Publications

List of Publications

40.        Guixà-González R, Albasanz JL, Rodriguez-Espigares I, Pastor M, Sanz F, Martí-Solano M, Manna5 M, Martinez-Seara H, Hildebrand PW, Martín M and Selent J: Access of membrane cholesterol to a G protein coupled receptor (2017) Nature Commun., 8:14505

39.        Ismer J, Rose AS, Tiemann JK, Goede A, Preissner R, Hildebrand PW.: SL2: an interactive webtool for modeling of missing segments in proteins (2017) Nucleic Acids Res, 8;44(W1):W390-4.

38.        Sprink T., Ramrath D, Yamamoto H., Yamamoto K., Loerke J., Ismer J., Hildebrand P.W., Scheerer P., Bürger J., Mielke T. and Spahn CMT (2016) Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association, Science Advances, 2(3):e1501502

37.        Rose A., Zacchariae U., Grubmüller H., Hofmann K.P., Scheerer P. and Hildebrand P.W. (2015) Role of Structural Dynamics at the Receptor G Protein Interface for Signal Transduction, PLoS ONE, 10(11):e0143399

36.        Yamamoto H., Collier M., Loerke J., Ismer J., et al., Hildebrand P.W., Scheerer P. and Spahn C.M.T. (2015), Molecular architecture of the ribosome-bound Hepatitis C virus internal ribosomal entry site RNA, EMBOJ, 34(24):3042-58

35         Barucker C. et al., Hildebrand P.W. McKinney A. and Multhaup G. (2015) Aβ42-oligomer interacting peptides (AIPs) render toxic amyloid-β42 species non-toxic and suppress the formation of fibrils, Sci Rep, 29;5:15410

34.        Brehm, A., et al., Hildebrand P.W., Brogan P., Krüger E., Aksentijevich I., Goldbach-Mansky R. (2015) Diverse proteasome subunit mutations link proteasome dysfunction and Type I interferon induction in CANDLE/PRAAS, J Clin Invest, 125(11):4196-211

33.        Prade E., Bittner H.J., Sarkar R., Amo J.M.L., Althoff-Ospelt G., Hildebrand P.W. and Reif B. (2015) Structural mechanism of the interaction of Alzheimer's disease Aβ fibrils with the NSAID sulindac sulfide, JBC, 290(48):28737-45.

32.        Kazmin R, Rose A, Szczepek M, Elgeti M, Ritter E, Piechnick R, Hofmann K.P., Scheerer P and Hildebrand P.W. and Bartl (2015) The activation pathway of human rhodopsin in comparison to bovine rhodopsin, JBC, 290(33):20117-27

31.        Rose, A. S. and Hildebrand P.W. (2015) A web application for molecular visualization, Nucleic Acids Res, 41, D576-9.

30.        Österreich, F., Bittner, H., Weise, C., Grohmann, L., Janke, L. K., Hildebrand, P.W., Multhaup, G., Munter, L. (2015) Impact of Amyloid Precursor Protein Hydrophilic Transmembrane Residues on Amyloid-beta Generation, Biochemistry, 17, 2777-84.

29.        Sommer, M. E., Elgeti, M., Hildebrand, P. W., Szczepek, M., Hofmann, K. P and Scheerer, P (2015) Structure-based biophysical analysis of the interaction of rhodopsin with G Protein and arrestin, Methods Enzymol., 556, 563-608.

28.        Szczepek, M., Beyrière, F., Hofmann, K. P., Elgeti, M., Kazmin, R., Rose, A., Bartl, F. J., Stetten von, D., Heck, M., Sommer, M. E., Hildebrand, P. W. and Scheerer, P (2014) Crystal structure of a common GPCR binding interface for G protein and arrestin, Nat. Commun., 10, 4801.

27.        Rose A.S., Elgeti M., Zacchariae U., Grubmüller H., Hofmann K.P., Scheerer P. and Hildebrand P.W. (2014) Position of transmembrane helix 6 determines receptor g protein coupling specificity. J Am Chem Soc, 32, 11244-7.

26.        Barucker C., Harmeier A., Weiske J., Fauler B., Albring K.F., Prokop S., Hildebrand P.W., Lurz R., Heppner F.L., Huber O., Multhaup G. (2014) Nuclear translocation uncovers the amyloid Peptide aβ42 as a regulator of gene transcription, J Biol Chem, 29, 20182-91.

25.        Budkevich T.V., Giesebrecht J., Ramrath D., Mielke T., Ismer J., Hildebrand P.W., Tung C.S., Nierhaus K.H., Sanbonmatsu K.Y. and Spahn C.M.T., Regulation of the mammalian elongation cycle by 40S subunit rolling: a eukaryotic-specific ribosome rearrangement, Cell, 1, 121-31.

24.        Munter L.M., Sieg H., Bethge T., Liebsch F., Bierkandt F.S., Schleeger M., Bittner H.J., Heberle J., Jakubowski N. and Hildebrand P.W., Multhaup G. (2013) Model peptides uncover the role of the BACE1 transmembrane sequence in metal-ion mediated oligomerization, J Am Chem Soc, 51, 19354-61.

23.        Rose, A., Theune, D., Goede, A. and Hildebrand, P.W. (2013) MP:PD - A data base of internal packing densities, internal waters and internal cavities in helical membrane proteins. Nucleic Acids Res, 42, D347-51.

22.        Elgeti M., Rose A.S., Bartl F.J., Hildebrand P.W., Hofmann K.P. and Heck M. (2013) Precision vs. flexibility in GPCR signalling. J Am Chem Soc, 33, 12305-12.

