Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Burak Gulen"'
Autor:
Joel Fauser, Burak Gulen, Vivian Pogenberg, Christian Pett, Danial Pourjafar-Dehkordi, Christoph Krisp, Dorothea Höpfner, Gesa König, Hartmut Schlüter, Matthias J. Feige, Martin Zacharias, Christian Hedberg, Aymelt Itzen
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
The ER chaperone BiP is critical for the unfolded protein response and tightly regulated through reversible AMPylation by FICD, but the structural basis is unknown. Here the authors use thiol-reactive nucleotide derivatives to stabilize the transient
Externí odkaz:
https://doaj.org/article/5b881075f8d343709870eb7b338a3da3
Autor:
Jiqing Du, Marie-Kristin von Wrisberg, Burak Gulen, Matthias Stahl, Christian Pett, Christian Hedberg, Kathrin Lang, Sabine Schneider, Aymelt Itzen
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The Legionella effector DrrA AMPylates the host protein Rab1 during infection, but the mechanism is still under debate. Here, the authors provide structural insights into the low-affinity DrrA:Rab1 interaction, showing that Rab1 allosterically activa
Externí odkaz:
https://doaj.org/article/db46eaf2179e4b49abbf39b105a93816
Autor:
Anton S Petrov, Chad R Bernier, Burak Gulen, Chris C Waterbury, Eli Hershkovits, Chiaolong Hsiao, Stephen C Harvey, Nicholas V Hud, George E Fox, Roger M Wartell, Loren Dean Williams
Publikováno v:
PLoS ONE, Vol 9, Iss 2, p e88222 (2014)
Accurate secondary structures are important for understanding ribosomes, which are extremely large and highly complex. Using 3D structures of ribosomes as input, we have revised and corrected traditional secondary (2°) structures of rRNAs. We identi
Externí odkaz:
https://doaj.org/article/753e7f655e844b92ae3b749e03d9e869
Publikováno v:
FEBS Lett
Small GTPases orchestrate numerous cellular pathways, acting as molecular switches and regulatory hubs to transmit molecular signals and because of this, they are often the target of pathogens. During infection, pathogens manipulate host cellular net
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfcf3d5e13992ce3d4aac581d2d113de
https://doi.org/10.1002/1873-3468.14516
https://doi.org/10.1002/1873-3468.14516
Autor:
Burak Gulen, Aymelt Itzen
Publikováno v:
Trends in Microbiology. 30:350-363
AMPylation, a post-translational modification (PTM) first discovered in the late 1960s, is catalyzed by adenosine monophosphate (AMP)-transferring enzymes. The observation that filamentation-induced-by-cyclic-AMP (fic) enzymes are associated with thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1daddf41a6fe2d52efb123143b1e5e64
https://doi.org/10.1016/j.tim.2021.08.003
https://doi.org/10.1016/j.tim.2021.08.003
Autor:
Amanda K. Casey, Hillery F. Gray, Suneeta Chimalapati, Genaro Hernandez, Andrew T. Moehlman, Nathan Stewart, Hazel A. Fields, Burak Gulen, Kelly A. Servage, Karoliina Stefanius, Aubrie Blevins, Bret M. Evers, Helmut Krämer, Kim Orth
Publikováno v:
Proceedings of the National Academy of Sciences. 119
The proper balance of synthesis, folding, modification, and degradation of proteins, also known as protein homeostasis, is vital to cellular health and function. The unfolded protein response (UPR) is activated when the mechanisms maintaining protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06a7572e9a56427de8aab757ba238a25
https://doi.org/10.1073/pnas.2208317119
https://doi.org/10.1073/pnas.2208317119
Autor:
Maria Ahmad, Vasanta L Chivukula, Caeden D. Meade, Aparna Maddala, Holly M McCann, Aakash Sharma, Anton S. Petrov, Burak Gulen, Claudia Alvarez-Carreño, Chad R. Bernier, Loren Dean Williams, Petar I. Penev
Publikováno v:
Nucleic Acids Research
ProteoVision is a web server designed to explore protein structure and evolution through simultaneous visualization of multiple sequence alignments, topology diagrams and 3D structures. Starting with a multiple sequence alignment, ProteoVision comput
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c3e322c09019430994beae063e23825
https://doi.org/10.1093/nar/gkab351
https://doi.org/10.1093/nar/gkab351
Publikováno v:
Bioconjugate Chemistry. 32:879-890
Structural characterization of macromolecular assemblies is often limited by the transient nature of the interactions. The development of specific chemical tools to covalently tether interacting proteins to each other has played a major role in vario
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7ba176f547f61f7857e23e5ca41c161
https://doi.org/10.1021/acs.bioconjchem.1c00118
https://doi.org/10.1021/acs.bioconjchem.1c00118
Autor:
Martin Zacharias, Christian Hedberg, Christoph Krisp, Joel Fauser, Matthias J. Feige, Christian Pett, Aymelt Itzen, Dorothea Höpfner, Danial Pourjafar-Dehkordi, Burak Gulen, Gesa König, Hartmut Schlüter, Vivian Pogenberg
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications 12(1), 2426 (2021). doi:10.1038/s41467-021-22596-0
Nature Communications
Nature Communications 12(1), 2426 (2021). doi:10.1038/s41467-021-22596-0
Nature Communications
Nature Communications 12(1), 2426 (2021). doi:10.1038/s41467-021-22596-0
To adapt to fluctuating protein folding loads in the endoplasmic reticulum (ER), the Hsp70 chaperone BiP is reversibly modified with adenosine monophosphate (AMP) by the ER
To adapt to fluctuating protein folding loads in the endoplasmic reticulum (ER), the Hsp70 chaperone BiP is reversibly modified with adenosine monophosphate (AMP) by the ER
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d40798e1b2f32b1564e04d9e1ffc15f
https://doaj.org/article/5b881075f8d343709870eb7b338a3da3
https://doaj.org/article/5b881075f8d343709870eb7b338a3da3
Autor:
Christian Pett, Christian Hedberg, Burak Gulen, Hartmut Schlüter, Joel Fauser, Michael F. Albers, Vivian Pogenberg, Aymelt Itzen, Christoph Krisp, Marie Rosselin
Publikováno v:
Nature Chemistry. 12:732-739
Various pathogenic bacteria use post-translational modifications to manipulate the central components of host cell functions. Many of the enzymes released by these bacteria belong to the large Fic family, which modify targets with nucleotide monophos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1baf586e4a4f86a1ece1f3455e018b1
https://doi.org/10.1038/s41557-020-0484-6
https://doi.org/10.1038/s41557-020-0484-6