SFB 1243 Cancer Evolution

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Hopfner, Karl-Peter

Prof. Dr. Karl-Peter Hopfner

Genzentrum, Department Biochemie, Ludwig-maximilians-Universität München


Department Biochemie
Ludwig-Maximilians-Universität München
Feodor-Lynen-Str. 25
81377 München

Phone: +49 (0)89 2180-76953

Website: Gene Center: Structural Molecular Biology

Work group

A10 Identifying and targeting escape mechanisms in AML using multispecific antibody derivatives

10 major publications related to project

Civril F, Deimling T, de Oliveira Mann CC, Ablasser A, Moldt M, Witte G, Hornung V and Hopfner KP (2013). Structural mechanism of cytosolic DNA sensing by cGAS. Nature, 498, 332-7.

Motz C, Schuhmann KM, Kirchhofer A, Moldt M, Witte G, Conzelmann KK and Hopfner KP (2013). Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science, 339, 690-3.

Tosi A, Haas C, Herzog F, Gilmozzi A, Berninghausen O, Ungewickell C, Gerhold CB, Lakomek K, Aebersold R, Beckmann R and Hopfner KP (2013). Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex. Cell, 154, 1207-19.

Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP and Hopfner KP (2012). Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat Struct Mol Biol., 19, 693-700.

Lammens K, Bemeleit DJ, Möckel C, Clausing E, Schele A, Hartung S, Schiller CB, Lucas M, Angermüller C, Söding J, Strässer K and Hopfner KP (2011). The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair. Cell, 145, 54-66.

Wollmann P, Cui S, Viswanathan R, Berninghausen O, Wells MN, Moldt M, Witte G, Butryn A, Wendler P, Beckmann R, Auble DT and Hopfner KP (2011). Structure and mechanism of the Swi2/Snf2 remodeller Mot1 in complex with its substrate TBP. Nature, 475, 403-7.

Myong S*, Cui S, Cornish PV, Kirchhofer A, Gack MU, Jung JU, Hopfner KP* and Ha T* (2009). Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA. Science, 323, 1070-4. *co-corresponding

Cui S, Eisenächer K, Kirchhofer K, Brzózka K, Lammens A, Lammens K, Fujita T, Conzelmann K, Krug A and Hopfner KP (2008). The regulatory domain is the triphosphate sensor of RIG-I. Molecular Cell, 29, 169-179.

Witte G, Hartung S, Büttner K, and Hopfner KP (2008). Structural biochemistry of a bacterial checkpoint protein reveals di-adenylate cyclase activity regulated by recombination intermediates. Molecular Cell, 30, 167-178.

Dürr H, Körner C, Müller M, Hickmann V and Hopfner KP (2005). X-Ray Structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase Core and Its Complex with DNA. Cell, 121, 363-373.