Publikationen von C Igreja

Shah, K.; He, S.; Turner, D.; Corbo, J.; Rebbani, K.; Dominguez, D.; Bateman, D.; Cheloufi, S.; Igreja, C.; Valkov, E. et al.; Murn, J.: Regulation by the RNA-binding protein Unkempt at its effector interface. Nature Communications 15 (1), 3159 (2024)

Sobti, M.; Mead, B.; Stewart, A.; Igreja, C.; Christie, M.: Molecular basis for GIGYF-TNRC6 complex assembly. RNA: A Publication of the RNA Society 29 (6), S. 724 - 734 (2023)

Christie, M.; Igreja, C.: eIF4E-homologous protein (4EHP): a multifarious cap-binding protein. The FEBS Journal 290 (2), S. 266 - 285 (2023)

Igreja, C.; Loschko, T.; Schäfer, A.; Sharma, R.; Quiobe, S.; Aloshy, E.; Witte, H.; Sommer, R.: Application of ALFA-Tagging in the Nematode Model Organisms Caenorhabditis elegans and Pristionchus pacificus. Cells 11 (23), 3875 (2022)

Weber, R.; Kleemann, L.; Hirschberg, I.; Chung, M.-Y.; Valkov, E.; Igreja, C.: DAP5 enables main ORF translation on mRNAs with structured and uORF-containing 5' leaders. Nature Communications 13 (1), 7510 (2022)

Han, Z.; Sieriebriennikov, B.; Susoy, V.; Lo, W.-S.; Igreja, C.; Dong, C.; Berasategui, A.; Witte, H.; Sommer, R.: Horizontally Acquired Cellulases Assist the Expansion of Dietary Range in Pristionchus Nematodes. Molecular Biology and Evolution 39 (2), msab370 (2022)

Igreja, C.; Sommer, R.: The Role of Sulfation in Nematode Development and Phenotypic Plasticity. Frontiers in Molecular Biosciences 9, 838148 (2022)

Weber, R.; Chung, M.-Y.; Keskeny, C.; Zinnall, U.; Landthaler, M.; Valkov, E.; Izaurralde, E.; Igreja, C.: 4EHP and GIGYF1/2 Mediate Translation-Coupled Messenger RNA Decay. Cell Reports 33 (2), 108262 (2020)

Räsch, F.; Weber, R.; Izaurralde, E.; Igreja, C.: 4E-T-bound mRNAs are stored in a silenced and deadenylated form. Genes and Development 34 (11-12), S. 847 - 860 (2020)

Peter, D.; Ruscica, V.; Bawankar, P.; Weber, R.; Helms, S.; Valkov, E.; Igreja, C.; Izaurralde, E.: Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated translational repression. Genes and Development 33 (19-20), S. 1355 - 1360 (2019)

Chang, C.-T.; Muthukumar, S.; Weber, R.; Levdansky, Y.; Chen, Y.; Bhandari, D.; Igreja, C.; Wohlbold, L.; Valkov, E.; Izaurralde, E.: A low-complexity region in human XRN1 directly recruits deadenylation and decapping factors in 5'-3' messenger RNA decay. Nucleic Acids Research (London) 47 (17), S. 9282 - 9295 (2019)

Hanet, A.; Räsch, F.; Weber, R.; Ruscica, V.; Fauser, M.; Raisch, T.; Kuzuoglu-Öztürk, D.; Chang, C.-T.; Bhandari, D.; Igreja, C. et al.; Wohlbold, L.: HELZ directly interacts with CCR4-NOT and causes decay of bound mRNAs. Life science alliance 2 (5), e201900405 (2019)

Ruscica, V.; Bawankar, P.; Peter, D.; Helms, S.; Igreja, C.; Izaurralde, E.: Direct role for the Drosophila GIGYF protein in 4EHP-mediated mRNA repression. Nucleic Acids Research (London) 47 (13), S. 7035 - 7048 (2019)

Keskeny, C.; Raisch, T.; Sgromo, A.; Igreja, C.; Bhandari, D.; Weichenrieder, O.; Izaurralde, E.: A conserved CAF40-binding motif in metazoan NOT4 mediates association with the CCR4-NOT complex. Genes and Development 33 (3-4), S. 236 - 252 (2019)

Grüner, S.; Weber, R.; Peter, D.; Chung, M.-Y.; Igreja, C.; Valkov, E.; Izaurralde, E.: Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast. Nucleic Acids Research (London) 46 (13), S. 6893 - 6908 (2018)

Peter, D.; Weber, R.; Sandmeir, F.; Wohlbold, L.; Helms, S.; Bawankar, P.; Valkov, E.; Igreja, C.; Izaurralde, E.: GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression. Genes and Development 31 (11), S. 1147 - 1161 (2017)

Grüner, S.; Peter, D.; Weber, R.; Wohlbold, L.; Chung, M.-Y.; Weichenrieder, O.; Valkov, E.; Igreja, C.; Izaurralde, E.: The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation. Molecular Cell 64 (3), S. 467 - 479 (2016)

Peter, D.; Weber, R.; Köne, C.; Chung, M.-Y.; Ebertsch, L.; Truffault, V.; Weichenrieder, O.; Igreja, C.; Izaurralde, E.: Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation. Genes and Development 29 (17), S. 1835 - 1849 (2015)

Peter, D.; Igreja, C.; Weber, R.; Wohlbold, L.; Weiler, C.; Ebertsch, L.; Weichenrieder, O.; Izaurralde, E.: Molecular architecture of 4E-BP translational inhibitors bound to eIF4E. Molecular Cell 57 (6), S. 1074 - 1087 (2015)

Igreja, C.; Peter, D.; Weiler, C.; Izaurralde, E.: 4E-BPs require non-canonical 4E-binding motifs and a lateral surface of eIF4E to repress translation. Nature Communications 5, 4790 (2014)