Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Felix Alexander Weyer"'
Autor:
Felix Alexander Weyer, Andrea Gumiero, Karine Lapouge, Gert Bange, Jürgen Kopp, Irmgard Sinning
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
N-terminal acetylation is a common eukaryotic protein modification that is primarily catalysed by the N-acetyl transferase complex A (NatA). Here, the authors present the crystal structure of NatA bound to Huntingtin yeast two-hybrid protein K (HypK)
Externí odkaz:
https://doaj.org/article/9c328f88012a4a40805c0b5463ad51b5
Autor:
Andrea Gumiero, Charlotte Conz, Genís Valentín Gesé, Ying Zhang, Felix Alexander Weyer, Karine Lapouge, Julia Kappes, Ulrike von Plehwe, Géza Schermann, Edith Fitzke, Tina Wölfle, Tamás Fischer, Sabine Rospert, Irmgard Sinning
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
In yeast, the heterodimeric ribosome-associated complex (RAC) acts in concert with the Hsp70 protein Ssb, forming a unique chaperone triad. Here the authors use structural and biochemical approaches to shed light on how translation and folding are co
Externí odkaz:
https://doaj.org/article/26b640aed56d4e9cb16591f7ffb42612
Autor:
Dirk Schwarzer, Trinh V. Dinh, Iris Finkemeier, Felix Alexander Weyer, Ruediger Hell, Dominik Layer, Pavlina Miklankova, Irmgard Sinning, Willy V. Bienvenut, Carmela Giglione, Marion Hoffrichter, Eric Linster, Jürgen Kopp, Annika Brünje, Markus Wirtz, Karine Lapouge, Julia Sindlinger, Thierry Meinnel, Wiebke Leemhuis
Publikováno v:
New Phytologist
New Phytologist, Wiley, 2020, ⟨10.1111/nph.16747⟩
New Phytologist, 2020, ⟨10.1111/nph.16747⟩
'New Phytologist ', vol: 228, pages: 554-569 (2020)
New Phytologist, Wiley, 2020, 228 (2), pp.554-669. ⟨10.1111/nph.16747⟩
New Phytologist, 2020, 228 (2), pp.554-669. ⟨10.1111/nph.16747⟩
New Phytologist, Wiley, 2020, ⟨10.1111/nph.16747⟩
New Phytologist, 2020, ⟨10.1111/nph.16747⟩
'New Phytologist ', vol: 228, pages: 554-569 (2020)
New Phytologist, Wiley, 2020, 228 (2), pp.554-669. ⟨10.1111/nph.16747⟩
New Phytologist, 2020, 228 (2), pp.554-669. ⟨10.1111/nph.16747⟩
International audience; In humans and plants, N-terminal acetylation plays a central role in protein homeostasis, affects 80 % of proteins in the cytoplasm and is catalyzed by five ribosome-associated N-acetyltransferases (NatA-E). Humans also posses
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fb74ba67b8a66ad17243c3431a9fcfc
https://hal.archives-ouvertes.fr/hal-02877932
https://hal.archives-ouvertes.fr/hal-02877932
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 20, Iss 4, p 838 (2019)
Volume 20
Issue 4
International Journal of Molecular Sciences, Vol 20, Iss 4, p 838 (2019)
Volume 20
Issue 4
Endotoxins are cell wall components of Gram-negative bacteria. A release of endotoxins into the human blood stream results in an inflammation reaction that can lead to life-threatening conditions like sepsis. Therefore, control for endotoxin contamin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c897905a3e2196a0530d5ee57e9e503
http://europepmc.org/articles/PMC6412962
http://europepmc.org/articles/PMC6412962
Publikováno v:
Nature structuralmolecular biology. 24(2)
Cotranslational chaperones assist de novo folding of nascent polypeptides, prevent them from aggregating and modulate translation. The ribosome-associated complex (RAC) is unique in that the Hsp40 protein Zuo1 and the atypical Hsp70 chaperone Ssz1 fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c92cb4f37da070a019806e95459c894e
https://pubmed.ncbi.nlm.nih.gov/28067917
https://pubmed.ncbi.nlm.nih.gov/28067917
Autor:
Charlotte Conz, Karine Lapouge, Tina Wölfle, Genís Valentín Gesé, Tamás Fischer, Irmgard Sinning, Géza Schermann, Sabine Rospert, Julia Kappes, Andrea Gumiero, Ulrike von Plehwe, Felix Alexander Weyer, Ying Zhang, Edith Fitzke
Publikováno v:
'Nature Communications ', vol: 7, pages: 13563-1-13563-12 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Nature Communications
Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue Ssb. We report the X-ray structure of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae079ce2f2cf5fce0b1b4e4644ec062f
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:45773
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:45773