Decoding the secrets of spider silk
Eisoldt, L., Smith, A.M. & Scheibel T.
Materials Today 14, 80–86

Recombinant spider silk particles as drug delivery vehicles
Lammel A., Schwab, M, Hofer, M., Winter, G. & Scheibel T.
Biomaterials 32, 2233–2240
doi: 10.1016/j.biomaterials.2010.11.060

pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk – Implications for fiber formation
Hagn, F., Thamm, C., Scheibel, T. & Kessler, H.
Angew. Chem. Int. Ed.,50, 2011
doi: 10.1002/anie.201003795

Spider silk: Understanding the Structure-Function Relationship of a Natural Fiber
Humenik, M., Scheibel, T. & Smith, A.
In: Progress in Molecular Biology and Translational Science, Vol. 103 Molecular Assembly in Natural and Engineered Systems, S. Horworka (ed). Academic Press, London. pp. 131-186

Biomimetic spinning of recombinant silk proteins
Kerl, D., Hardy, J.G. & Scheibel, T.
Mater. Res. Soc. Symp. Proc. 1239, VV07-20

Structural characterization and functionalization of engineered spider silk films
Spiess, K., Wohlrab, S. & Scheibel, T.
Sott Matter, 6, 4168–4174
doi: 10.1039/b927267d

Recombinant spider silk proteins for applications in biomaterials
Spiess, K., Lammel, A., Scheibel, T.
Macromol. Biosciences, 10 (9), 998-1007
doi: 10.1002/mabi.201000071

A conserved spider silk domain acts as a molecular switch that controls fibre assembly
Hagn, F., Eisoldt, L., Hardy, J.G., Vendrely, C., Coles, M., Scheibel, T. & Kessler, H.
Nature, 365, 239-242
doi: 10.1038/nature08936

Controlling silk fibroin particle features for drug delivery
Lammel, A. S., Hu, X., Park, H.-S., Kaplan, D. L. & Scheibel, T.
Biomaterials, 31 (16), 4583-4591
doi: 10.1016/j. biomaterials.2010.02.024

Towards the recombinant production of mussel byssal collagens
Hagenau, A. & Scheibel, T.
J. Adhesion, 86, 10-24
doi: 10.1080/00218460903417701

The role of salt and shear on the storage and assembly of spider silk proteins
Eisoldt, L., Hardy, J. G., Heim, M. & Scheibel, T. R.
J. Struct. Biol., 170, 413–419
doi: 10.1016/j.jsb.2009.12.027

Characterization of recombinantly produced spider flagelliform silk domains
Heim, M., Ackerschott, C. B. & Scheibel, T. R.
J. Struct. Biol., 170, 420–425
doi: 10.1016/j.jsb.2009.12.025

Advanced Biomaterials
Scheibel, T.
Macromolecular Biosciences, 10, 674
doi: 10.1002/mabi.201000195

Composite materials based on silk proteins
Hardy, J.G. & Scheibel, T.R.
Progr. Polymer Sci., 35 (9), 1093-1115
doi:10.1016/j.progpolymsci.2010.04.005

Hierarchical structures made of protein.The complex architecture of spider webs and their constituent silk proteins
Heim, M., Römer, L. & Scheibel, T.
Chem. Soc. Rev., 39, 156–164
doi: 10.1039/b813273a

Silk-based materials for biomedical applications
Leal-Egaña, A. & Scheibel, T.
Biotechnol. Appl. Biochem. 55, 155–167
doi:10.1042/BA20090229

Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM
Suhre, M.H., Hess, S., Golser, A.V., Scheibel, T.R.
J. Inorg. Biochem, 120 (12), 1711-1720
doi:10.1016/j.jinorgbio.2009.09.021    

Interfacial rheological properties of recombinant spider-silk proteins
Vézy, C., Hermanson, K.D., Scheibel, T.R. & Bausch, A.R.
Biointerphases, 4 (3), 43-46
doi: 10.1116/1.3174930

Structural analysis of proteinaceous components in byssal threads of the mussel Mytilus galloprovincialis
Hagenau, A., Scheidt, H.A., Serpell, L., Huster, D. & Scheibel, T.R.
Macromol. Biosciences, 9, 162-168
doi: 10.1002/mabi.200800271

The yeast Sup35NM domain propagates as a prion in mammalian cells
Krammer, C., Kryndushkin, D., Suhre, M.H., Kremmer, E., Hofmann, A., Pfeifer, A., Scheibel, T., Wickner, R., Schätzl, H. & Vorberg, I.
Proc. Natl. Acad. Sci. USA, 106, 462-467
doi: 10.1073/pnas.0811571106

Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion
Pirzer, T., Geisler, M., Scheibel, T. & Hugel, T.
Physical Biol. J., 6, 025004 (8pp)
doi:10.1088/1478-3975/6/2/025004

Functional amyloids used by organisms: A lesson in controlling assembly
Smith A.M. & Scheibel, T.
Macromol. Chem. Phys, 210
doi: 10.1002/macp.200900420