21.        Ismer, J., Rose, A., Goede, A., Johanna K. S. Tiemann, Rother, K. and Hildebrand, P.W. (2012) Voronoia4RNA - A database of atomic packing densities of RNA structures and their complexes. Nucleic Acids Res, 41, D280-4.

20.        Kaden,D., Harmeier, A., Weise, C., Munter, L.M., Althoff, V., Rost, B.R., Hildebrand, P.W., Schmitz, D., Schaefer, M., Lurz, R., et al. (2012) Novel APP/Aβ mutation K16N produces highly toxic heteromeric Aβ oligomers. EMBO Mol Med, 7, 647-59.

19.        Piechnick, R., Ritter, E., Hildebrand, P.W., Ernst, O.P., Scheerer, P., Hofmann, K. and Heck, M. (2012) The effect of channel mutations on the uptake and release of the retinal ligand in opsin. Proc Natl Acad Sci U S A, 109, 5247-52.

18.        Botev, A., Munter, L.M., Wenzel, R., Richter, L., Althoff, V., Ismer, J., Gerling, U., Weise, C., Koksch, B., Hildebrand, P.W. et al. (2011) The Amyloid Precursor Protein C-Terminal Fragment C100 Occurs in Monomeric and Dimeric Stable Conformations and Binds gamma-Secretase Modulators. Biochemistry, 50, 828-35.

17.        Muhs, M., Yamamoto, H., Ismer, J., Takaku, H., Nashimoto, M., Uchiumi, T., Nakashima, N., Mielke, T., Hildebrand, P.W., Nierhaus, K.H. et al. (2011) Structural basis for the binding of IRES RNAs to the head of the ribosomal 40S subunit. Nucleic Acids Res., 39, 5264-75.

16.        Ratje, A.H., Loerke, J., Mikolajka, A., Brunner, M., Hildebrand, P.W., Starosta, A.L., Donhofer, A., Connell, S.R., Fucini, P., Mielke, T. et al. (2010) Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites. Nature, 468, 713-716.

15.        Richter, L., Munter, L.M., Ness, J., Hildebrand, P.W., Dasari, M., Unterreitmeier, S., Bulic, B., Beyermann, M., Gust, R., Reif, B. et al. (2010) Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization. Proc Natl Acad Sci U S A, 107, 14597-14602.

14.        Rose, A., Goede, A. and Hildebrand, P.W. (2010) MPlot--a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins. Nucleic Acids Res, 38, W602-8.

13.        Munter, L.M., Botev, A., Richter, L., Hildebrand, P.W., Althoff, V., Weise, C., Kaden, D. and Multhaup, G. (2010) Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GxxxG motif. J Biol Chem, 285, 21636-21643.

12.        Hildebrand, P.W., Scheerer, P., Park, J.H., Choe, H.W., Piechnick, R., Ernst, O.P., Hofmann, K.P. and Heck, M. (2009) A ligand channel through the G protein coupled receptor opsin. PLoS ONE, 4, e4382.

11.        Scheerer, P., Heck, M., Goede, A., Park, J.H., Choe, H.W., Ernst, O.P., Hofmann, K.P. and Hildebrand, P.W. (2009) Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface. Proc Natl Acad Sci U S A, 106, 10660-10665.

10.        Harmeier, A., Wozny, C., Rost, B.R., Munter, L.M., Hua, H., Georgiev, O., Beyermann, M., Hildebrand, P.W., Weise, C., Schaffner, W. et al. (2009) Role of amyloid-beta glycine 33 in oligomerization, toxicity, and neuronal plasticity. J Neurosci, 29, 7582-7590.

9.         Rose, A., Lorenzen, S., Goede, A., Gruening, B. and Hildebrand, P.W. (2009) RHYTHM--a server to predict the orientation of transmembrane helices in channels and membrane-coils. Nucleic Acids Res, 37, W575-580.

8.         Hildebrand, P.W., Goede, A., Bauer, R.A., Gruening, B., Ismer, J., Michalsky, E. and Preissner, R. (2009) SuperLooper--a prediction server for the modeling of loops in globular and membrane proteins. Nucleic Acids Res, 37, W571-574.

7.         Hofmann, K.P., Scheerer, P., Hildebrand, P.W., Choe, H.W., Park, J.H., Heck, M. and Ernst, O.P. (2009) A G protein-coupled receptor at work: the rhodopsin model. Trends Biochem Sci, 34, 540-552.

6.         Rother, K., Hildebrand, P.W., Goede, A., Gruening, B. and Preissner, R. (2009) Voronoia: analyzing packing in protein structures. Nucleic Acids Res, 37, D393-395.

5.         Scheerer, P., Park, J.H., Hildebrand, P.W., Kim, Y.J., Krauss, N., Choe, H.W., Hofmann, K.P. and Ernst, O.P. (2008) Crystal structure of opsin in its G-protein-interacting conformation. Nature, 455, 497-502.

4.         Hildebrand, P.W., Gunther, S., Goede, A., Forrest, L., Frommel, C. and Preissner, R. (2008) Hydrogen-bonding and packing features of membrane proteins: functional implications. Biophys J, 94, 1945-1953.

3.         Hildebrand, P.W., Lorenzen, S., Goede, A. and Preissner, R. (2006) Analysis and prediction of helix-helix interactions in membrane channels and transporters. Proteins, 64, 253-262.

2.         Hildebrand, P.W., Rother, K., Goede, A., Preissner, R. and Frommel, C. (2005) Molecular packing and packing defects in helical membrane proteins. Biophys J, 88, 1970-1977.

1.         Hildebrand, P.W., Preissner, R. and Frömmel, C. (2004) Structural features of transmembrane helices. FEBS Lett, 559, 145-151.

letzte Änderung: 01.06.2017