How to find us How to contact us General Lab Research News Feed Undergrad Student Link Links
General Lab Research Research Projects Hsp104 / Molecular Disaggregase Research Projects Hsp93 / Chloroplast Import Publication List Job Offers
Equipment and Techniques/Methods (Absorbance, Fluoresecence, Gel Electrophoresis, Optical measurements, LASER, Time-resolved flourscence decay, Protein expression and purification, Molecular biology, Yeast genetics, Yeast Cell biology, Analytical ultracentrifugation, Arabidopsis biology)
PI. / CV Lab Members Former Lab Members
Publications Announcements Talks Safety Teaching
Open positions and projects Applications forms and how to apply Positions for PostDocs Positions for PhDs Undergraduate/Rotation Student Projects What you will use and learn How to find us How to contact us
Open positions and projects Undergraduate/Rotation Student Projects Application forms and How to Apply What you will use and learn Teaching
Dr. Stefan Walter
Assistant Professor
sgwalter@umich.edu

Office
4140A Nat. Sci.
830 N. University
Ann Arbor, MI 48103
(734) 764-1341

Lab
4140 Nat. Sci.
(734) 936-2973
Research > Publication List

Publications

Franzmann TM, Czekalla A, Walter SG. (2011). The regulatory circuits of the AAA+ disaggregase HSP104. J Biol Chem. . [Epub ahead of print]. Read Publication.

Gu L, Eisman EB, Dutta S, Franzmann TM, Walter S, Gerwick WH, Skiniotis G, Sherman DH. (2011). Tandem acyl carrier proteins in the curacin biosynthetic pathway promote consecutive multienzyme reactions with a synergistic effect. Angew Chem Int Ed Engl. . 50 2795-8. Read Publication.

Franzmann, T.M., Menhorn, P., Walter, S., & Buchner, J. (2008). Activation of the Chaperone Hsp26 Is Controlled by the Rearrangement of Its Thermosensor Domain. Mol. Cell. 29, 207-216. Read Publication.

Schaupp, A., Marcinowski, M. Grimminger, V., Bösl, B., & Walter, S. (2007). Protein Processing by the Molecular Chaperone Hsp104. J. Mol. Biol. 370, 674-686. Read Publication.

Bösl, B., Grimminger, V. & Walter S. (2006). The Molecular Chaperone Hsp104 - A Molecular Machine for Protein Disaggregation. J. Struct. Biol. 156: 139-148. Read Publication.

Narayanan, S., Walter, S. & Reif, B. . (2006). Yeast prion protein Sup35 fibril formation proceeds via addition and subtraction of oligomers. ChemBioChem. 7, 757-765.

Bösl, B., Grimminger, V. & Walter S. (2005). Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J. Biol. Chem. 280: 38170-38176. Read Publication.

Catharino, S., Buchner, J. & Walter S.. (2005). Characterization of oligomeric intermediates in the fibrilization pathway of the yeast prion Ure2p. Biol. Chem. 386: 633-641. Read Publication.

Haslbeck, M., Miess, A., Stromer, T., Walter, S. & Buchner J. (2005). Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J. Biol. Chem. 280: 23861-8. Read Publication.

Franzmann, T.M., Wühr, M., Richter, K., Walter, S. & Buchner J. . (2005). The Activation Mechanism of Hsp26 does not Require Dissociation of the Oligomer. J. Mol. Biol. 350: 1083-93. Read Publication.

Richter, K., Walter, S. & Buchner, J. (2004). The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 342: 1403-1413. Read Publication.

Grimminger, V., Richter, K., Imhof, A., Buchner, J. & Walter S.. (2004). The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J. Biol. Chem. 279: 7378-7383. Read Publication.

News Feed