Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Matthias Uthoff"'
Autor:
Vanessa Boll, Thomas Hermanns, Matthias Uthoff, Ilka Erven, Eva-Maria Hörner, Vera Kozjak-Pavlovic, Ulrich Baumann, Kay Hofmann
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract Besides the regulation of many cellular pathways, ubiquitination is important for defense against invading pathogens. Some intracellular bacteria have evolved deubiquitinase (DUB) effector proteins, which interfere with the host ubiquitin sy
Externí odkaz:
https://doaj.org/article/78ddc7d56803469990a2ec1df90271a2
Autor:
Yu Cao, Florian Kümmel, Elke Logemann, Jan M. Gebauer, Aaron W. Lawson, Dongli Yu, Matthias Uthoff, Beat Keller, Jan Jirschitzka, Ulrich Baumann, Kenichi Tsuda, Jijie Chai, Paul Schulze-Lefert
In plants, host–pathogen coevolution often manifests in reciprocal, adaptive genetic changes through variations in host nucleotide-binding leucine-rich repeat immune receptors (NLR) and virulence-promoting pathogen effectors. In grass powdery milde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92d6084c74b826892e3a8ddc2448d644
https://doi.org/10.1101/2023.05.05.539654
https://doi.org/10.1101/2023.05.05.539654
Autor:
Vanessa Boll, Thomas Hermanns, Matthias Uthoff, Ilka Erven, Eva-Maria Hörner, Vera Kozjak-Pavlovic, Ulrich Baumann, Kay Hofmann
Besides the regulation of many cellular pathways, ubiquitination is important for the defence against invading pathogens. Some intracellular bacteria have evolved deubiquitinase (DUB) effector proteins, which interfere with the host ubiquitin system
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70afc643e6a75205c7a57a0812e4ba2d
https://doi.org/10.21203/rs.3.rs-2647839/v1
https://doi.org/10.21203/rs.3.rs-2647839/v1
Autor:
Ulrich Baumann, Matthias Uthoff
Publikováno v:
Journal of Structural Biology. 204:199-206
Two crystal structures of a transmembrane helix-lacking FtsH construct from Aquifex aeolicus have been determined at 2.9 A and 3.3 A resolution in space groups R32 and P312, respectively. Both structures are virtually identical despite different crys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3466fe8d09aca37f808015045c90f68
https://doi.org/10.1016/j.jsb.2018.08.009
https://doi.org/10.1016/j.jsb.2018.08.009
Autor:
Magdalena Schacherl, Christian Pichlo, Denzel, Thomas Hermanns, Matthias Uthoff, Christine Toelzer, S. Ocal, S. Ruegenberg, K. Chojnacki, Kay Hofmann, Karsten Niefind, Ulrich Baumann
Publikováno v:
Acta Crystallogr F Struct Biol Commun
The identification of initial lead conditions for successful protein crystallization is crucial for structural studies using X-ray crystallography. In order to reduce the number of false-negative conditions, an emerging number of fluorescence-based m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25bd7ce3e87f98a0c804f0262e7ff4f3
https://doi.org/10.1107/s2053230x18005253
https://doi.org/10.1107/s2053230x18005253
Autor:
Matthias, Uthoff, Ulrich, Baumann
Publikováno v:
Journal of structural biology. 204(2)
Two crystal structures of a transmembrane helix-lacking FtsH construct from Aquifex aeolicus have been determined at 2.9 Å and 3.3 Å resolution in space groups R32 and P312, respectively. Both structures are virtually identical despite different cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::214e7058fb2575d0a072235d5466e813
https://pubmed.ncbi.nlm.nih.gov/30118817
https://pubmed.ncbi.nlm.nih.gov/30118817
Autor:
Ulrich Baumann, Matthias Uthoff
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 74:a89-a89
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::702dd8b9140b00fafaa26f7e15ab3589
https://doi.org/10.1107/s0108767318099105
https://doi.org/10.1107/s0108767318099105
Autor:
Sinan Oecal, Corvin Ernst, Ulrich Baumann, Heinrich Sticht, Frank Zaucke, Jan M. Gebauer, Matthias Uthoff, Eileen Socher
Publikováno v:
The Journal of biological chemistry. 291(24)
Heat shock protein 47 (HSP47) is an endoplasmic reticulum (ER)-resident collagen-specific chaperone and essential for proper formation of the characteristic collagen triple helix. It preferentially binds to the folded conformation of its clients and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fde21a0c17f557f9cfa9c6f1f670680
https://pubmed.ncbi.nlm.nih.gov/27129216
https://pubmed.ncbi.nlm.nih.gov/27129216