Silk-inspired polymers and proteins
Hardy, J.G. & Scheibel, T.
Biochem. Soc. Trans. 37, 677–681
doi:10.1042/BST0370677

Mimicking biopolymers on a molecular scale: Nano(bio)technology based on engineered proteins
Grunwald, I., Rischka, K., Kast, S.M., Scheibel, T. & Bargel, H.
Phil. Trans. Roy. Soc. London: A, 367, 1727-1747
doi:10.1098/rsta.2009.0012

Production and processing of spider silk proteins
Hardy, J.G. & Scheibel, T.
Journal of Polymer Science: Part A: Polymer Chemistry, 47, 3957–3963
doi: 10.1002/pola.23484

Spider Silk: From Soluble Protein to Extraordinary Fibers
Heim, M., Keerl, D. & Scheibel, T.
Angew. Chem. Int. Ed., 48, 2 – 15
doi: 10.1002/anie.200803341

The elaborate structure of spider silk: Structure and function of a natural high performance fiber
Roemer, L. & Scheibel, T.
Prion 2, 154-161

Spinnenseide: Was Spiderman wissen sollte
Scheibel, T.
BioSpektrum, 15, 23-25

Hierarchical structures made of protein. The complex architecture of spider webs and their constituent silk proteins
Heim, M., Römer, L. & Scheibel, T.
Chem. Soc. Rev., 39, 156–164
doi: 10.1039/b813273a

Formulation of poorly water-soluble substances using self-assembling spider silk protein
Liebmann, B., Hummerich, D., Scheibel, T. & Fehr, M.
Colloids and Surfaces A: Physicochem. Eng. Aspects, Epub ahead of print

Assembly mechanism of recombinant spider silk proteins
Rammensee, S., Slotta, U., Scheibel, T. & Bausch, A.
Proc. Natl. Acad. Sci. USA. 105, 6590-6595

Processing conditions for spider silk microsphere formation
Lammel, A., Schwab, M., Slotta, U., Winter, G. & Scheibel, T.
ChemSusChem 5, 413-416

Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces
Horinek, D., Serr, A., Geisler, M., Pirzer, T., Slotta, U., Lud, S.Q., Garrido, J.A., Scheibel, T., Hugel, T. & Netz, R.R.
Proc. Natl. Acad. Sci. USA. 105, 2842-2847

Influence of Hofmeister salts on the adhesion of spider silk proteins onto hydrophobic substrates: an AFM-based single molecule study
Geisler, M., Pirzer, T., Ackerschott, C., Lud, S., Garrido, J., Scheibel, T. & Hugel, T.
Langmuir 24, 1350-1355

Prion protein/protein interactions: Fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells
Krammer, C., Suhre, M.H., Kremmer, E., Diemer, C., Hess, S., Schätzl, H.M., Scheibel, T. & Vorberg, I.
FASEB J. 22, 762-773

Molecular Design of Performance Proteins with Repetitive Sequences: Recombinant Flagelliform Spider Silk as Basis for Biomaterials
Vendrely, C., Ackerschott, C., Roemer, L. & Scheibel, T.
In: Methods in Molecular Biology, 474, 3-14

The elaborate structure of spider silk: Structure and function of a natural high performance fiber
Roemer, L. & Scheibel, T.
Prion 2, 154-16

Polymeric materials based on silk proteins
Hardy J.G., Roemer, L.M. & Scheibel, T.
Polymer 49, 4309-4327

Spinnen wie die Spinnen
Roemer, L. & Scheibel, T.
Nachrichten aus der Chemie 56, 516-519

Spinnenseidenproteine als pharmazeutischer Hilfsstoff
Weidenauer, U. & Scheibel, T.
Deutsche Apothekerzeitung 148, 3152-3154

Spider silk
Slotta, U., Spieß, K. & Scheibel, T.
In: The Functional Fold. Useful Amyloid Structures in Nature, S. P. Jarvis & A. S. Mostaert (eds). Pan Stanford Publishing, Singapore

Proteins: Polymers of natural origin
Lammel, A., Keerl, D., Römer, L. & Scheibel, T.
In: Biomaterials: Chemistry and Physics, J. Hu, (ed.). pp. 1-22

The elaborate structure of spider silk: Structure and function of a natural high performance fiber
Roemer, L. & Scheibel, T.
T. Scheibel (ed.) In: Fibrous proteins; Landes Biosciences, USA

Transparente Folien aus Spinnenseide - Ein Hocheistungsmaterial aus der Natur in neuem Gewand
Spieß, K., Römer, L.M. &Scheibel, T.
GIT Labor-Fachzeitschrift, 11/2007, pp. 928-931

Permeability of silk microcapsules made by the interfacial adsorption of protein
Hermanson, K.D., Harasima, M.B., Scheibel, T. & Bausch, A.R.
Phys. Chem. Chem. Phys. 9, 6442-6446

Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions
Dong, J., Bloom, J.D., Goncharov, V., Chattopadhyay, M., Millhauser, G.L., Lynn, D.G.,
Scheibel, T. & Lindquist, S.
J. Biol. Chem. 282, 34204-34212

