Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Vamsi K, Moparthi"'
Autor:
Lavanya Moparthi, Viktor Sinica, Vamsi K. Moparthi, Mohamed Kreir, Thibaut Vignane, Milos R. Filipovic, Viktorie Vlachova, Peter M. Zygmunt
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
The authors report how the cold and heat sensing properties of the pain receptor TRPA1 are separately modulated by the C-terminal intracellular domain, and in concert with either the S1–S4 or the S5–S6 transmembrane domain.
Externí odkaz:
https://doaj.org/article/82871199457c46ae864c798a7f5cf7dd
Publikováno v:
PLoS ONE, Vol 14, Iss 8, p e0218300 (2019)
Dps proteins (DNA-binding proteins from starved cells) have been found to detoxify H2O2. At their catalytic centers, the ferroxidase center (FOC), Dps proteins utilize Fe2+ to reduce H2O2 and therefore play an essential role in the protection against
Externí odkaz:
https://doaj.org/article/3351b6999fa642d8a8543c84049ce56b
Publikováno v:
PLoS ONE, Vol 14, Iss 8, p e0218300 (2019)
'PloS One ', vol: 14, pages: e0218300-1-e0218300-22 (2019)
PLoS ONE
'PloS One ', vol: 14, pages: e0218300-1-e0218300-22 (2019)
PLoS ONE
Dps proteins (DNA-binding proteins from starved cells) have been found to detoxify H2O2. At their catalytic centers, the ferroxidase center (FOC), Dps proteins utilize Fe2+ to reduce H2O2 and therefore play an essential role in the protection against
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75ecf5e4215af506864efad79f5dbaec
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-390470
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-390470
Autor:
Jérôme Wenger, Karin Stensjö, Christoph Howe, Patrícia Raleiras, Satish Babu Moparthi, Vamsi K. Moparthi
Publikováno v:
Biochimica et Biophysica Acta (BBA)-Bioenergetics
Biochimica biophysica acta (BBA)-Bioenergetics
Biochimica biophysica acta (BBA)-Bioenergetics, 2019, 1860 (10), pp.148063. ⟨10.1016/j.bbabio.2019.148063⟩
Biochimica biophysica acta (BBA)-Bioenergetics, Elsevier, 2019, 1860 (10), pp.148063. ⟨10.1016/j.bbabio.2019.148063⟩
Biochimica biophysica acta (BBA)-Bioenergetics
Biochimica biophysica acta (BBA)-Bioenergetics, 2019, 1860 (10), pp.148063. ⟨10.1016/j.bbabio.2019.148063⟩
Biochimica biophysica acta (BBA)-Bioenergetics, Elsevier, 2019, 1860 (10), pp.148063. ⟨10.1016/j.bbabio.2019.148063⟩
International audience; Ferritin-like proteins Dps (DNA-binding protein from starved cells) store iron and play a key role in the iron homeostasis in bacteria, yet their iron releasing machinery remains largely unexplored. The electron donor proteins
Autor:
Karin Stensjö, Ann Magnuson, Konstantinos Vavitsas, Vamsi K. Moparthi, Xin Li, Gustaf Sandh, Ievgen Dzhygyr
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857:1766-1776
Cyanobacteria are photosynthetic prokaryotes that are considered biotechnologically prominent organisms for production of high-value compounds. Cyanobacteria are subject to high-light intensities, ...
Autor:
Brijesh Kumar, Torbjörn Drakenberg, Cecilia Hägerhäll, Vamsi K. Moparthi, Yusra Al-Eryani, Eva Sperling, Kamil Górecki
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837(1):178-185
NADH:quinone oxidoreductase or complex I is a large membrane bound enzyme complex that has evolved from the combination of smaller functional building blocks. Intermediate size enzyme complexes exist in nature that comprise some, but not all of the p
Autor:
Kamil Górecki, Yusra Al-Eryani, Vamsi K. Moparthi, Egle Virzintiene, Leonard T. Shumbe, Cecilia Hägerhäll
Publikováno v:
FEBS Letters. 587:3341-3347
MrpA and MrpD are homologous to NuoL, NuoM and NuoN in complex I over the first 14 transmembrane helices. In this work, the C-terminal domain of MrpA, outside this conserved area, was investigated. The transmembrane orientation was found to correspon
Autor:
Vamsi K, Moparthi, Xin, Li, Konstantinos, Vavitsas, Ievgen, Dzhygyr, Gustaf, Sandh, Ann, Magnuson, Karin, Stensjö
Publikováno v:
Biochimica et biophysica acta. 1857(11)
Cyanobacteria are photosynthetic prokaryotes that are considered biotechnologically prominent organisms for production of high-value compounds. Cyanobacteria are subject to high-light intensities, which is a challenge that needs to be addressed in de
Autor:
Cecilia Hägerhäll, Vamsi K. Moparthi
Publikováno v:
Journal of Molecular Evolution
The NADH:quinone oxidoreductase (complex I) has evolved from a combination of smaller functional building blocks. Chloroplasts and cyanobacteria contain a complex I-like enzyme having only 11 subunits. This enzyme lacks the N-module which harbors the
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807(4):427-436
The complex I subunits NuoL, NuoM and NuoN are homologous to two proteins, MrpA and MrpD, from one particular class of Na+/H+ antiporters. In many bacteria MrpA and MrpD are encoded by an operon comprising 6-7 conserved genes. In complex I these prot