: two proteins involved in the delivery of heparan sulfate proteoglycan from the trans-Golgi network to the plasma membrane.

Ann N Y Acad Sci. 733:344-56


Nickel W., Huber L.A., Kahn R.A., Kipper N., Barthel A., Fasshauer D., and Söling H.D.

ADP ribosylation factor and a 14-kD polypeptide are associated with heparan sulfate-carrying post-trans-Golgi network secretory vesicles in rat hepatocytes.

J. Cell Biol. 125: 721-32

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DNF Publications


Eitel M, Francis WR, Varoqueaux F, Daraspe J, Osigus HJ, Krebs S, Vargas S, Blum H, Williams GA, Schierwater B, Wörheide G.

Comparative genomics and the nature of placozoan species.

PLoS Biol. 2018 Jul 31;16(7):e2005359



Hoon M, Krishnamoorthy V, Gollisch T, Falkenburger B, Varoqueaux F.

Loss of Neuroligin3 specifically downregulates retinal GABAAα2 receptors without abolishing direction selectivity.

PLoS One. 2017 Jul 14;12(7):e0181011


Book chapters and conference reports


Fasshauer, D., Schütte, C. and Jahn, R.

82nd International Titisee Conference held from October 25 to 29, 2000. Mechanisms of membrane fusion.

B.I.F. FUTURA Vol. 16, No. 1, 13-23 (Conference report)

Download PDF


Fasshauer, D. und Jahn, R.

Mechanismen intrazellulärer Membranfusion.

Biospektrum No. 1, 2731 (review article; german)

Download PDF


Winter, U. & Fasshauer, D.

Mechanism of SNARE assembly and disassembly.

Landes Bioscience (Book chapter)

Download PDF


Group members

Dirk Fasshauer Associate Professor

Dirk Fasshauer

Associate Professor

Dirk Fasshauer studied biology and received his doctorate degree from the University of Göttingen in 1994. He worked as a post-doctoral fellow at Yale University from 1995 to 1997 and then moved to the Max Planck Institute for Biophysical Chemistry in Göttingen and from 2002, headed the “Structural Biochemistry” Research Group in the Department of Neurobiology. In 2009 he joined the DNF as associate professor.

Aisima Chatzi Souleiman

Aisima Chatzi Souleiman

Postdoctoral Fellow

Aisima studied Chemical and Biological Engineering at Koc University, Turkey. In her doctoral thesis, she dealt with finding allosteric networks in proteins and nanobody modeling. In 2020, she started as a postdoc at the Barth Lab, EPFL, where she studied reprogramming and modeling signaling properties in de-novo proteins. She joined the group as a postdoc in 2022.

Carlos Pulido Quetglas

Carlos Pulido Quetglas

Postdoctoral Fellow

Carlos received a BSc in Biology from the University of the Balearic Islands in 2014. Then he completed his master in Bioinformatics in 2017 at University Pompeu Fabra in Barcelona. In 2021, he finished his PhD in Biomedical Sciences at the University of Bern, where he worked on NGS analysis of cancer cell lines and designs of CRISPR-Cas9 libraries. In October 2021, he joined the group as a Postdoc.

Iman Bentahar

Iman Bentahar

PhD student

Iman obtained her B.Sc. in Biochemistry in June 2016 at the Mohamed Khidher University in Algeria.Then, she obtained her Master in Molecular biology, Immunology, and Microbiology Specialities at the Eotvos Lorand University, Hungary. She started her PhD thesis in November 2020.

Michela Dall’Angelo

Michela Dall’Angelo

PhD student

Michela studied Molecular and Medical biotechnology and received her Master's degree in March 2020 at the University of Verona, Italy, with a bioinformatic thesis about RNA sequencing analysis on lymphoma cancer. She started her PhD in August 2020.

Deepak Yadav

Deepak Yadav

PhD student

Deepak received his Master's degree in Bioinformatics from IIIT Hyderabad in 2013. He worked as a researcher at TRDDC (TCS Research) Pune from 2013 to 2020, with the research focus on NGS analysis, metagenomics and network biology. He started his PhD thesis in November 2020.





Snare DB Overview

In the SNAREs section of the database you have the possibility to view our classified sequences (SNAREs -> View DB) or to de novo classify protein sequences (SNAREs -> Find Motif). If you choose to view our classified sequences, you find additional information for each of the fields on the ViewDB site by clicking the question mark behind the field. If you choose to de novo classify protein sequences you may paste any protein sequence into the text field of the Find Motif site and hit the Submit-button. The results will be displayed shortly after.

Snare DB


AAA DB Overview

In the AAAs section of the database you have the possibility to view our classified sequences (AAAs -> View Database) or to de novo classify protein sequences (AAAs -> Scan Sequence against HMMs). If you choose to view our classified sequences, you find additional information for each of the fields on the ViewDB site by clicking the question mark behind the field. If you choose to de novo classify protein sequences you may paste any protein sequence into the text field of the Find Motif site and hit the Submit-button. The results will be displayed shortly after.



RAB DB Overview

In the Rabs section of the database you have the possibility to view our classified sequences (Rabs -> View Database) or to de novo classify protein sequences (Rabs -> Scan Sequence against HMMs). If you choose to view our classified sequences, you find additional information for each of the fields on the ViewDB site by clicking the question mark behind the field. If you choose to de novo classify protein sequences you may paste any protein sequence into the text field of the Find Motif site and hit the Submit-button. The results will be displayed shortly after.




UNIL Génopode
CH-1015 Lausanne

Dirk Fasshauer

Email: dirk.fasshauer [ at ]
Phone: +41 21 692 4282