Alternate assembly pathways of the amyloidogenic yeast prion determinant
Sup35p-NM
Hess, S., Lindquist, S. & Scheibel, T.
EMBO Rep. 8,1196-1201

Structural changes of thin films from recombinant spider silk proteins upon post treatment
Metwalli, E., Slotta, U., Darko, C., Roth, S., Scheibel, T. & Papadakis, C.
Applied Physics A 89, 655-661

Biotechnological production of spider silk proteins enables new applications
Vendrely, C. & Scheibel, T.
Macromol. Bioscience 7, 401-409

Effect of OPMD-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1
Lodderstedt, G., Hess, S., Hause, G., Scheuermann, T., Scheibel, T. & Schwarz, E.
FEBS Lett. 274, 346-355

Spider silk’s amphiphilic properties are important for spinning
Exler, J., Huemmerich, D. & Scheibel, T.
Angew. Chem. Int. Ed. 46, 3559-3562

Spider silk and amyloid fibrils – a structural comparison
Slotta, U., Hess, S., Spieß, K., Stromer, T., Serpell, L. & Scheibel, T.
Macromolecular Bioscience 7, 183-188

Engineered microcapsules made of reconstituted spider silk
Hermanson, K., Huemmerich, D., Scheibel, T. & Bausch, A.
Adv. Materials 19, 1810-1815

Conquering isoleucine auxotrophy of Escherichia coli BLR(DE3) to recombinantly produce spider silk proteins in minimal media
Schmidt, M., Romer, L., Strehle, M. & Scheibel, T.
Biotechnol Lett. 29, 1741-1744

Herstellung und Anwendung von Spinnenseide
Roemer, L. & Scheibel, T.
In: Bionik: Patente aus der Natur, A. Kesel, D. Zehren (eds.). 3. Bionik Konferenz 2006, Bremen, pp. 130-139

Folding, self-assembly and conformational switches of proteins.
SenGupta, S. & Scheibel, T.
In: Protein Folding-Misfolding: Some Current Concepts of Protein Chemistry,
J. Zbilut & T. Scheibel (eds.). Nova publisher, pp. 1-33

Films from recombinant spider silk proteins
Huemmerich, D., Slotta U. & Scheibel, T.
Applied Physics A 82, 219-222

Statistical approaches for investigating silk properties
Zbilut, J.P., Scheibel, T., Huemmerich, D., Webber, C.L., Colafranceschi, M. & Giuliani, A.
Applied Physics A 82, 243-251

Preparation and mechanical properties of layers made of recombinant spider silk proteins and silk from silk worm
Junghans, F., Conrad, U., Scheibel, T., Heilmann, A. & Spohn, U.
Applied Physics A 82, 253-260

Rheological characterisation of recombinant spider silk nanofiber networks
Rammensee, S., Huemmerich, D., Hermanson, K., Scheibel, T. & Bausch, A.
Applied Physics A 82, 261-264

Structural analysis of films cast from recombinant spider silk proteins
Slotta, U. Tammer, M., Kremer, F., Koelsch, P. & Scheibel, T.
Supramol. Chem. 18, 465-471

Mechanical properties of recombinant spider silk proteins
Scheibel, T.
Applied Physics A 82, 191-192

Protein aggregation as a cause for disease
Scheibel, T. & Buchner, J.
In: Molecular chaperones in health and disease; Handbook of experimental pharmacology 172, M. Gaestel (ed.). Springer Verlag Berlin Heidelberg, pp. 199-219

Biophysical characterisation of prion proteins
Vendrely, C. & Scheibel, T.
In: Trends in Prion research, B.V. Doupher (ed.). Nova publisher, pp. 251-284

Biosynthesis of an elastin-mimetic polypeptide with two different chemical functional groups within the repetitive elastin fragment
Junger, A., Kaufmann, D. & Scheibel, T.
Macromol. Biosci. 5, 494-501

Spatial stochastic resonance in protein hydrophobicity
Zbilut, J.P., Scheibel, T., Huemmerich, D., Webber, C.L., Colafranceschi, M. & Giuliani, A.
Physics Letters A 346, 33-41

The elongation of yeast prion fibers involves separable steps of association and conversion
Scheibel, T., Bloom, J. & Lindquist, S.
Proc. Natl. Acad. Sci. USA 101, 2287-2292

Primary structure elements of dragline silks and their contribution to protein solubility and assembly
Huemmerich, D., Helsen, C.W., Oschmann, J., Rudolph, R. & Scheibel, T.
Biochemistry 43, 13604-13612

Novel assembly properties of recombinant spider dragline silk protein
Huemmerich, D., Scheibel, T., Vollrath, F., Cohen, S., Gat, U. & Ittah, S.
Curr. Biol. 14, 2070-2074

Amyloid formation of a yeast prion determinant
Scheibel, T.
J. Mol. Neurosci. 23, 13-22

Spider silks: recombinant synthesis, assembly, spinning, and engineering of sythetic proteins
Scheibel, T.
Microbial Cell Factories 3, 14

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