Functional dissection of the proton pumping modules of mitochondrial complex I.

Autor: Stefan Dröse, Stephanie Krack, Lucie Sokolova, Klaus Zwicker, Hans-Dieter Barth, Nina Morgner, Heinrich Heide, Mirco Steger, Esther Nübel, Volker Zickermann, Stefan Kerscher, Bernhard Brutschy, Michael Radermacher, Ulrich Brandt

Publikováno v: PLoS Biology, Vol 9, Iss 8, p e1001128 (2011)

Mitochondrial complex I, the largest and most complicated proton pump of the respiratory chain, links the electron transfer from NADH to ubiquinone to the pumping of four protons from the matrix into the intermembrane space. In humans, defects in com

Externí odkaz: https://doaj.org/article/0c7b2c6cd91b4b7aa58153adf4b3d4a5

SYNCRIP-Dependent Nox2 mRNA Destabilization Impairs ROS Formation in M2-Polarized Macrophages

Autor: Andreas von Knethen, Tilo Knape, Ilka Wittig, Annika Klara Giegerich, Laura Kuchler, Ralf P. Brandes, Lisa Katharina Sha, Heinrich Heide, Katrin Schröder, Michael Sze Ka Wong, Bernhard Brüne

Publikováno v: Antioxidants & Redox Signaling. 21:2483-2497

During sepsis, macrophages are alternatively activated toward an M2-like phenotype on contact with apoptotic cells (ACs) or their secretion products. Simultaneously, NADPH oxidase-dependent reactive oxygen species (ROS) formation is attenuated, thus

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aca86a861191707f8a6ff4c46f484a18
https://doi.org/10.1089/ars.2013.5760

ND3, ND1 and 39kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I

Autor: Amanda Birch, Alexander Galkin, Ilka Wittig, Matthew Fuszard, Catherine H. Botting, Paola Labarbuta, Heinrich Heide, Marion Babot, Sara Kee

Publikováno v: Babot, M, Labarbuta, P, Birch, A, Kee, S, Fuszard, M, Botting, C H, Wittig, I, Heide, H & Galkin, A 2014, ' ND3, ND1 and 39 kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I ', Biochimica et Biophysica Acta-Bioenergetics, vol. 1837, no. 6, pp. 929-939 . https://doi.org/10.1016/j.bbabio.2014.02.013
Biochimica et Biophysica Acta

An intriguing feature of mitochondrial complex I from several species is the so-called A/D transition, whereby the idle enzyme spontaneously converts from the active (A) form to the de-active (D) form. The A/D transition plays an important role in ti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ce217f5d33abe3985996ad0de475c3f

Endo-PDI is required for TNFα-induced angiogenesis

Autor: Livia L Camargo, Ralf P. Brandes, Anja Mieth, Heinrich Heide, Andreas Weigert, Krishnaraj Rajalingam, Lucia Rossetti Lopes, Andrea Babelova, Ilka Wittig, Juliane Mooz

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Protein disulfide isomerase (PDI) and its homologs are oxidoreductases facilitating protein folding in the ER. Endo-PDI (also termed ERp46) is highly expressed in endothelial cells. It belongs to the PDI family but its physiological function is large

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::973881a33fdef5eddc0e0bf984f71cd3
https://doi.org/10.1016/j.freeradbiomed.2013.09.028

The Polarity Protein Scrib Is Essential for Directed Endothelial Cell Migration

Autor: Johannes A. Eble, Benno Jungblut, Katalin Wandzioch, U. Ruth Michaelis, Michael Potente, Jean-Paul Borg, Marie-Josée Santoni, Emmanouil Chavakis, Heinrich Heide, Christoph Kruse, Ralf P. Brandes, Yosif Manavski, David Kaluza

Publikováno v: Circulation Research. 112:924-934

Rationale: Polarity proteins are involved in the apico-basal orientation of epithelial cells, but relatively little is known regarding their function in mesenchymal cells. Objective: We hypothesized that polarity proteins also contribute to endotheli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13c44e7dd6ac4d3fddf6d172ea94e4ba
https://doi.org/10.1161/circresaha.112.300592