Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Joel Fauser"'
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
Monoclonal Anti-AMP Antibodies Are Sensitive and Valuable Tools for Detecting Patterns of AMPylation
Autor:
Dorothea Höpfner, Joel Fauser, Marietta S. Kaspers, Christian Pett, Christian Hedberg, Aymelt Itzen
Publikováno v:
iScience, Vol 24, Iss 7, Pp 102731- (2021)
Externí odkaz:
https://doaj.org/article/e9e9859a3fee4d0c910e1668ada63c79
Monoclonal Anti-AMP Antibodies Are Sensitive and Valuable Tools for Detecting Patterns of AMPylation
Autor:
Dorothea Höpfner, Joel Fauser, Marietta S. Kaspers, Christian Pett, Christian Hedberg, Aymelt Itzen
Publikováno v:
iScience, Vol 23, Iss 12, Pp 101800- (2020)
Summary: AMPylation is a post-translational modification that modifies amino acid side chains with adenosine monophosphate (AMP). Recently, a role of AMPylation as a universal regulatory mechanism in infection and cellular homeostasis has emerged, dr
Externí odkaz:
https://doaj.org/article/555092eab7f54de6a6233f1f99eb48b5
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
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
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
Monoclonal Anti-AMP Antibodies Are Sensitive and Valuable Tools for Detecting Patterns of AMPylation
Autor:
Joel Fauser, Christian Hedberg, Aymelt Itzen, Dorothea Höpfner, Marietta S. Kaspers, Christian Pett
Publikováno v:
iScience, Vol 24, Iss 7, Pp 102731-(2021)
iScience
iScience, Vol 23, Iss 12, Pp 101800-(2020)
iScience
iScience, Vol 23, Iss 12, Pp 101800-(2020)
Summary AMPylation is a post-translational modification that modifies amino acid side chains with adenosine monophosphate (AMP). Recently, a role of AMPylation as a universal regulatory mechanism in infection and cellular homeostasis has emerged, dri
Publikováno v:
Bioconjugate chemistry. 31(8)
Protein immobilization has gained high interest in recent years for its valuable applications in life sciences involving drug delivery and protein arrays. Herein, we combine sortase-mediated protein immobilization with the versatility of magnetic nan
Autor:
D. Hoepfner, Aymelt Itzen, Christian Hedberg, Christian Pett, Marietta S. Kaspers, Joel Fauser
AMPylation is a post-translational modification that modifies amino acid side chains with adenosine monophosphate (AMP). Recent progress in the field reveals an emerging role of AMPylation as a universal regulatory mechanism in infection and cellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::827725b430c58730a540b97071a5fa09
https://doi.org/10.1101/2020.06.23.164731
https://doi.org/10.1101/2020.06.23.164731