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1.
Schmid, P.W.N.* et al.: Imbalances in the eye lens proteome are linked to cataract formation. Nat. Struct. Mol. Biol. 28, 143–151 (2021)
2.
Zhang, M.* et al.: Cryo-EM structure of an activated GPCR-G protein complex in lipid nanodiscs. Nat. Struct. Mol. Biol. 28, 258-267 (2021)
3.
Vogl, A.M.* et al.: Publisher Correction: Global site-specific neddylation profiling reveals that NEDDylated cofilin regulates actin dynamics (Nature Structural & Molecular Biology, (2020), 27, 2, (210-220), 10.1038/s41594-019-0370-3). Nat. Struct. Mol. Biol., DOI: 10.1038/s41594-020-0395-7 (2020)
4.
Vogl, A.M.* et al.: Global site-specific neddylation profiling reveals that NEDDylated cofilin regulates actin dynamics. Nat. Struct. Mol. Biol. 27, 210-220 (2020)
5.
Beltran, M.* et al.: G-tract RNA removes Polycomb repressive complex 2 from genes. Nat. Struct. Mol. Biol. 26, 899-909 (2019)
6.
Beltran, M.* et al.: Author Correction: G-tract RNA removes Polycomb repressive complex 2 from genes (Nature Structural & Molecular Biology, (2019), 26, 10, (899-909), 10.1038/s41594-019-0293-z). Nat. Struct. Mol. Biol., DOI: 10.1038/s41594-019-0341-8 (2019)
7.
Kaiser, C.J.O.* et al.: The structure and oxidation of the eye lens chaperone αA-crystallin. Nat. Struct. Mol. Biol. 26, 1141-1150 (2019)
8.
Hanna, C.W.* et al.: MLL2 conveys transcription-independent H3K4 trimethylation in oocytes. Nat. Struct. Mol. Biol. 25, 73-82 (2018)
9.
Edelmann, F. et al.: Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex. Nat. Struct. Mol. Biol. 24, 152-161 (2017)
10.
Kebede, A.F.* et al.: Histone propionylation is a mark of active chromatin. Nat. Struct. Mol. Biol. 24, 1048–1056 (2017)
11.
Marjanović, M.P.* et al.: MacroH2A1.1 regulates mitochondrial respiration by limiting nucleas NAD+ consumption. Nat. Struct. Mol. Biol. 24, 902-910 (2017)
12.
Anvarian, Z.* et al.: Axin cancer mutants form nanoaggregates to rewire the Wnt signaling network. Nat. Struct. Mol. Biol. 23, 324-332 (2016)
13.
Zierer, B.K.* et al.: Importance of cycle timing for the function of the molecular chaperone Hsp90. Nat. Struct. Mol. Biol. 23, 1020-1028 (2016)
14.
Mainz, A.* et al.: The  chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client Nat. Struct. Mol. Biol. 22, 898-905 (2015)
15.
Schlundt, A. et al.: Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation. Nat. Struct. Mol. Biol. 21, 671-678 (2014)
16.
Höfig, K.P. et al.: Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay. Nat. Struct. Mol. Biol. 20, 73-81 (2013)
17.
Holdermann, I.* et al.: Chromodomains read the arginine code of post-translational targeting. Nat. Struct. Mol. Biol. 19, 260-263 (2012)
18.
de Almeida, S.F.* et al.: Splicing enhances recruitment of methyltransferase HYPB/Setd2 and methylation of histone H3 Lys36. Nat. Struct. Mol. Biol. 18, 977-984 (2011)
19.
Koch, F.* et al.: Transcription initiation platforms and GTF recruitment at tissue-specific enhancers and promoters. Nat. Struct. Mol. Biol. 18, 956-963 (2011)
20.
Tripsianes, K. et al.: Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins. Nat. Struct. Mol. Biol. 18, 1414-1420 (2011)