Startseite UR
Einträge von Heizinger, Leonhard auf dem Publikationsserver
 | Eine Stufe nach oben |
Anzahl der Einträge: 9.
2021
Heizinger, Leonhard und Merkl, Rainer 
(2021)
Evidence for the preferential reuse of sub‐domain motifs in primordial protein folds.
Proteins: Structure, Function, and Bioinformatics 89, S. 1167-1179.
Hoffmeister, Helen, Fuchs, Andreas , Komives, Elizabeth, Groebner‐Ferreira, Regina, Strobl, Laura, Nazet, Julian, Heizinger, Leonhard, Merkl, Rainer, Dove, Stefan und Längst, Gernot
(2021)
Sequence and functional differences in the ATPase domains of CHD3 and SNF2H promise potential for selective regulability and drugability.
The FEBS Journal 288, S. 4000-4023.
2020
Hasler, Daniele , Meduri, Rajyalakshmi, Bąk, Maciej , Lehmann, Gerhard, Heizinger, Leonhard, Wang, Xin, Li, Zhi-Tong, Sement, François M., Bruckmann, Astrid, Dock-Bregeon, Anne-Catherine , Merkl, Rainer, Kalb, Reinhard, Grauer, Eva, Kunstmann, Erdmute, Zavolan, Mihaela, Liu, Mo-Fang, Fischer, Utz , Meister, Gunter und make_name_string expected hash reference
(2020)
The Alazami Syndrome-Associated Protein LARP7 Guides U6 Small Nuclear RNA Modification and Contributes to Splicing Robustness.
Molecular Cell 77 (5), 1014-1031.e13.
Volltext nicht vorhanden.
, Meduri, Rajyalakshmi, Bąk, Maciej , Lehmann, Gerhard, Heizinger, Leonhard, Wang, Xin, Li, Zhi-Tong, Sement, François M., Bruckmann, Astrid, Dock-Bregeon, Anne-Catherine , Merkl, Rainer, Kalb, Reinhard, Grauer, Eva, Kunstmann, Erdmute, Zavolan, Mihaela, Liu, Mo-Fang, Fischer, Utz , Meister, Gunter und make_name_string expected hash reference
(2020)
The Alazami Syndrome-Associated Protein LARP7 Guides U6 Small Nuclear RNA Modification and Contributes to Splicing Robustness.
Molecular Cell 77 (5), 1014-1031.e13.
Volltext nicht vorhanden.
2019
Semmelmann, Florian, Hupfeld, Enrico, Heizinger, Leonhard, Merkl, Rainer und Sterner, Reinhard
(2019)
A Fold-Independent Interface Residue Is Crucial for Complex Formation and Allosteric Signaling in Class I Glutamine Amidotransferases.
Biochemistry 58 (22), S. 2584-2588.
Volltext nicht vorhanden.
(2019)
A Fold-Independent Interface Residue Is Crucial for Complex Formation and Allosteric Signaling in Class I Glutamine Amidotransferases.
Biochemistry 58 (22), S. 2584-2588.
Volltext nicht vorhanden.
2018
Schwartz, Uwe, Németh, Attila, Diermeier, Sarah , Exler, Josef H., Hansch, Stefan, Maldonado, Rodrigo, Heizinger, Leonhard , Merkl, Rainer und Längst, Gernot
(2018)
Characterizing the nuclease accessibility of DNA in human cells to map higher order structures of chromatin.
Nucleic Acids Research 2018 (1), S. 1-16.
2017
Merkl, Rainer, Verprinsky, Valery, Plach, Maximilian G. und Heizinger, Leonhard
(2017)
Assessing in silico the recruitment and functional spectrum of bacterial enzymes from secondary metabolism.
BMC Evolutionary Biology 17 (36), S. 1-15.
Plach, Maximilian G., Semmelmann, Florian, Busch, Florian, Busch, Markus, Heizinger, Leonhard, Wysocki, Vicki H. , Merkl, Rainer und Sterner, Reinhard
(2017)
Evolutionary diversification of protein–protein interactions by interface add-ons.
Proceedings of the National Academy of Sciences 114 (40), E8333-E8342.
Volltext nicht vorhanden.
, Merkl, Rainer und Sterner, Reinhard
(2017)
Evolutionary diversification of protein–protein interactions by interface add-ons.
Proceedings of the National Academy of Sciences 114 (40), E8333-E8342.
Volltext nicht vorhanden.
2015
Merkl, Rainer, Žváček, Clemens, Heizinger, Leonhard und Friedrichs, Gerald
(2015)
An assessment of catalytic residue 3D ensembles for the prediction of enzyme function.
BMC Bioinformatics 16 (359), S. 1-8.
2014
Diermeier, Sarah Daniela Helena , Kolovos, Petros , Heizinger, Leonhard, Schwartz, Uwe, Georgomanolis, Theodore, Zirkel, Anne, Wedemann, Gero , Grosveld, Frank, Knoch, Tobias A., Merkl, Rainer, Cook, Peter R., Längst, Gernot und Papatonis, Argyris
(2014)
TNFα signalling primes chromatin for NF-κB binding and induces rapid and widespread nucleosome repositioning.
Genome Biology 15 (12).
Universitätsbibliothek
Publikationsserver
Kontakt:
Publizieren: oa@ur.de
0941 943 -4239 oder -69394
Dissertationen: dissertationen@ur.de
0941 943 -3904
Forschungsdaten: datahub@ur.de
0941 943 -5707